FUNCTION: Probably functions as a manganese efflux pump. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MntP (TC 9.B.29) family.


FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRA4 sub- subfamily.


FUNCTION: Involved in the metabolism of ADP-ribose 1',2'-cyclic phosphate which is produced as a consequence of tRNA splicing. SUBCELLULAR LOCATION: Golgi apparatus. SIMILARITY: Belongs to the 2H phosphoesterase superfamily. CPD1 family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AIR synthase family.


FUNCTION: May be involved in microtubule organization and stabilization. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Nucleus Cytoplasm Cleavage furrow Note=Cell-cycle-dependent association with the centrosome. Colocalizes with a subpopulation of microtubules. Does not associate with microtubules during mitosis but reassociates with microtubules during cytokinesis. Localizes to the central portions of a small subset of microtubules in interphase cells and a subpopulation of microtubules in the cleavage furrow, not present in the mitotic spindle (By similarity).


FUNCTION: Binds 7-ketocholesterol. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the OSBP family.


FUNCTION: Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4- methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family.


FUNCTION: Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR- boxes. SIMILARITY: Belongs to the NrdR family.


FUNCTION: Part of the ABC transporter complex GsiABCD involved in glutathione import. Probably responsible for the translocation of the substrate across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family.


FUNCTION: Irreversibly relaxes supercoiled DNA and catalyzes double- stranded breakage. Acts also as a ribosome inactivating protein. SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily.


FUNCTION: Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons. SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 1 subfamily.


SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the UPF0312 family. Type 1 subfamily.


FUNCTION: Major function may be to aid in digestion of the blood meal. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase S1 family.


FUNCTION: Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. SIMILARITY: Belongs to the L-aspartate dehydrogenase family.


FUNCTION: Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.


FUNCTION: May be involved in positioning the distal bud pole signal. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Found at presumptive bud sites, bud tips, and the distal poles of daughter cells. SIMILARITY: To yeast BUD9.


FUNCTION: May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power. Is involved in nitrate assimilation. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.


FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein; Stromal side. SIMILARITY: In the C-terminal section; belongs to the peptidase M41 family. SIMILARITY: In the central section; belongs to the AAA ATPase family.


FUNCTION: Protein transport. Probably involved in vesicular traffic. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Early endosome membrane; Lipid-anchor Melanosome. SIMILARITY: Belongs to the small GTPase superfamily. Rab family.


SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein Late endosome. SIMILARITY: Belongs to the TMEM192 family.


FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the AccA family.


FUNCTION: Stationary phase-essential protein not required for growth on nonfermentable carbon sources. SIMILARITY: Belongs to the SPG4 family.


SIMILARITY: Belongs to the PPR family. P subfamily.


FUNCTION: Also exhibits in vitro acyl transferase activity, transferring the acyl moiety of short-chain amides to hydroxylamine to form hydroxamates. FUNCTION: Catalyzes the hydrolysis of short-chain aliphatic amides to their corresponding organic acids with release of ammonia. SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. Aliphatic amidase family.


FUNCTION: Acts as a negative regulator of innate and adaptive immunity by maintaining immune homeostasis. Negative regulator of Toll-like receptor and T-cell receptor function. Prevents hyperresponsiveness of the immune system and maintains immune homeostasis. Inhibits JUN/AP1 and NF-kappa-B activation. Promotes Fas-induced apoptosis (By similarity). SIMILARITY: Belongs to the TNFAIP8 family. TNFAIP8L2 subfamily.


FUNCTION: Probably functions as a manganese efflux pump. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MntP (TC 9.B.29) family.


FUNCTION: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds domoate > kainate >> L-glutamate = quisqualate >> AMPA = NMDA (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Postsynaptic cell membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIK3 subfamily.


FUNCTION: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Maltooligosaccharide importer (TC 3.A.1.1.1) family.


FUNCTION: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Nucleus membrane; Peripheral membrane protein; Cytoplasmic side Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. SIMILARITY: Belongs to the NPL4 family.


FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the complex I NDUFA9 subunit family.


FUNCTION: May possess sialyltransferase-like activity in vitro. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 29 family.


FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation. SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the VPS37 family.


FUNCTION: Splits dipeptides with a prolyl residue in the C-terminal position. SIMILARITY: Belongs to the peptidase M24B family. Bacterial-type prolidase subfamily.


FUNCTION: Binds to bile acids and is involved in enterohepatic bile acid metabolism. Required for efficient apical to basolateral transport of conjugated bile acids in ileal enterocytes (By similarity). Stimulates gastric acid and pepsinogen secretion (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.


FUNCTION: Plays a major role in the induction and maintenance of cellular transformation. E6 associates with host UBE3A/E6-AP ubiquitin- protein ligase and modulates its activity. Protects host keratinocytes from apoptosis by mediating the degradation of host BAK1. May also inhibit host immune response. SUBCELLULAR LOCATION: Host cytoplasm Host nucleus. SIMILARITY: Belongs to the papillomaviridae E6 protein family.


FUNCTION: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. SIMILARITY: Belongs to the peptidase M67A family.


FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity). SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the eukaryotic ATPase epsilon family.


FUNCTION: Seed storage protein. SUBCELLULAR LOCATION: Protein storage vacuole. SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.


FUNCTION: Seems to be required for the assembly of the photosystem I complex. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Ycf4 family.


FUNCTION: Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the methylthiotransferase family. RimO subfamily.


FUNCTION: Participates in the control of the reentry into the cell cycle following pheromone treatment. SIMILARITY: Belongs to the FAR11 family.


FUNCTION: May influence the maintenance, growth, or differentiation of chemosensory cilia on the apical dendrites of olfactory neurons. Major component of the extracellular matrix of the olfactory neuroepithelium. SUBCELLULAR LOCATION: Secreted, extracellular space.


FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the heme-copper respiratory oxidase family.


FUNCTION: Low-affinity transporter for external inorganic phosphate (Pi). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. phosphate:H(+) symporter (TC 2.A.1.9) family.


FUNCTION: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the type II topoisomerase GyrB family.


FUNCTION: May play a role in abiotic stress response. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ADIPOR family.


FUNCTION: Binds to sodium channels (Nav) and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active on insects. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Alpha subfamily.


SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SMIM13 family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the mite group 7 allergen family.


FUNCTION: DNA-binding global transcriptional regulator which is involved in the adaptive response to starvation and acts by directly or indirectly controlling the expression of numerous genes in response to nutrient availability. During rapid exponential growth, CodY is highly active and represses genes whose products allow adaptation to nutrient depletion. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CodY family.


FUNCTION: Necessary for sperm flagellar function. Plays a role in motile ciliogenesis. May help to recruit STK36 to the cilium or apical surface of the cell to initiate subsequent steps of construction of the central pair apparatus of motile cilia (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, flagellum axoneme Cytoplasm, cytoskeleton, cilium axoneme Cell projection, cilium, flagellum Note=Detected on the sperm flagellum axoneme. Detected in the central apparatus of the axoneme. Colocalizes with SPAG6 on microtubules (By similarity).


FUNCTION: Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto- arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4- amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido- arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. SIMILARITY: In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily. SIMILARITY: In the N-terminal section; belongs to the Fmt family. UDP- L-Ara4N formyltransferase subfamily.


FUNCTION: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M17 family.


FUNCTION: The products of the Gag polyproteins of infectious retroviruses perform highly complex orchestrated tasks during the assembly, budding, maturation, and infection stages of the viral replication cycle. During viral assembly, the proteins form membrane associations and self-associations that ultimately result in budding of an immature virion from the infected cell. Gag precursors also function during viral assembly to selectively bind and package two plus strands of genomic RNA. Endogenous Gag proteins may have kept, lost or modified their original function during evolution. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Note=Cytoplasmic membrane (in a transfection system). SIMILARITY: Belongs to the beta type-B retroviral Gag protein family. HERV class-II K(HML-2) gag subfamily.


