FUNCTION: Converts big endothelin-1 to endothelin-1. May also have methyltransferase activity (By similarity). May play a role in amyloid- beta processing (PubMed:12464614). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein Cytoplasmic vesicle, secretory vesicle membrane. SIMILARITY: In the C-terminal section; belongs to the peptidase M13 family. SIMILARITY: In the N-terminal section; belongs to the methyltransferase superfamily.


FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a variety of xenobiotic and endogenous compounds, including dopamine, T3 (triiodo-L-thyronine), T4 (thyroxine), flavonoids, isoflavonoids, and other phenolic compounds. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the sulfotransferase 1 family.


FUNCTION: Functions as an RNA ligase, in vitro. The ligation reaction entails three nucleotidyl transfer steps. In the first step, the RNA ligase reacts with ATP in the absence of nucleic acid to form a covalent ligase-AMP intermediate and release pyrophosphate. In step 2, the ligase-AMP binds to the nucleic acid and transfers the adenylate to the 5'-PO4 terminus to form an adenylylated intermediate. In step 3, the RNA ligase directs the attack of the 3'-OH on the 5'- phosphoanhydride linkage, resulting in a repaired 3'-5' phosphodiester and release of AMP. Exhibits selectivity for single-stranded RNA substrates and may not have nick-sealing activity on double-stranded DNA-RNA hybrids. May play a role in maintaining RNA integrity under stress conditions, for example in response to reactive oxygen species (ROS).


FUNCTION: Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pentraxin family.


FUNCTION: Essential protein. DNA ligase that seals nicks in double- stranded DNA during DNA replication, DNA recombination and DNA repair. Involved in repair of both single strand breaks (SSBs) and double strand breaks (DSBs). Required in the endosperm for embryogenesis, probably to repair DNA-breaks generated by DME. SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. SIMILARITY: Belongs to the ATP-dependent DNA ligase family.


FUNCTION: Functions as glutathione transferase (PubMed:25158856). Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate (PubMed:25158856). Mitigates neuronal oxidative stress during normal postnatal development and in response to oxidative stresses probably through GSH antioxidant defense mechanism (PubMed:25158856). May play a role in EPS8 signaling. Binds glutathione (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the LanC-like protein family.


FUNCTION: Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains. SIMILARITY: Belongs to the PKI family.


FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the complex I NDUFA5 subunit family.


FUNCTION: Methylesterase shown to have carboxylesterase activity in vitro. SIMILARITY: Belongs to the AB hydrolase superfamily. Methylesterase family.


FUNCTION: Involved in mitochondrial fission. Has a partially redundant function to MDV1 in acting as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the WD repeat MDV1/CAF4 family.


FUNCTION: Acetylxylan esterase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family. AxeA subfamily.


FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required to maintain the reduced state of SoxR. Probably transfers electron from NAD(P)H to SoxR (PubMed:12773378). FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Required to maintain the reduced state of SoxR. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NqrDE/RnfAE family.


FUNCTION: Encapsidates the genome in a ratio of 1 N per 6 ribonucleotides, protecting it from nucleases. The nucleocapsid (NC) has a helical structure with either 12.35 or 11.64 N per turn, approximately 20 nm in diameter, with a hollow central cavity approximately 5 nm in diameter. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. During replication, encapsidation by N is coupled to RNA synthesis and all replicative products are resistant to nucleases. N is released in the blood following lysis of measles infected cells, it interacts then with human FCGR2B on immune cells, inducing apoptosis and blocking inflammatory immune response. Ntail binds to a protein on human thymic epithelial cells, termed Nucleoprotein Receptor (NR), inducing growth arrest. SUBCELLULAR LOCATION: Virion Host cytoplasm. SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.


FUNCTION: Non-catalytic component of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP), which catalyzes pseudouridylation of rRNA and is required for ribosome biogenesis. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. The H/ACA snoRNP complex mediates pseudouridylation at position 93 in U2 snRNA. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the GAR1 family.


FUNCTION: Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. Note=Colocalized with FtsZ to the nascent septal site. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Note=Colocalized with FtsZ to the nascent septal site. SIMILARITY: Belongs to the EzrA family.


FUNCTION: Multifunctional nucleolar protein that terminates ribosomal gene transcription, mediates replication fork arrest and regulates RNA polymerase I transcription on chromatin. Plays a dual role in rDNA regulation, being involved in both activation and silencing of rDNA transcription. Interaction with BAZ2A/TIP5 recovers DNA-binding activity. SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Nucleus, nucleoplasm Note=May be localized to the nucleolus in an NPM1/B23-dependent manner. May be displaced from the nucleolus into the nucleoplasm in an CDKN2A/ARF-dependent manner. May shuttle back and forth from nucleoplasm to nucleolus.


FUNCTION: May regulate B-cell receptor (BCR)-induced immature and primary B-cell apoptosis. Plays a role as negative regulator of the canonical NF-kappa-B-activating branch. Controls spontaneous apoptosis through the regulation of BCL2L1 abundance. SUBCELLULAR LOCATION: Membrane raft Note=In a mouse immature B-cell line WEHI-231.


FUNCTION: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induce an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host apical cell membrane; Single-pass type I membrane protein Note=Targeted to the apical plasma membrane in epithelial polarized cells through a signal present in the transmembrane domain. Associated with glycosphingolipid- and cholesterol-enriched detergent-resistant lipid rafts. SIMILARITY: Belongs to the influenza viruses hemagglutinin family.


FUNCTION: Part of the ABC transporter complex CntABCDF (Opp1) involved in the uptake of metal in complex with the metallophore staphylopine (StP). Involved in the import of divalent metals ions such as nickel, cobalt and zinc. Probably responsible for energy coupling to the transport system (PubMed:23279021, PubMed:29581261). Plays a major role in nickel/cobalt import in zinc-depleted conditions. Contributes to virulence. Required for full urease activity in vitro (PubMed:23279021). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily.


FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Beta-3/CHRNB3 sub- subfamily.


FUNCTION: Catalyzes the hydrolysis of inorganic orthophosphate from phytate. Releases 5 of the 6 phosphate groups to yield the end product myo-inositol 2-monophosphate. Specific for phytate. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the histidine acid phosphatase family.


FUNCTION: One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. FUNCTION: One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. SIMILARITY: Belongs to the universal ribosomal protein uL24 family.


FUNCTION: May be involved in sperm maturation and/or fertilization. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.


FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. Required for UMP biosynthesis via de novo pathway. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.


FUNCTION: Sterol O-acyltransferase that catalyzes the formation of stery esters. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the membrane-bound acyltransferase family. Sterol o-acyltransferase subfamily.


FUNCTION: The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. Also has a role in transcription- coupled histone modification. Important for TATA site selection by TBP. Directly or indirectly regulates the DNA-binding properties of the TATA box-binding protein, and the relative activities of different TATA elements (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm.


SIMILARITY: Belongs to the transferase hexapeptide repeat family.


FUNCTION: Catalyzes the dehydrogenation of D-galactose by either NAD(+) or NADP(+). Oxidizes following sugars in decreasing order: D-fucose > D-galactose > L-arabinose > 2-deoxy-D-galactose >> 4-deoxy-D-galactose > 2-deoxy-2-amino-D-galactose. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Gfo/Idh/MocA family.


