FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. Required for the recruitment of STIL to the centriole and for STIL-mediated centriole amplification (By similarity). Phosphorylates CEP131 and PCM1 which is essential for proper organization and integrity of centriolar satellites (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Nucleus, nucleolus Cleavage furrow Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Associates with centrioles throughout the cell cycle. Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDC5/Polo subfamily.


FUNCTION: [Defensin alpha 5]: Exhibits bacteriostatic activity against Gram-positive bacteria S.aureus and L.monocytogenes and Gram-negative bacterium E.coli, antifungal activity against C.neoformans and microbicidial activity against Gram-positive bacteria S.aureus and L.monocytogenes. FUNCTION: [Defensin alpha 4]: Exhibits bacteriostatic activity against Gram-positive bacteria S.aureus and L.monocytogenes and Gram-negative bacterium E.coli, antifungal activity against C.neoformans and microbicidial activity against Gram-positive bacteria S.aureus and L.monocytogenes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha-defensin family.


FUNCTION: E4-type SUMO ligase that promotes SUMO chain formation in a SCE1-dependent manner and thus contributes to a pathway for proteolytic removal of sumoylation substrates. Involved in stress responses (e.g. osmotic, salt and abscisic acid ABA) and sulfur metabolism. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PIAL protein ligase family.


FUNCTION: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the EF-Ts family.


FUNCTION: J region of the variable domain of T cell receptor (TR) beta chain that participates in the antigen recognition (PubMed:24600447). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation (PubMed:23524462). The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity (PubMed:15040585). SUBCELLULAR LOCATION: Cell membrane.


FUNCTION: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc- pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY subfamily. SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY subfamily.


FUNCTION: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL4, CXCL5, CXCL6, CXCL7, CXCL10 and CXCL11. SUBCELLULAR LOCATION: Secreted.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the adenylyl cyclase class-1 family.


SIMILARITY: Belongs to the mannitol dehydrogenase family. UxaB subfamily.


FUNCTION: Probably part of a binding-protein-dependent transport system YphDEF. Probably responsible for energy coupling to the transport system. SIMILARITY: Belongs to the ABC transporter superfamily.


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


FUNCTION: DNA-dependent ATPase, acting on dsDNA with a 3'-ssDNA tail, unwinding with 3'-to 5'-polarity. Also highly efficient on nicked DNA. Involved in the post-incision events of nucleotide excision repair (By similarity). FUNCTION: DNA-dependent ATPase, acting on dsDNA with a 3'-ssDNA tail, unwinding with 3'-to 5'-polarity. A minimal tail of 18 nt is required for activity. Also highly efficient on nicked DNA. Involved in the post-incision events of nucleotide excision repair, as well as in nitrosative and oxidative stress response and possibly in persistence in the host. Inhibits RecA-mediated DNA strand exchange; this does not require ATPase activity. When combined with UvrA greatly inhibits RecA- mediated DNA strand exchange (By similarity). FUNCTION: DNA-dependent ATPase, acting on dsDNA with a 3'-ssDNA tail, unwinding with 3'-to 5'-polarity. A minimal tail of 18 nt is required for activity. Also highly efficient on nicked DNA. Involved in the post-incision events of nucleotide excision repair, as well as in nitrosative and oxidative stress response and possibly in persistence in the host. Inhibits RecA-mediated DNA strand exchange; this does not require ATPase activity. When combined with UvrA greatly inhibits RecA- mediated DNA strand exchange. SIMILARITY: Belongs to the helicase family. UvrD subfamily.


FUNCTION: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity). SIMILARITY: Belongs to the MoaE family.


FUNCTION: Catalyzes the acetylation of L-2,4-diaminobutyrate (DABA) to gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) with acetyl coenzyme A. SIMILARITY: Belongs to the acetyltransferase family. EctA subfamily.


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


FUNCTION: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme. SIMILARITY: Belongs to the flavokinase family.


FUNCTION: Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization. SUBCELLULAR LOCATION: Presynaptic cell membrane Postsynaptic cell membrane Note=Colocalizes with GABRB1.


FUNCTION: Required for non-photochemical quenching (NPQ), a mechanism that converts and dissipates the harmful excess absorbed light energy into heat and protect the photosynthetic apparatus from photo-oxidative damage (PubMed:27335457, PubMed:29555769, PubMed:30782831). Is able to sense luminal acidification of the thylakoid membranes, which occurs along with elevated electron flow caused by excess light, and to induce a large, fast, and reversible pH-dependent quenching in LHCII- containing membranes (PubMed:27335457). Mediates excitation energy transfer from light-harvesting complex II (LHCII) to photosystem I (PSI), rather than photosystem II (PSII), at low pH, which mimics the acidified lumen of the thylakoid membranes in high light-exposed chloroplasts (PubMed:29555769, PubMed:30782831). Activates PSI- dependent fluorescence quenching in addition to dissipating excitation energy in LHCII to avoid photooxidative stress under excess light (PubMed:29555769, PubMed:30782831). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family.