SIMILARITY: Belongs to the UPF0352 family.


SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family.


SIMILARITY: Belongs to the sulfatase family.


FUNCTION: Involved in nuclear pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus, Cajal body Nucleus, nucleoplasm Cytoplasm Note=Present in coiled bodies and an interchromatin network. Redistributed throughout the cytoplasm upon entry into mitosis. SIMILARITY: Belongs to the RRM U1 A/B'' family.


FUNCTION: N-acetylglutamate synthase involved in arginine biosynthesis. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the acetyltransferase family.


FUNCTION: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Therefore, by controlling the phosphorylation state of HPr, HPrK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion. SIMILARITY: Belongs to the HPrK/P family.


FUNCTION: Is capable of binding multiple equivalents of a variety of divalent and trivalent metals, including Cu(2+) and Fe(3+) but also Mn(2+), Ni(2+), Mg(2+) and Zn(2+). Is able to bind up to six Cu(2+) atoms. It is proposed to be a metal scavenging protein that has a role in cellular copper management in N.europaea. SUBCELLULAR LOCATION: Periplasm.


FUNCTION: Minor structural protein present in one or two copies per virion. Does not seem to play a role in capsid assembly, but is essential for production of infectious virus (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm.


FUNCTION: Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the pescadillo family.


FUNCTION: Receptor for corticotropin (ACTH). This receptor is mediated by G proteins (G(s)) which activate adenylate cyclase (cAMP). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: May regulate expression of the erythromycin resistance protein.


FUNCTION: Copper metallochaperone essential for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Binds two copper ions and delivers them to the metallochaperone SCO1 which transports the copper ions to the Cu(A) site on the cytochrome c oxidase subunit II (MT-CO2/COX2). SUBCELLULAR LOCATION: Mitochondrion intermembrane space Cytoplasm. SIMILARITY: Belongs to the COX17 family.


SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein. SIMILARITY: Belongs to the AIM34 family.


FUNCTION: Regulatory protein for the xylBAFGHR operon.


FUNCTION: Minor structural protein present in one or two copies per virion. Does not seem to play a role in capsid assembly, but is essential for production of infectious virus (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the vesivirus VP2 protein family.


FUNCTION: Involved in gonadal development. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome (EE) transport from the hyphal tip. Required for localization of dynein to the mitotic spindle poles. Recruits additional proteins to the dynein complex at SPBs. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle pole Note=Localizes to the plus ends of microtubules at the hyphal tip and the mitotic spindle poles. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, spindle pole Note=Localizes to the plus ends of microtubules at the hyphal tip and the mitotic spindle poles. SIMILARITY: Belongs to the WD repeat LIS1/nudF family.


SIMILARITY: Belongs to the serine/threonine dehydratase family. DsdA subfamily.


FUNCTION: Involved in the catabolism of branched amino acids such as leucine. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the HMG-CoA lyase family.


SIMILARITY: To M.tuberculosis Rv2656c.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the EccD/Snm4 family.


FUNCTION: N-malonyltransferase; part of the Fusarium detoxification of benzoxazolinone cluster 2 (FDB2) involved in the degradation of benzoxazolinones produced by the host plant (PubMed:19302487, PubMed:26808652). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (PubMed:11876429). The first step in the detoxification of benzoxazolinones involves the hydrolysis of the cyclic ester bond of benzoxazolinones by the FDB1 cluster gamma-lactamase MBL1 to aminophenols (PubMed:26808652, PubMed:12788712). MBL1 is able to convert BOA into 2-aminophenol (2- AP), as well as MBOA into 5-methoxy-2-aminophenol (2-AMP) (PubMed:26808652, PubMed:12788712). The FDB2 cluster N- malonyltransferase FDB2/NAT1 then metabolizes aminophenols via N- malonylation to non-toxic malonamic acids (PubMed:19302487, PubMed:12788712). FDB2/NAT1 converts 2-AP into N-(2-hydroxyphenyl) malonamic acid (HPMA) and 2-AMP into N-(2-hydroxy-4-methoxyphenyl) malonamic acid (HMPMA) (PubMed:19302487, PubMed:12788712). The duplicated dienlactone hydrolases DLH1 and DLH2 may provide redundant function for hydrolyzing the lactone moiety in the BOA molecule (Probable). The roles of the amidases an other enzymes encoded by the 2 FDB clusters have not been identified so far (Probable). SIMILARITY: Belongs to the arylamine N-acetyltransferase family.


SIMILARITY: To A.aeolicus aq_1211 and aq_1583.


FUNCTION: Acts as component of the retriever complex. The retriever complex is a heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos such as integrin alpha-5/beta-1 (ITGA5:ITGB1). The recruitment of the retriever complex to the endosomal membrane involves CCC and WASH complexes. In the endosomes, drives the retrieval and recycling of NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo essential for the homeostatic maintenance of numerous cell surface proteins associated with processes that include cell migration, cell adhesion, nutrient supply and cell signaling. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association with the CCC complex and cooperation with the WASH complex on early endosomes. Seems not to be required for CCC complex stability. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein Endosome Note=Endosome location is dependent of the association with the CCC and WASH complexes. SIMILARITY: Belongs to the VPS35L family.


FUNCTION: Regulates the earliest stages of development of the anterior neural plate. Plays a role in forebrain development by inhibiting the expression of otx2 and pax6 in the rostral region of the anterior neural plate. Necessary for both neural differentiation and neural patterning. Controls Spemann organizer development. May act as a transcriptional repressor (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Enters the cytoplasm in the presence of zyx. SIMILARITY: Belongs to the ANF homeobox family.


FUNCTION: Binds and inhibits CYCD2-1/CDKA-1 complex kinase activity. May target specifically CDKA-1. SUBCELLULAR LOCATION: Nucleus, nucleoplasm Note=Distributed in a ponctuate pattern. SIMILARITY: Belongs to the CDI family. ICK/KRP subfamily.


FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network Endoplasmic reticulum. SIMILARITY: Belongs to the TRAPP small subunits family. BET3 subfamily.


FUNCTION: Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm Rough endoplasmic reticulum Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). SIMILARITY: Belongs to the eukaryotic ribosomal protein eS21 family.


FUNCTION: Functions as a component of numerous distinct DCX (DDB1-CUL4- X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. In the DCX complexes, acts as a scaffolding subunit required to stabilize the complex. SIMILARITY: Belongs to the DDA1 family.


FUNCTION: May be involved in the specific maturation or degradation of a number of bioactive peptides. May play a role in the contractions of the heart, gut and testes, and in spermatid differentiation. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the peptidase M2 family.


FUNCTION: Has antibacterial activity against Gram-positive bacterium S.pneumoniae Serotype 14. Is also active against Gram-negative bacteria M.catarrhalis 1857, and non-typeable H.influenzae strains 86-028NP and 1128. Has antifungal activity against C.albicans. May have a role in maintaining sterility in the middle ear (PubMed:14996845). May act as a ligand for C-C chemokine receptor CCR6. Positively regulates the sperm motility and bactericidal activity in a CCR6-dependent manner. Binds to CCR6 and triggers Ca2+ mobilization in the sperm which is important for its motility (By similarity). SUBCELLULAR LOCATION: Secreted Membrane Note=Associates with tumor cell membrane-derived microvesicles. SIMILARITY: Belongs to the beta-defensin family.


FUNCTION: Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2- selenouridine (Se2U-RNA). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiouridine (geS2U) and subsequent selenation of the latter derivative to 2-selenouridine (Se2U) in the tRNA chain. SIMILARITY: Belongs to the SelU family.