FUNCTION: Plays a role in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Enhances SYVN1 stability. Plays a role in LPL maturation and secretion. Required for normal differentiation of the pancreas epithelium, and for normal exocrine function and survival of pancreatic cells. May play a role in Notch signaling. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the sel-1 family.


FUNCTION: Plays a role in the inhibition of both the innate and adaptive immune responses. Possesses two N-terminal domains that bind the Fc region of IgG and two domains that form a tripartite complex with complement factors C3b and CFH. By recruiting CFH and C3b, the secreted form acts as a potent complement inhibitor of the alternative pathway-mediated lysis. SUBCELLULAR LOCATION: Secreted Cell membrane Note=Occurs both extracellularly and associated with the cytoplasmic membrane where only the domains I and II are exposed to the extracellular media. Membrane association occurs via binding to lipoteichoic acid. SIMILARITY: Belongs to the immunoglobulin-binding protein Sbi family.


FUNCTION: Required for insertion of 4Fe-4S clusters. SIMILARITY: Belongs to the HesB/IscA family.


FUNCTION: May be a tumor suppressor gene.


FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the profilin family.


FUNCTION: May be involved in thiamine metabolism. Does not possess 5- formyltetrahydrofolate cyclo-ligase activity in vitro. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the 5-formyltetrahydrofolate cyclo-ligase family.


SIMILARITY: Belongs to the papillomaviridae E5 protein family.


SIMILARITY: Belongs to the VapA/VapI family.


FUNCTION: Condenses choline with CDP-diglyceride to produce phosphatidylcholine and CMP. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I family.


FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space. SUBCELLULAR LOCATION: Cell junction, tight junction Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the claudin family.


FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains, and of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). Involved in resistance to cadmium poisoning. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Note=Anchored via the membrane protein CUE1 to the endoplasmic reticulum membrane. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.


FUNCTION: Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place. FUNCTION: Determines the virion's shape: spherical or filamentous. Clinical isolates of influenza are characterized by the presence of significant proportion of filamentous virions, whereas after multiple passage on eggs or cell culture, virions have only spherical morphology. Filamentous virions are thought to be important to infect neighboring cells, and spherical virions more suited to spread through aerosol between hosts organisms. SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein; Cytoplasmic side Host nucleus. SIMILARITY: Belongs to the influenza viruses Matrix protein M1 family.


SUBCELLULAR LOCATION: Secreted Note=Sperm surface. SIMILARITY: Belongs to the beta-microseminoprotein family.


FUNCTION: Catalyzes specifically the NADPH-dependent reduction of coenzyme A disulfide. SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide oxidoreductase family.


FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor. Is also involved in the biosynthesis of the bis-MGD form of the Moco cofactor (Mo-bisMGD) in which the metal is symmetrically ligated by the dithiolene groups of two MGD molecules. Is necessary and sufficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofactor, which implies formation and efficient insertion of the cofactor into the enzyme without the need of a chaperone. Is specific for GTP since other nucleotides such as ATP and GMP cannot be utilized. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MobA family.


FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose through a modified Entner-Doudoroff pathway. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Glucose 1-dehydrogenase subfamily.


FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. FUNCTION: Activates biotin to form biotinyl-5'-adenylate and transfers the biotin moiety to biotin-accepting proteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: In the C-terminal section; belongs to the type III pantothenate kinase family. SIMILARITY: In the N-terminal section; belongs to the biotin--protein ligase family.


FUNCTION: Mediates cleavage of dimethylsulfonioproprionate (DMSP) into dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which sulfur is transported from oceans to the atmosphere and is a key component of the ocean sulfur cycle. SIMILARITY: Belongs to the aspartate/glutamate racemases family. ALMA1 subfamily.


FUNCTION: Effector that acts as a broad suppressor of cell death to interrupt plant immunity. Inhibits cell death induced by cell death- inducing proteins, including the PAMP elicitor INF1 from P.infestans. SUBCELLULAR LOCATION: Secreted Host cytoplasm Host nucleus. SIMILARITY: Belongs to the RxLR effector family.


FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. The beta chain is a component of adult hemoglobin A and D. SIMILARITY: Belongs to the globin family.


FUNCTION: Promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the NGF-beta family.


FUNCTION: May be a cytokine that affects the growth, movement, or activation state of cells that participate in immune and inflammatory response. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.


FUNCTION: Autophagy receptor required for selective macroautophagy (aggrephagy) (PubMed:34471133, PubMed:16286508, PubMed:20168092, PubMed:24128730, PubMed:28404643, PubMed:22622177, PubMed:33509017). Functions as a bridge between polyubiquitinated cargo and autophagosomes (PubMed:34471133). Interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family (PubMed:16286508, PubMed:20168092, PubMed:24128730, PubMed:28404643, PubMed:22622177). Along with WDFY3, involved in the formation and autophagic degradation of cytoplasmic ubiquitin- containing inclusions (p62 bodies, ALIS/aggresome-like induced structures). Along with WDFY3, required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:24128730, PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). May be involved in cell differentiation, apoptosis, immune response and regulation of K(+) channels. Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). SUBCELLULAR LOCATION: Cytoplasm, cytosol Preautophagosomal structure Late endosome. Lysosome. Cytoplasmic vesicle, autophagosome. Nucleus. Endoplasmic reticulum. Nucleus, PML body Cytoplasm, myofibril, sarcomere Note=In cardiac muscle, localizes to the sarcomeric band (By similarity). Commonly found in inclusion bodies containing polyubiquitinated protein aggregates. In neurodegenerative diseases, detected in Lewy bodies in Parkinson disease, neurofibrillary tangles in Alzheimer disease, and HTT aggregates in Huntington disease. In protein aggregate diseases of the liver, found in large amounts in Mallory bodies of alcoholic and nonalcoholic steatohepatitis, hyaline bodies in hepatocellular carcinoma, and in SERPINA1 aggregates. Enriched in Rosenthal fibers of pilocytic astrocytoma. In the cytoplasm, observed in both membrane-free ubiquitin-containing protein aggregates (sequestosomes) and membrane-surrounded autophagosomes. Colocalizes with TRIM13 in the perinuclear endoplasmic reticulum. Co- localizes with TRIM5 in cytoplasmic bodies. When nuclear export is blocked by treatment with leptomycin B, accumulates in PML bodies.


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


FUNCTION: Responsible for transport of beta-galactosides into the cell, with the concomitant import of a proton (symport system). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Oligosaccharide:H(+) symporter (OHS) (TC 2.A.1.5) family.


FUNCTION: Catalyzes the desulfonation of aliphatic sulfonates. SIMILARITY: Belongs to the SsuD family.


FUNCTION: Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle Cytoplasmic vesicle, secretory vesicle membrane; Peripheral membrane protein Secreted Note=Associated with the secretory granule membrane through direct binding to lipid rafts in intragranular conditions. SIMILARITY: Belongs to the peptidase M14 family.


FUNCTION: Involved in heme degradation (PubMed:15205415, PubMed:22627893, PubMed:28481076, PubMed:28607990). Catalyzes the degradation of heme to biliverdin, with the release of iron (PubMed:22627893, PubMed:28607990). Forms biliverdin beta and delta (PubMed:28607990). Binds heme with high efficiency (PubMed:15205415, PubMed:22627893). SIMILARITY: Belongs to the heme oxygenase HugZ/HutZ family.


