FUNCTION: Involved in the post-translational conjugation of arginine to the N-terminal aspartate or glutamate of a protein. This arginylation is required for degradation of the protein via the ubiquitin pathway. Component of the N-end rule pathway with ATE1 and PRT6 (PubMed:19255443, PubMed:19620738, PubMed:22020282). The N-end rule pathway regulates seed after-ripening, seedling sugar sensitivity, seedling lipid breakdown, and abscisic acid (ABA) sensitivity of germination (PubMed:19255443). The end-rule pathway regulates various aspects of leaf and shoot development (PubMed:19620738). Involved in the oxygen-dependent N-arginylation of RAP2-12, an activator of hypoxic gene expression. This N-terminal modification leads to ubiquitination by PRT6 and subsequent degradation of RAP2-12 under aerobic conditions (PubMed:22020282). Involved in disease resistance (PubMed:27173012). The end-rule pathway plays a role in regulating the timing and amplitude of the immune response following infection with the bacterial pathogen Pseudomonas syringae pv tomato (PubMed:27173012). Regulates the biosynthesis of plant-defense metabolites such as glucosinolates, and the biosynthesis and response to the phytohormone jasmonate (JA), which plays a key role in plant immunity (PubMed:27173012). SIMILARITY: Belongs to the R-transferase family.


FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May recruit the E2 ubiquitin-conjugating enzymes to the complex (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CDC26 family.


SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the LpqB lipoprotein family.


SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the bZIP family. Fos subfamily.


FUNCTION: Heme-based oxygen sensor protein displaying phosphodiesterase (PDE) activity toward c-di-GMP in response to oxygen availability. Involved in the modulation of intracellular c-di-GMP levels, in association with DosC which catalyzes the biosynthesis of c-di-GMP (diguanylate cyclase activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Has very poor PDE activity on cAMP (PubMed:15995192) but is not active with cGMP, bis(p-nitrophenyl) phosphate or p-nitrophenyl phosphate (PubMed:11970957). Via its PDE activity on c-di-GMP, DosP regulates biofilm formation through the repression of transcription of the csgBAC operon, which encodes curli structural subunits.


FUNCTION: [Isoform Secreted glycoprotein G]: Helps the virus escape antibody-dependent restriction of replication by acting as an antigen decoy and by modulating the activity of leukocytes bearing Fc-gamma receptors. FUNCTION: [Isoform Membrane-bound glycoprotein G]: Attaches the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection. Interacts with host CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate the immune response and facilitate infection. Unlike the other paramyxovirus attachment proteins, lacks both neuraminidase and hemagglutinating activities. SUBCELLULAR LOCATION: [Isoform Secreted glycoprotein G]: Secreted Note=The protein is shed from infected cells before the appearance of progeny virus. The initiation at the downstream methionine removes a portion of the transmembrane domain. The remaining hydrophobic portion of the sG protein is essential for translocating it into the lumen of the ER during translation and would likely maintain its membrane association until a proteolytic event releases the mature sG protein into the medium. SUBCELLULAR LOCATION: [Isoform Membrane-bound glycoprotein G]: Virion membrane; Single-pass type II membrane protein Host cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the pneumoviruses glycoprotein G family.


FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR). SIMILARITY: Belongs to the AIR carboxylase family. Class I subfamily.


FUNCTION: Activation of RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the RuBisCO activase family.


FUNCTION: Purine salvage pathway enzyme which catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1- diphosphate (PRPP) to the N9 position of hypoxanthine to yield IMP (inosine 5'-monophosphate). To a lesser extent, can also act on guanine leading to GMP, but shows a highly less efficient activity with xanthine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family.


FUNCTION: Possesses GTPase activity. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rab family.


FUNCTION: Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain (By similarity). SIMILARITY: In the N-terminal section; belongs to the TrpC family. SIMILARITY: In the C-terminal section; belongs to the TrpF family.


FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 18 family.


FUNCTION: Glutamate-gated receptor that probably acts as non-selective cation channel. May be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family.


FUNCTION: Protein kinase which plays an important role in mitotic cell cycle progression (PubMed:17101132, PubMed:31409757, PubMed:19941817). Required for microtubule nucleation activity of the centrosome, robust mitotic spindle formation and cytokinesis (PubMed:17586473, PubMed:19414596, PubMed:31409757, PubMed:19941817, PubMed:26522158). Phosphorylates EML4 at 'Ser-146', promoting its dissociation from microtubules during mitosis which is required for efficient chromosome congression (PubMed:31409757). Phosphorylates RPS6KB1 (By similarity). Acts as an essential activator of the NLRP3 inflammasome assembly independently of its kinase activity (PubMed:26642356, PubMed:36442502). Acts by unlocking NLRP3 following NLRP3 tranlocation into the microtubule organizing center (MTOC), relieving NLRP3 autoinhibition and promoting formation of the NLRP3:PYCARD complex, and activation of CASP1 (PubMed:26642356, PubMed:31189953, PubMed:36442502). Serves as a cellular switch that enforces mutual exclusivity of the inflammasome response and cell division: interaction with NEK9 prevents interaction with NLRP3 and activation of the inflammasome during mitosis (PubMed:26642356, PubMed:31189953). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Present at centrosome throughout the cell cycle (PubMed:17586473). Also detected at spindle midzone of the anaphase cells and eventually concentrates at the midbody (PubMed:17586473). Interaction with ANKS3 prevents its translocation to the nucleus (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily.


FUNCTION: Transcription factor involved in somitogenesis and neurogenesis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the paired homeobox family. Unc-4 subfamily.


FUNCTION: LRR receptor kinase that may be involved in defense response. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Note=Localizes in the plasma membrane. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


FUNCTION: Cytochrome P450 monooxygenase that hydroxylates polyporic acid produced by the nonribosomal peptide synthetase acyN to produce the less toxic metabolite ascocorynin (PubMed:35477441). The hydrophobic substrate polyporic acid might approach the active site from the membrane and, after hydroxylation into ascocorynin, leaves into the cytoplasm (Probable). MO6277 appears vital to avoid high-level accumulation of polyporic acid in the fungal membrane (PubMed:35477441). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Involved in the uptake of non-siderophore and siderophore sources of iron. Has a role in the retention of iron in the cell wall and periplasmic space. SUBCELLULAR LOCATION: Secreted, cell wall Membrane; Lipid-anchor, GPI-anchor.


FUNCTION: Required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH. SIMILARITY: Belongs to the arrestin family. PalF/RIM8 subfamily.


SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor.


FUNCTION: Coat protein that is involved in the localization of trans- Golgi network (TGN) membrane proteins that contain acidic cluster sorting motifs. Controls the endosome-to-Golgi trafficking of furin and mannose-6-phosphate receptor by connecting the acidic-cluster- containing cytoplasmic domain of these molecules with the adapter- protein complex-1 (AP-1) of endosomal clathrin-coated membrane pits (By similarity). Required for normal ER Ca2+ handling in lymphocytes. Together with WDR37, it plays an essential role in lymphocyte development, quiescence and survival. Required for stabilizing peripheral lymphocyte populations (PubMed:33630350). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network Note=Localizes in the perinuclear region, probably the TGN. SIMILARITY: Belongs to the PACS family.


FUNCTION: Involved in fetal development, T-cell function and adrenal gland growth homeostasis (By similarity). Negatively regulates adrenal cells survival. Plays a role in steroidogenesis, modulates steroidogenic enzymes expression and cortisol production (By similarity). SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(o) ATP synthase) 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 (PubMed:19436713, PubMed:29247468). F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(o) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk (PubMed:19436713, PubMed:29247468, PubMed:29440423). 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. Subunits alpha and beta form the catalytic core in F(1) (PubMed:19436713, PubMed:29440423). 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 (Probable). Contrary to the procyclic, insect form that requires F(1)F(o) ATP synthase for ATP synthesis, the bloodstream form relies on ATP hydrolysis by F(1)F(o) ATP synthase to maintain its mitochondrial membrane potential (PubMed:29247468). SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.