FUNCTION: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Attractants increase the level of methylation while repellents decrease the level of methylation, the methyl groups are added by the methyltransferase CheR and removed by the methylesterase CheB. FUNCTION: Receptor for the attractant L-serine and related amino acids. Is also responsible for chemotaxis away from a wide range of repellents, including leucine, indole, and weak acids. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein Note=Found predominantly at cell poles. SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein family.


FUNCTION: Low-affinity, high capacity permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. Cationic amino acid transporter (CAT) (TC 2.A.3.3) family.


FUNCTION: Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the BamC family.


FUNCTION: Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RbsD / FucU family. RbsD subfamily.


FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL19 family.


FUNCTION: As part of the spliceosome, plays a role in pre-mRNA splicing. Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the cyclophilin-type PPIase family.


FUNCTION: Involved in the degradation of chitin. ChbG is essential for growth on the acetylated chitooligosaccharides chitobiose and chitotriose but is dispensable for growth on cellobiose and chitosan dimer, the deacetylated form of chitobiose. Deacetylation of chitobiose-6-P and chitotriose-6-P is necessary for both the activation of the chb promoter by the regulatory protein ChbR and the hydrolysis of phosphorylated beta-glucosides by the phospho-beta-glucosidase ChbF. Catalyzes the removal of only one acetyl group from chitobiose-6-P to yield monoacetylchitobiose-6-P, the inducer of ChbR and the substrate of ChbF. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the YdjC deacetylase family. ChbG subfamily.


FUNCTION: The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase T1A family.


FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Essential component of the endosomal pH-sensing machinery (By similarity). May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH (By similarity). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Endosome membrane. SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.


FUNCTION: Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Lumenal side Note=Loosely bound to the inner thylakoid membrane surface in chloroplasts (PubMed:1920431). SIMILARITY: Belongs to the plastocyanin family.


FUNCTION: Associates with NCBP1/CBP80 to form an alternative cap- binding complex (CBC) which plays a key role in mRNA export. NCBP3 serves as adapter protein linking the capped RNAs (m7GpppG-capped RNA) to NCBP1/CBP80. Unlike the conventional CBC with NCBP2 which binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus, the alternative CBC with NCBP3 does not bind snRNA and associates only with mRNA thereby playing a role in only mRNA export. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the NCBP3 family.


FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by specifically elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme ube2c/ubch10 on APC/C substrates, enhancing the degradation of APC/C substrates by the proteasome and promoting mitotic exit. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.


FUNCTION: Component of the 40S ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. FUNCTION: Component of the 40S ribosomal subunit (PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Note=Localized in the granular component (GC) region of the nucleolus. Methylation is required for its localization in the GC region. Colocalizes with NPS1 in the GC region of the nucleolus. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Note=Localized in the granular component (GC) region of the nucleolus. Methylation is required for its localization in the GC region. Colocalizes with NPS1 in the GC region of the nucleolus. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS10 family.


FUNCTION: Global regulator with both positive and negative effects that mediates modulation of several genes involved in virulence. Also, modulates the expression of genes not previously implicated in pathogenesis (By similarity). SIMILARITY: Belongs to the rot family.


FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MsrQ family.


FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates (By similarity). SIMILARITY: Belongs to the FPG family.


SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family.


FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CybS family.


FUNCTION: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal- beta-1,3-GalNAc sequence of glycoproteins and glycolipids forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto a GalNAc residue inside the backbone core chains. Prefers O-glycans to glycoproteins or glycolipids. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 29 family.


FUNCTION: Involved in 1,2-propanediol (1,2-PD) utilization within the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation by catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate. SUBCELLULAR LOCATION: Bacterial microcompartment. SIMILARITY: Belongs to the PduL family.


FUNCTION: Involved in the pyrimidine salvage pathway. SIMILARITY: In the N-terminal section; belongs to the uridine kinase family. SIMILARITY: In the C-terminal section; belongs to the UPRTase family.


FUNCTION: Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. SIMILARITY: Belongs to the aldehyde dehydrogenase family. AstD subfamily.


FUNCTION: Involved in the transposition of the insertion sequence IS3. FUNCTION: Involved in the transposition of the insertion sequence IS3. SIMILARITY: Belongs to the transposase 8 family.


