FUNCTION: Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain (By similarity). SUBCELLULAR LOCATION: Mitochondrion intermembrane space Note=Loosely associated with the inner membrane. SIMILARITY: Belongs to the cytochrome c family.


FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. May increase spectral sensitivity in dim light. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. DHOase family. Class II DHOase subfamily.


FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from g1 to s phase. E2F2 binds specifically to RB1 in a cell-cycle dependent manner. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the E2F/DP family.


FUNCTION: This is a 2S seed storage protein. SIMILARITY: Belongs to the 2S seed storage albumins family.


FUNCTION: Fatty acid 2-hydroxylase involved in the alpha-hydroxylation of sphingolipid-associated very long-chain fatty acids (VLCFA). Probably involved in the resistance response to oxidative stress. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sterol desaturase family.


FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. SIMILARITY: Belongs to the NDK family.


SIMILARITY: Belongs to the glycosyl hydrolase 1 family.


FUNCTION: Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway. SIMILARITY: Belongs to the non-flavoprotein flavin reductase family. RutF subfamily.


FUNCTION: Antimicrobial peptide with activity against Gram-negative and Gram-positive bacteria (MIC=13 uM against E.coli, MIC=25 uM against S.aureus) and fungi (MIC=25 uM against C.albicans) (PubMed:15556063). Also shows hemolytic activity (HC(50)=50 uM) (PubMed:15556063). In vitro, shows moderate inhibitory activity against HIV (PubMed:20086159). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Brevinin subfamily.


FUNCTION: Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 or PEX21 receptors (PubMed:8858167, PubMed:20154681). The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm (PubMed:20154681). Mechanistically, PEX5 (or PEX21) receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix (PubMed:20154681). SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peroxin-13 family.


FUNCTION: Sulfotransferase that catalyzes the transfer of sulfate to the position 2 of uronyl residues. Has mainly activity toward iduronyl residues in dermatan sulfate, and weaker activity toward glucuronyl residues of chondroitin sulfate. Has no activity toward desulfated N- resulfated heparin (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 3 family.


FUNCTION: Moderately selective excitatory receptor for orexin-A and, with a lower affinity, for orexin-B neuropeptide. Triggers an increase in cytoplasmic Ca(2+) levels in response to orexin-A binding. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Potentially plays a role in the Ras signal transduction pathway. Capable of suppressing v-Ras transformation in vitro (By similarity).


SIMILARITY: Belongs to the glycosyltransferase 25 family.


FUNCTION: Alpha-ketoglutarate-dependent dioxygenase that in vitro catalyzes the regio- and stereoselective hydroxylation of L-lysine, leading to (4R)-4-hydroxy-L-lysine. SIMILARITY: Belongs to the clavaminate synthase family.


FUNCTION: Has antifungal activity. Inhibits mycelial growth of wood rotting fungi P.chrysosporium MTCC 787, S.commune ITCC 3751, G.trabeum MTCC 355, P.agaricans ITCC 761, C.versicolor MTCC 138, P.versicolor ITCC 13, P.placenta MTCC 144 and P.friabilis ITCC 335. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Catalyzes the reversible dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.


FUNCTION: Inhibits growth of Gram-positive (S.aureus, B.subtilis) and Gram-negative (E.coli, P.aeruginosa) bacteria and fungi (C.albicans). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cationic peptide 04 (cupiennin) family. 05 subfamily.


FUNCTION: Its physiological role is not yet clear. SIMILARITY: Belongs to the acylphosphatase family.


FUNCTION: Transcriptional repressor that contribute to growth arrest during terminal macrophage differentiation by repressing target genes involved in Ras-dependent proliferation. Represses MMP1 promoter activity. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ETS family.


FUNCTION: Activates transcription of the blt gene in response to structurally dissimilar drugs.


FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core (PubMed:20722388). The first step of notoamide biosynthesis involves coupling of L-proline and L-tryptophan by the bimodular NRPS notE, to produce cyclo-L-tryptophan-L-proline called brevianamide F (PubMed:20722388). The reverse prenyltransferase notF then acts as a deoxybrevianamide E synthase and converts brevianamide F to deoxybrevianamide E via reverse prenylation at C-2 of the indole ring leading to the bicyclo[2.2.2]diazaoctane core (PubMed:20722388). Deoxybrevianamide E is further hydroxylated at C-6 of the indole ring, likely catalyzed by the cytochrome P450 monooxygenase notG, to yield 6-hydroxy-deoxybrevianamide E (Probable). 6-hydroxy-deoxybrevianamide E is a specific substrate of the prenyltransferase notC for normal prenylation at C-7 to produce 6- hydroxy-7-prenyl-deoxybrevianamide, also called notoamide S (PubMed:20722388). As the proposed pivotal branching point in notoamide biosynthesis, notoamide S can be diverted to notoamide E through an oxidative pyran ring closure putatively catalyzed by either notH cytochrome P450 monooxygenase or the notD FAD-linked oxidoreductase (Probable). This step would be followed by an indole 2,3-epoxidation- initiated pinacol-like rearrangement catalyzed by the notB FAD- dependent monooxygenase leading to the formation of notoamide C and notoamide D (PubMed:22188465). On the other hand notoamide S is converted to notoamide T by notH (or notD), a bifunctional oxidase that also functions as the intramolecular Diels-Alderase responsible for generation of (+)-notoamide T (Probable). To generate antipodal (-)- notoaminide T, notH' (or notD') in Aspergillus versicolor is expected to catalyze a Diels-Alder reaction leading to the opposite stereochemistry (Probable). The remaining oxidoreductase notD (or notH) likely catalyzes the oxidative pyran ring formation to yield (+)- stephacidin A (Probable). The FAD-dependent monooxygenase notI is highly similar to notB and is predicted to catalyze a similar conversion from (+)-stephacidin A to (-)-notoamide B via the 2,3- epoxidation of (+)-stephacidin A followed by a pinacol-type rearrangement (Probable). Finally, it remains unclear which enzyme could be responsible for the final hydroxylation steps leading to notoamide A and sclerotiamide (Probable). SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.


FUNCTION: Antifibrinolytic and antimicrobial serine protease inhibitor. Inhibits trypsin, plasmin and microbial serine proteases but not chymotrypsin, thrombin and elastase. Inhibits the plasmin-mediated degradation of fibrin to fibrin degradation products. Also binds to bacterial and fungal surfaces and exhibits antimicrobial activity against fungi as well as Gram-positive and Gram-negative bacteria. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the serine protease inhibitor-like (TIL domain- containing) family.


FUNCTION: Plays a major role in the induction and maintenance of cellular transformation. E6 associates with host UBE3A/E6-AP ubiquitin- protein ligase and modulates its activity. Sequesters tumor suppressor TP53 in the host cytoplasm and modulates its activity by interacting with host EP300 that results in the reduction of TP53 acetylation and activation. In turn, apoptosis induced by DNA damage is inhibited. E6 protects also host keratinocytes from apoptosis by mediating the degradation of host BAK1. May also inhibit host immune response. SUBCELLULAR LOCATION: Host cytoplasm Host nucleus. SIMILARITY: Belongs to the papillomaviridae E6 protein family.