FUNCTION: Receptor for netrin required for axon guidance (PubMed:22685302, PubMed:10399920). Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding (PubMed:10399920, PubMed:22685302). NTN1/Netrin-1 binding might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion (PubMed:28483977). Axon repulsion in growth cones may also be caused by its association with DCC that may trigger signaling for repulsion (PubMed:10399920). Might also collaborate with DSCAM in NTN1-mediated axon repulsion independently of DCC (PubMed:22685302). Also involved in corticospinal tract axon guidance independently of DCC (PubMed:9126743, PubMed:9389662, PubMed:12451134). Involved in dorsal root ganglion axon projection towards the spinal cord (By similarity). It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell surface Synapse, synaptosome Cell projection, dendrite Cell projection, axon Cell projection, growth cone Cell projection, lamellipodium Cell projection, filopodium. SIMILARITY: Belongs to the unc-5 family.


FUNCTION: Myoactive. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pyrokinin family.


SIMILARITY: Belongs to the UPF0180 family.


SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein family.


FUNCTION: Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization. Acts as a chaperone for ALOX5 (5LO), influencing both its stability and activity in leukotrienes synthesis (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Nucleus. SIMILARITY: Belongs to the actin-binding proteins ADF family. Coactosin subfamily.


SUBCELLULAR LOCATION: Host cytoplasmic vesicle membrane; Peripheral membrane protein. Host cytoplasm. Note=Binds non-covalently to intracellular lipid bilayers.


FUNCTION: Catalyzes the oxidation of NADH generated inside the Mitochondrion. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side Note=Bound to the mitochondrial inner membrane facing the matrix site. SIMILARITY: Belongs to the NADH dehydrogenase family.


FUNCTION: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. SUBCELLULAR LOCATION: Secreted Host cell Note=Secreted via type III secretion system 1 (SPI-1 TTSS), and delivered into the host cell. SIMILARITY: Belongs to the SopA E3 ligase family.


FUNCTION: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. FixP subunit is required for transferring electrons from donor cytochrome c via its heme groups to FixO subunit. From there, electrons are shuttled to the catalytic binuclear center of FixN subunit where oxygen reduction takes place. The complex also functions as a proton pump (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CcoP / FixP family.


FUNCTION: Upon intracranial injection in mice, as25a (the toxin without the two 4-hydroxyprolines) provokes paralysis of the hind limbs and death with a dose of 240 pmol. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.


FUNCTION: RNA-binding protein involved in post-transcriptional regulation through transcript degradation. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, P-body. SIMILARITY: Belongs to the VTS1 family.


FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 3 subfamily.


FUNCTION: Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors. SUBCELLULAR LOCATION: Postsynapse Presynapse. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. GPRK subfamily.


FUNCTION: Required for pre-mRNA splicing as component of the spliceosome. Promotes exon-junction complex (EJC) assembly. SUBCELLULAR LOCATION: Nucleus Nucleus speckle Note=Concentrates around speckles, which are sites of pre-mRNA synthesis and processing, where it colocalizes with EJC core proteins. SIMILARITY: Belongs to the CWC22 family.


FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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 (By similarity). FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family.


FUNCTION: Catalyzes the reversible interconversion of fructoselysine with its C-3 epimer, psicoselysine. May allow S.flexneri to utilize psicoselysine for growth. SIMILARITY: Belongs to the FrlC family.


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the universal stress protein B family.


FUNCTION: Retroviral proteases have roles in the processing of the primary translation products and the maturation of the viral particle. Endogenous Pro proteins may have kept, lost or modified their original function during evolution. SIMILARITY: Belongs to the peptidase A2 family. HERV class-II K(HML-2) subfamily.


FUNCTION: Negatively regulates TGF-beta-induced signaling; in cooperation with SKI prevents the translocation of SMAD2 from the nucleus to the cytoplasm in response to TGF-beta. Acts as an adapter that mediates the specific recognition of LIMK1 by CDC42BPA and CDC42BPB in the lamellipodia. LRAP25-mediated CDC42BPA/CDC42BPB targeting to LIMK1 and the lamellipodium results in LIMK1 activation and the subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation. SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm Cell projection, lamellipodium Note=Co-localizes with CDC42BPA, CDC42BPB and LIMK1 in the lamellipodium. SIMILARITY: Belongs to the FAM89 family.


FUNCTION: Acts with RNA polymerase to initiate transcription from early gene promoters. Is recruited by the RPO-associated protein of 94 kDa (RAP94) to form the early transcription complex, which also contains the core RNA polymerase. ETF heterodimer binds to early gene promoters (By similarity). SUBCELLULAR LOCATION: Virion Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome. This is necessary because viral early mRNAs are synthesized within minutes after virus entry into the cell and are extruded through pores in the core particle. SIMILARITY: Belongs to the helicase family. VETF subfamily.


FUNCTION: Protein kinase involved in the regulation of actin cytoskeleton organization and endocytosis (PubMed:9885245, PubMed:10087264, PubMed:11694597, PubMed:11739778). Phosphorylates PAN1 which disrupts the interaction between PAN1 and END3, and between PAN1 and SLA1 (PubMed:9885245, PubMed:11739778, PubMed:13679512). Phosphorylates SCD5 (PubMed:12956961, PubMed:13679512). Preferentially, phosphorylates substrates on threonine residues in a [L/I/V/M]-x-x- [Q/N/T/S]-x-T-G motif (PubMed:9885245, PubMed:11739778, PubMed:12956961, PubMed:13679512). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch Note=Cortical actin patches. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. SIMILARITY: Belongs to the V-ATPase E subunit family. SIMILARITY: Belongs to the V-ATPase E subunit family.


FUNCTION: Phosphatase that hydrolyzes imidodiphosphate, 3- phosphohistidine and 6-phospholysine. Has broad substrate specificity and can also hydrolyze inorganic diphosphate, but with lower efficiency (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the HAD-like hydrolase superfamily.


FUNCTION: Involved in spore outer coat assembly. May be part of a cross-linked insoluble skeleton that surrounds the spore, serves as a matrix for the assembly of additional outer coat material, and confers structural stability to the final structure.


FUNCTION: Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Nucleus matrix Note=Throughout the cytoplasm (but not on the cytoplasmic cables) and major component of the cortical actin cytoskeleton. SIMILARITY: Belongs to the actin-binding proteins ADF family.


FUNCTION: Plays a role in virus cell tropism, and may be required for efficient virus replication in macrophages. SIMILARITY: Belongs to the asfivirus MGF 505 family.


FUNCTION: DNA-binding protein that binds to both single- and double- stranded DNA. Binds preferentially to UV-damaged DNA. May be involved in DNA-metabolic processes. SIMILARITY: Belongs to the WD repeat DDB2/WDR76 family.


SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Note=Cell surface localization requires the ITAM-bearing Fc receptor FCER1G to overcome ER retention. SIMILARITY: Belongs to the CD300 family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.


FUNCTION: Nitrilase that hydrolyzes preferentially fumaronitrile, while 3-phenylpropionitrile, beta-cyano-L-alanine and 4-cyanopyridine are transformed at much lower rates. SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. Nitrilase family.


FUNCTION: Acts as negative regulator of seedling photomorphogenesis. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. It is required for pilus biogenesis (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.


FUNCTION: Catalyzes the transfer of N-acetylneuraminyl groups onto glycan chains in glycoproteins (PubMed:10742600, PubMed:29251719). Shows a preference for N-acetylgalactosamine (GalNAc) residues already modified by the addition of galactose or galactose followed by sialic acid in alpha-2,3 linkage (PubMed:10742600). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 29 family.