FUNCTION: Allele DRB1*07:01: Upon EBV infection, presents latent antigen EBNA2 peptide (PRSPTVFYNIPPMPLPPSQL) to CD4-positive T cells, driving oligoclonal expansion and selection of a dominant virus- specific memory T cell subset with cytotoxic potential to directly eliminate virus-infected B cells (PubMed:31308093). May present to T- helper 1 cells several HRV-16 epitopes derived from capsid proteins VP1 (PRFSLPFLSIASAYYMFYDG) and VP2 (VPYVNAVPMDSMVRHNNWSL), contributing to viral clearance (PubMed:27591323). In the context of tumor immunesurveillance, may present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (MTEYKLVVVGAVGVGKSALTIQLI), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies (PubMed:22929521). In metastatic epithelial tumors, presents to intratumoral CD4-positive T cells a KRAS neoantigen (MTEYKLVVVGAVGVGKSALTIQLI) carrying G12V hotspot driver mutation and may mediate tumor regression (PubMed:30282837). FUNCTION: Allele DRB1*03:01: May present to T-helper 1 cells an HRV-16 epitope derived from capsid protein VP2 (NEKQPSDDNWLNFDGTLLGN), contributing to viral clearance (PubMed:27591323). Displays self- peptides derived from retinal SAG (NRERRGIALDGKIKHE) and thyroid TG (LSSVVVDPSIRHFDV) (PubMed:25413013). Presents viral epitopes derived from HHV-6B gH/U48 and U85 antigens to polyfunctional CD4-positive T cells with cytotoxic activity implicated in control of HHV-6B infection (PubMed:31020640). Presents several immunogenic epitopes derived from C. tetani neurotoxin tetX, playing a role in immune recognition and long-term protection (PubMed:19830726). FUNCTION: Allele DRB1*13:01: Presents viral epitopes derived from HHV- 6B antigens to polyfunctional CD4-positive T cells implicated in control of HHV-6B infection. FUNCTION: Allele DRB1*04:01: Presents an immunodominant bacterial epitope derived from M. tuberculosis esxB/culture filtrate antigen CFP- 10 (EISTNIRQAGVQYSR), eliciting CD4-positive T cell effector functions such as IFNG production and cytotoxic activity (PubMed:15265931). May present to T-helper 1 cells an HRV-16 epitope derived from capsid protein VP2 (NEKQPSDDNWLNFDGTLLGN), contributing to viral clearance (PubMed:27591323). Presents tumor epitopes derived from melanoma- associated TYR antigen (QNILLSNAPLGPQFP and DYSYLQDSDPDSFQD), triggering CD4-positive T cell effector functions such as GMCSF production (PubMed:8642306). Displays preferentially citrullinated self-peptides derived from VIM (GVYATR/citSSAVR and SAVRAR/citSSVPGVR) and ACAN (VVLLVATEGR/ CitVRVNSAYQDK) (PubMed:24190431). Displays self- peptides derived from COL2A1 (PubMed:9354468). FUNCTION: Allele DRB1*04:02: Displays native or citrullinated self- peptides derived from VIM. FUNCTION: Allele DRB1*04:05: May present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies. FUNCTION: A beta chain of antigen-presenting major histocompatibility complex class II (MHCII) molecule. In complex with the alpha chain HLA- DRA, displays antigenic peptides on professional antigen presenting cells (APCs) for recognition by alpha-beta T cell receptor (TCR) on HLA-DRB1-restricted CD4-positive T cells. This guides antigen-specific T-helper effector functions, both antibody-mediated immune response and macrophage activation, to ultimately eliminate the infectious agents and transformed cells (PubMed:29884618, PubMed:22327072, PubMed:27591323, PubMed:8642306, PubMed:15265931, PubMed:31495665, PubMed:16148104). Typically presents extracellular peptide antigens of 10 to 30 amino acids that arise from proteolysis of endocytosed antigens in lysosomes (PubMed:8145819). In the tumor microenvironment, presents antigenic peptides that are primarily generated in tumor- resident APCs likely via phagocytosis of apoptotic tumor cells or macropinocytosis of secreted tumor proteins (PubMed:31495665). Presents peptides derived from intracellular proteins that are trapped in autolysosomes after macroautophagy, a mechanism especially relevant for T cell selection in the thymus and central immune tolerance (PubMed:17182262, PubMed:23783831). The selection of the immunodominant epitopes follows two processing modes: 'bind first, cut/trim later' for pathogen-derived antigenic peptides and 'cut first, bind later' for autoantigens/self-peptides (PubMed:25413013). The anchor residue at position 1 of the peptide N-terminus, usually a large hydrophobic residue, is essential for high affinity interaction with MHCII molecules (PubMed:8145819). FUNCTION: Allele DRB1*01:01: Displays an immunodominant epitope derived from Bacillus anthracis pagA/protective antigen, PA (KLPLYISNPNYKVNVYAVT), to both naive and PA-specific memory CD4- positive T cells (PubMed:22327072). Presents immunodominant HIV-1 gag peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls viral load (PubMed:29884618). May present to T-helper 1 cells several HRV-16 epitopes derived from capsid proteins VP1 (PRFSLPFLSIASAYYMFYDG) and VP2 (PHQFINLRSNNSATLIVPYV), contributing to viral clearance (PubMed:27591323). Displays commonly recognized peptides derived from IAV external protein HA (PKYVKQNTLKLAT and SNGNFIAPEYAYKIVK) and from internal proteins M, NP and PB1, with M-derived epitope (GLIYNRMGAVTTEV) being the most immunogenic (PubMed:8145819, PubMed:9075930, PubMed:25413013, PubMed:32668259). Presents a self- peptide derived from COL4A3 (GWISLWKGFSF) to TCR (TRAV14 biased) on CD4-positive, FOXP3-positive regulatory T cells and mediates immune tolerance to self (PubMed:28467828). May present peptides derived from oncofetal trophoblast glycoprotein TPBG 5T4, known to be recognized by both T-helper 1 and regulatory T cells (PubMed:31619516). Displays with low affinity a self-peptide derived from MBP (VHFFKNIVTPRTP) (PubMed:9075930). FUNCTION: Allele DRB1*05:01: Presents an immunodominant HIV-1 gag peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls viral load. FUNCTION: (Microbial infection) Acts as a receptor for Epstein-Barr virus on lymphocytes. FUNCTION: Allele DRB1*15:01: May present to T-helper 1 cells an HRV-16 epitope derived from capsid protein VP2 (SNNSATLIVPYVNAVPMDSM), contributing to viral clearance (PubMed:27591323). Displays a self- peptide derived from MBP (ENPVVHFFKNIVTPR) (PubMed:9782128, PubMed:25413013). May present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies. FUNCTION: Allele DRB1*11:01: Displays an immunodominant HIV-1 gag peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls viral load (PubMed:29884618). May present to T-helper 1 cells an HRV-16 epitope derived from capsid protein VP2 (SDRIIQITRGDSTITSQDVA), contributing to viral clearance (PubMed:27591323). Presents several immunogenic epitopes derived from C. tetani neurotoxin tetX, playing a role in immune recognition and longterm protection (PubMed:19830726). In the context of tumor immunesurveillance, may present tumor-derived neoantigens to CD4-positive T cells and trigger anti-tumor helper functions (PubMed:31495665). FUNCTION: Allele DRB1*15:02: Displays an immunodominant HIV-1 gag peptide (FRDYVDRFYKTLRAEQASQE) on infected dendritic cells for recognition by TRAV24-TRBV2 TCR on CD4-positive T cells and controls viral load (PubMed:29884618). May present to T-helper 1 cells an immunogenic epitope derived from tumor-associated antigen WT1 (KRYFKLSHLQMHSRKH), likely providing for effective antitumor immunity in a wide range of solid and hematological malignancies (PubMed:19120973). FUNCTION: Allele DRB1*04:04: May present to T-helper 1 cells several HRV-16 epitopes derived from capsid proteins VP1 (HIVMQYMYVPPGAPIPTTRN) and VP2 (RGDSTITSQDVANAVVGYGV), contributing to viral clearance (PubMed:27591323). Displays preferentially citrullinated self-peptides derived from VIM (SAVRAR/citSSVPGVR) (PubMed:24190431). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Endoplasmic reticulum membrane; Single-pass type I membrane protein Lysosome membrane; Single-pass type I membrane protein Late endosome membrane; Single-pass type I membrane protein Autolysosome membrane Note=The MHC class II complex transits through a number of intracellular compartments in the endocytic pathway until it reaches the cell membrane for antigen presentation (PubMed:18305173). Component of immunological synapses at the interface between T cell and APC (PubMed:29884618).


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family. MdtL (TC 2.A.1.2.22) subfamily.


FUNCTION: Amphipathic alpha-helical peptide with no antimicrobial activity (PubMed:18584916, PubMed:18795798). Does not display anti- leishmania activity (PubMed:18584916). Does not show hemolytic activity (LC(50)>116 uM) (PubMed:18584916, PubMed:18795798). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Temporin subfamily.


FUNCTION: Part of a gene cluster involved in the biosynthesis of thioplatensimycin (thioPTM) and platensimycin (PTM), potent and selective inhibitors of bacterial and mammalian fatty acid synthases (PubMed:21825154, PubMed:29915173). Catalyzes the hydroxylation of 3- amino-4-hydroxybenzoate (3,4-AHBA) to 3-amino-2,4-dihydroxybenzoate (3,2,4-ADHBA) (Probable). SIMILARITY: Belongs to the 6-hydroxynicotinate 3-monooxygenase family.


FUNCTION: Low-affinity sodium-dicarboxylate cotransporter, that mediates the entry of citric acid cycle intermediates, such as succinate, citrate, fumarate and alpha-ketoglutarate (2-oxoglutarate) into the small intestine and renal proximal tubule (PubMed:10966927) (By similarity). Can transport citrate in a Na(+)-dependent manner, recognizing the divalent form of citrate rather than the trivalent form which is normally found in blood (PubMed:10966927). Transports the dicarboxylate into the cell with a probable stoichiometry of 3 Na(+) for 1 divalent dicarboxylate, rendering the process electrogenic (By similarity). Has a critical role in renal dicarboxylate transport (PubMed:17410095). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SLC13A/DASS transporter (TC 2.A.47) family. NADC subfamily.


FUNCTION: May act as scaffolding protein, and as adapter protein to couple membrane receptors to intracellular signaling pathways. Acts as a mediator of cell spreading and actin cytoskeleton rearrangement. Core component of the CTLH E3 ubiquitin-protein ligase complex that mediates ubiquitination and subsequent proteasomal degradation of target proteins. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side Nucleus Note=Predominantly cytoplasmic. SIMILARITY: Belongs to the RANBP9/10 family.


FUNCTION: Modulates RecA activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RecX family.


FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate. FUNCTION: Catalyzes two reactions: the first one is the production of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP and beta GAR; the second, a side reaction, is the production of acetyl phosphate and ADP from acetate and ATP. SIMILARITY: Belongs to the PurK/PurT family.