FUNCTION: Enhances all basic T-cell responses to a foreign antigen, namely proliferation, secretion of lymphokines, up-regulation of molecules that mediate cell-cell interaction, and effective help for antibody secretion by B-cells. Essential both for efficient interaction between T and B-cells and for normal antibody responses to T-cell dependent antigens. Does not up-regulate the production of interleukin- 2, but superinduces the synthesis of interleukin-10. Prevents the apoptosis of pre-activated T-cells. Plays a critical role in CD40- mediated class switching of immunoglobin isotypes (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.


FUNCTION: Involved in 20S proteasome assembly. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PSMG1 family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SURF1 family.


FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity). Protects spores from cellular damage caused by UV LIGHT. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.


FUNCTION: Orphan nuclear receptor and probable transcription activator, required during development (PubMed:10772806, PubMed:15314147). Plays a role in male tail tip morphogenesis regulating the expression of the transcription factor dmd-3 in a negative feedback loop (PubMed:21408209). Regulates vulval precursor cell (VPC) differentiation, in concert with homeobox protein lin-39 (PubMed:15314147). Involved in promoting embryogenesis, in concert with homeobox protein nob-1 (PubMed:15314147). May play a role in modulation of lifespan and immunity (PubMed:29748542). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family.


FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the division septum. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.


FUNCTION: Upon acetylcholine binding, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-1/CHRNA1 sub- subfamily.


FUNCTION: Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RTCB. Together with ddx1, acts by facilitating the guanylylation of RTCB, a key intermediate step in tRNA ligation (By similarity). SIMILARITY: Belongs to the archease family.


FUNCTION: May act as a lysosomal receptor (By similarity). May be involved in macropinocytosis and fluid phase exocytosis. SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane protein Note=Localizes to membranes of endolysosomal vesicles and macropinosomes. SIMILARITY: Belongs to the CD36 family.


FUNCTION: Serine/threonine protein kinase that plays a role in the regulation of gene transcription. The kinase activity is induced by various effectors including AR or MAP2K6/MAPKK6. Phosphorylates the DNA-binding domain of androgen receptor/AR and thereby inhibits AR- mediated transcription. Inhibits also ESR1-mediated transcription. May play a role in cytoskeleton regulation by interacting with IQGAP1. May protect cells from apoptosis through phosphorylation of BAD. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cotranslocates into nucleus with AR in response to androgen induction. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.


FUNCTION: Transcription activator of STM and KNAT6. Involved in molecular mechanisms regulating shoot apical meristem (SAM) formation during embryogenesis and organ separation. Required for the fusion of septa of gynoecia along the length of the ovaries. Activates the shoot formation in callus in a STM-dependent manner. Seems to act as an inhibitor of cell division. SUBCELLULAR LOCATION: Nucleus.


SIMILARITY: Belongs to the UPF0735 family.


FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of various drimane-type sesquiterpene esters, compounds that exhibit diverse biological activities and are widely present in eukaryotes (PubMed:34468074). The pathway begins with the synthesis of the backbone drimenol by the terpene cyclase drtB using farnesyl pyrophosphate (FPP) as substrate (PubMed:34468074). The cytochrome P450 monooxygenase drtD is then responsible for the hydroxylations at C-6, C-9 and C-12, as well as the oxidation of hydroxyl groups at C-6 and C-11 to a ketone and an aldehyde, respectively (PubMed:34468074). Then, the biosynthesis can go in two directions, either the hydroxylated drimenol is further hydroxylated at C-2 and C-3 by an enzyme(s) not associated with the drt cluster, or the FAD-binding oxidoreductase drtC further oxidizes C-11 or C-12 to form the butyrolactone ring (PubMed:34468074). DrtB, drtD and drtC are solely responsible for the formation of the different drimane structures observed during drimane sesquiterpenes biosynthesis (PubMed:34468074). The polyketide synthase drtA synthesizes different lengths (C6 and C8) of PKS chains, which are then oxidized to varying degrees by the short-chain dehydrogenase drtF (PubMed:34468074). Finally, these PKS chains are transferred onto drimane sesquiterpenes by the acyltransferase drtE, forming the sesquiterpene esters (PubMed:34468074). In addition to the different fatty acyl-CoA chains produced by drtA, drtE is also able to use cinnamoyl-CoA as a substrate (PubMed:34468074). SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family.


SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Histone-like protein which promotes nucleosome sliding of ATP-dependent nucleosome remodeling complexes (PubMed:10856248, PubMed:11447119). Part of the chromatin-accessibility complex (CHRAC) which uses energy/ATP to increase the general accessibility of DNA in chromatin (PubMed:10856248, PubMed:11447119). As an heterodimer with Chrac-14, binds DNA and facilitates nucleosome sliding by Acf (PubMed:16260604). As part of the CHRAC complex, required for oogenesis (PubMed:26851213). SUBCELLULAR LOCATION: Nucleus.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the bacterial ribosomal protein bL33 family.


FUNCTION: Cleaves both 3' and 5' ssDNA extremities of branched DNA structures. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NucS endonuclease family.


SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 12 subfamily.


FUNCTION: Inhibits trypsin.


FUNCTION: Catalyzes the conversion of limonene-1,2-epoxide to limonene- 1,2-diol. Can use both the (-) and (+) isomers of limonene-1,2-epoxide as substrates and also has some activity with 1-methylcyclohexene oxide, cyclohexene oxide and indene oxide as substrates. SIMILARITY: Belongs to the limonene-1,2-epoxide hydrolase family.


FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E- (2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the thioester dehydratase family. FabA subfamily.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase gamma chain family.


FUNCTION: Has a post-transcriptional repressor function in flagellum biogenesis. Associates with the 5'-UTR of fljK mRNA and promotes its degradation. SIMILARITY: Belongs to the FlbT family.


FUNCTION: O-acyltransferase; part of the gene cluster B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA (PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN (PubMed:22329759). Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD- binding monooxygenases ausB and ausC, and the dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4 (PubMed:22329759). The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide (PubMed:22329759). Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol (PubMed:22329759). Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation (PubMed:22234162, PubMed:22329759). Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O- acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional (PubMed:29076725). SIMILARITY: Belongs to the fumigaclavine B O-acetyltransferase family.


FUNCTION: Causes a slow progressive depressant flaccid paralysis, when injected into S.falculata blowfly larvae. Inhibits dose-dependently the total sodium (Nav) currents both in dorsal root ganglia neurons and in ventricular myocytes. Is toxic to mice by intravenous injection, but not by subcutaneous or intracerebroventricular injection. Produces antiarrhythmia in rat. Is then active on both mammals and insects. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family.


FUNCTION: Plays a role in ciliogenesis. SUBCELLULAR LOCATION: Cytoplasm Cell projection, cilium Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. SIMILARITY: Belongs to the HYLS1 family.


FUNCTION: Probable component of a centromeric complex involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere Note=Localizes exclusively in the centromeres. SIMILARITY: Belongs to the CENP-N/CHL4 family.


FUNCTION: Iron-sulfur protein (IP) subunit of the succinate dehydrogenase complex (mitochondrial respiratory chain complex II), responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.


FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 22 family.


FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. SUBCELLULAR LOCATION: Nucleus membrane; Peripheral membrane protein Nucleus, nuclear pore complex Note=Localizes at the nuclear basket and at or near the nuclear entry to the gated channel of the pore. SIMILARITY: Belongs to the nucleoporin interacting component (NIC) family.


FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular lipids, exerting anti-inflammatory and immunosuppressive functions (PubMed:10455175, PubMed:10681567). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines (PubMed:10455175). In draining lymph nodes, selectively hydrolyzes diacyl and alkenyl forms of phosphatidylethanolamines, releasing omega-3 polyunsaturated fatty acids (PUFAs) such as eicosapentaenoate and docosahexaenoate that are precursors of the anti-inflammatory lipid mediators, resolvins (By similarity). During the resolution phase of acute inflammation drives docosahexaenoate-derived resolvin D1 synthesis, which suppresses dendritic cell activation and T-helper 1 immune response (By similarity). May act in an autocrine and paracrine manner (By similarity). Via a mechanism independent of its catalytic activity, promotes differentiation of regulatory T cells (Tregs) and participates in the maintenance of immune tolerance (By similarity). May contribute to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family.


FUNCTION: Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan. May serve as a universal non- classical progesterone receptor in the uterus. Intracellular heme chaperone required for delivery of labile, or signaling heme, to the nucleus. Plays a role in adipocyte function and systemic glucose homeostasis. In brown fat, which has a high demand for heme, delivery of labile heme in the nucleus regulates the activity of heme-responsive transcriptional repressors such as NR1D1 and BACH1. SUBCELLULAR LOCATION: Membrane; Single- pass membrane protein Nucleus envelope Endoplasmic reticulum. SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily.


FUNCTION: Component of the proteinaceous fiber-like linker between two centrioles, required for centrosome cohesion. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localizes to the proteinaceous linker between the proximal ends of the centrioles.


FUNCTION: Algogenic for animals, human and insects (PubMed:7826413). At high concentrations (0.5-1 uM), it acts as a pore-forming protein that forms nonselective cation channels both in cell and artificial membranes (PubMed:7826413). It is weakly selective for cation over anions channel conductance is identical in both directions. At lower concentrations (1-10 nM), this heterodimer inhibits cardiac L-type calcium currents in isolated rat cardiac ventricular myocytes (PubMed:10336635). SUBCELLULAR LOCATION: Secreted Target cell membrane. SIMILARITY: Belongs to the ectatomin family. Ectatomin-Et subfamily.


FUNCTION: S-layer protein. The S-layer is a paracrystalline mono- layered assembly of proteins which coat the surface of the cell. In H.hispanica, the S-layer contains two different glycoproteins, Slg1 and Slg2, which share highly similar amino acid sequences. SUBCELLULAR LOCATION: Secreted, cell wall, S-layer Cell membrane. SIMILARITY: Belongs to the halobacterial S-layer protein family.


FUNCTION: Calcium-dependent NADPH oxidase that generates superoxide. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family.


FUNCTION: Controls V(D)J recombination during T-cell development by repressing T-cell receptor (TCR) beta enhancer function. Binds to scaffold/matrix attachment region beta (S/MARbeta), an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Represses cyclin D1 transcription by recruiting HDAC1 to its promoter, thereby diminishing H3K9ac, H3S10ph and H4K8ac levels. Promotes TP53 activation, which causes cell cycle arrest and inhibits tumor growth (PubMed:12494467). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BANP/SMAR1 family.


FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Upon expression in E.coli and in M.smegmatis partially inhibits cell growth and colony formation; its toxic effect is neutralized by coexpression with cognate antitoxin MazE6. Acts as an mRNA interferase on ssRNA, cleaving between the second and third bases in the sequences CUCCU and UUCCU (PubMed:18485066). Further experiments demonstrate that it digests between the first and second bases of UCCUU, yielding a 5'- hydroxyl end; digests M.tuberculosis mRNA (in coding as well as the 5'- and 3'-UTR regions) and 23S rRNA, digests E.coli 16S rRNA both alone and in the 70S ribosome but no data for M.tuberculosis 16S rRNA cleavage was presented. 23S and 16S rRNA digestion occurs in predicted single-stranded regions, the 16S rRNA UCCUU site is in the anti-Shine- Dalgarno site and would cleave off the last 7 nucleotides (PubMed:24709835). Non-cognate antitoxins VapB27 and VapB40 partially neutralize toxicity in vivo (PubMed:20876537). FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Acts as an endoribonuclease on single-strand RNA, cleaving between the second and third bases in the sequences CUCCU and UUCCU. Neutralized by coexpression with cognate antitoxin MazE2. FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Acts as an endoribonuclease on single-strand RNA, cleaving between the second and third bases in the sequences CUCCU and UUCCU. Neutralized by coexpression with cognate antitoxin MazE6. SUBCELLULAR LOCATION: Secreted. Note=Following 6 weeks of nutrient starvation. SIMILARITY: Belongs to the PemK/MazF family.


FUNCTION: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites (PubMed:6765947, PubMed:15890657). Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl- CoA/(S)-methylmalonyl-CoA (PubMed:6765947, PubMed:15890657). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA at a much lower rate (PubMed:6765947). Other alternative minor substrates include (2E)- butenoyl-CoA/crotonoyl-CoA (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the AccD/PCCB family.


FUNCTION: Inhibits cell division during the SOS response. Affects a later stage of the cell division protein assembly, after the assembly of the Z ring, by probably suppressing recruitment of FtsL and/or DivIC to the division machinery. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the YneA family.


FUNCTION: Thrombin-like snake venom serine protease that coagulates fibrinogen by inducing a fast degradation of the alpha chain (FGA) from human citrated plasma, and a slow degradation of beta chain (FGB). Potently induces platelet aggregation in both platelet rich plasma and washed platelet preparations in a concentration-dependent fashion. Shows amidolytic activities. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.


FUNCTION: Catalyzes the addition of a mannose residue from GDP-D- mannose to GlcAGroAc2 to generate 1,2-di-O-C16/C18:1-(alpha-D- mannopyranosyl)-(1-4)-(alpha-D-glucopyranosyluronic acid)-(1-3)- glycerol(ManGlcAGroAc2). FUNCTION: Catalyzes the addition of a mannose residue from GDP-D- mannose to GlcAGroAc2 to generate 1,2-di-O-C16/C18:1-(alpha-D- mannopyranosyl)-(1-4)-(alpha-D-glucopyranosyluronic acid)-(1-3)- glycerol(ManGlcAGroAc2). SIMILARITY: Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.


SIMILARITY: Belongs to the BICDR family.


FUNCTION: Ligand-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli. Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca(2+)-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis. SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein Cell projection, dendritic spine membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Note=Mostly, but not exclusively expressed in postsynaptic dendritic spines. SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV1 sub-subfamily.


SIMILARITY: To methylmalonyl-CoA mutase.


FUNCTION: Catalyzes the transfer of the methyl group from monomethylamine to the corrinoid cofactor of MtmC. SIMILARITY: Belongs to the monomethylamine methyltransferase family.


FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross- linking of the peptide subunits). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: In the C-terminal section; belongs to the transpeptidase family. SIMILARITY: In the N-terminal section; belongs to the glycosyltransferase 51 family.


FUNCTION: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. Also able to produce homospermidine from putrescine. SIMILARITY: Belongs to the deoxyhypusine synthase family.


FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.


FUNCTION: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (PubMed:2007593, PubMed:9299349, PubMed:9654444). Preferentially, cleaves after an arginine at position P2 (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the peptidase M16 family.