FUNCTION: Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Contributes to the structuring of the Rrp41 active site. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNase PH family. Rrp42 subfamily.


FUNCTION: Probably involved in maintaining Golgi structure. SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein.


FUNCTION: Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ABC1 family. UbiB subfamily.


FUNCTION: Regulation of fluid secretion. Stimulates primary urine secretion by Malpighian tubules and causes a dose-dependent stimulation of cAMP levels in the tubules. May act as clearance peptide in that it may remove metabolic waste from the hemolymph. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the sauvagine/corticotropin-releasing factor/urotensin I family.


FUNCTION: Exhibits the same spectroscopical features and blue-light induced photochemistry as plants phototropins, with the reversible formation of a blue-shifted photoproduct, assigned to an FMN-cysteine thiol adduct. Positive regulator in the activation of the general stress transcription factor sigma-B (By similarity).


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CTL (choline transporter-like) family.


FUNCTION: May function as a nucleosome assembly factor during rapid embryonic cell divisions. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NASP family.


SIMILARITY: Belongs to the UPF0179 family.


FUNCTION: Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as the external driving force. In the TIM22 complex, it may act as a docking point for the soluble 70 kDa complex that guides the target proteins in transit through the aqueous mitochondrial intermembrane space. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the small Tim family.


FUNCTION: Catalyzes the ATP-independent decarboxylation of (R)- mevalonate 3,5-bisphosphate to isopentenyl phosphate. Functions in an alternative mevalonate pathway, only present in extreme acidophiles of the Thermoplasmatales order, which passes through mevalonate 3- phosphate rather than mevalonate 5-phosphate. SIMILARITY: Belongs to the mevalonate 3,5-bisphosphate decarboxylase family.


FUNCTION: Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. FUNCTION: Antibacterial peptide with narrow spectrum of activity. Inhibits the formation of NO by neuronal nitric oxide synthase. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Caerin subfamily. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Caerin subfamily.


FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. SUBCELLULAR LOCATION: Cellular chromatophore membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RnfG 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 (By similarity). SIMILARITY: Belongs to the plastocyanin family.


FUNCTION: Has antibacterial activity against E.coli and S.aureus strains. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Esculentin subfamily.


FUNCTION: Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases. Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell projection, microvillus Secreted Note=Colocalizes with actin in membrane protrusions at wounding edges. Co-localizes with RDX, EZR and MSN in microvilli.


FUNCTION: Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate. Makes part of a pathway for isoleucine biosynthesis, i.e. the citramalate-dependent pathway. Also displays a low alpha-isopropylmalate synthase activity, using 2-oxoisovalerate as substrate, but is unable to use 2-oxoglutarate. SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase family.


FUNCTION: May play a role in inducing apoptosis during endoplasmic reticulum (ER) stress and in the inhibition of proliferation and tumorigenicity. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein.


FUNCTION: In vitro, binds efficiently double-stranded RNAs in a non- sequence specific manner.


FUNCTION: Catalyzes the NADPH-specific reduction of 1,5-anhydro-D- fructose to 1,5-anhydro-D-mannitol. SIMILARITY: Belongs to the Gfo/Idh/MocA family.


FUNCTION: Catalyzes the transfer of the 4'-phosphopantetheine moiety from coenzyme A to a serine residue in the acyl-carrier domain of carboxylic acid reductase Car, thus converting apo-Car to fully active holo-Car. Is probably also responsible for the activation of other proteins with phosphopantetheine attachment sites. SIMILARITY: Belongs to the P-Pant transferase superfamily.


FUNCTION: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in cytokinesis. Involved in recruiting VPS4A and/or VPS4B and SPAST to the midbody of dividing cells (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Endosome Late endosome membrane; Peripheral membrane protein Note=Localizes to the midbody of dividing cells, colocalizing with CEP55 and CHMP5. Localized at the periphery of the Fleming body (By similarity). SIMILARITY: Belongs to the SNF7 family.


FUNCTION: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. Note=Tonoplast. SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.


FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP2 subfamily.


FUNCTION: Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices. This capsid constitutes the middle concentric layer of the viral mature particle. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes. VP6 is required for the transcription activity of the DLP. SUBCELLULAR LOCATION: Virion Note=Component of the intermediate capsid. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. SIMILARITY: Belongs to the rotavirus VP6 family.


FUNCTION: Scaffolding protein involved in the icosahedric procapsid assembly. Coassembles with the capsid proteins to form the procapsid. The scaffolding protein is found within the capsid as a serie of concentric shells. During DNA packaging, the scaffolding protein molecules are released from the procapsid. SUBCELLULAR LOCATION: Note=Present in about 147 copies in the prohead but not present in mature virions. SIMILARITY: Belongs to the phi29likevirus scaffolding protein family.


FUNCTION: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Peptidoglycan hydrolase (autolysin) specifically acting on polyglycine interpeptide bridges of the cell wall peptidoglycan. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M23B family.


FUNCTION: Converts protoheme IX and farnesyl diphosphate to heme O. SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UbiA prenyltransferase family.


FUNCTION: Functions as an organic anion/dicarboxylate exchanger that couples organic anion uptake indirectly to the sodium gradient. Transports organic anions such as estrone 3-sulfate (E1S) and urate in exchange for dicarboxylates such as glutarate or ketoglutarate (2- oxoglutarate) (PubMed:15846473). Plays an important role in the excretion of endogenous and exogenous organic anions, especially from the kidney and the brain. Responsible for the transport of prostaglandin E2 (PGE2) and prostaglandin F2(alpha) (PGF2(alpha)) in the basolateral side of the renal tubule. May be involved in the basolateral transport of steviol, a metabolite of the popular sugar substitute stevioside. May participate in the detoxification/ renal excretion of drugs and xenobiotics, such as the histamine H(2)-receptor antagonists fexofenadine and cimetidine, the antibiotic benzylpenicillin (PCG), the anionic herbicide 2,4-dichloro- phenoxyacetate (2,4-D), the diagnostic agent p-aminohippurate (PAH), the antiviral acyclovir (ACV), and the mycotoxin ochratoxin (OTA), by transporting these exogenous organic anions across the cell membrane in exchange for dicarboxylates such as 2-oxoglutarate (PubMed:15846473) (By similarity). Contributes to the renal uptake of potent uremic toxins (indoxyl sulfate (IS) and 3-carboxy-4-methyl-5-propyl-2- furanpropionate (CMPF)), pravastatin, PCG, E1S and dehydroepiandrosterone sulfate (DHEAS), and is partly involved in the renal uptake of temocaprilat (an angiotensin-converting enzyme (ACE) inhibitor) (By similarity). May contribute to the release of cortisol in the adrenals (By similarity). Involved in one of the detoxification systems on the choroid plexus (CP), removes substrates such as E1S or taurocholate (TC), PCG, 2,4-D and PAH, from the cerebrospinal fluid (CSF) to the blood for eventual excretion in urine and bile (By similarity). Also contributes to the uptake of several other organic compounds such as the prostanoids prostaglandin E(2) and prostaglandin F(2-alpha), L-carnitine, and the therapeutic drugs allopurinol, 6- mercaptopurine (6-MP) and 5-fluorouracil (5-FU) (By similarity). Mediates the transport of PAH, PCG, and the statins pravastatin and pitavastatin, from the cerebrum into the blood circulation across the blood-brain barrier (BBB). In summary, plays a role in the efflux of drugs and xenobiotics, helping reduce their undesired toxicological effects on the body (By similarity). SUBCELLULAR LOCATION: Basolateral cell membrane; Multi- pass membrane protein Note=Localizes on the brush border membrane of the choroid epithelial cells. Localizes to the basolateral membrane of the proximal tubular cells. Localized on the abluminal and possibly, luminal membrane of the brain capillary endothelial cells (BCEC). SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily. Organic cation transporter (TC 2.A.1.19) family.


SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.


FUNCTION: Receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (By similarity). Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection (By similarity). May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response (By similarity). During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage (By similarity). Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation (By similarity). Can also negatively regulate apoptosis (PubMed:12191471). Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3 (PubMed:12191471). Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8 (PubMed:12191471). Phosphorylates YY1, protecting YY1 from cleavage by CASP7 during apoptosis (By similarity). Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV (By similarity). Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, ATF4, SRF, MAX, JUN, FOS, MYC and MYB (By similarity). Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function (By similarity). Mediates sequential phosphorylation of FNIP1, promoting its gradual interaction with Hsp90, leading to activate both kinase and non-kinase client proteins of Hsp90 (By similarity). Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1 (By similarity). Acts as an ectokinase that phosphorylates several extracellular proteins (By similarity). During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV (By similarity). Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation (By similarity). Plays an important role in the circadian clock function by phosphorylating BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry (PubMed:19330005). Phosphorylates FMR1, promoting FMR1-dependent formation of a membraneless compartment (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily.


FUNCTION: Plays a central role in chromosome cohesion during mitosis by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms. May act by preventing phosphorylation of the STAG2 subunit of cohesin complex at the centromere, ensuring cohesin persistence at centromere until cohesin cleavage by ESPL1/separase at anaphase. Essential for proper chromosome segregation during mitosis and this function requires interaction with PPP2R1A. Its phosphorylated form is necessary for chromosome congression and for the proper attachment of spindle microtubule to the kinetochore. Necessary for kinetochore localization of PLK1 and CENPF. May play a role in the tension sensing mechanism of the spindle-assembly checkpoint by regulating PLK1 kinetochore affinity. Involved in centromeric enrichment of AUKRB in prometaphase. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere Chromosome, centromere, kinetochore Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localizes to the inner centromere throughout prophase until metaphase and disappears at anaphase. Centromeric localization requires the presence of BUB1 and the interaction with PPP2R1A. Colocalizes with NEK2 at the kinetochore. Colocalizes with and SS18L1 at the kinetochore. Phosphorylation by AUKRB and the presence of BUB1 are required for localization to the kinetochore. Isoform 1 primarily localizes to kinetochores during G2 phase and mitotic prophase, metaphase, and anaphase and does not appear to be associated with kinetochores during late mitosis. Isoform 3 is found at the centrosome in interphase and at spindle poles in mitosis and its spindle pole localization is PLK1 dependent. Isoform 3 does not localize to kinetochores during any stages of the cell cycle. SIMILARITY: Belongs to the shugoshin family.


FUNCTION: Exhibits arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity (PubMed:12368295, PubMed:12686563). It can remove sulfate from the C-6 position of glucosamine within specific subregions of intact heparin (PubMed:12368295, PubMed:12686563). Diminishes HSPG (heparan sulfate proteoglycans) sulfation, inhibits signaling by heparin-dependent growth factors, diminishes proliferation, and facilitates apoptosis in response to exogenous stimulation (PubMed:12686563). SUBCELLULAR LOCATION: Endoplasmic reticulum Golgi apparatus, Golgi stack Cell surface. SUBCELLULAR LOCATION: [Extracellular sulfatase Sulf-2 secreted form]: Secreted. SIMILARITY: Belongs to the sulfatase family.


FUNCTION: Transcription factor involved in regulating gene activity following the primary growth factor response. Binds to the DNA sequence 5'-TGA[GC]TCA-3' (By similarity). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to an AP-1 consensus sequence and its transcriptional activity (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. Jun subfamily.


SIMILARITY: To equivalent protein in phage 82.


FUNCTION: Involved in cell death (apoptosis). SIMILARITY: Belongs to the peptidase C14B family.


FUNCTION: Lipid transport protein (LTP) involved in non-vesicular transfer of lipids between membranes. Functions in phosphoinositide- coupled directional transport of various lipids by carrying the lipid molecule in a hydrophobic pocket and transferring it between membranes through the cytosol. Involved in maintenance of intracellular sterol distribution and homeostasis (PubMed:15173322, PubMed:16156791, PubMed:23934110, PubMed:26206936). Catalyzes the lipid countertransport between the endoplasmic reticulum (ER) and the plasma membrane (PM). Specifically exchanges phosphatidylserine (PS) with phosphatidylinositol 4-phosphate (PI4P), delivering phosphatidylserine to the PM in exchange for PI4P, which is delivered to the ER-localized PI4P phosphatase SAC1 for degradation. Thus, by maintaining a PI4P gradient at the ER/PM interface, SAC1 drives PS transport (PubMed:23934110, PubMed:26206936). Binds phosphatidylserine and PI4P in a mutually exclusive manner (PubMed:26206936). Also binds phosphatidic acid (PA) (PubMed:16156791). SUBCELLULAR LOCATION: Cytoplasm Cell membrane Endoplasmic reticulum membrane Note=Localizes to the cortical endoplasmic reticulum at the endoplasmic reticulum-plasma membrane contact sites. SIMILARITY: Belongs to the OSBP family.


SIMILARITY: Belongs to the slowmo family.


SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SMIM12 family.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL13 family.


FUNCTION: May act as a short alcohol-polyol-sugar dehydrogenase possibly related to carbohydrate metabolism and the acquisition of desiccation tolerance. May also be involved in signal transduction (By similarity). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Has a regulatory effect on thylakoid protein phosphorylation. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. Note=Can interact with the inner surface of the stroma-exposed thylakoid regions.


FUNCTION: Chemotactic factor that mediates inflammatory response by attracting neutrophils, basophils, and T-cells to clear pathogens and protect the host from infection. Also plays an important role in neutrophil activation. Released in response to an inflammatory stimulus, exerts its effect by binding to the G-protein-coupled receptors CXCR1 and CXCR2, primarily found in neutrophils, monocytes and endothelial cells. G-protein heterotrimer (alpha, beta, gamma subunits) constitutively binds to CXCR1/CXCR2 receptor and activation by IL8 leads to beta and gamma subunits release from Galpha (GNAI2 in neutrophils) and activation of several downstream signaling pathways including PI3K and MAPK pathways. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.


FUNCTION: Could act as a modulator of glutaredoxin biological activity (By similarity). May play a role in cytoskeleton organization (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell projection, ruffle membrane Nucleus. SIMILARITY: Belongs to the SH3BGR family.


FUNCTION: Regulates mitochondrial transport during axon regeneration. Increases the proportion of motile mitochondria by recruiting stationary mitochondria into the motile pool. Enhances mitochondria movement and neurite growth in both adult axons and embryonic neurons. Promotes neuronal survival and axon regeneration after nerve injury. May link mitochondria to the Trak1-kinesin motor complex via its interaction with MIRO1. SUBCELLULAR LOCATION: Mitochondrion Mitochondrion outer membrane; Single- pass membrane protein. SIMILARITY: Belongs to the eutherian X-chromosome-specific Armcx family.


FUNCTION: Plays an essential role in hormone and neurotransmitter calcium-dependent exocytosis and endocytosis (PubMed:7901002, PubMed:17301173, PubMed:18167541, PubMed:20484665, PubMed:22411134, PubMed:28813412). Part of the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the presynaptic plasma membrane (PubMed:14665625, PubMed:16888141, PubMed:19571812). STX1A and SNAP25 are localized on the plasma membrane while VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs from the N-terminal SNARE motifs to the C-terminal anchors leads to the formation of the SNARE complex, which brings membranes into close proximity and results in final fusion (PubMed:14665625, PubMed:16888141, PubMed:19571812). Participates in the calcium-dependent regulation of acrosomal exocytosis in sperm (By similarity). Also plays an important role in the exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-1) (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Single-pass type IV membrane protein Cell membrane Synapse, synaptosome Note=Colocalizes with KCNB1 at the cell membrane (PubMed:17301173). Colocalizes with PLCL1 at the cell membrane (PubMed:22673903). SIMILARITY: Belongs to the syntaxin family.