FUNCTION: Belongs to an operon involved in the translocation of Yop proteins across the bacterial membranes or in the specific control of this function. FUNCTION: Belongs to an operon involved in the translocation of Yop proteins across the bacterial membranes or in the specific control of this function.


FUNCTION: Vacuolar-sorting receptor (VSR) involved in clathrin-coated vesicles sorting from Golgi apparatus to vacuoles. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein Golgi apparatus membrane; Single-pass type I membrane protein Cytoplasmic vesicle, clathrin-coated vesicle membrane; Single-pass type I membrane protein Prevacuolar compartment membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the VSR (BP-80) family.


FUNCTION: Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT. SIMILARITY: Belongs to the HMD family.


FUNCTION: Involved in spore wall assembly. May be a component of the mitochondrial RNase MRP (MtMRP), a ribonucleoprotein endoribonuclease involved in the cleaving RNA transcripts to generate primers for DNA replication in mitochondria. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the SHE10 family.


FUNCTION: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys- 4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ROX family. NO66 subfamily.


FUNCTION: Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain subfamily. Type I alpha-neurotoxin sub-subfamily.


FUNCTION: Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily.


FUNCTION: Snake venom phospholipase A2 homolog that lacks catalytic activity (By similarity). Shows myotoxic activities (By similarity). Induces local edema a few hours after injection (5-10 ug) in the hind paw (PubMed:12959640). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.


FUNCTION: Putative pheromone receptor implicated in the regulation of social and reproductive behavior. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Accessory protein required for glutamate-gated currents. May participate in the gating of non-NMDA (N-methyl-D-aspartate) ionotropic glutamate receptors such as glr-1. SUBCELLULAR LOCATION: Postsynaptic cell membrane; Single- pass type I membrane protein Synapse Note=Colocalizes with glr-1 at the cell surface. Enriched at postsynaptic membranes.


FUNCTION: Interacts with TGF-beta receptor type-1 (TGFBR1) and inhibits dissociation of activated SMAD2 from TGFBR1, impeding its nuclear accumulation and resulting in impaired TGF-beta signaling. May also affect FOXO, Hippo and Wnt signaling. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the MELT/VEPH family.


FUNCTION: Transcriptional repressor which may act as a negative- feedback regulator of CLOCK-BMAL1 transcriptional activity in the circadian-clock mechanism. May stimulate BMAL1-dependent phosphorylation of CLOCK (PubMed:17310242, PubMed:19414601). However, the physiogical relevance of these observations is unsure, since experiments in knockout mice showed that CIPC is not critially required for basic circadian clock (PubMed:25862660). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol Note=Predominantly localizes to the nucleus, where it co-localizes with CLOCK. At the G1/S boundary, partially translocated to the cytosol.


FUNCTION: Inhibits the enzymatic activity of phospholipase A2 (PA2). SUBCELLULAR LOCATION: Secreted Note=Secreted in blood plasma. SIMILARITY: Belongs to the CNF-like-inhibitor family.


FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. SUBCELLULAR LOCATION: Cytoplasm Melanosome Dynein axonemal particle. SIMILARITY: Belongs to the heat shock protein 90 family.


SUBCELLULAR LOCATION: Cytoplasm Cell septum Cell tip.


FUNCTION: Transcription activator essential for the anti-viral defense called virus basal resistance response pathway (PubMed:11041886, PubMed:15629774, PubMed:18785827, PubMed:24418554). Not involved in HRT-mediated hypersensitive response (HR) and resistance to TCV (PubMed:18785827). Binds DNA non specifically (PubMed:15629774). Activated by proteolytic cleavage through regulated intramembrane proteolysis (RIP) (By similarity). FUNCTION: (Microbial infection) Compromised function in defense response pathway when interacting with the invading viral capsid protein (CP) of turnip crinkle virus (TCV) due to abnormal subcellular localization. SUBCELLULAR LOCATION: Nucleus Endomembrane system; Single-pass membrane protein Note=(Microbial infection) Nuclear localization is blocked by its interaction with the coat protein (CP) of turnip crinkle virus (TCV), thus leading to its accumulation in inclusion-like structures peripheral to the nuclei.


FUNCTION: Multifunctional enzyme involved in mRNA capping. Catalyzes the formation of the 5' cap structure on the viral plus-strand transcripts. Specifically binds to GTP and displays guanylyltransferase and methyltransferase activities. Has affinity for ssRNA but not for dsRNA. Capping activity is non-specific and caps RNAs that initiate with either a G or an A residue. Together with VP1 polymerase, forms a VP1-VP3 complex positioned near the channels situated at each of the five-fold vertices of the core. Following infection, the outermost layer of the virus is lost, leaving a double-layered particle (DLP) made up of the core and VP6 shell. VP1 then catalyzes the transcription of fully conservative plus-strand genomic RNAs that are capped by VP3 and extruded through the DLP's channels into the cytoplasm where they function as mRNAs for translation of viral proteins. DLPs probably have an RNA triphosphatase activity as well, whereas open cores do not. FUNCTION: Counteracts the host innate immune response thanks to its phosphodiesterase that degrades the 5'-triphosphorylated, 2'-5' linked adenylate oligomers produced by the host cell IFN-inducible 2',5'- oligoadenylate synthetase (OAS). The host RNaseL is therefore not activated. SUBCELLULAR LOCATION: Virion Note=Attached inside the inner capsid as a minor component. There are about 11 to 12 copies per virion. SIMILARITY: Belongs to the rotavirus VP3 family.


FUNCTION: Scaffold protein involved in DNA single-strand break repair by mediating the assembly of DNA break repair protein complexes. Negatively regulates ADP-ribosyltransferase activity of PARP1 during base-excision repair in order to prevent excessive PARP1 activity. Recognizes and binds poly-ADP-ribose chains: specifically binds auto- poly-ADP-ribosylated PARP1, limiting its activity. SUBCELLULAR LOCATION: Nucleus Chromosome Note=Moves from the nucleoli to the global nuclear chromatin upon DNA damage. Recruited to DNA damage sites fowwing interaction with poly-ADP-ribose chains.


FUNCTION: [Cytochrome b-c1 complex subunit 9]: Component of the ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII). UQCRFS1 undergoes proteolytic processing once it is incorporated in the complex III dimer. One of the fragments, called subunit 9, corresponds to its mitochondrial targeting sequence (MTS) (By similarity). The proteolytic processing is necessary for the correct insertion of UQCRFS1 in the complex III dimer, but the persistence of UQCRFS1-derived fragments may prevent newly imported UQCRFS1 to be processed and assembled into complex III and is detrimental for the complex III structure and function (By similarity). FUNCTION: [Cytochrome b-c1 complex subunit Rieske, mitochondrial]: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b- c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster. It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q(0) site in cytochrome b to cytochrome c1 (By similarity). Incorporation of UQCRFS1 is the penultimate step in complex III assembly (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Rieske iron-sulfur protein family.


FUNCTION: Promotes integrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells (By similarity). SUBCELLULAR LOCATION: Secreted Secreted, extracellular space, extracellular matrix.


FUNCTION: Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. LepA subfamily.


FUNCTION: As part of the intermicrovillar adhesion complex/IMAC plays a role in epithelial brush border differentiation, controlling microvilli organization and length. Plays a role in assembly of the complex (PubMed:26812018). May play a role in cellular response to endoplasmic reticulum stress (By similarity). SUBCELLULAR LOCATION: Cell projection, microvillus Note=Localizes at the tip of microvilli (PubMed:26812018). May associate with endoplasmic reticulum membranes (By similarity).