FUNCTION: Glycoprotein which is a component of the gelatinous extracellular matrix in the cupulae of the vestibular organ. SUBCELLULAR LOCATION: [Zona pellucida-like domain-containing protein 1, secreted form]: Secreted, extracellular space, extracellular matrix. SUBCELLULAR LOCATION: [Zona pellucida-like domain-containing protein 1]: Cytoplasmic vesicle membrane; Single-pass type I membrane protein.


FUNCTION: Member of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form the 43S pre-initiation complex (43S PIC). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity). SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EIF2G subfamily.


FUNCTION: Transcription factor that plays a positive role in salt stress tolerance. Interacts with TIFY11A/JAZ9 and binds to the promoter of some potassium ion transporter genes to regulate potassium homeostasis during salt stress. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bHLH protein family.


FUNCTION: Functions as an electron carrier between membrane-bound cytochrome b6-f and photosystem I in oxygenic photosynthesis. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. SIMILARITY: Belongs to the cytochrome c family. PetJ subfamily.


FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase essential for assembly or catalytic function. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity). SIMILARITY: Belongs to the V-ATPase E subunit family.


SIMILARITY: Belongs to the UPF0270 family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family. Eye pigment precursor importer (TC 3.A.1.204) subfamily.


FUNCTION: Methylates DNA on the 6th position of adenine (N(6)- methyladenosine) (PubMed:25936839). N(6)-methyladenosine (m6A) DNA is involved in epigenetic transgenerational inheritance (PubMed:25936839). SIMILARITY: Belongs to the MT-A70-like family.


FUNCTION: Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes. Has also methyltransferase activity toward non-histone proteins. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET7 subfamily.


FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the amidase family. GatA subfamily.


FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. SUBCELLULAR LOCATION: Vacuole membrane; Peripheral membrane protein. SIMILARITY: Belongs to the V-ATPase C subunit family.


FUNCTION: Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors. Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Upon activation of IL6ST/gp130 signaling by interleukin-6 (IL6), binds to the IL6- responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA (By similarity). Acts as a regulator of inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): deacetylation and oxidation of lysine residues by LOXL3, leads to disrupt STAT3 dimerization and inhibit its transcription activity (By similarity). Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1 (By similarity). Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation. May play an apoptotic role by transctivating BIRC5 expression under LEP activation (By similarity). Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity (By similarity). Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion. Plays an important role in host defense in methicillin-resistant S.aureus lung infection by regulating the expression of the antimicrobial lectin REG3G (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Shuttles between the nucleus and the cytoplasm. Translocated into the nucleus upon tyrosine phosphorylation and dimerization, in response to signaling by activated FGFR1, FGFR2, FGFR3 or FGFR4. Constitutive nuclear presence is independent of tyrosine phosphorylation. Predominantly present in the cytoplasm without stimuli. Upon leukemia inhibitory factor (LIF) stimulation, accumulates in the nucleus (By similarity). The complex composed of BART and ARL2 plays an important role in the nuclear translocation and retention of STAT3. SIMILARITY: Belongs to the transcription factor STAT family.


FUNCTION: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light- driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. SUBCELLULAR LOCATION: Plastid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbI family.


FUNCTION: Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways (PubMed:29378087). Catalyzes the biosynthesis of squalene (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the phytoene/squalene synthase family.


FUNCTION: May regulate MYC transcription factors. Involved in epidermal cell fate specification such as trichome and root hair development, seed mucilage production, and anthocyanin biosynthesis by acting at the dihydroflavonol-4-reductase (DFR) step. Together with GL1 and GL3, promotes trichome formation. Activates the transcription of GL2. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Required for proper cell wall integrity and for the correct assembly of the mannoprotein outer layer of the cell wall. Important for apical bud growth (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor Secreted, cell wall Note=Identified as GPI-anchored plasma membrane protein (GPI-PMP) as well as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer. SIMILARITY: Belongs to the SPS2 family.


FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes retinyl esters (By similarity). Hydrolyzes p-nitrophenyl butyrate (PNPB), triacylglycerol and monoacylglycerol. Shows higher activity against PNPB, a short-chain fatty acid ester, than against triolein, a long-chain fatty acid ester. Shows no detectable activity against diacylglycerol, cholesterol ester or phospholipids. May play a role in adipocyte lipolysis. SUBCELLULAR LOCATION: Lipid droplet Cytoplasm, cytosol Endoplasmic reticulum Microsome. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.


FUNCTION: Acts as a non-catalytic accessory component of a dynein complex. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the dynein light chain family.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eL19 family.


FUNCTION: GTP-binding protein involved in transport from the endoplasmic reticulum to the Golgi apparatus (PubMed:11149932, PubMed:8138575). Activated by the guanine nucleotide exchange factor PREB (PubMed:11149932, PubMed:8138575). Involved in the selection of the protein cargo and the assembly of the COPII coat complex (PubMed:11149932, PubMed:8138575). Synergizes with the cargo receptor SURF4 to mediate the export of lipoproteins from the endoplasmic reticulum, thereby regulating lipoprotein delivery and the maintenance of lipid homeostasis (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Golgi apparatus, Golgi stack membrane; Peripheral membrane protein Note=Associated with the endoplasmic reticulum and Golgi stacks, in particular in the juxta-nuclear Golgi region. SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.


FUNCTION: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB). SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the STAM family.


SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.


FUNCTION: Antimicrobial peptide with activity against Gram-positive and Gram-negative bacteria, and fungi. Has hemolytic activity. SUBCELLULAR LOCATION: Secreted Target cell membrane. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily.


FUNCTION: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in endosomal cargo sorting. SUBCELLULAR LOCATION: Endosome. SIMILARITY: Belongs to the BLI1 family.


FUNCTION: Binds activated protein C. Enhances protein C activation by the thrombin-thrombomodulin complex; plays a role in the protein C pathway controlling blood coagulation (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.


FUNCTION: Catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigB subfamily.


FUNCTION: Malate dehydrogenase; catalyzes a reversible NAD-dependent dehydrogenase reaction involved in central metabolism and redox homeostasis. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.


FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' (PubMed:17650508). Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocates to the plasma membrane upon Ca(2+) binding. SIMILARITY: Belongs to the peptidase C2 family.


FUNCTION: Essential virulence determinant. This protein is a protein tyrosine phosphatase. The essential function of YopH in Yersinia pathogenesis is host-protein dephosphorylation. It contributes to the ability of the bacteria to resist phagocytosis by peritoneal macrophages. SUBCELLULAR LOCATION: Secreted. Note=Secreted via type III secretion system. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class subfamily.


FUNCTION: Insecticidal neurotoxin that induces irreversible neuromuscular blockade in house crickets (A.domesticus). Modifies presynaptic voltage-gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neurons. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 07 (Beta/delta-agtx) family. 04 (aga-5) subfamily.


FUNCTION: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbM family.


FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'phage' integrase family. XerD subfamily.


FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion Mitochondrion inner membrane; Peripheral membrane protein Mitochondrion intermembrane space. SIMILARITY: Belongs to the complex I NDUFB7 subunit family.


FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The nbp35-cfd1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily.