FUNCTION: Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA surveillance system in mitochondria; regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. SUBCELLULAR LOCATION: Nucleus Mitochondrion matrix Mitochondrion matrix, mitochondrion nucleoid. SIMILARITY: Belongs to the DExH box helicase family.


SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the EfeM/EfeO family.


FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the RnfG family.


FUNCTION: Probable neurotoxin with unknown target. Possibly targets ion channels. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation. SIMILARITY: Belongs to the plant globin family.


FUNCTION: Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex. Also required for correct spindle orientation. Does not appear to be required for the removal of spindle assembly checkpoint (SAC) proteins from the kinetochore upon bipolar spindle attachment. Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non- processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track) (By similarity). Plays a role in cell migration (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Chromosome, centromere, kinetochore Nucleus. Cytoplasm, cytoskeleton, spindle pole Note=Localizes to the nucleus in interphase and to the kinetochore in early prometaphase. Relocalizes to the mitotic spindle pole before metaphase and is subsequently lost from the spindle poles after chromosome congression is completed. Removal of this protein from the kinetochore requires the dynein/dynactin complex. SIMILARITY: Belongs to the Spindly family.


FUNCTION: Peroxisomal import receptor that mediates the peroxisomal import of both malate synthases MLS1 and MLS2 in oleate-grown cells (PubMed:27678487, PubMed:27663510). Recognizes the C-terminal peroxisomal targeting signal PTS1 sequence SKL of MLS1 and MLS2, probably via its TPR domains (PubMed:27678487). Interacts with the PTS1-receptor docking protein PEX14 but not with peroxins PEX1, PEX3 through to PEX8, PEX10, PEX11, PEX12, PEX13, PEX15, PEX17, PEX18, PEX19 and PEX21 (PubMed:27678487). SUBCELLULAR LOCATION: Cytoplasm Peroxisome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the peroxisomal targeting signal receptor family.


FUNCTION: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the light-harvesting chlorophyll a/b-binding (LHC) protein family.


FUNCTION: Heterotrimeric guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins. Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels. Stimulates the activity of receptor-regulated K(+) channels. May play a role in cell division. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Membrane; Lipid-anchor Note=Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody. SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.


FUNCTION: Is required to sustain N(2)-dependent growth in the presence of low levels of carbon monoxide (CO). Probably acts by protecting the N(2) fixation ability of the nitrogenase complex, which is inactivated in the presence of CO. SIMILARITY: Belongs to the CowN family.


FUNCTION: Required, with sphingomyelinase, to effect target cell lysis (hemolysis). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neutral sphingomyelinase family.


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


FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N- acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that in bacteria anchors the lipopolysaccharide to the outer membrane of the cell. The target for the lipopolysaccharides produced in the chloroplast could either be the cell envelope of the eukaryote or the plastid membrane. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the LpxC family.


FUNCTION: Recognizes and binds polyubiquitin chains (PubMed:11584278, PubMed:16138082). Acts as a linker between the 19S proteasome and polyubiquitinated proteins via UBA domain interactions with ubiquitin for their subsequent degradation. Aspartic protease. Appears to act as negative regulator of constitutive exocytosis. May act at the level of secretory vesicle docking and fusion as a competitive inhibitor of SNARE assembly. Required for S-phase checkpoint control (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the DDI1 family.


FUNCTION: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase family.


FUNCTION: Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). Required for the synthesis of lipophosphoglycan (LPG), a cell surface glycoconjugate (By similarity). Necessary for the attachment of the galactosyl residue to the mannose within the phosphoglycan repeats of the nascent LPG chain (By similarity). Also required for addition of phosphoglycan to acid phosphatase (By similarity). Not required for normal growth (By similarity). Has ATPase activity (PubMed:29568220). Binds heparin with micromolar affinity which may facilitate infection of host cells (PubMed:29568220). SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the heat shock protein 90 family.