FUNCTION: Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH and follitropin/follicle stimulating hormone/FSH. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycoprotein hormones subunit alpha family.


SIMILARITY: Belongs to the phosphohexose mutase family.


FUNCTION: TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. May function as a coactivator by serving as a site of protein-protein contact between activators like Sp1 (or btd) and TFIID complex. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TAF4 family.


FUNCTION: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.


FUNCTION: Catalyzes the phosphorylation of fructose to fructose-6-P. Has also low level glucokinase activity in vitro. Is not able to phosphorylate D-ribose, D-mannitol, D-sorbitol, inositol, and L- threonine. SIMILARITY: Belongs to the ROK (NagC/XylR) family.


SIMILARITY: Belongs to the bacterial ribosomal protein bS21 family. SIMILARITY: Belongs to the bacterial ribosomal protein bS21 family.


FUNCTION: Galactinol synthase involved in the biosynthesis of raffinose family oligosaccharides (RFOs) that function as osmoprotectants. May promote plant stress tolerance (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyltransferase 8 family. Galactosyltransferase subfamily.


FUNCTION: Regulatory subunit of the slx1-slx4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SLX4 family.


SUBCELLULAR LOCATION: Mitochondrion. Membrane; Single- pass membrane protein. SIMILARITY: Belongs to the LCL3 family.


FUNCTION: May be involved in secondary cell wall biosynthesis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TALE/KNOX homeobox family.


FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of asperthecin, an anthraquinone pigment (PubMed:18978088, PubMed:21866960). Polyketide synthase (PKS) aptA catalyzes the formation of the aromatic polyketide from acetyl coenzyme A and seven malonyl coenzyme A molecules (PubMed:18978088). Polyketide is subsequently hydrolyzed by the action of the hydrolase aptB into endocrocin-9-anthrone (PubMed:18978088). Endocrocin-9-anthrone is then oxidized into endocrocin by the monooxygenase aptC (PubMed:18978088). Endocrocin is likely to decarboxylate spontaneously to form emodin which explains why there is no decarboxylase in the asperthecin biosynthesis cluster (PubMed:18978088). Finally, aptC or another endogenous oxygenase catalyzes additional oxidation steps to form asperthecin (PubMed:18978088). SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.


FUNCTION: Dephosphorylates Wzc. Required for the extracellular polysaccharide colanic acid synthesis. Probably involved in the export of colanic acid from the cell to medium. Involved in protection of cells against contact-dependent growth inhibition (CDI). SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein phosphatase family.


FUNCTION: Involved in specifying the paraxial, but not dorsal, mesoderm. May regulate the expression of T-box transcription factors required for mesoderm formation and differentiation, such as brachyury T, wnt8, vegt and eomes (By similarity). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. FUNCTION: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis. SIMILARITY: Belongs to the thymidylate kinase family. SIMILARITY: Belongs to the thymidylate kinase family.


FUNCTION: Tubulin-folding protein; involved in the final step of the tubulin folding pathway. SUBCELLULAR LOCATION: Cytoplasm Note=Detected predominantly in the photoreceptor connecting cilium. SIMILARITY: Belongs to the TBCC family.


SIMILARITY: Belongs to the UPF0342 family.


FUNCTION: Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. Acts as a positive regulator of Wnt signaling pathway by promoting beta-catenin (CTNNB1) nuclear accumulation. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes in the cytoplasm in the absence of Wnt stimulation and in the nucleus in the presence of Wnt stimulation. SIMILARITY: Belongs to the GID8 family.


FUNCTION: Catalyzes the epimerization a variety of hydrophobic dipeptides. Epimerase activity is highest with L-Ala-L-Tyr, and lower with L-Ala-L-Met, L-Ala-L-Phe, L-Tyr-L-Ala, L-Tyr-L-Met and L-Tyr-L-Trp (in vitro). SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family.


FUNCTION: Oxidative deamination of branched-chain amino acids. The catabolism of valine is the major source of fatty acid precursors for macrolide biosynthesis and a vital source of antibiotic precursors. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.


FUNCTION: Involved in iron cellular uptake. Seems to be internalized and then recycled back to the cell membrane. Binds a single atom of iron per subunit. Could also bind zinc. SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the transferrin family.


FUNCTION: Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and retaining phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding of STAT1 in the nucleus (By similarity). SUBCELLULAR LOCATION: [Isoform P3]: Host nucleus. SUBCELLULAR LOCATION: [Isoform P2]: Host cytoplasm. SUBCELLULAR LOCATION: [Phosphoprotein]: Virion. Host cytoplasm. SUBCELLULAR LOCATION: [Isoform P5]: Host nucleus. SIMILARITY: Belongs to the lyssavirus protein P family.


FUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion (By similarity). In myoblasts, may regulate PIEZO1-dependent cortical actomyosin assembly involved in myotube formation (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cell cortex Note=Colocalizes with F-actin, MYH9 and PIEZO1 at the actomyosin cortex in myoblasts.


SIMILARITY: Belongs to the UPF0401 family.


FUNCTION: Glutathione peroxidase-like protein that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress (PubMed:10480913, PubMed:11445588). Has peroxidase activity using thioredoxin or glutathione as a reducing power (PubMed:20572871, PubMed:22659048). Involved in peroxisome formation (PubMed:22659048). SUBCELLULAR LOCATION: Peroxisome matrix Mitochondrion outer membrane; Peripheral membrane protein. SIMILARITY: Belongs to the glutathione peroxidase family.


FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments (By similarity). SIMILARITY: Belongs to the F-actin-capping protein alpha subunit family.


FUNCTION: Part of the glycosylphosphatidylinositol-N- acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PIGC family.


FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the production of the antimicrobial trichothecene harzianum A (HA) that plays a role in Botrytis cinerea antagonistic activity and plant defense priming (PubMed:21642405, PubMed:29623313). The biosynthesis of harzianum A begins with the cyclization of farnesyl diphosphate to trichodiene and is catalyzed by the trichodiene synthase TRI5 (PubMed:21642405). Trichodiene undergoes a series of oxygenations catalyzed by the cytochrome P450 monooxygenase TRI4. TRI4 controls the addition of 3 oxygens at C-2, C-11, and the C-12, C-13-epoxide to form the intermediate isotrichodiol (PubMed:21642405). Isotrichodiol then undergoes a non-enzymatic isomerization and cyclization to form 12,13- epoxytrichothec-9-ene (EPT) which is further converted to trichodermol by the cytochrome P450 monooxygenase TRI11 via C-4 hydroxylation (PubMed:21642405). The last step of HA synthesis is esterification of an octatriendioyl moiety to the C-4 oxygen of trichodermol. The octatriendioyl moiety is probably produced by the polyketide synthase TRI17 and the esterification performed by the trichothecene O- acetyltransferase TRI3 (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: E3 ubiquitin ligase that plays a role in the maintenance of muscle cell boundaries and muscle dense bodies, which establish the adhesion sites of the muscle cells to the extracellular matrix (PubMed:15210732). Ubiquitinates the LIM domain protein unc-95, thereby regulating its dislocalization from muscle dense bodies and weakening the link between the muscle cells and the hypodermis (PubMed:20385102, PubMed:15210732). Regulation of unc-95 dissociation from muscle dense bodies by ubiquitination plays an important role in ecdysis during molting (PubMed:20385102). Plays a role in the cessation of distal tip cell migration at the end of larval morphogenesis (PubMed:22285439). Acts as a negative regulator of autophagy (PubMed:23093945). SUBCELLULAR LOCATION: Cell junction Cell junction, focal adhesion Cell membrane Note=Colocalizes with deb-1/vinculin in muscle dense bodies. SIMILARITY: Belongs to the RNF5 family.