FUNCTION: Crucial for commitment to meiosis but it is not sufficient itself for the commitment. May be a splicing regulator.


FUNCTION: Acts as negative regulator of seedling photomorphogenesis (PubMed:18540109). Acts as a negative regulator of blue light-mediated inhibition of hypocotyl elongation through increase of bioactive gibberellin levels (PubMed:20872270). Acts as a repressor of thermotolerance by modulating expression of a set of heat shock- responsive genes (PubMed:23238922). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Cytochrome c2 is found mainly in purple, non-sulfur, photosynthetic bacteria where it functions as the electron donor to the oxidized bacteriochlorophyll in the photophosphorylation pathway. However, it may also have a role in the respiratory chain and is found in some non-photosynthetic bacteria. SIMILARITY: Belongs to the cytochrome c family.


FUNCTION: Heterodimer: postsynaptic neurotoxin. FUNCTION: Monomer: snake venom phospholipase A2 (PLA2) that shows hemolytic activity and inhibition of platelet aggregation. The hemolytic activity occurs only in presence of fatty acids (unsaturated fatty acids facilitate induce a strong hemolytic activity, whereas saturated fatty acids induce a slight activity). The inhibition of platelet aggregation is almost maximal when aggregation is induced by collagen, and arachidonic acid, whereas it is only of 30% when the aggregation is induced by ADP. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. D49 sub-subfamily.


FUNCTION: Probably mediates the hydrolysis of some nucleoside diphosphate derivatives. SIMILARITY: Belongs to the Nudix hydrolase family.


FUNCTION: The B regulatory subunit may modulate substrate selectivity and catalytic activity, and may also direct the localization of the catalytic enzyme to a particular subcellular compartment. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 family.


FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by PDX2. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme- catalyzed isomerization of RBP and G3P, respectively. Also plays an indirect role in resistance to singlet oxygen-generating photosensitizers. SIMILARITY: Belongs to the PdxS/SNZ family.


SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP (TC 1.C.40) family.


FUNCTION: Involved in the assembly of a N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins. Probably mediates or contributes to the translocation of the dolichol-phosphate-mannose across the membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the AglR/Agl15 family.


FUNCTION: Mainly functions as an acyl-CoA ligase catalyzing the ATP- dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates (PubMed:15469937, PubMed:15699031). Can mediate the levels of long-chain fatty acids (LCFA) in the cell by facilitating their transport across membranes (PubMed:15699031). SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.


FUNCTION: Required for the efficient initiation of filament assembly. FUNCTION: Required for the efficient initiation of filament assembly. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FlgN family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family.


FUNCTION: The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SHG1 family.


FUNCTION: Required in the presynaptic motoneuron to down-regulate the levels of wnd and restrain synaptic terminal growth at the neuromuscular junction (NMJ). SUBCELLULAR LOCATION: Synapse. SIMILARITY: Belongs to the FBXO45/Fsn family.


FUNCTION: Probable secreted effector that may act as a pathogen- associated molecular pattern (PAMP) recognized by the plant immune system (PubMed:32117400). Seems not to induce necrosis, neither in several susceptible or resistant Vitis species nor in the dicot model plant Nicotiana benthamiana (PubMed:32117400, PubMed:35152834). SUBCELLULAR LOCATION: Secreted Host cytoplasm. SIMILARITY: Belongs to the Necrosis inducing protein (NPP1) family.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eS27 family.


FUNCTION: [Isoform 1]: Plays a role in protecting cells against TNF- alpha-induced apoptosis by preventing the recruitment of FADD and caspase 8 to the apoptotic complex I, composed of TRADD, TRAF2 and RIPK1/RIP. FUNCTION: Involved in gene transcription regulation (PubMed:28106301, PubMed:21730289). Acts in concert with the corepressor URI1 to regulate androgen receptor AR-mediated transcription (PubMed:11854421, PubMed:21730289). Together with URI1, associates with chromatin to the NKX3-1 promoter region (PubMed:21730289). Negatively regulates the transcriptional activity of the estrogen receptor ESR1 by inducing its translocation into the cytoplasm (PubMed:28106301). May act as nuclear chaperone that facilitates the formation of the NF-kappa-B enhanceosome and thus positively regulates NF-kappa-B transcription activity (PubMed:17620405, PubMed:21307340). Potential component of mitochondrial-associated LRPPRC, a multidomain organizer that potentially integrates mitochondria and the microtubular cytoskeleton with chromosome remodeling (PubMed:17554592). Increasing concentrations of UXT contributes to progressive aggregation of mitochondria and cell death potentially through its association with LRPPRC (PubMed:17554592). Suppresses cell transformation and it might mediate this function by interaction and inhibition of the biological activity of cell proliferation and survival stimulatory factors like MECOM (PubMed:17635584). SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle pole Note=Predominantly localizes to the nucleus (PubMed:16221885). Localizes to spindle pole during mitosis (PubMed:16221885). SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. SIMILARITY: Belongs to the UXT family.


FUNCTION: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the peptidase M10A family.


FUNCTION: Transcription factor that may coregulate the expression of the gene cluster that mediates the biosynthesis of the lipopeptide antibiotics leucinostatins that show extensive biological activities, including antimalarial, antiviral, antibacterial, antifungal, and antitumor activities, as well as phytotoxic. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Ribosome-binding protein involved in ribosome hibernation, a process during which ribosomes are stabilized in an inactive state and preserved from proteasomal degradation (By similarity). Acts via its association with eiF5a (EIF5A and EIF5A2) at the polypeptide exit tunnel of the ribosome, preventing mRNA translation (By similarity). Involved in ribosome hibernation in the mature oocyte by preventing mRNA translation, leading to ribosome inactivation (By similarity). Ribosomes, which are produced in large quantities during oogenesis, are stored and translationally repressed in the oocyte and early embryo (By similarity). Also acts as a negative regulator of autophagy (PubMed:20537536). Involved in mediating interferon-gamma-induced cell death (PubMed:7828849). SIMILARITY: Belongs to the DAP-DAPL1 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 100 family.


FUNCTION: Essential tubulin-folding protein involved in the final step of the tubulin folding pathway. Required for continuous microtubule cytoskeleton organization, mitotic division, cytokinesis, and to couple cell cycle progression to cell division in embryos and endosperms. Not essential for cell viability. Binds probably to the multimeric supercomplex, stimulating GTP hydrolysis by the bound beta-tubulin and the release of the alpha-/beta-tubulin heterodimer. SUBCELLULAR LOCATION: Cytoplasm Note=Not associated with microtubular arrays. SIMILARITY: Belongs to the TBCC family.


FUNCTION: Acts upon elastin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.


FUNCTION: Positively regulates the expression of about fifteen genes involved in acid resistance such as gadA, gadB and gadC. Depending on the conditions (growth phase and medium), can repress gadW (By similarity). Negatively regulates perA expression in acidic conditions and positively regulates it in alkaline conditions.


SIMILARITY: Belongs to the universal ribosomal protein uL13 family.