FUNCTION: The envelope glycoprotein gp160 precursor down-modulates cell surface CD4 antigen by interacting with it in the endoplasmic reticulum and blocking its transport to the cell surface. FUNCTION: Surface protein gp120 (SU) may target the virus to gut- associated lymphoid tissue (GALT) by binding host ITGA4/ITGB7 (alpha- 4/beta-7 integrins), a complex that mediates T-cell migration to the GALT. Interaction between gp120 and ITGA4/ITGB7 would allow the virus to enter GALT early in the infection, infecting and killing most of GALT's resting CD4+ T-cells. This T-cell depletion is believed to be the major insult to the host immune system leading to AIDS (By similarity). FUNCTION: The surface protein gp120 is a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. DCs are professional antigen presenting cells, critical for host immunity by inducing specific immune responses against a broad variety of pathogens. They act as sentinels in various tissues where they take up antigen, process it, and present it to T-cells following migration to lymphoid organs. SIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. Virion capture also seems to lead to MHC-II-restricted viral antigen presentation, and probably to the activation of SIV-specific CD4+ cells (By similarity). FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 to maintain the highly conserved coreceptor-binding site in a cryptic conformation, protected from neutralizing antibodies. These changes are transmitted to the transmembrane protein gp41 and are thought to activate its fusogenic potential by unmasking its fusion peptide (By similarity). FUNCTION: The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl- ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity). FUNCTION: The transmembrane protein gp41 (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes. The virus undergoes clathrin- dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane; Peripheral membrane protein Host cell membrane; Peripheral membrane protein Host endosome membrane; Peripheral membrane protein Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag (By similarity). SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein Host endosome membrane; Single-pass type I membrane protein Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag.


FUNCTION: O-linked mannose beta-1,4-N-acetylglucosaminyltransferase that transfers UDP-N-acetyl-D-glucosamine to the 4-position of the mannose to generate N-acetyl-D-glucosamine-beta-1,4-O-D- mannosylprotein. Involved in the biosynthesis of the phosphorylated O- mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N- acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 61 family.


FUNCTION: Involved in the transfer of acetyl-CoA into mitochondria. May also be involved in the metabolism of acetate and of ethanol. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. SIMILARITY: Belongs to the carnitine/choline acetyltransferase family.


FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to heparan sulfate. The substrate-specific O-sulfation generates an enzyme-modified heparan sulfate which acts as a binding receptor to Herpes Simplex Virus-1 (HSV-1) and permits its entry. Unlike 3-OST-1, does not convert non- anticoagulant heparan sulfate to anticoagulant heparan sulfate. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the sulfotransferase 1 family.


FUNCTION: ATP-dependent microtubule severing protein. Stimulates microtubule minus-end depolymerization and poleward microtubule flux in the mitotic spindle. Regulates microtubule stability in the neuromuscular junction synapse. Involved in lipid metabolism by regulating the size and distribution of lipid droplets. Involved in axon regeneration by regulating microtubule severing. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton Chromosome Lipid droplet Note=Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles. SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily.


FUNCTION: Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGO-Y14 heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGO-Y14 heterodimer interacts with the EJC key regulator PYM leading to EJC disassembly in the cytoplasm (By similarity). EJC core heterodimers play essential roles in plant growth and development, and pollen and seed development (PubMed:25230811, PubMed:24820023). The MAGO-Y14 heterodimer selectively binds to the UDT1 (UNDEVELOPED TAPETUM 1) pre-mRNA transcript and regulates the splicing of UDT1, a key regulator in stamen development (PubMed:24820023). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. SIMILARITY: Belongs to the mago nashi family.


FUNCTION: Inhibits voltage-gated ion channels. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O2 superfamily.


FUNCTION: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the mycotoxin citrinin, a hepato- nephrotoxic compound to humans due to inhibition of respiration complex III (Ref.1, PubMed:29189834). The pathway begins with the synthesis of a keto-aldehyde intermediate by the citrinin PKS (pksCT also named citS) from successive condensations of 4 malonyl-CoA units, presumably with a simple acetyl-CoA starter unit (Ref.1, PubMed:29189834). Release of the keto-aldehyde intermediate is consistent with the presence of the C-terminal reductive release domain (Ref.1). CitA collaborates with citS by catalyzing the hydrolysis of ACP-bound acyl intermediates to free the ACP from stalled intermediates (PubMed:29189834). CitB then catalyzes the oxidation of the C-12 methyl of the ketone intermediate to an alcohol intermediate which is further oxidized by the oxidoreductase citC to produce a bisaldehyde intermediate (Ref.1). The fourth catalytic step is catalyzed by the citD aldehyde dehydrogenase (Ref.1). The final transformation is the reduction of C-3 by citE to provide the chemically stable citrinin nucleus (Ref.1). CitE appears highly selective for its substrate as its presence in any context other than a full complement of citS and citA-D does not result in observable new compounds (Ref.1). SIMILARITY: Belongs to the LovG family.


FUNCTION: Thiol protease inhibitor. Has papain inhibitory activity in vitro. May be involved in immune responses against invading Gram- negative bacteria. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cystatin family.


FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. SIMILARITY: In the C-terminal section; belongs to the NAD synthetase family.