SUBCELLULAR LOCATION: Cytoplasm, cytosol.


FUNCTION: May be required for cytoplasm to vacuole transport (Cvt) and pexophagy. SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein Endomembrane system; Peripheral membrane protein Note=Endosome and other perivacuolar punctate structures. SIMILARITY: Belongs to the sorting nexin family.


SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein.


FUNCTION: Incorporates a polar amino acid serine into membranes and facilitates the synthesis of two serine-derived lipids, phosphatidylserine and sphingolipids. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TDE1 family.


FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK1 appears to be a negative regulator of the insulin signaling pathway. Modulates integrin activation by competing with talin for the same binding site on ITGB3. SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, perinuclear region. SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus. SIMILARITY: Belongs to the DOK family. Type A subfamily.


SIMILARITY: Belongs to the adenoviridae pVIII family.


FUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed (By similarity). Plays a role in ciliogenesis (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the villin/gelsolin family.


FUNCTION: [NGAPQPFVRF-amide]: Acts as a ligand for the npr-22 receptor in vitro. FUNCTION: [AMRNALVRF-amide]: Potent inhibitor of the activity of the dissected pharyngeal myogenic muscle system (PubMed:16187307). Acts as a ligand for the npr-22 receptor in vitro (PubMed:16377032). FUNCTION: FMRFamides and FMRFamide-like peptides are neuropeptides. FUNCTION: [ASGGMRNALVRF-amide]: Acts as a ligand for the npr-22 receptor in vitro. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.


FUNCTION: Converts phytoene into zeta-carotene via the intermediary of phytofluene by the symmetrical introduction of two double bonds at the C-11 and C-11' positions of phytoene with a concomitant isomerization of two neighboring double bonds at the C9 and C9' positions from trans to cis. SUBCELLULAR LOCATION: Plastid, chloroplast Plastid, chromoplast Membrane; Peripheral membrane protein Note=Exists as an inactive soluble form and an active membrane-bound form. SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.


FUNCTION: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the tropomodulin family.


FUNCTION: Involved in connections of major cytoskeletal structures to the plasma membrane. SUBCELLULAR LOCATION: Cell junction, adherens junction Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytoskeleton.


FUNCTION: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7- methylguanosine cap of a subset of mRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit D family.


FUNCTION: Possesses low quercetin 3-O-glucosyltransferase activity in vitro. SIMILARITY: Belongs to the UDP-glycosyltransferase family.


FUNCTION: Hemerythrin is a respiratory protein in blood cells of certain marine worms. The oxygen-binding site in each chain contains two iron atoms. SIMILARITY: Belongs to the hemerythrin family.


FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Golgi apparatus Cytoplasmic vesicle Note=Detected on osteoblast plasma membrane lipid rafts. After ligand binding, the activated receptor is rapidly internalized and degraded (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.


FUNCTION: Self assembles to form an icosahedral capsid. Most capsid appear to be large particles with an icosahedral symmetry of T=4 and consist of 240 copies of capsid protein, though a fraction forms smaller T=3 particles consisting of 180 capsid proteins. Entering capsid are transported along microtubules to the nucleus. Phosphorylation of the capsid is thought to induce exposure of nuclear localization signal in the C-terminal portion of the capsid protein that allows binding to the nuclear pore complex via the importin (karyopherin-) alpha and beta. Capsids are imported in intact form through the nuclear pore into the nuclear basket, where it probably binds NUP153. Only capsids that contain the mature viral genome can release the viral DNA and capsid protein into the nucleoplasm. Immature capsids get stucked in the basket. Capsids encapsulate the pre-genomic RNA and the P protein. Pre-genomic RNA is reverse transcribed into DNA while the capsid is still in the cytoplasm. The capsid can then either be directed to the nucleus, providing more genome for transcription, or bud through the endoplasmic reticulum to provide new virions (By similarity). SUBCELLULAR LOCATION: [Capsid protein]: Virion Host cytoplasm. SIMILARITY: Belongs to the avihepadnavirus core antigen family.


FUNCTION: Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover (By similarity). Ccr4 has 3'-5' RNase activity with a strong preference for polyadenylated substrates and also low exonuclease activity towards single-stranded DNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CCR4/nocturin family.


FUNCTION: Involved in the purine-salvage pathway (PubMed:35338694). Catalyzes the NADPH-dependent conversion of GMP to IMP (PubMed:35338694). Is not essential for viability, but may contribute to the regulation of the purine nucleotide pool by recycling GMP to IMP (PubMed:35338694). SIMILARITY: Belongs to the IMPDH/GMPR family. GuaB1 subfamily.


FUNCTION: Low-affinity glutamine synthetase (PubMed:14757761). May contribute to the homeostatic control of glutamine synthesis in roots. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutamine synthetase family.


FUNCTION: Responsible for the transport of succinate and fumarate, but not malate, across the membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family.


FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short subfamily. SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short subfamily.


FUNCTION: Ribosome-inactivating protein of type 1, inhibits protein synthesis in animal cells. SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily.


FUNCTION: Plays a role in the protection against host NK cell cytotoxicity by interacting with and modulating the activity of the host inhibitory leukocyte Ig-like receptor 1/LILRB1, which is expressed on monocytes, dendritic cells, as well as subsets of T and NK cells. UL18 exerts an inhibitory effect on LIR-1+ NK cells, while it stimulates LIR-1- NK cell (By similarity). SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein.


FUNCTION: Lea proteins are late embryonic proteins abundant in higher plant seed embryos. SIMILARITY: Belongs to the small hydrophilic plant seed protein family.


FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Has RNase activity (By similarity). Is very toxic upon expression in E.coli. Its toxic activity is probably neutralized by the cognate antitoxin RelB3. SIMILARITY: Belongs to the RelE toxin family.


FUNCTION: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.


FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GPI family. SIMILARITY: Belongs to the GPI family.


FUNCTION: Catalyzes the NAD(P)H-dependent reduction of 2-oxoglutarate, phenylpyruvate and (4-hydroxyphenyl)pyruvate, leading to the respective 2-hydroxycarboxylate in vitro. Shows a preference for NADPH over NADH as a redox partner. Do not catalyze the reverse reactions. SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family.


FUNCTION: Required for efficient biogenesis of the 60S ribosomal subunit. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the RSA3 family.


FUNCTION: Involved in the synthesis of UDP-N-acetylgalactosamine (UDP- GalNAc). Catalyzes the conversion of glucosamine-6-phosphate (GlcN-6-P) to galactosamine-6-phosphate (GalN-6-P). SIMILARITY: Belongs to the PGI/PMI family.


FUNCTION: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR). SIMILARITY: Belongs to the PurK/PurT family.


FUNCTION: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Most efficiently cleaves the synthetic substrate Met- Leu-methylcoumaryl-7-amide (Met-Leu-MCA), and slowly hydrolyzes Leu- Gln-, Lys-Ala-, Leu-Arg, and Ala-Asn-MCA. Is likely involved in amino acid metabolism and bacterial growth/survival of asaccharolytic P.endodontalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources. SIMILARITY: Belongs to the peptidase S46 family.


FUNCTION: Oxalyl-CoA synthetase acting exclusively against oxalate (PubMed:22447686, PubMed:27326693). Follows a two-step reaction mechanism, wherein oxalate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield oxalyl-CoA (By similarity). No activity with malonate, succinate, malate, acetate, formate, lactate, glycolate, glyoxylate or glutarate (PubMed:22447686). Required for oxalate degradation, normal seed development and defense against oxalate-producing fungal pathogens (PubMed:22447686). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0060 family.