FUNCTION: Involved in the regulation of cell adhesion and cytoskeleton organization. Component of an integrin containing attachment complex, which is required for muscle development and maintenance (PubMed:22253611). During embryonic development, required to recruit cpna-1, unc-89 and myofilaments to newly forming integrin attachments composed of integrins pat-2/pat-3, pat-4 and unc-112 (PubMed:12781130, PubMed:23283987). Also required to reposition the integrin-based attachments so that they form the highly ordered array of dense body and M-line attachments that are characteristic of mature muscle cells (PubMed:12781130, PubMed:23283987). During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles (PubMed:16495308). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, myofibril, sarcomere, M line Perikaryon Cell projection, axon Note=Colocalizes with integrins and pat- 4/ILK (PubMed:12781130). Colocalizes to M line and dense bodies with cpna-1 (PubMed:23283987). SIMILARITY: Belongs to the parvin family.


FUNCTION: Probably a ribosomal protein or a ribosome-associated protein. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the chloroplast-specific ribosomal protein cS23 family.


FUNCTION: Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-6 superfamily.


FUNCTION: Binds GTP but lacks intrinsic GTPase activity and is resistant to Rho-specific GTPase-activating proteins. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the small GTPase superfamily. Rho family.


FUNCTION: Reductase; part of the gene cluster that mediates the biosynthesis of pyranterreones, a family of antioxidative compounds (PubMed:32077283). The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase pytA that condenses 4 malonyl-CoA units ato the acetyl starter unit by the modular PKS of pytA (PubMed:32077283). The acyl chain is then connected to an L-serine through the amide bond by the modular NRPS of pytA (PubMed:32077283). A tetramic acid is formed and released from the PKS-NRPS pytA to give pyranterreone 5 with the help of the thioesterase pytI (PubMed:32077283). Pyranterreone 5 could be methylated by pytC to afford pyranterreone 6 (Probable). Both pyranterreones 5 and 6 are subsequently oxidized by the FAD-linked oxidoreductase pytB and the cytochrome P450 monooxygenase pytD to form the fused gamma-pyrone core, resulting in pyranterreones 7 and 11, respectively (PubMed:32077283). The hydroxy group at C-8 of pyranterreones 7 and 11 are dehydrated by the aspartyl protease pytH to form a delta-7 double bond to give pyranterreones 3 and 1, 2 accordingly (PubMed:32077283). The exo- methylene of pyranterreone 3 could be reduced into a pendant methyl by reductase pytE to provide pyranterreone 4, also known as cordylactam (Probable). Pyranterreone 4 can be reconverted to pyranterreone 3 through pytB-catalyzed dehydrogenation or further oxidized to pyranterreones 9 and 10 (Probable). SIMILARITY: Belongs to the avfA family.


FUNCTION: Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the WD repeat BOP1/ERB1 family.


FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi. SUBCELLULAR LOCATION: Golgi apparatus membrane Endoplasmic reticulum. SIMILARITY: Belongs to the TRAPP small subunits family. TRAPPC4 subfamily.


FUNCTION: Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (PubMed:24561204). Can also demethylate N(6)-methyladenosine in single-stranded DNA (in vitro) (By similarity). Requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:24561204). SUBCELLULAR LOCATION: Nucleus speckle. SIMILARITY: Belongs to the alkB family.


FUNCTION: Transcription factor playing an important role in primary neurulation and in epithelial development. Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' acting as an activator and repressor on distinct target genes. SUBCELLULAR LOCATION: Nucleus Membrane Note=detected at cell-cell contact areas. SIMILARITY: Belongs to the grh/CP2 family. Grainyhead subfamily.


SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase family.


SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family.


SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane protein. Note=Associated with membranes of intracellular organelles. SIMILARITY: To T.californica electromotor neuron-associated protein 2.


FUNCTION: Suppresses the RNA silencing-based antiviral response in Drosophila cells. SUBCELLULAR LOCATION: Host cytoplasm Host nucleus.


FUNCTION: Involved in pre-mRNA splicing and spliceosome disassembly. Promotes release of excised lariat intron from the spliceosome by acting as a receptor for PRP43. This targeting of PRP43 leads to disassembly of the spliceosome with the separation of the U2, U5, U6 snRNPs and the NTC complex. SUBCELLULAR LOCATION: Cytoplasm Nucleus.


FUNCTION: Plays a role in T lymphocyte development and the optimal generation of CD4/CD8 double-positive thymocytes (By similarity). Inhibitor of GSK3A, possibly by sequestering GSK3A in cytoplasmic vesicles and impairing its translocation to the nucleus. Consequently, impairs GSK3A-dependent transcriptional program and regulation of the DNA damage response occurring during T cells proliferation (PubMed:29382851). Required for the survival of peripheral T cells, natural killer (NK) and NK T-cell development and the maintenance of normal liver function (By similarity). May promote the survival of mature T lymphocytes upon cytokine withdrawal (By similarity). May regulate Ca(2+) homeostasis by modulating lysosomal Ca(2+) stores, preventing its accumulation in the absence of T cell activation (By similarity). May play a role in mitochondrial DNA segregation in hematopoietic tissues (By similarity). Is a regulator of liver endothelial cell homeostasis (By similarity). SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type IV membrane protein Endosome, multivesicular body membrane; Single-pass type IV membrane protein Endosome membrane; Single-pass type IV membrane protein Note=The mitochondrial localization originally reported was observed with C-terminally tagged protein and was not confirmed in later publications. SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family. IAN subfamily.


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. DHA1 family. MdtH (TC 2.A.1.2.21) subfamily.


FUNCTION: Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2 (By similarity). Hydrolyzes lysyl-AMP (AMP-N-epsilon-(N-alpha- acetyl lysine methyl ester)) generated by lysine tRNA ligase (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the HINT family.


FUNCTION: DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. SUBCELLULAR LOCATION: Cytoplasm, nucleoid.


FUNCTION: Morphogenic protein required for the assembly of the outer coat of the endospore. Is also a regulatory protein for the expression of cotA, cotB, cotC, cotH and other genes encoding spore outer coat proteins. SUBCELLULAR LOCATION: Spore coat Note=Localizes between the two coat layers in the mature spore. SIMILARITY: Belongs to the CotE family.


FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate in the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the ELO family. ELOVL7 subfamily.


FUNCTION: Required for the assembly of mature ribosomes and ribosome biogenesis. Together with EFL1, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Required for normal levels of protein synthesis. May play a role in cellular stress resistance. May play a role in cellular response to DNA damage. May play a role in cell proliferation (By similarity). FUNCTION: Required for the assembly of mature ribosomes and ribosome biogenesis. Together with EFL1, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Required for normal levels of protein synthesis. May play a role in cellular stress resistance. May play a role in cellular response to DNA damage. May play a role in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus Nucleus, nucleoplasm Cytoplasm, cytoskeleton, spindle Note=Primarily detected in the cytoplasm, and at low levels in nucleus. Detected in the nucleolus during G1 and G2 phase of the cell cycle, and diffusely distributed in the nucleus during S phase. Detected at the mitotic spindle. Colocalizes with the microtubule organizing center during interphase (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Nucleus, nucleoplasm. Cytoplasm, cytoskeleton, spindle. Note=Primarily detected in the cytoplasm, and at low levels in nucleus and nucleolus (PubMed:19602484, PubMed:17475909). Detected in the nucleolus during G1 and G2 phase of the cell cycle, and diffusely distributed in the nucleus during S phase. Detected at the mitotic spindle. Colocalizes with the microtubule organizing center during interphase (PubMed:19759903). SIMILARITY: Belongs to the SDO1/SBDS family.