FUNCTION: A beta subtype methylase that recognizes the double-stranded sequence 5'-GANTC-3' and methylates non-modifed A-2 on the hemimethylated, post-replicative DNA (Probable) (PubMed:12654995) (By similarity). Opens a bubble in the DNA at the recognition site, allowing precise recognition of the sequence and ensuring enzyme specificity (PubMed:31601797). Functions only in the predivisional cell. Responsible for 5'-GANTC-3' methylation in the cell; methylation of hemimethylated sites generated after replication fork passage occurs late in the predivisional cell, near completion of chromosome replication but prior to cell division. Contributes to the accurate cell-cycle control of DNA replication and cellular morphology (By similarity). FUNCTION: A beta subtype methylase that recognizes the double-stranded sequence 5'-GANTC-3' and methylates non-modifed A-2 on the hemimethylated, post-replicative DNA (PubMed:12654995) (Probable). Functions only in the predivisional cell. Responsible for 5'-GANTC-3' methylation in the cell; remethylation of hemimethylated sites generated after replication fork passage occurs late in the predivisional cell, near completion of chromosome replication but prior to cell division. Constitutive expression of the methylase leads to morphologically aberrant cells as well as cells that have undergone additional chromosome replication. Contributes to the accurate cell- cycle control of DNA replication and cellular morphology (PubMed:8289276, PubMed:8577742). Opens a bubble in the DNA at the recognition site, allowing precise recognition of the sequence and ensuring enzyme specificity (By similarity). Can fully replace its ortholog in R.meliloti (PubMed:9294447). SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.


FUNCTION: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OXA1/ALB3/YidC family. Type 2 subfamily.


FUNCTION: Regulates the dimerization of homeodomain protein HNF-1-alpha and enhances its transcriptional activity. FUNCTION: Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2 (By similarity). SIMILARITY: Belongs to the pterin-4-alpha-carbinolamine dehydratase family.


FUNCTION: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Aux/IAA family.


SIMILARITY: Belongs to the 14-3-3 family.


FUNCTION: Catalyzes the ATP dependent decarboxylation of (R)-5- diphosphomevalonate to form isopentenyl diphosphate (IPP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoids and sterol synthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.


FUNCTION: Endoplasmic reticulum and mitochondria-associated protein that probably functions as a regulator of cellular redox state and thereby regulates protein post-translational modification, protein folding and mitochondrial activity. Indirectly regulates neuronal proliferation, migration, and organization in the developing brain. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein Mitochondrion membrane Note=Localizes to endoplasmic reticulum mitochondria-associated membrane (MAMs) that connect the endoplasmic reticulum and the mitochondria.


FUNCTION: A hormone that controls sex pheromone production in females and pheromone responsiveness in male. Also mediates visceral muscle contractile activity (myotropic activity) (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pyrokinin family.


FUNCTION: Probable receptor, which may be involved in the internalization of lipophilic molecules and/or signal transduction. May act as a tumor suppressor (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein Membrane, coated pit. SIMILARITY: Belongs to the LDLR family.


FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates the degradation of the iron exporter ferroportin/SLC40A1 and thus regulates iron homeostasis. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein Cytoplasm. SIMILARITY: Belongs to the RBR family. RNF217 subfamily.


SIMILARITY: Belongs to the AAR2 family.


FUNCTION: May self assemble to form an icosahedral capsid. Most abundant protein in the virion. SUBCELLULAR LOCATION: Virion.


FUNCTION: Krueppel is a gap class segmentation protein. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.


FUNCTION: A translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Usually binds in the 5'- UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding, thus repressing translation. Its main target seems to be the major flagellin gene, while its function is anatagonized by FliW. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CsrA/RsmA family.


FUNCTION: Guanine-nucleotide releasing factor that promotes the exchange of Ran-bound GDP by GTP, and thereby plays an important role in RAN-mediated functions in nuclear import and mitosis. Contributes to the generation of high levels of chromosome-associated, GTP-bound RAN, which is important for mitotic spindle assembly and normal progress through mitosis. Via its role in maintaining high levels of GTP-bound RAN in the nucleus, contributes to the release of cargo proteins from importins after nuclear import (By similarity). Involved in the regulation of onset of chromosome condensation in the S phase (PubMed:2300055, PubMed:2022190). Binds both to the nucleosomes and double-stranded DNA (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome Cytoplasm Note=Predominantly nuclear in interphase cells. Binds to mitotic chromosomes.


FUNCTION: Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)) (By similarity). SUBCELLULAR LOCATION: Cytoplasm Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Prevacuolar compartment membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the sorting nexin family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsiE family.


FUNCTION: Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. SSU72 is required for 3'-end formation of snoRNAs (By similarity). FUNCTION: Processively dephosphorylates Ser-5 of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (RPB1). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SSU72 phosphatase family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PAL/histidase family.


FUNCTION: Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, psmd11a is required for proteasome assembly (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytosol. SIMILARITY: Belongs to the proteasome subunit S9 family.


FUNCTION: Catalyzes the formation of apha-1,4 glycosidic bonds adding glucose residue from UDPG to the growing chain of glycogen. SIMILARITY: Belongs to the glycosyltransferase 3 family.


FUNCTION: Component of the tagatose-1,6-bisphosphate aldolase GatYZ that is required for full activity and stability of the Y subunit. Could have a chaperone-like function for the proper and stable folding of GatY. When expressed alone, GatZ does not show any aldolase activity. Is involved in the catabolism of galactitol. SIMILARITY: Belongs to the GatZ/KbaZ family. GatZ subfamily.


FUNCTION: Globally modulates RNA abundance by binding to RNase E (Rne) and regulating its endonucleolytic activity. Can modulate Rne action in a substrate-dependent manner by altering the composition of the degradosome. Modulates RNA-binding and helicase activities of the degradosome. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RraA family.


FUNCTION: Involved in the biogenesis of the 60S ribosomal subunit. May play a part in the quality control of pre-60S particles (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS8 family. Ribosome biogenesis protein NSA2 subfamily.


FUNCTION: Catalyzes the ATP- and formate-dependent formylation of 5- aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'-monophosphate (FAICAR) in the absence of folates. SIMILARITY: Belongs to the phosphohexose mutase family.


FUNCTION: Antimicrobial peptide with activity against Gram-negative and Gram-positive bacteria (MIC=50 uM against E.coli, MIC=6 uM against S.aureus) and fungi (MIC=13 uM against C.albicans) (PubMed:15556063). Shows hemolytic activity on human erythrocytes (HC(50)=25 uM) (PubMed:15556063). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily.


FUNCTION: Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to promote the degradation of host IKBKB, leading to NF-kappa-B down- regulation and subsequent apoptosis. Ion channel activity has also been suggested, however, formation of cation-selective channel has been reconstituted ex-vivo in lipid bilayers. It is thus unsure that this activity plays a role in vivo. SUBCELLULAR LOCATION: Host membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the HIV-1 VPU protein family.


FUNCTION: Probable thiol-disulfide oxidoreductase that may participate in various redox reactions. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the thioredoxin family.


FUNCTION: Required for the activity of the bacterial transport system of putrescine and spermidine. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.