FUNCTION: May be involved (but not essential) in spermatogenesis. SUBCELLULAR LOCATION: Nucleus Note=Localized predominantly in the nucleus of haploid round spermatid.


FUNCTION: Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein Note=One of the very few enzymes located there. SIMILARITY: Belongs to the phospholipase A1 family.


FUNCTION: Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine. In vitro, dephosphorylates p-nitrophenyl phosphate (pNPP). SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side Note=Translocates to cytoplasm in response to apoptotic stimuli such as staurosporine treatment. SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class dual specificity subfamily.


FUNCTION: Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. Xpt subfamily.


FUNCTION: Phosphatase that has a high activity toward phosphoethanolamine (PEA) and phosphocholine (PCho) (By similarity). Involved in the generation of inorganic phosphate for bone mineralization (PubMed:15050893). SUBCELLULAR LOCATION: Extracellular vesicle Note=Localizes to special class of extracellular vesicles, named matrix vesicles (MVs), which are released by osteogenic cells. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PHOSPHO family.


FUNCTION: Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of azaphilones, a class of fungal metabolites characterized by a highly oxygenated pyrano-quinone bicyclic core and exhibiting a broad range of bioactivities (PubMed:22921072). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Inhibits a wide spectrum of lactic acid bacteria. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bacteriocin class IIA/YGNGV family.


FUNCTION: Bet counteracts the innate antiretroviral activity of APOBEC3 family defense factors by inhibiting their incorporation into virions. May be implicated in the establishment and/or maintenance of viral persistance. Bet is required for viral replication (By similarity). SUBCELLULAR LOCATION: [Isoform Bel-2]: Host nucleus. SUBCELLULAR LOCATION: [Isoform Bet]: Host cytoplasm Host nucleus Secreted Note=Bet is highly expressed in infected cells, where it localizes to both cytoplasm and nucleus (PubMed:11884565). Also secreted and internalized by non-infected surrounding cells (PubMed:11884565).


FUNCTION: Involved in cytokinin-mediated development. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the SOFL plant protein family.


FUNCTION: ATP-dependent RNA helicase involved in mRNA splicing. May destabilize the U1/5'-splice site duplex to permit an effective competition for the 5'-splice site by the U6 snRNA, resulting in the switch between U1 and U6 at the 5'-splice site. May also act to unwind the U4/U6 base-pairing interaction in the U4/U6/U5 snRNP, facilitating the first covalent step of splicing (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DDX23/PRP28 subfamily.


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


FUNCTION: Required in both the classical and alternate pathways of the complement system. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SIMILARITY: Belongs to the complex I 51 kDa subunit family.


FUNCTION: Depressant insect beta-toxins cause a transient contraction paralysis followed by a slow flaccid paralysis. They bind voltage- independently at site-4 of sodium channels (Nav) and block action potentials, primarily by depolarizing the axonal membrane and suppressing the sodium current. This depressant toxin is active only on insects. It is found in a relatively small amount in the venom, and its activity on insects is 10-fold higher compared to other known depressant toxins. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (4 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily.


FUNCTION: GRF is released by the hypothalamus and acts on the adenohypophyse to stimulate the secretion of growth hormone. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glucagon family.


FUNCTION: Might be involved in growth regulation, and in myelinization in the peripheral nervous system. FUNCTION: Might be involved in growth regulation, and in myelinization in the peripheral nervous system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PMP-22/EMP/MP20 family.


SUBCELLULAR LOCATION: Host membrane; Single-pass type I membrane protein.


FUNCTION: Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor. SIMILARITY: Belongs to the AG-peptide AGP family.


FUNCTION: Required for protein translocation and folding in the endoplasmic reticulum (ER). Functions as a nucleotide exchange factor for the ER lumenal chaperone HSPA5. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the SIL1 family.


FUNCTION: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes (PubMed:23408433). Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4- aminobutanoate and beta-alanine, respectively (PubMed:23408433). Catalyzes the oxidation of 4-(trimethylamino)butanal and 4- guanidinobutanal to 4-trimethylammoniobutanoate and 4- guanidinobutanoate, respectively (PubMed:23408433). Catalyzes the oxidation of betaine aldehyde to glycine betaine (PubMed:23408433). SIMILARITY: Belongs to the aldehyde dehydrogenase family.


FUNCTION: Enhances the tyrosine carboxypeptidase activity of VASH1 and VASH2, thereby promoting the removal of the C-terminal tyrosine residue of alpha-tubulin (PubMed:29146869, PubMed:31270470, PubMed:31235911, PubMed:31324789, PubMed:31171830, PubMed:31235910). This activity is critical for spindle function and accurate chromosome segregation during mitosis since microtuble detyronisation regulates mitotic spindle length and postioning (PubMed:31171830). Also required to enhance the solubility and secretion of VASH1 and VASH2 (PubMed:20736312, PubMed:27879017, PubMed:30607023). Plays a role in axon and excitatory synapse formation (PubMed:31235911). SUBCELLULAR LOCATION: Cytoplasm Secreted Cytoplasm, cytoskeleton Note=Detected both intracellularly and extracellularly (By similarity). Within cells, localizes mainly to the apical part of the cell (By similarity). SIMILARITY: Belongs to the SVBP family.


FUNCTION: The exact function of MaoXI is not known. SIMILARITY: Belongs to the copper/topaquinone oxidase family.


FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=Associates with F-actin stress fibers. SIMILARITY: Belongs to the tropomyosin family.


FUNCTION: Epimerizes UDP-galactose to UDP-glucose. SIMILARITY: Belongs to the polysaccharide synthase family.


FUNCTION: Siderocalin-like lipocalin tightly binding a variety of bacterial ferric siderophores, also binds long-chain unsaturated fatty acids such as linoleic acid, oleic acid, arachidonic acid and, with a lower affinity, long chain saturated fatty acids such as steraic acid. May act as an antibacterial factor, through dual ligand specificity, both as a siderophore-sequestrating molecule and a lysophosphatidic acid (LPA) sensor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.


FUNCTION: Important for the metabolism of amino acids and Krebs-cycle related organic acids. In plants, it is involved in nitrogen metabolism and in aspects of carbon and energy metabolism. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Involved in cell wall lipids remodeling and in virulence (PubMed:26157429, PubMed:26902658, PubMed:28198348). Restricts the biofilm growth and is essential for the optimal intracellular survival of M.tuberculosis (PubMed:28198348). Shows esterase activity with a preference for short-chain esters, particularly pNP-acetate (C2) and pNP-butyrate (C4) (PubMed:26902658). Has weaker activity with pNP- octanoate (C8), pNP-laurate (C12) and pNP-myristate (C14) (PubMed:26902658). Shows weak long-chain triacylglycerol (TAG) hydrolase activity in vitro (PubMed:16354661). Not necessary for PPE17 stability or for its localization on the mycobacterial surface (PubMed:23469198). SUBCELLULAR LOCATION: Secreted, cell wall Note=Cell wall associated protein. SIMILARITY: Belongs to the mycobacterial PE family.


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


FUNCTION: Myosin regulatory subunit that plays an essential to maintain muscle integrity during early development (By similarity). Plays a role in muscle contraction (PubMed:15256600).