FUNCTION: Lysosomal integral membrane protein that may regulate MTORC1 complex translocation to lysosomes. SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GPR137 family.


SUBCELLULAR LOCATION: Mitochondrion Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bS16 family.


FUNCTION: Functions as transcription repressor.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ribonuclease N1/T1 family.


FUNCTION: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates (By similarity). Has a palmitoyltransferase activity toward NCDN and regulates NCDN association with endosome membranes through this palmitoylation. FUNCTION: Has also a palmitoyltransferase activity-independent function in DNA virus-triggered and CGAS-mediated innate immune response (PubMed:25299331). Functions as an activator of STING1 by promoting its cGAMP-induced oligomerization and the recruitment of downstream signaling components (PubMed:25299331). SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Golgi apparatus. SIMILARITY: Belongs to the DHHC palmitoyltransferase family.


FUNCTION: May function in the secretion of milk-fat droplets. May act as a specific membrane-associated receptor for the association of cytoplasmic droplets with the apical plasma membrane (By similarity). Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Secreted. SIMILARITY: Belongs to the immunoglobulin superfamily. BTN/MOG family.


SIMILARITY: Belongs to the PQQ oxidoreductase GdhB family.


FUNCTION: May be involved in the transport of nicotianamine-chelated metals. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the YSL (TC 2.A.67.2) family.


FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:28351989, PubMed:32786047). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:28351989, PubMed:32786047). It probably triggers the ubiquitin- mediated degradation of different substrates (PubMed:28351989, PubMed:32786047). Mediates the proteasomal-dependent degradation of ATG6, a component of the autophagosome complex (PubMed:28351989). Requires TRAF1A/MUSE14 and TRAF1B/MUSE13 to target ATG6 for ubiquitination and subsequent regulation of autophagosome assembly (PubMed:28351989). Modulates directly the ubiquitination and proteasomal-dependent degradation of FREE1, a component of the ESCRT-I complex (PubMed:32786047, PubMed:32753431). Modulates directly the ubiquitination and proteasomal-dependent degradation of ELC/VPS23A, a component of the ESCRT-I complex (PubMed:32753431). SUBCELLULAR LOCATION: Endosome, multivesicular body Cytoplasmic vesicle, autophagosome. SIMILARITY: Belongs to the SINA (Seven in absentia) family.


FUNCTION: Integrase is necessary for integration of the phage into the host genome by site-specific recombination. In conjunction with excisionase, integrase is also necessary for excision of the prophage from the host genome. SIMILARITY: Belongs to the 'phage' integrase family.


FUNCTION: Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR- mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of host BAD. FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network- associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase- ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impair the membrane fusion event necessary for subsequent virion penetration. FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. FUNCTION: Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T- lymphocytes into apoptosis. SUBCELLULAR LOCATION: Host cell membrane; Lipid-anchor; Cytoplasmic side Virion Secreted Host Golgi apparatus membrane Note=TGN localization requires PACS1. Associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved. SIMILARITY: Belongs to the lentivirus primate group Nef protein family.


FUNCTION: Essential for elastic fiber formation, is involved in the assembly of continuous elastin (ELN) polymer and promotes the interaction of microfibrils and ELN (By similarity). Stabilizes and organizes elastic fibers in the skin, lung and vasculature. Promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. Vascular ligand for integrin receptors which may play a role in vascular development and remodeling (PubMed:11805835). May act as an adapter that mediates the interaction between FBN1 and ELN (By similarity). SUBCELLULAR LOCATION: Secreted Secreted, extracellular space, extracellular matrix Note=co-localizes with ELN in elastic fibers. SIMILARITY: Belongs to the fibulin family.


FUNCTION: Required for proper 34S pre-rRNA processing and 60S ribosome subunit assembly. FUNCTION: Required for proper 34S pre-rRNA processing and 60S ribosome subunit assembly. SUBCELLULAR LOCATION: Nucleus, nucleolus. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the NIP7 family.


FUNCTION: Receptor for alpha-ketoglutarate. Seems to act exclusively through a G(q)-mediated pathway. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and specificity for either ATP or GTP is provided by different beta subunits. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit family.


FUNCTION: Transcription factor that binds to sequence with multiple copies of 5'-TTC[CG]G-3' present in its own promoter and that of the HNRPA2B1 gene. Down-regulates transcription of these genes. Binds to the retinoic acid response element (RARE) 5'-AGGGTTCACCGAAAGTTCA-3'. Activates the proenkephalin gene independently of promoter binding, probably through protein-protein interaction. Regulates epithelial cell proliferation and side-branching in the mammary gland. Required for neural tube closure and skeletal patterning. Controls the expression of peripheral tissue antigens in pancreatic lymph nodes. Transcriptional activator of EIF4G3. May also involved in behavior (By similarity). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Catalyzes the synthesis of GDP-perosamine from GDP-4-keto-6- deoxy-D-mannose and L-glutamate. Can use only L-glutamate as amino donor. In vitro, can also use GDP-4-keto-3,6-dideoxymannose to produce GDP-3-deoxyperosamine. Involved in the formation of S-LPS, which is required for attachment of the protein S-layer to the outer membrane surface. SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.


FUNCTION: Catalyzes the cleavage of the N-acyl linkage of the ceramides (Cers) to yield sphingosine (Sph) and free fatty acid. Also catalyzes the synthesis of Cers from Sph and fatty acid. Cers containning C6-C24 fatty acids are well hydrolyzed, and Cers with mono unsaturated fatty acids are much more hydrolyzed than those with saturated fatty acids. SIMILARITY: Belongs to the neutral ceramidase family.


FUNCTION: May have hydrolase activity. SIMILARITY: Belongs to the FAH family.


FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b560 family.


FUNCTION: Is a positive regulator of ciliogenesis, playing a crucial role in the initial steps of axoneme extension. It acts as a substrate- adapter for CUL3-RING ubiquitin ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of TCHP, a protein involved in ciliogenesis down-regulation (PubMed:25270598). May be involved in endoplasmic reticulum calcium ion homeostasis (PubMed:25983243). SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Lectin-like receptor for natural killer (NK) cells. Heterodimer formation with KLRE1 mediates NK cell cytolytic activity. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein.


FUNCTION: Stimulates membrane curvature formation and subsequent endoplasmic reticulum exit site (ERES) establishment by recruiting PI3K complex I, leading to COPII vesicle-mediated transport (By similarity). Promotes endoplasmic reticulum (ER) exit of cGAMP-activated STING1 oligomers (PubMed:32690950). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Detected in the nucleus and cell soma of pyramidal neurons in the brain cortex and Purkinje cells, as well as in neurons in the granular layer in the cerebellum. SIMILARITY: Belongs to the STEEP1 family.