FUNCTION: [Interleukin-6 receptor subunit alpha]: Signaling via the membrane-bound IL6R is mostly regenerative and anti-inflammatory (Probable). Drives naive CD4(+) T cells to the Th17 lineage, through 'cluster signaling' by dendritic cells (PubMed:27893700). FUNCTION: Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation leads to the regulation of the immune response, acute-phase reactions and hematopoiesis. The interaction with membrane-bound IL6R and IL6ST stimulates 'classic signaling', the restricted expression of the IL6R limits classic IL6 signaling to only a few tissues such as the liver and some cells of the immune system. Whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells. FUNCTION: [Soluble interleukin-6 receptor subunit alpha]: Soluble form of IL6 receptor (sIL6R) that acts as an agonist of IL6 activity (PubMed:11113088). The IL6:sIL6R complex (hyper-IL6) binds to IL6ST/gp130 on cell surfaces and induces signaling also on cells that do not express membrane-bound IL6R in a process called IL6 'trans- signaling'. sIL6R is causative for the pro-inflammatory properties of IL6 and an important player in the development of chronic inflammatory diseases (By similarity). In complex with IL6, is required for induction of VEGF production (By similarity). Plays a protective role during liver injury, being required for maintenance of tissue regeneration (PubMed:11113088). 'Trans-signaling' in central nervous system regulates energy and glucose homeostasis (PubMed:28402851). SUBCELLULAR LOCATION: [Soluble interleukin-6 receptor subunit alpha]: Secreted. SUBCELLULAR LOCATION: [Interleukin-6 receptor subunit alpha]: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the type I cytokine receptor family. Type 3 subfamily.


FUNCTION: Snake venom natriuretic peptide that exhibits hypotensive and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3) (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the natriuretic peptide family.


FUNCTION: Secreted effector that partially suppresses the host cell death induced by cell death-inducing proteins. SUBCELLULAR LOCATION: Secreted Host nucleus Host cytoplasm. SIMILARITY: Belongs to the RxLR effector family.


FUNCTION: Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress (By similarity). Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC- 3'. Activity suppressed by insulin (By similarity). Main regulator of redox balance and osteoblast numbers and controls bone mass (By similarity). Orchestrates the endocrine function of the skeleton in regulating glucose metabolism (By similarity). Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity (By similarity). Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP (By similarity). Acts as an inhibitor of glucose sensing in pancreatic beta cells by acting as a transcription repressor and suppressing expression of PDX1 (By similarity). In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC1 and PCK1 (By similarity). Also promotes gluconeogenesis by directly promoting expression of PPARGC1A and G6PC1 (By similarity). Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1 (By similarity). Promotes neural cell death (By similarity). Mediates insulin action on adipose tissue (By similarity). Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake (By similarity). Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells (By similarity). Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner (By similarity). Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (PubMed:26436652). Regulates endothelial cell (EC) viability and apoptosis in a PPIA/CYPA-dependent manner via transcription of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Shuttles between the cytoplasm and nucleus (By similarity). Largely nuclear in unstimulated cells (By similarity). In osteoblasts, colocalizes with ATF4 and RUNX2 in the nucleus. Serum deprivation increases localization to the nucleus, leading to activate expression of SOX9 and subsequent chondrogenesis (By similarity). Insulin-induced phosphorylation at Ser-253 by PKB/AKT1 leads, via stimulation of Thr-24 phosphorylation, to binding of 14-3-3 proteins and nuclear export to the cytoplasm where it is degraded by the ubiquitin-proteasomal pathway (By similarity). Phosphorylation at Ser-249 by CDK1 disrupts binding of 14-3-3 proteins and promotes nuclear accumulation (By similarity). Phosphorylation by NLK results in nuclear export (By similarity). Translocates to the nucleus upon oxidative stress-induced phosphorylation at Ser-212 by STK4/MST1 (By similarity). SGK1-mediated phosphorylation also results in nuclear translocation. Retained in the nucleus under stress stimuli including oxidative stress, nutrient deprivation or nitric oxide. Methylated form is nuclear (By similarity). PPIA/CYPA stimulates its nuclear accumulation (By similarity). Deacetylation by SIRT6, promotes its translocation into the cytoplasm (By similarity).


FUNCTION: Pectin methylesterase (PME) inhibitor that regulates de- methylesterification of pectins in the apical meristem and affects primordia formation and phyllotactic patterning. SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the PMEI family.


FUNCTION: Giardins are involved in parasite attachment to the intestinal mucosa and in the cytoskeletal disassembly and reassembly that marks the transition from infectious trophozoite to transmissible cyst. They may interact with other cytoskeletal proteins such as microtubules in the microribbons or crossbridges, to maintain the integrity of the ventral disk (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the annexin family. Giardin subunit alpha subfamily.


FUNCTION: Removes the 2'-phosphate from RNA via an intermediate in which the phosphate is ADP-ribosylated by NAD followed by a presumed transesterification to release the RNA and generate ADP-ribose 1''-2''- cyclic phosphate (APPR>P). May function as an ADP-ribosylase. SIMILARITY: Belongs to the KptA/TPT1 family.


FUNCTION: Major structural component of sperm fibrous sheath. Plays a role in sperm motility (PubMed:12167408). SUBCELLULAR LOCATION: Cell projection, cilium, flagellum Note=Localizes to the principle piece of the sperm flagellum. SIMILARITY: Belongs to the AKAP110 family.


FUNCTION: C-5 sterol desaturase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:24785759). ERG3A and ERG3BB catalyze the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase ERG1 and the lanosterol synthase ERG7. Then, the delta(24)-sterol C-methyltransferase ERG6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by CYP51A, CYP51B and CYP51C, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. CYP51B encodes the enzyme primarily responsible for sterol 14-alpha-demethylation, and plays an essential role in ascospore formation. CYP51A encodes an additional sterol 14-alpha-demethylase, induced on ergosterol depletion and responsible for the intrinsic variation in azole sensitivity. The third CYP51 isoform, CYP51C, does not encode a sterol 14-alpha- demethylase, but is required for full virulence on host wheat ears. The C-14 reductase ERG24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases ERG25, the sterol-4-alpha-carboxylate 3-dehydrogenase ERG26 and the 3-keto-steroid reductase ERG27, leads to the production of fecosterol via 4-methylfecosterol. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum. The C- 8 sterol isomerase ERG2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturases ERG3A and ERG3BB then catalyze the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturases ERG5A and ERG5B further convert 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen- 3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C- 24(28) sterol reductase ERG4 to produce ergosterol (Probable). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sterol desaturase family.


FUNCTION: Acts as a transcriptional transactivator of ELL and ELL2 elongation activities. SUBCELLULAR LOCATION: Nucleus speckle Nucleus, Cajal body. SIMILARITY: Belongs to the EAF family.


FUNCTION: Mediates the conversion of L-galactonate to 2-dehydro-3- deoxy-L-galactonate, the second step in D-galacturonate catabolic process. SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family.


FUNCTION: Component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. Component of the mitotic checkpoint complex (MCC) which inhibits the ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) by preventing its activation by CDC20. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: To yeast protein kinase BUB1 in its non-catalytic N- terminal domain.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase epsilon chain family.


FUNCTION: Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. CcmA exporter (TC 3.A.1.107) family.


FUNCTION: Component of the kinesin II motor complex (composed of kap-1 and the heterodimeric motor proteins klp-11 and klp-20) which is required for intraflagellar transport (IFT) (PubMed:20833139, PubMed:20498083). Heterodimerizes with klp-11 to form a 'processive' molecular motor upon IFT cargo binding, which, within the kinesin II motor complex, binds to and moves along microtubules in a unidirectional manner (without dissociation of the heterodimer), and in turn, is responsible for the IFT of cargo (PubMed:20498083). Specifically, the kinesin II motor complex, together with the kinesin motor protein osm-3 moves along microtubules and is required for anterograde IFT along the middle segment of the sensory neuron cilia (PubMed:17000880, PubMed:20833139, PubMed:28479320). In particular, the kinesin II motor complex delivers specific ciliary cargo proteins such as che-3 which are related to motility to ciliary tips (PubMed:28479320). This is likely mediated by IFT complexes A and B (PubMed:28479320). SUBCELLULAR LOCATION: Cell projection, cilium Cytoplasm, cytoskeleton Note=In particular, localizes to the base and transition zone of cilia. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Kinesin II subfamily.