FUNCTION: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. Acts as a ligand for IGF1R. Binds to the alpha subunit of IGF1R, leading to the activation of the intrinsic tyrosine kinase activity which autophosphorylates tyrosine residues in the beta subunit thus initiatiating a cascade of down-stream signaling events leading to activation of the PI3K-AKT/PKB and the Ras-MAPK pathways. Binds to integrins. Its binding to integrins and subsequent ternary complex formation with integrins and IGFR1 are essential for IGF1 signaling. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insulin family.


FUNCTION: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TatC family.


FUNCTION: Essential for the assembly of ubiquinol-cytochrome c reductase. It has a direct effect on the correct occurrence of the Rieske protein, core 4, core 5 and apocytochrome b (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CBP4 family.


FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the shikimate kinase family. AroL subfamily. SIMILARITY: Belongs to the shikimate kinase family. AroL subfamily.


FUNCTION: Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF- ubiquinone oxidoreductase. Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism. ETFB binds an AMP molecule that probably has a purely structural role. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the ETF beta-subunit/FixA family.


FUNCTION: Involved in the cleavage of the C1-C2 bond of 3D-(3,5/4)- trihydroxycyclohexane-1,2-dione (THcHDO) to yield 5-deoxy-glucuronate (5DG). SIMILARITY: Belongs to the TPP enzyme family.


FUNCTION: Methyltransferase involved in ribosomal biogenesis. Specifically catalyzes the N1-methylation of the pseudouridine corresponding to position 914 in M.jannaschii 16S rRNA. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase NEP1 family.


FUNCTION: Squalene synthase; part of the gene cluster that mediates the biosynthesis of squalestatin S1 (SQS1, also known as zaragozic acid A), a heavily oxidized fungal polyketide that offers potent cholesterol lowering activity by targeting squalene synthase (SS) (PubMed:28605916). Catalyzes the condensation of 2 two farnesyl pyrophosphate moieties to form squalene (By similarity). The presence of a gene encoding a squalene synthase supports the identification of the cluster as being responsible for SQS1 production and suggests a likely mechanism for self-resistance (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the phytoene/squalene synthase family.


FUNCTION: Required for growth under high-pressure and low-temperature conditions. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DLT1 family.


FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity). SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.


SIMILARITY: Belongs to the ANP32 family.


FUNCTION: Inhibits voltage-gated potassium channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 12 subfamily.


FUNCTION: Acts as a pheromone, induces cells to develop competence for genetic transformation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ComC family.


FUNCTION: Promotes hydrolysis of glycogen and lipids, and raises the blood sugar level. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glucagon family.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (By similarity). SIMILARITY: Belongs to the complex I 24 kDa subunit family.


FUNCTION: Has aromatic amino acid transaminase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Activity on G(z)-alpha is inhibited by phosphorylation of the G-protein. Activity on G(z)-alpha and G(i)- alpha-1 is inhibited by palmitoylation of the G-protein (By similarity).


FUNCTION: Delta-conotoxins bind to site 6 of voltage-gated sodium channels (Nav) and inhibit the inactivation process. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O1 superfamily.


SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 family.


FUNCTION: Glutathione S-transferase that catalyzes the nucleophilic attack of the sulfur atom of glutathione on the electrophilic groups of a wide range of exogenous and endogenous compounds. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). It also catalyzes the isomerization of D5- androstene-3,17-dione (AD) into D4-androstene-3,17-dione and may therefore play an important role in hormone biosynthesis. Through its glutathione-dependent peroxidase activity toward the fatty acid hydroperoxide (13S)-hydroperoxy-(9Z,11E)-octadecadienoate/13-HPODE it is also involved in the metabolism of oxidized linoleic acid. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GST superfamily. Alpha family.


SIMILARITY: Belongs to the SNF2/RAD54 helicase family.


FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. FUNCTION: Could be involved in the conversion of sugars, which are a major phenomenon in the rehydration process. SIMILARITY: Belongs to the transketolase family.


FUNCTION: Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the protein disulfide isomerase family.


FUNCTION: RNA-binding nucleolar protein required for pre-rRNA processing. Involved in production of 18S rRNA and assembly of small ribosomal subunit (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the NOP9 family.


FUNCTION: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (PubMed:28283058). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs (By similarity). In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation (PubMed:28283058). Specifically degrades pre-mRNAs with a defective m7G cap and is part of a pre-mRNA capping quality control (PubMed:28283058). Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end- capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (PubMed:28283058). Also possesses RNA 5'- pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DXO/Dom3Z family.


FUNCTION: Potentiates the contractile activity of bradykinin on the isolated guinea-pig ileum. Inhibits the hydrolysis of bradykinin by angiotensin-converting enzyme (ACE) and also inhibits the conversion of angiotensin I to angiotensin II by kininase II from guinea-pig ileum tissue. Also increases the depressor effect of bradykinin on arterial blood pressure in the anaesthetized rat. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Scorpion BPP (group 1) family.


FUNCTION: Probable sorting receptor which regulates endocytosis and secretion of the wnt ligand egl-20 (PubMed:18160346, PubMed:18160347, PubMed:21076391). Recycling of mig-14 from the plasma membrane to the Golgi apparatus by the retromer complex is essential for its function (PubMed:18160346, PubMed:18160347, PubMed:21076391). Its endosomal trafficking is regulated by its association with sorting nexin snx-3 on early endosomes and the mtm-6/mtm-9 myotubularin complex (PubMed:21076391). Required in embryonic development for endoderm specification and the correct positioning and orientation of the mitotic spindles and division planes in blastomere cells (PubMed:9288749, PubMed:16678095). Functions during vulval development, playing a role in vulval precursor cell fate specification (PubMed:11063687, PubMed:18077322). During development, specifically regulates the migration of HSN neurons, the left Q neuroblast (QL) and its descendants and the distal tip cells of the gonads (PubMed:8898225, PubMed:10388818, PubMed:11063687, PubMed:18160346, PubMed:18160347). Positioning of Q neuroblasts may be both dependent and independent of hox gene mab-5 (PubMed:8898225). Involved in establishing ALM and PLM neuronal cell polarity (PubMed:18160346). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Early endosome membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Basal cell membrane; Multi-pass membrane protein Late endosome membrane; Multi-pass membrane protein Note=Traffics between endosomal cell membrane and the Golgi apparatus membrane and the cell membrane to mediate wnt/egl-20 secretion (PubMed:18160347, PubMed:21076391). Co-localizes with snx-3 on intracellular punctae and early endosomes to facilitate recycling and wnt/egl-20 secretion (PubMed:21076391). Localizes to the basolateral cell membrane of intestine cells, but not the apical cell membrane (PubMed:26115433). SIMILARITY: Belongs to the wntless family.


FUNCTION: ATP-dependent microtubule severing protein. Microtubule severing may promote reorganization of cellular microtubule arrays and the release of microtubules from the microtubule organizing center following nucleation. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton Note=Forms an intramembrane hairpin- like structure in the membrane. SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily.


FUNCTION: Involved in the recognition of invading microorganisms. Binds specifically to beta-1,3-glucan and activates the phenoloxidase cascade (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insect beta-1,3-glucan binding protein family.


FUNCTION: Involved in chlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.


FUNCTION: Serine/threonine protein kinase which phosphorylates VIME. May play a specific role in the dynamic behavior of the intermediate filament cytoskeleton by phosphorylation of VIME (By similarity). Not essential for the survival of KRAS-dependent AML cell lines. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK subfamily.