FUNCTION: Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, LST8 interacts directly with MTOR and enhances its kinase activity. In nutrient-poor conditions, stabilizes the MTOR-RPTOR interaction and favors RPTOR- mediated inhibition of MTOR activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser- 657' (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the WD repeat LST8 family.


SIMILARITY: Belongs to the coronaviruses ns2a protein family.


FUNCTION: Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CobD/CbiB family.


FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL29 family.


FUNCTION: Transcriptional repressor which functions as a downstream effector of Notch signaling in cardiovascular development. Specifically required for the Notch-induced endocardial epithelial to mesenchymal transition, which is itself criticial for cardiac valve and septum development. May be required in conjunction with HEY1 to specify arterial cell fate or identity. Promotes maintenance of neuronal precursor cells and glial versus neuronal fate specification. Binds preferentially to the canonical E box sequence 5'-CACGTG-3'. Represses transcription by the cardiac transcriptional activators GATA4 and GATA6 and by the neuronal bHLH factors ASCL1/MASH1 and NEUROD4/MATH3. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HEY family.


FUNCTION: Activates the tRNA-splicing ligase complex by facilitating the enzymatic turnover of catalytic subunit RtcB. Acts by promoting the guanylylation of RtcB, a key intermediate step in tRNA ligation. Can also alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently (By similarity). SIMILARITY: Belongs to the archease family.


FUNCTION: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking. SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Multi-pass membrane protein Cytoplasmic vesicle membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATG9 family.


FUNCTION: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post- translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. CRY1 and CRY2 have redundant functions but also differential and selective contributions at least in defining the pace of the SCN circadian clock and its circadian transcriptional outputs. More potent transcriptional repressor in cerebellum and liver than CRY2, though more effective in lengthening the period of the SCN oscillator. On its side, CRY2 seems to play a critical role in tuning SCN circadian period by opposing the action of CRY1. With CRY2, is dispensable for circadian rhythm generation but necessary for the development of intercellular networks for rhythm synchrony. Capable of translocating circadian clock core proteins such as PER proteins to the nucleus. Interacts with CLOCK-BMAL1 independently of PER proteins and is found at CLOCK-BMAL1-bound sites, suggesting that CRY may act as a molecular gatekeeper to maintain CLOCK-BMAL1 in a poised and repressed state until the proper time for transcriptional activation. Represses the CLOCK-BMAL1 induced transcription of BHLHE40/DEC1. Represses the CLOCK-BMAL1 induced transcription of ATF4, MTA1, KLF10 and NAMPT (By similarity). May repress circadian target genes expression in collaboration with HDAC1 and HDAC2 through histone deacetylation. Mediates the clock-control activation of ATR and modulates ATR-mediated DNA damage checkpoint. In liver, mediates circadian regulation of cAMP signaling and gluconeogenesis by binding to membrane-coupled G proteins and blocking glucagon-mediated increases in intracellular cAMP concentrations and CREB1 phosphorylation. Inhibits hepatic gluconeogenesis by decreasing nuclear FOXO1 levels that down-regulates gluconeogenic gene expression (By similarity). Besides its role in the maintenance of the circadian clock, is also involved in the regulation of other processes. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by binding to glucocorticoid response elements (GREs). Plays a key role in glucose and lipid metabolism modulation, in part, through the transcriptional regulation of genes involved in these pathways, such as LEP or ACSL4 (By similarity). Represses PPARD and its target genes in the skeletal muscle and limits exercise capacity (By similarity). Plays an essential role in the generation of circadian rhythms in the retina (By similarity). Represses the transcriptional activity of NR1I2 (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus Note=Translocated to the nucleus through interaction with other clock proteins such as PER2 or BMAL1. SIMILARITY: Belongs to the DNA photolyase class-1 family.


SIMILARITY: Belongs to the GDAP2 family.


FUNCTION: N-acetylglucosaminyltransferase involved in the Golgi- specific modification of N-linked glycans. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein Vacuole membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the GNT1 family.


SIMILARITY: Belongs to the chlamydial CPn_0512/CT_425/TC_0708 family.


FUNCTION: Key enzyme in triglyceride metabolism (PubMed:9188470, PubMed:16179346, PubMed:10727238). Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:9188470, PubMed:16179346, PubMed:10727238). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (By similarity). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (By similarity). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:9188470). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Extracellular side Secreted Secreted, extracellular space, extracellular matrix Note=Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells (PubMed:9188470). Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles (PubMed:9555944). SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.


FUNCTION: Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. It is crucial for expression of a set of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons (By similarity). May confer liver- specific regulation of delayed-early genes induced later in the G1 phase of regeneration along with HMR. SUBCELLULAR LOCATION: Cytoplasm Nucleus. Note=Mostly nuclear; oxidative stress promotes cytoplasmic localization. SIMILARITY: Belongs to the nuclear hormone receptor family. NR4 subfamily.


FUNCTION: The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes. While the SecYEG complex is essential for assembly of a number of proteins and complexes, the SecDF-YajC-YidC subcomplex facilitates these functions. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the YajC family.


FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2). SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.


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


FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non- coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. RNA polymerase complexes are composed of mobile elements that move relative to each other. In Pol II, RPB5 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. Seems to be the major component in this process. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase subunit family.


FUNCTION: Plays a critical role in cytoplasmic virus egress. Participates in the final step of tegumentation and envelope acquisition within the host cytoplasm by directly interacting with the capsid. Upon virion binding to target cell, a signaling cascade is triggered to disrupt the interaction with the capsid, thereby preparing capsid uncoating. SUBCELLULAR LOCATION: Virion tegument Host cytoplasm Host nucleus Note=Localizes in the host nucleus up to 18 hours postinfection, but at later times localizes to punctate, cytoplasmic structures. SIMILARITY: Belongs to the herpesviridae cytoplasmic envelopment protein 2 family.


FUNCTION: ATP-dependent zinc metalloprotease. Plays a role in the formation and regulation of the mitochondrial permeability transition pore (mPTP) and its proteolytic activity is dispensable for this function (PubMed:26387735). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the AAA ATPase family. SIMILARITY: In the C-terminal section; belongs to the peptidase M41 family.


FUNCTION: Colony queen number, a major feature of social organization, is associated with worker genotype for Gp-9. Colonies are headed by either a single reproductive queen (monogyne form) or multiple queens (polygyne form). Differences in worker Gp-9 genotypes between social forms may cause differences in workers' abilities to recognize queens and regulate their numbers (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the PBP/GOBP family.


FUNCTION: Amino-acid racemase that catalyzes the interconversion of L- lysine and D-lysine. To a lesser extent, is also able to interconvert arginine enantiomers (Ref.1, PubMed:23118975). Cannot use methionine, asparagine, alanine, leucine, glutamine, phenylalanine and histidine as substrates (Ref.1). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Periplasmic side Periplasm. SIMILARITY: Belongs to the alanine racemase family. Bsr subfamily.


FUNCTION: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein; Periplasmic side. SIMILARITY: Belongs to the CcmE/CycJ family.


FUNCTION: Involved in melatonin biosynthesis (PubMed:29901843). Can function as acetylserotonin O-methyltransferase (PubMed:29901843). Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine) (PubMed:29901843). Involved in the regulation of jasmonate- and brassinosteroid-mediated plant growth and defense responses (PubMed:26864209). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.


FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of isofumigaclavines, fungal ergot alkaloids (PubMed:28620689). The tryptophan dimethylallyltransferase ifgA catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4- dimethylallyl-L-tryptophan (PubMed:28620689). The second step is catalyzed by the methyltransferase ifgB that methylates 4- dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of N-methyl-dimethylallyl-L-tryptophan (PubMed:28620689). The catalase ifgD and the FAD-dependent oxidoreductase ifgC then transform N-methyl-dimethylallyl-L-tryptophan to chanoclavine-I which is further oxidized by ifgE in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:28902217). The chanoclavine-I aldehyde reductases ifgG and/or fgaOx3 reduce chanoclavine-I aldehyde to dihydrochanoclavine-I aldehyde that spontaneously dehydrates to form 6,8-dimethyl-6,7- didehydroergoline (PubMed:28620689, PubMed:28902217). The festuclavine dehydrogenases ifgF1 and/or ifgF2 then catalyze the reduction of 6,8- dimethyl-6,7-didehydroergoline to form festuclavine (PubMed:28620689). Hydrolysis of festuclavine by a yet undetermined cytochrome P450 monooxygenase (called ifgH) then leads to the formation of isofumigaclavine B which is in turn acetylated by ifgI to isofumigaclavine A (PubMed:28620689). Penicillium roqueforti has interestingly at least two sets of genes for the consumption of chanoclavine-I aldehyde on three different loci, the OYEs ifgG/fgaOx3 and the festuclavine synthase homologs ifgF1/ifgF2 (PubMed:28620689, PubMed:28902217). The reason for the duplication of these genes is unclear, probably to ensure the conversion of chanoclavine-I aldehyde by differential gene expression under various environmental conditions (PubMed:28902217). SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family.


FUNCTION: Glutathione S-transferase-like protein; part of the gene cluster that mediates the biosynthesis of the mycotoxin fusarin C (PubMed:23932525). Within the cluster, FUS1, FUS2, FUS8 and FUS9 are sufficient for fusarin production (PubMed:23932525). The other FUS cluster members are not essential for fusarin C biosynthesis (PubMed:23932525). SIMILARITY: Belongs to the GST superfamily.


FUNCTION: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the sirtuin family. Class III subfamily.


FUNCTION: Component of the large ribosomal subunit (PubMed:36517592). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:36517592). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm Endoplasmic reticulum Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). SIMILARITY: Belongs to the eukaryotic ribosomal protein eL34 family.


FUNCTION: May act as an organizer for the correct association of several proteins in the surrounding of the head-tail connector protein gp8.


FUNCTION: Potentially involved in T-cell development. Recombinant protein shows chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritics cells but is inactive on peripheral blood lymphocytes and neutrophils. Binds to CCR9. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4 (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.


FUNCTION: Extracellular zinc metalloprotease. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase M4 family.


FUNCTION: Major component of the acid-resistance (AR) system allowing enteric pathogens to survive the acidic environment in the stomach. Exchanges extracellular arginine for its intracellular decarboxylation product agmatine (Agm) thereby expelling intracellular protons. Probably undergoes several conformational states in order to translocate the substrate across the membrane; keeps the substrate accessible to only 1 side of the membrane at a time by opening and closing 3 membrane-internal gates. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. Basic amino acid/polyamine antiporter (APA) (TC 2.A.3.2) family.


FUNCTION: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of the bibenzoquinone oosporein, a metabolite required for fungal virulence that acts by evading host immunity to facilitate fungal multiplication in insects (PubMed:26305932). The non-reducing polyketide synthase OpS1 produces orsellinic acid by condensing acetyl- CoA with 3 malonyl-CoA units (PubMed:26305932). Orsellinic acid is then hydroxylated to benzenetriol by the hydroxylase OpS4 (PubMed:26305932). The intermediate is oxidized either nonenzymatically to 5,5'-dideoxy- oosporein or enzymatically to benzenetetrol by the oxidoreductase OpS7 (PubMed:26305932). The latter is further dimerized to oosporein by the catalase OpS5 (PubMed:26305932). OpS6 probably functions en route for protecting cells against oxidative stress by scavenging any leaked free radical form of benzenetetrol by activating the thiol group of glutathione (PubMed:26305932). SIMILARITY: Belongs to the multicopper oxidase family.


FUNCTION: Part of the ABC transporter complex NikABCDE involved in nickel import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Nickel importer (TC 3.A.1.5.3) family.


FUNCTION: Acts as a negative regulator of autophagy. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the PHF23 family.


FUNCTION: Catalyzes the oxidation of methanol to yield formaldehyde. While the in vivo electron acceptor is not known, N,N-dimethyl-4- nitrosoaniline (NDMA) can serve this function in vitro and is reduced to 4-(hydroxylamino)-N,N-dimethylaniline. It can also use various other primary alcohols, polyols and formaldehyde. In addition, MNO is able to produce methylformate from methanol plus formaldehyde, and possesses a formaldehyde dismutase and a NADH-dependent formaldehyde reductase activity. SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase family.


FUNCTION: E3 UFM1-protein ligase that mediates ufmylation of target proteins. SIMILARITY: Belongs to the UFL1 family.


FUNCTION: Transcriptional repressor that binds to the consensus sequence 5'-CGGACGTT-3' and to the RB1 promoter. Transcriptional activator that promotes histone H4 gene transcription at the G1/S phase transition in conjunction with NPAT. Also activates transcription of the ATM and PRKDC genes. Autoregulates its expression by associating with its own promoter (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Associated with discrete nuclear foci.


FUNCTION: The central subunit of the protein translocation channel SecYE. Consists of two halves. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SecY/SEC61-alpha family.


FUNCTION: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX24/MAK5 subfamily.


FUNCTION: Can convert prostaglandin E2 to prostaglandin F2-alpha. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldo/keto reductase family.


FUNCTION: Vacuolar cation/proton exchanger (CAX). Translocates Ca(2+) and other metal ions into vacuoles using the proton gradient formed by H(+)-ATPase and H(+)-pyrophosphatase (By similarity). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Note=Tonoplast. SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. Cation/proton exchanger (CAX) subfamily.


FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL42 family.


FUNCTION: May bind amino acids. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Involved in DNA damage response and double-strand break (DSB) repair. Component of the BRCA1-A complex, acting as a central scaffold protein that assembles the various components of the complex and mediates the recruitment of BRCA1. The BRCA1-A complex specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at DSBs. This complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. SUBCELLULAR LOCATION: Nucleus Note=Localizes at sites of DNA damage at double-strand breaks (DSBs). SIMILARITY: Belongs to the FAM175 family. Abraxas subfamily.


FUNCTION: This protein binds tightly to and inhibits papain and cathepsin B. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cystatin family.


FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol (PubMed:16154994, PubMed:16647063, PubMed:9020103, PubMed:32433614, PubMed:32433613, PubMed:32944968). Plays a role in lipoprotein assembly and dietary cholesterol absorption (PubMed:16154994, PubMed:9020103). Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) preferentially as susbstrate: shows a higher activity towards an acyl-CoA substrate with a double bond at the delta-9 position (9Z) than towards saturated acyl-CoA or an unsaturated acyl-CoA with a double bond at the delta-7 (7Z) or delta-11 (11Z) positions (PubMed:11294643, PubMed:32433614). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.


FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to an N-unsubstituted glucosamine linked to a 2-O-sulfo iduronic acid unit on heparan sulfate. Catalyzes the O-sulfation of glucosamine in IdoUA2S-GlcNS and also in IdoUA2S-GlcNH2. Unlike HS3ST1/3-OST-1, does not convert non- anticoagulant heparan sulfate to anticoagulant heparan sulfate (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 1 family.


FUNCTION: Thiol protease important for the overall degradation of proteins in lysosomes (By similarity). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter (PubMed:12869695). In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells. Also mediates invariant chain processing in cortical thymic epithelial cells. Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation (By similarity). Secreted form generates endostatin from COL18A1 (By similarity). Critical for cardiac morphology and function. Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation (By similarity). Required for maximal stimulation of steroidogenesis by TIMP1 (By similarity). SUBCELLULAR LOCATION: Lysosome Apical cell membrane; Peripheral membrane protein; Extracellular side Cytoplasmic vesicle, secretory vesicle, chromaffin granule Secreted, extracellular space Secreted Note=Localizes to the apical membrane of thyroid epithelial cells. Released at extracellular space by activated dendritic cells and macrophages. SIMILARITY: Belongs to the peptidase C1 family.


FUNCTION: Antimicrobial peptide. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Long chain multifunctional peptide (group 2) family.


FUNCTION: Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal. Involved in the regulation of lymphangiogenesis. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Pasteurella leukotoxins are exotoxins that attack host leukocytes and especially polymorphonuclear cells, by causing cell rupture. The leukotoxin binds to the host LFA-1 integrin and induces a signaling cascade leading to many biological effects, including tyrosine phosphorylation of the CD18 tail, elevation of the intracellular Ca(2+) and lysis of the host cell (By similarity). This leukotoxin is a major contributor to the pathogenesis of lung injury in ovine pneumonic pasteurellosis. It has also weak hemolytic activity. FUNCTION: Pasteurella leukotoxins are exotoxins that attack host leukocytes and especially polymorphonuclear cells, by causing cell rupture. The leukotoxin binds to the host LFA-1 integrin and induces a signaling cascade leading to many biological effects, including tyrosine phosphorylation of the CD18 tail, elevation of the intracellular Ca(2+) and lysis of the host cell (By similarity). This leukotoxin is a major contributor to the pathogenesis of lung injury in bovine pneumonic pasteurellosis. It has also weak hemolytic activity. SUBCELLULAR LOCATION: Secreted Host cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RTX prokaryotic toxin (TC 1.C.11) family.


FUNCTION: Catalytic subunit of the tRNA-splicing ligase complex that acts by directly joining spliced tRNA halves to mature-sized tRNAs by incorporating the precursor-derived splice junction phosphate into the mature tRNA as a canonical 3',5'-phosphodiester. May act as an RNA ligase with broad substrate specificity, and may function toward other RNAs. SIMILARITY: Belongs to the RtcB family.


FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sigma-70 factor family. RpoD/SigA subfamily.


FUNCTION: Catalyzes the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA (PubMed:22332816). Generates the bulk of the acetoacetyl-CoA precursor required for the cytosol-localized, mevalonate-derived isoprenoid biosynthesis (PubMed:22332816). The generated isoprenoids are required for normal growth and development (PubMed:22332816). Essential protein during embryogenesis (PubMed:15266054). SUBCELLULAR LOCATION: Cytoplasm Peroxisome. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.


FUNCTION: Component of the PAF1 complex (PAF1C) which is involved in histone modifications such as methylation on histone H3 'Lys-4' (H3K4me3) (PubMed:20363855). Involved in regulation of flowering time. Required for the expression of the flowering repressors and FLC and MADS-box genes of the MAF family (PubMed:15472079). Involved in the control of seed dormancy and germination (PubMed:21799800). SUBCELLULAR LOCATION: Nucleus.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CutC family.


FUNCTION: Sodium-phosphate symporter which preferentially transports the monovalent form of phosphate with a stoichiometry of two sodium ions per phosphate ion (PubMed:11003594, PubMed:23968976, PubMed:26822507, PubMed:30721528). Plays a critical role in the determination of bone quality and strength by providing phosphate for bone mineralization (PubMed:30721528). Required to maintain normal cerebrospinal fluid phosphate levels (PubMed:26822507). Mediates phosphate-induced calcification of vascular smooth muscle cells (VCMCs) and can functionally compensate for loss of SLC20A1 in VCMCs (PubMed:23968976). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family.


FUNCTION: Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family.


SIMILARITY: Belongs to the universal ribosomal protein uL15 family.


FUNCTION: Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high- temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to various amine acceptors such as putrescine (1,4-diaminobutane), 1,3-diaminopropane, sym- norspermidine and spermidine. The biosynthesis of caldopentamine from norspermine has been also observed, but with a very low activity. The reaction involves a nucleophilic attack on the C-3 methylene of the propylamine moiety adjacent to the positively charged sulfur of decarboxy-AdoMet. S-adenosylmethioninamine is the only amino donor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the spermidine/spermine synthase family.


FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface (By similarity). AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules (By similarity). AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6- regulated, non-clathrin pathway. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (By similarity). The AP-2 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs (By similarity). The surface region interacting with to the Y-X-X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at Thr-156 in membrane-associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (By similarity). Plays a role in endocytosis of frizzled family members upon Wnt signaling (By similarity). SUBCELLULAR LOCATION: Cell membrane Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV. SIMILARITY: Belongs to the adaptor complexes medium subunit family.


FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate (PubMed:14715930). The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (Probable). SIMILARITY: Belongs to the PNP/UDP phosphorylase family.


FUNCTION: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP). SIMILARITY: Belongs to the ribose 1,5-bisphosphokinase family.


FUNCTION: Putative ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 03 (Tx2) family. 02 subfamily. HNTX-XV sub-subfamily.


FUNCTION: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin inhibits fetal and adult muscle-type nAChR (IC(50)=52.1 nM towards alpha-1-beta-1-gamma-delta/CHRNA1-CHRNB1-CHRNG-CHRND, and IC(50)=102.8 nM towards alpha-1-beta-1-delta-epsilon/CHRNA1-CHRNB1- CHRND-CHRNE). Shows potent activity on the synthetic AChR alpha-1-beta- 1-delta/CHRNA1-CHRNB1-CHRND (IC(50)=16.9 nM). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin A superfamily.


FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes (PubMed:11027622). May have a role in muscle signal transduction (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. PDE7 subfamily.


FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily.


FUNCTION: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ExbB/TolQ family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the globin family.


SIMILARITY: Belongs to the UPF0398 family.


FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family.


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


FUNCTION: Possesses a potent antimicrobial activity against Gram- positive and Gram-negative bacteria. Probably acts by disturbing membrane functions with its amphipathic structure (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family.