FUNCTION: Tissue-specific DNA-binding transcription factor involved in the development and differentiation of target cells. Functions either as activator or repressor modulating the rate of target gene transcription through RNA polymerase II enzyme in a promoter-dependent manner. Binds to the consensus octamer motif 5'-AT[A/T]A[T/A]T[A/T]A-3' of promoter of target genes. Plays a fundamental role in the gene regulatory network essential for retinal ganglion cell (RGC) differentiation. Binds to an octamer site to form a ternary complex with ISL1; cooperates positively with ISL1 and ISL2 to potentiate transcriptional activation of RGC target genes being involved in RGC fate commitment in the developing retina and RGC axon formation and pathfinding. Inhibits DLX1 and DLX2 transcriptional activities preventing DLX1- and DLX2-mediated ability to promote amacrine cell fate specification. In cooperation with TP53 potentiates transcriptional activation of BAX promoter activity increasing neuronal cell apoptosis. Negatively regulates BAX promoter activity in the absence of TP53. Acts as a transcriptional coactivator via its interaction with the transcription factor ESR1 by enhancing its effect on estrogen response element (ERE)-containing promoter. Antagonizes the transcriptional stimulatory activity of POU4F1 by preventing its binding to an octamer motif. Involved in TNFSF11-mediated terminal osteoclast differentiation. SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm. SIMILARITY: Belongs to the POU transcription factor family. Class-4 subfamily.


FUNCTION: Participates in a complex which severs microtubules in an ATP-dependent manner. May act to target the enzymatic subunit of this complex to sites of action such as the centrosome. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, spindle Note=Predominantly cytoplasmic. Localized to the interphase centrosome and mitotic spindle poles. SIMILARITY: Belongs to the WD repeat KATNB1 family.


SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Cdh family.


FUNCTION: Required during biogenesis of c-type cytochromes (cytochrome c6 and cytochrome f) at the step of heme attachment. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Ccs1/CcsB family.


FUNCTION: Catalyzes the formation of flavonols from dihydroflavonols. It can act on dihydrokaempferol to produce kaempferol, on dihydroquercetin to produce quercitin and on dihydromyricetin to produce myricetin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family.


FUNCTION: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome f family.


FUNCTION: Promotes transcriptional elongation by Su(Tpl)/ELL. Essential for development (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EAF family.


FUNCTION: This protein functions as a defense against chitin containing fungal pathogens. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase class II subfamily.


FUNCTION: Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-4-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. This receptor-destroying activity is important for virus release as it probably helps preventing self-aggregation and ensures the efficient spread of the progeny virus from cell to cell. May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. May become a target for both the humoral and the cellular branches of the immune system. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein Note=In infected cells becomes incorporated into the envelope of virions during virus assembly at the endoplasmic reticulum and cis Golgi. However, some may escape incorporation into virions and subsequently migrate to the cell surface. SIMILARITY: Belongs to the influenza type C/coronaviruses hemagglutinin-esterase family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M20A family.


FUNCTION: RNA-dependent RNA polymerase, which replicates the viral genome composed of 2 RNA segments, RNA1 and RNA2. Does not need an exogenous primer. Also possesses a terminal nucleotidyl transferase (TNTase) activity. The TNTase catalyzes the addition of nucleotide to the 3'-end of plus- and minus-stranded RNAs, probably to repair the 3'- end nucleotide loss. Forms the open necked connection to the cytosol of the virus-induced replication vesicles. Mediates viral RNA1 recruitment. SUBCELLULAR LOCATION: Host mitochondrion outer membrane; Single-pass membrane protein Note=Part of the 30- to 90-nm invaginations of the host mitochondrial outer membrane that form the viral replication complexes vesicules. Has a N-terminal membrane- spanning mitochondrial anchor. SIMILARITY: Belongs to the nodaviridae RNA polymerase family.


FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 2 family.


FUNCTION: As a component of the AMPAR complex, modifies AMPA receptor (AMPAR) gating. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Synapse. SIMILARITY: Belongs to the GSG1 family.


FUNCTION: Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic release factor 1 family.


FUNCTION: Member of the two-component regulatory system ArlS/ArlR. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Copper amine oxidase that can use putrescine and spermidine as substrates (PubMed:23915037). Required for abscisic acid- (ABA) and polyamine- (PA) and H(2)O(2)-dependent induced nitric oxide (NO) biosynthesis (PubMed:21471330). Involved in ABA signal transduction and in responses to osmotic stress (PubMed:21471330). SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the copper/topaquinone oxidase family.


FUNCTION: Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant. FUNCTION: Regulates transcriptional attenuation of the pyrimidine nucleotide (pyr) operon by binding in a uridine-dependent manner to specific sites on pyr mRNA. This disrupts an antiterminator hairpin in the RNA and favors formation of a downstream transcription terminator, leading to a reduced expression of downstream genes (Probable). SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily.


FUNCTION: Catalyzes the reversible phosphorolytic cleavage of trehalose. Phosphorolysis is specific for trehalose, but D-xylose, D- galactose, L-arabinose, D-fucose, L-fucose, D-glucosamine and 2-deoxy D-glucose can act as substitutes for D-glucose in the synthetic reaction. SIMILARITY: Belongs to the glycosyl hydrolase 65 family.


FUNCTION: Part of the gene cluster that mediates the biosynthesis of lolitrems, indole-diterpene mycotoxins that are potent tremorgens in mammals, and are synthesized by clavicipitaceous fungal endophytes in association with their grass hosts (PubMed:23468653). The geranylgeranyl diphosphate (GGPP) synthase ltmG is proposed to catalyze the first step in lolitrem biosynthesis (PubMed:16765617, PubMed:15991026). LtmG catalyzes a series of iterative condensations of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP (PubMed:16765617, PubMed:15991026). GGPP then condenses with indole-3- glycerol phosphate to form 3-geranylgeranylindole, an acyclic intermediate, to be incorporated into paxilline (PubMed:16765617). Either ltmG or ltmC could be responsible for this step, as both are putative prenyl transferases (PubMed:16765617). The FAD-dependent monooxygenase ltmM then catalyzes the epoxidation of the two terminal alkenes of the geranylgeranyl moiety, which is subsequently cyclized by ltmB, to paspaline (PubMed:16765617, PubMed:15991026). The cytochrome P450 monooxygenases ltmQ and ltmP can sequentially oxidize paspaline to terpendole E and terpendole F (PubMed:22750140). Alternatively, ltmP converts paspaline to an intermediate which is oxidized by ltmQ to terpendole F (PubMed:22750140). LtmF, ltmK, ltmE and ltmJ appear to be unique to the epichloe endophytes (PubMed:16765617, PubMed:15991026). The prenyltransferase ltmF is involved in the 27-hydroxyl-O-prenylation (PubMed:22750140). The cytochrome P450 monooxygenase ltmK is required for the oxidative acetal ring formation (PubMed:22750140). The multi- functional prenyltransferase ltmE is required for C20- and C21- prenylations of the indole ring of paspalanes and acts together with the cytochrome P450 monooxygenase ltmJ to yield lolitremanes by multiple oxidations and ring closures (PubMed:22750140). The stereoisomer pairs of lolitriol and lolitrem N or lolitrem B and lolitrem F may be attributed to variations in the way in which ring closure can occur under the action of ltmJ (PubMed:22750140). While the major product of this pathway is lolitrem B, the prenyl transferases and cytochrome P450 monooxygenases identified in this pathway have a remarkable versatility in their regio- and stereo-specificities to generate a diverse range of metabolites that are products of a metabolic grid rather than a linear pathway (PubMed:22750140). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ltmS family.


FUNCTION: Acts as a neurotoxin by inhibiting an ion channel. SUBCELLULAR LOCATION: Secreted.


FUNCTION: As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GerABKA family.