FUNCTION: Intracellular cholesterol transporter which acts in concert with NPC1 and plays an important role in the egress of cholesterol from the lysosomal compartment. Unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes is transferred by NPC2 to the cholesterol-binding pocket in the N-terminal domain of NPC1. May bind and mobilize cholesterol that is associated with membranes. NPC2 binds cholesterol with a 1:1 stoichiometry. Can bind a variety of sterols, including lathosterol, desmosterol and the plant sterols stigmasterol and beta-sitosterol (By similarity). The secreted form of NCP2 regulates biliary cholesterol secretion via stimulation of ABCG5/ABCG8-mediated cholesterol transport (By similarity). FUNCTION: Intracellular cholesterol transporter which acts in concert with NPC1 and plays an important role in the egress of cholesterol from the lysosomal compartment (PubMed:17018531, PubMed:11125141, PubMed:18772377, PubMed:29580834, PubMed:15937921). Unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes is transferred by NPC2 to the cholesterol-binding pocket in the N-terminal domain of NPC1 (PubMed:17018531, PubMed:18772377, PubMed:27238017). May bind and mobilize cholesterol that is associated with membranes (PubMed:18823126). NPC2 binds cholesterol with a 1:1 stoichiometry (PubMed:17018531). Can bind a variety of sterols, including lathosterol, desmosterol and the plant sterols stigmasterol and beta-sitosterol (PubMed:17018531). The secreted form of NCP2 regulates biliary cholesterol secretion via stimulation of ABCG5/ABCG8-mediated cholesterol transport (By similarity). SUBCELLULAR LOCATION: Secreted Endoplasmic reticulum Lysosome Note=Interaction with cell-surface M6PR mediates endocytosis and targeting to lysosomes. SUBCELLULAR LOCATION: Secreted Endoplasmic reticulum Lysosome Note=Interaction with cell-surface M6PR mediates endocytosis and targeting to lysosomes. SUBCELLULAR LOCATION: Secreted Endoplasmic reticulum Lysosome Note=Interaction with cell-surface M6PR mediates endocytosis and targeting to lysosomes. SIMILARITY: Belongs to the NPC2 family.


FUNCTION: Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LplA family.


FUNCTION: Required for 20S pre-rRNA processing. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the TSR2 family.


FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit central domain. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit. SIMILARITY: Belongs to the universal ribosomal protein uS8 family.


FUNCTION: [Isoform 2]: Forms toxic aggregates that disrupt spore maturation. FUNCTION: [Isoform 1]: Localizes isoform 2 to the vacuole thereby facilitating its degradation. FUNCTION: Promotes unequal transmission of alleles from the parental zygote to progeny spores by acting as poison/antidote system where the poison and antidote proteins are produced from the same locus; the poison component is trans-acting and targets all spores within an ascus whereas the antidote component is spore-specific, leading to poisoning of all progeny that do not inherit the allele. SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm Cytoplasm Spore membrane; Multi-pass membrane protein Vacuole membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Note=Localizes in trans to all spores within an ascus. Localization to the spore vacuole is dependent on isoform 1. SUBCELLULAR LOCATION: [Isoform 1]: Spore membrane; Multi-pass membrane protein Vacuole membrane; Multi-pass membrane protein Note=Contained within spores expressing the isoform and localizes isoform 2 to the vacuole. SIMILARITY: Belongs to the WTF family.


SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PRM5 family.


FUNCTION: May act as the primary docking protein directing membrane turnover and assembly of the transient receptor potential channels trpc4 and trpc5. Binds phospholipids (By similarity). SIMILARITY: Belongs to the SOLO family.


SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily.


FUNCTION: Cell-surface receptor that plays a role in cell-cell interactions, as well as cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases. Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell projection, microvillus Secreted Note=Colocalizes with actin in membrane protrusions at wounding edges. Co-localizes with RDX, EZR and MSN in microvilli.


FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H1/H5 family.


FUNCTION: Catalyzes the transmethylation of nonepinephrine (noradrenaline) to form epinephrine (adrenaline), using S-adenosyl-L- methionine as the methyl donor (PubMed:13863458). Other substrates include phenylethanolamine, octopamine and normetanephrine (PubMed:13863458). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. NNMT/PNMT/TEMT family.


FUNCTION: Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L- arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 54 family.


FUNCTION: Involved in lineage commitment of primary hemopoietic progenitors by restricting erythroid formation and enhancing myeloid formation. Interferes with erythropoietin-induced erythroid terminal differentiation by preventing cells from exiting the cell cycle through suppression of CDKN1B/p27Kip1 levels. Suppresses COP1 activity via CSN3 which activates p53 and induces cell cycle arrest. Binds DNA and affects the expression of a number of genes so may function as a transcription factor in the nucleus (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell projection, cilium Cytoplasm, cytoskeleton, cilium basal body Note=Shuttles between the cytoplasm and nucleus. SIMILARITY: Belongs to the MLF family.


FUNCTION: Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, beta-glycerol phosphate, and alpha-D-glucose-1- phosphate. Cannot hydrolyze glucose-6-phosphate, fructose-6-phosphate, NAD(+) or 5'-AMP. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate. SIMILARITY: Belongs to the inositol monophosphatase superfamily. FBPase class 4 family.


FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MFAP1 family.


FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin (PubMed:9045804). SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.


FUNCTION: E3 ubiquitin ligase essential for DNA replication origin activation during S phase. Acts as a replication origin selector which selects the origins to be fired and catalyzes the multi-mono- ubiquitination of a subset of chromatin-bound ORC3 and ORC5 during S- phase. SUBCELLULAR LOCATION: Chromosome Note=Association to chromatin is cell cycle-regulated, absent from mitotic chromosomes, is associated with chromatin from G1 and partially released from chromatin from mid S-phase.


FUNCTION: RPGW-amide, KPGW-amide and TPGW-amide tetrapeptides are involved in control of muscle contraction and may function as neurotransmitters. These peptides increase tension of the pedal retractor muscle and, in conjunction with FMRF-amide, increase peak tension of the anterior byssus retractor muscle (ABRM).


FUNCTION: Together with RGLG1, mediates the ubiquitination and subsequent proteasomal degradation of the target protein PP2CA. Functions as positive regulator of abscisic acid (ABA) signaling through ABA-dependent degradation of PP2CA, a major inhibitor of ABA signaling. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.


FUNCTION: Ets-related protein that functions as a negative regulator of photoreceptor development acting antagonistically to pnt and the proneural signal mediated by RAS (PubMed:1505027, PubMed:1495974, PubMed:8033205). It acts upstream of SINA to inhibit R7 development (PubMed:1505027, PubMed:1495974). SUBCELLULAR LOCATION: Nucleus Note=In undifferentiated cells during the early stages of eye development. SIMILARITY: Belongs to the ETS family.


FUNCTION: TAFs are components of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription. Required for the expression of a subset of ethylene- responsive genes (By similarity). Involved in the negative regulation of cytokinin sensitivity. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TAF12 family.


FUNCTION: Antibacterial peptide mostly active against Gram-positive bacteria (PubMed:20605792). It acts by selectively inhibiting peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio) thus inhibiting cell wall synthesis (PubMed:20605792). It does not disrupt cell membranes (PubMed:20605792). Is noticeably more potent than Cg-Defh1 (PubMed:20605792). SUBCELLULAR LOCATION: Secreted Target cell membrane. SIMILARITY: Belongs to the invertebrate defensin family.


FUNCTION: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ChlB/BchB/BchZ family.


FUNCTION: The beta subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells (PubMed:7485470, PubMed:10722662, PubMed:11909858). Plays a structural and regulatory role in the assembly and membrane targeting of a functionally active pump (PubMed:7485470, PubMed:10722662, PubMed:11909858). Within a transport cycle, the transfer of a H(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation of the alpha subunit that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2) (By similarity). Interacts with the phosphorylation domain of the alpha subunit and functions as a ratchet, stabilizing the lumenal-open E2 conformation and preventing the reverse reaction of the transport cycle (By similarity). SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II membrane protein Cell membrane; Single-pass type II membrane protein Note=Localized in the apical canalicular membrane of parietal cells. SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.