FUNCTION: Probably involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutamine synthetase family.


FUNCTION: Inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit, thus contributing to the regulation of glucose metabolism. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.


FUNCTION: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins. SUBCELLULAR LOCATION: Secreted Host nucleus Note=Accumulates at the margin of the nucleolus, but is absent within it. SIMILARITY: Belongs to the RxLR effector family.


FUNCTION: May be involved in electron transfer from bc1 complex to aa3. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the cytochrome c family.


FUNCTION: Component of the spindle pole body (SPB) required for the proper execution of spindle pole body (SPB) duplication. Potential role in cross-linking filaments or anchoring other molecules. It is essential for growth (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body Note=Tightly associated with the nucleus. It is present in a granular pattern that excludes the nucleolus. SIMILARITY: Belongs to the SPC110 family.


SIMILARITY: Belongs to the NPIP family.


FUNCTION: Negatively regulates the activity of MCU, the mitochondrial inner membrane calcium uniporter, and thereby modulates calcium uptake into the mitochondrion. Does not form functional calcium channels by itself. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MCU (TC 1.A.77) family.


FUNCTION: Envelope protein part of the entry-fusion complex responsible for the virus membrane fusion with host cell membrane during virus entry. Also plays a role in cell-cell fusion (syncytium formation). SUBCELLULAR LOCATION: Virion membrane; Single-pass type II membrane protein Note=Component of the mature virion (MV) membrane (Probable). The mature virion is located in the cytoplasm of infected cells and is probably released by cell lysis. SIMILARITY: Belongs to the orthopoxvirus OPG143 family.


FUNCTION: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the histone H2A family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.


FUNCTION: May act as a regulatory factor during viral transcription.


SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the distal-less homeobox family.


FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide. SUBCELLULAR LOCATION: Periplasm Note=Is attached to the inner membrane when interacting with the MsrQ subunit. SIMILARITY: Belongs to the MsrP family.


FUNCTION: Low-affinity glucose transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family.


FUNCTION: A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA (By similarity). GTPase that impacts interactions between enteropathogenic E.coli (EPEC) and epithelial cells and also has an effect on motility (PubMed:9622352). FUNCTION: A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA. FUNCTION: A 50S ribosomal subunit assembly protein with GTPase and nucleotide-independent chaperone activity, required for 50S subunit assembly at low temperatures, may also play a role in translation (PubMed:30305394). Genetic and deletion evidence suggests this is involved in ribosome assembly at low temperatures; it may also affect translation (Probable) (PubMed:25777676, PubMed:30305394). Involved in incorporation of ribosomal protein L6 into precursor 44S ribosomal particles at low temperatures. Also has chaperone activity which does not require nucleotides (PubMed:30305394). Binds GDP, ppGpp and GDPCP (a nonhydrolyzable GTP analog) with similar affinity; the conformation of the protein does not significantly change upon nucleotide binding (PubMed:26163516, PubMed:26283392). Interacts with ribosomes (Ref.12, PubMed:26283392). Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA. Ribosome binding alters its conformation (PubMed:26283392). Genetically its function does not overlap LepA, and it acts in a different pathway during ribosome assembly than does RNA helicase DeaD (PubMed:25777676). GTPase that affects interactions between enteropathogenic E.coli (EPEC) and epithelial cells (PubMed:9622352). Probably regulates expression of proteins required for (at least) K5 polysaccharide production (Probable). Deletion mutants of bipA are suppressed by an rluC deletion, which no longer modifies uracils 955, 2504 and 2580 to pseudouridine in 23S rRNA; there are 5 other pseudouridine synthases in E.coli, only rluC suppresses this phenotype. Mutating 23S rRNA so the 3 uracils are other nucleotides also suppresses the bipA deletion; pseudouridine-2504 is required for ribosome assembly and translational accuracy (PubMed:18820021, PubMed:25777676). SUBCELLULAR LOCATION: Cytoplasm Note=Binds to ribosomes. SUBCELLULAR LOCATION: Cytoplasm Note=Associates with 70S ribosomes and 30S and 50S subunits in the presence of GMPPNP (a nonhydrolyzable GTP analog) at both 20 and 37 degrees Celsius; no change in ribosome association is seen in the presence of ppGpp or when the stringent response is triggered. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. BipA subfamily.


FUNCTION: RNA-binding protein involved in pre-mRNA splicing. Interacts with the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome. Involved in regulating splice site selection. Binds preferentially RNA with A/C rich sequences and poly-C stretches. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the KHDC4 family.


FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. Involved in the biosynthesis of the dTDP-L-rhamnose which is a component of the critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which connects the galactan region of arabinogalactan to peptidoglycan via a phosphodiester linkage. FUNCTION: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. Involved in the biosynthesis of the dTDP-L-rhamnose which is a component of the critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which connects the galactan region of arabinogalactan to peptidoglycan via a phosphodiester linkage. SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.


FUNCTION: Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate (PubMed:10824116). Also has N-acetylmannosamine (ManNAc) kinase activity (PubMed:10824116). Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway (PubMed:22692205). Also involved in innate immunity by promoting detection of bacterial peptidoglycan by NOD2: acts by catalyzing phosphorylation of muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan, to generate 6-O-phospho-muramyl dipeptide, which acts as a direct ligand for NOD2 (PubMed:36002575). SIMILARITY: Belongs to the eukaryotic-type N-acetylglucosamine kinase family.


SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyl hydrolase 99 family.


SIMILARITY: To B.subtilis YcdC.


FUNCTION: This peptide activates mouse sensory neuron-specific G- protein coupled receptors MRGPRX1, but not human receptors (PubMed:30243794). In vivo, causes hyperactivity in mice when injected intracranially (PubMed:11738233). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.


SIMILARITY: Belongs to the TPP enzyme family.


SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the GPAT/DAPAT family. SIMILARITY: Belongs to the GPAT/DAPAT family.


FUNCTION: Involved in meiotic recombination in association with MSH5. Required for reciprocal recombination and proper segregation of homologous chromosomes at meiosis. Promotes homologous recombination through facilitating chiasma formation during prophase I. Involved in the control of class I crossovers formation. SUBCELLULAR LOCATION: Nucleus Note=In pollen mother cells during meiosis, localizes to unsynapsed axes during leptotene and zygotene, but is not present on synapsed regions of zygotene nuclei. SIMILARITY: Belongs to the DNA mismatch repair MutS family.


FUNCTION: Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the mitochondrial Rho GTPase family.


FUNCTION: Regulator of protein phosphatase 1 (PP1) required for neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. Acts as an activator of PP1 by interacting with PPP1CA and preventing phosphorylation of PPP1CA at 'Thr-320'. During neural tube closure, localizes to the ventral neural tube and activates PP1, leading to down-regulate cell proliferation within cranial neural tissue and the neural retina. Also acts as a regulator of migration of enteric neural crest cells (ENCCs) by activating PP1, leading to dephosphorylation and subsequent activation of cofilin (COF1 or COF2) and repression of the integrin signaling through the RHO/ROCK pathway (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell projection, lamellipodium. SIMILARITY: Belongs to the phosphatase and actin regulator family.


FUNCTION: This methylothroph organism uses azurin in the electron transport chain involved in methylamine/methanol oxidation. SUBCELLULAR LOCATION: Periplasm.