FUNCTION: Catalyzes the amidation of bile acids (BAs) with the amino acid taurine (PubMed:9215542). Selective for taurine conjugation of cholyl CoA and only taurine-conjugated BAs are found in bile (PubMed:9215542). Amidation of BAs in the liver with taurine prior to their excretion into bile is an important biochemical event in bile acid metabolism (By similarity). This conjugation (or amidation) plays several important biological roles in that it promotes the secretion of BAs and cholesterol into bile and increases the detergent properties of BAs in the intestine, which facilitates lipid and vitamin absorption (By similarity). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids (By similarity). In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Peroxisome. SIMILARITY: Belongs to the C/M/P thioester hydrolase family.


FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the GcvH family.


FUNCTION: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WD repeat TRM82 family.


SIMILARITY: Belongs to the UPF0340 family.


FUNCTION: Binds lactose. May play a role in fruiting body formation (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted, cell wall.


FUNCTION: Is a potent glycoprotein Ibalpha (GP1BA) antagonist. Concentration-dependently inhibits botrocetin-, ristocetin- and low dose thrombin-induced platelet aggregation. Inhibits platelet adhesion only through inhibiting the vWF interaction with GP1BA, but has minimal effect on other platelet receptors, such as alpha-IIb/beta-3 (ITGA2B/ITGB3) or alpha-2/beta-1 (ITGA2/ITGB1). Causes an instant severe thrombocytopenia in rats and is not lethal to mice. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family.


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


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family.


FUNCTION: Guanine nucleotide exchange factor for the Rho family of Ras- related GTPases. Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly.


FUNCTION: May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell junction, tight junction. SIMILARITY: Belongs to the ELL/occludin family.


FUNCTION: Microtubule-based anterograde translocator for membranous organelles. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Kinesin II subfamily.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family.


FUNCTION: Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes. SIMILARITY: Belongs to the NADH:flavin oxidoreductase/NADH oxidase family. NamA subfamily.


FUNCTION: May be involved in viral replication. SIMILARITY: Belongs to the peptidase C14A family.


FUNCTION: Catalyzes the radical-mediated synthesis of 5-amino-5-(4- hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D- ribitylamino)uracil and L-tyrosine. SIMILARITY: Belongs to the radical SAM superfamily. CofH family.


FUNCTION: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p- aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. PabB, in the absence of PabA, can catalyze the formation of ADC in the presence of exogenous ammonia. SIMILARITY: Belongs to the anthranilate synthase component I family.


FUNCTION: May act as a neurotransmitter or neuromodulator. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the allatostatin family.


FUNCTION: Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein Host endosome membrane; Single-pass type I membrane protein Host Golgi apparatus membrane; Single-pass type I membrane protein Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). SIMILARITY: Belongs to the herpesviridae glycoprotein B family.


FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond. Plays an important role in various cellular processes. SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.


FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1. SIMILARITY: Belongs to the 14-3-3 family.


FUNCTION: This enzyme is an effector of chloramphenicol resistance in bacteria. SIMILARITY: Belongs to the transferase hexapeptide repeat family.


FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems (PubMed:26213965). The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (Probable). Condensation of indole- 3-glycerol phosphate with GGPP by the prenyl transferase penC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-dependent monooxygenase penM leads to a epoxidized-GGI that is substrate of the terpene cyclase penB for cyclization to yield paspaline (Probable). Paspaline is subsequently converted to 13- desoxypaxilline by the cytochrome P450 monooxygenase penP, the latter being then converted to paxilline by the cytochrome P450 monooxygenase penQ (PubMed:26213965). Paxilline is converted to beta-paxitriol via C- 10 ketoreduction by the short-chain dehydrogenase PC-15 which can be monoprenylated at the C-20 by the indole diterpene prenyltransferase penD (Probable). A two-step elimination (acetylation and elimination) process performed by the O-acetyltransferase PC-16 and the P.simplicissimum ptmI-ortholog not yet identified in P.crustosum, leads to the production of the prenylated form of penijanthine (Probable). The FAD-linked oxidoreductase ptmO then converts the prenylated form of penijanthine into PC-M5 which is in turn transformed into PC-M4 by the aromatic dimethylallyltransferase PC-22 (Probable). A series of oxidation steps involving 4 cytochrome P450 monooxygenases (PC-21, PC- 05, PC-23, PC-20) and a FAD-dependent monooxygenase (PC-14) are required for the transformation of PC-M4 to penitrems A and E. Synthesis of these final products is proposed to proceed via penitrems D and C (PC-21, PC-05, PC-14) and penitrems B and F (PC-21, PC-05, PC- 14, PC-23) (Probable). SIMILARITY: Belongs to the FPP/GGPP synthase family.


FUNCTION: Acts as a transcriptional repressor. Represses the promoter activity of the CDC25C gene stimulated by NFYA. May play a role in retinal development where it regulates the composition of bipolar cell populations, by promoting differentiation of bipolar OFF-type cells. In the brain, may promote maintenance and suppress differentiation of neural progenitor cells in the developing cortex. SUBCELLULAR LOCATION: Nucleus Note=Colocalizes with EFNB1 intracellular domain in the nucleus. SIMILARITY: Belongs to the ZHX family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nematode receptor-like protein sre family.


FUNCTION: Ca(2+)-regulated actin-binding protein which plays an important role in actin bundling. May have a unique function in the morphogenesis of neuronal cells which form ganglia. Required for SREC1- mediated regulation of neurite-like outgrowth. Plays a role in regenerative sensory axon outgrowth and remodeling processes after peripheral injury in neonates. Involved in the formation of long fine actin-containing filopodia-like structures in fibroblast. Plays a role in ciliogenesis (PubMed:15247299, PubMed:18160648). In podocytes, controls lamellipodia formation through the regulation of EGF-induced diacylglycerol generation by PLCE1 and ARP2/3 complex assembly (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection, lamellipodium Cell junction, focal adhesion Cell projection, neuron projection Cell projection, axon Note=In podocytes, present in the F- actin-enriched cell periphery that generates lamellipodia and focal adhesions. SIMILARITY: Belongs to the villin/gelsolin family.


FUNCTION: Terpene cyclase/mutase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids nectripenoids A and B, as well as cochliquninone D and isocochliquninone E (PubMed:29797385). The pathway probably begins with the HR-PKS ntnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS ntnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of nectripenoids (Probable). The FAD-dependent monooxygenase ntnJ then performs an oxidative decarboxylation at C11 of the ntnH/ntnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation (Probable). The membrane-bound polyprenyl transferase ntnF then introduces a farnesyl group before the FAD- dependent monooxygenase ntnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by ntnA (Probable). The terpene cyclase/mutase ntnI then initiates the sequential tricyclic ring formation through protonation of the terminal epoxide and catalyzes the regioselective and stereoselective 6/6/6-tricyclic ring formation (Probable). The cytochrome P450 monooxygenase ntnM may then hydroxylate C1' (Probable). SIMILARITY: Belongs to the terpene cyclase/mutase family.


FUNCTION: Negatively regulates B-cell proliferation following stimulation through the B-cell receptor. May play an important role in maintenance of marginal zone (MZ) B-cells. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the GAPT family.


FUNCTION: Involved in bacteriochlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.


FUNCTION: Major calcium-binding protein of the Golgi which may have a role in calcium homeostasis (PubMed:7890746). Acts as a non-receptor guanine nucleotide exchange factor which binds to and activates alpha subunits of guanine nucleotide-binding proteins (G proteins) (By similarity). SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane; Peripheral membrane protein; Lumenal side Cytoplasm Secreted Note=A small fraction of the protein may be cytoplasmic. SIMILARITY: Belongs to the nucleobindin family.