FUNCTION: Structural component of the virion that acts as a cement protein on the capsid exterior and forms triskelion structures consisting of three molecules that stabilize three hexon trimers at the center of each icosahedral facet and fixes the peripentonal hexons. Dispensable for assembly. During virus entry, recruits the anterograde motor kinesin-1 to the capsid docked at the nuclear pore complex thereby subjecting the docked capsid to a pulling force. The resulting tension leads to capsid disruption, dispersion of capsid fragments toward cell periphery and eventually viral DNA entry into the host nucleus. SUBCELLULAR LOCATION: Virion Host nucleus Note=Located in the canyons between the hexons on the outer surface of the capsid. Forms a sort of hairnet on the outer side of the virion. Present in 240 copies per virion. SIMILARITY: Belongs to the adenoviridae hexon-interlacing protein family.


FUNCTION: Binds estrogens with an affinity similar to that of ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. Locally synthesized estrogens may act via ER beta, in addition to ER alpha, to mediate seasonal or developmental effects on nearby song nuclei. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 subfamily.


FUNCTION: Involved in the regulation of ptsG expression by binding and inactivating Mlc. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MtfA family.


SIMILARITY: Belongs to the RutC family.


FUNCTION: Iol operon repressor.


FUNCTION: Adapter molecule that plays a key role in the activation of pro-inflammatory NF-kappa-B signaling following detection of bacterial pathogen-associated molecular pattern metabolites (PAMPs) (PubMed:12566447, PubMed:15492226, PubMed:26068852, PubMed:28877472, PubMed:28222186, PubMed:30111836). Promotes activation of an innate immune response by inducing the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism (PubMed:15492226, PubMed:26068852). TIFA-dependent innate immune response is triggered by ADP-D-glycero- beta-D-manno-heptose (ADP-Heptose), a potent PAMP present in all Gram- negative and some Gram-positive bacteria: ADP-Heptose is recognized by ALPK1, which phosphorylates TIFA at Thr-9, leading to TIFA homooligomerization and subsequent activation of pro-inflammatory NF- kappa-B signaling (PubMed:30111836). SUBCELLULAR LOCATION: Cytoplasm Note=Colocalizes with lysosomal marker LAMP2 following homooligomerization and subsequent activation. SIMILARITY: Belongs to the TIFA family.


FUNCTION: Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors (PubMed:10688651, PubMed:12359225, PubMed:12873986, PubMed:15194700, PubMed:17344214, PubMed:18242580, PubMed:22306293, PubMed:23084476). Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene (PubMed:17344214). May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:12873986). 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 (PubMed:12359225). Activated by IL31 through IL31RA (PubMed:15194700). 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 (PubMed:28065600). Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1 (PubMed:17344214). Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation (By similarity). May play an apoptotic role by transctivating BIRC5 expression under LEP activation (PubMed:18242580). Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity (PubMed:23084476). Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion (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. The complex composed of BART and ARL2 plays an important role in the nuclear translocation and retention of STAT3. Identified in a complex with LYN and PAG1. SIMILARITY: Belongs to the transcription factor STAT family.


FUNCTION: Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel (PubMed:19671703, PubMed:23975098). Channel properties are modulated by subunit assembly. Mediates IK(NI) current in myoblasts. Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Nucleus inner membrane; Multi-pass membrane protein Cell projection, dendrite Cell projection, axon Presynaptic cell membrane Perikaryon Postsynaptic density membrane Early endosome membrane Note=Perinuclear KCNH1 is located to NPC-free islands. SIMILARITY: Belongs to the potassium channel family. H (Eag) (TC 1.A.1.20) subfamily. Kv10.1/KCNH1 sub-subfamily.


FUNCTION: HMWC (high-molecular-weight cytochrome c precursor), ORF2, ORF3, ORF4, ORF5, ORF6 in the HMC operon form a transmembrane protein complex that allows electron flow from the periplasmic hydrogenase to the cytoplasmic enzymes that catalyze reduction of sulfates. ORF6 is a redox protein. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Ammonium transporter probably involved in ammonium uptake from the soil. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2) family.


FUNCTION: N-acetyl-galactosamine and D-galactose specific lectin. Binds the Tn-antigen structure GalNAc-alpha-1-O-Ser, the T-antigen structure Gal-beta1-3-GalNAc and IgA. SIMILARITY: Belongs to the jacalin lectin family.


FUNCTION: Chaperone that functions as a gatekeeper on the extracellular side of the Sec translocon. Facilitates the translocation of precursor proteins across Sec by interacting with the translocating substrate. Also plays a role in the release of newly synthesized secreted proteins at the extracellular exit site of the Sec translocon. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein; Extracellular side Note=Located at the lateral gate of SecY. SIMILARITY: Belongs to the PpiD chaperone family.


FUNCTION: Creation of an extracellular membrane face which guides the wrapping process and ultimately compacts adjacent lamellae. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the myelin P0 protein family.


FUNCTION: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Also plays a role in base excision repair (BER) probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. SUBCELLULAR LOCATION: Nucleus Nucleus, PML body. SIMILARITY: Belongs to the replication factor A protein 1 family.


FUNCTION: Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins, such as MEIS2 or ILF2. Normal degradation of key regulatory proteins is required for normal limb outgrowth and expression of the fibroblast growth factor FGF8. Maintains presynaptic glutamate release and consequently cognitive functions, such as memory and learning, by negatively regulating large- conductance calcium-activated potassium (BK) channels in excitatory neurons. Likely to function by regulating the assembly and neuronal surface expression of BK channels via its interaction with KCNT1 (By similarity). May also be involved in regulating anxiety-like behaviors via a BK channel-independent mechanism (By similarity). Plays a negative role in TLR4 signaling by interacting with TRAF6 and ECSIT, leading to inhibition of ECSIT ubiquitination, an important step of the signaling (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the CRBN family.


FUNCTION: Receptor-like kinase involved in the control of pollen germination and pollen tube polar growth (PubMed:23024212). Can phosphorylate ROPGEF1 in vitro (PubMed:23024212). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


FUNCTION: A cytochrome P450 monooxygenase involved in corticoid and androgen biosynthesis. Catalyzes 17-alpha hydroxylation of C21 steroids, which is common for both pathways. A second oxidative step, required only for androgen synthesis, involves an acyl-carbon cleavage. The 17-alpha hydroxy intermediates, as part of adrenal glucocorticoids biosynthesis pathway, are precursors of cortisol. Hydroxylates steroid hormones, pregnenolone and progesterone to form 17-alpha hydroxy metabolites, followed by the cleavage of the C17-C20 bond to form C19 steroids, dehydroepiandrosterone (DHEA) and androstenedione. Has 16- alpha hydroxylase activity. Catalyzes 16-alpha hydroxylation of 17- alpha hydroxy pregnenolone, followed by the cleavage of the C17-C20 bond to form 16-alpha-hydroxy DHEA. Also 16-alpha hydroxylates androgens, relevant for estriol synthesis. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane Microsome membrane. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Smooth muscle cells (SM) and cardiac muscle cells-specific transcriptional factor which uses the canonical single or multiple CArG boxes DNA sequence. Acts as a cofactor of serum response factor (SRF) with the potential to modulate SRF-target genes. Plays a crucial role in cardiogenesis, urinary bladder development, and differentiation of the smooth muscle cell lineage (myogenesis) (By similarity). SUBCELLULAR LOCATION: Nucleus.