FUNCTION: Also catalyzes the fourth step in glycosylation of the serine-rich repeat protein PsrP in this bacteria. Can transfer the sugar from UDP-glucose (and much less well from UDP-galactose) to the terminal sugar moiety of PsrP-GlcNAc-Glc-Gal or of PsrP-GlcNAc-Glc-Glc. FUNCTION: Involved in the polymorphic O-glycosylation of the serine- rich repeat protein PsrP. Catalyzes the third step in glycosylation PsrP in this bacteria. Transfers glucose from UDP-glucose to the terminal glucose moiety of already-glycosylated PsrP (using truncated substrates with PsrP SSR1-GlcNAc-Glc). Has a marked preference for PsrP substrate that has already been modified by GlcNAc and glucose. In vitro has hydrolytic activity against UDP-glucose and to a lesser extent against UDP-galactose. SIMILARITY: Belongs to the glycosyltransferase 2 family.


FUNCTION: Binds to DNA non-specifically. Could be a regulatory factor involved in maltose metabolism. SIMILARITY: Belongs to the SfsA family.


FUNCTION: Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of dicer1, ago2 and tarbp2. Within the RLC/miRLC, dicer1 and tarbp2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto ago2. ago2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from dicer1 and tarbp2. May also play a role in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by dicer1. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TARBP2 family.


SIMILARITY: Belongs to the coronaviruses 12.7 kDa protein family.


FUNCTION: Adapter protein involved in neuronal nitric-oxide (NO) synthesis regulation via its association with nNOS/NOS1. The complex formed with NOS1 and synapsins is necessary for specific NO and synapsin functions at a presynaptic level. Mediates an indirect interaction between NOS1 and RASD1 leading to enhance the ability of NOS1 to activate RASD1. Competes with DLG4 for interaction with NOS1, possibly affecting NOS1 activity by regulating the interaction between NOS1 and DLG4. In kidney podocytes, plays a role in podosomes and filopodia formation through CDC42 activation (PubMed:33523862). SUBCELLULAR LOCATION: Cell projection, filopodium Cell projection, podosome.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the alpha/beta interferon family.


FUNCTION: Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity (By similarity). Capable of producing kinin potentiating peptides (By similarity). SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the peptidase C1 family.


FUNCTION: ATP-binding RNA helicase involved in 40S ribosomal subunit biogenesis and is required for the normal formation of 18S rRNAs through pre-rRNA processing at A0, A1 and A2 sites. Required for vegetative growth (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX49/DBP8 subfamily.


FUNCTION: Regulatory component of the cyclin D2-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. SUBCELLULAR LOCATION: Nucleus Cytoplasm Nucleus membrane Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.


FUNCTION: Has a role in the perception of gravity.


FUNCTION: Cell adhesion molecule that mediates both heterotypic cell- cell contacts via its interaction with CD6, as well as homotypic cell- cell contacts. Promotes T-cell activation and proliferation via its interactions with CD6 (By similarity). Contributes to the formation and maturation of the immunological synapse via its interactions with CD6 (By similarity). Mediates homotypic interactions with cells that express ALCAM. Mediates attachment of dendritic cells onto endothelial cells via homotypic interaction. Inhibits endothelial cell migration and promotes endothelial tube formation via homotypic interactions. Required for normal organization of the lymph vessel network. Required for normal hematopoietic stem cell engraftment in the bone marrow. Plays a role in hematopoiesis; required for normal numbers of hematopoietic stem cells in bone marrow. Promotes in vitro osteoblast proliferation and differentiation (By similarity). Promotes neurite extension, axon growth and axon guidance; axons grow preferentially on surfaces that contain ALCAM (By similarity). Mediates outgrowth and pathfinding for retinal ganglion cell axons (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell projection, axon Cell projection, dendrite Note=Detected at the immunological synapse, i.e, at the contact zone between antigen- presenting dendritic cells and T-cells. Colocalizes with CD6 and the TCR/CD3 complex at the immunological synapse.


FUNCTION: This protein is one of many from the eggshell of the gypsy moth. SIMILARITY: Belongs to the chorion protein family.


FUNCTION: Transcription factor that binds to GC box promoter elements. Selectively activates mRNA synthesis from genes containing tandem repeats of GC boxes but represses genes with a single GC box. Acts as an epidermal circadian transcription factor regulating keratinocyte proliferation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.


FUNCTION: Required for tolerance to alcohol. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic. Accumulates in the nucleus specifically upon alcohol stress. Shuttles between the nucleus and the cytoplasm in a XPO1-dependent manner.


FUNCTION: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Nucleus. SIMILARITY: Belongs to the WD repeat ARPC1 family.


FUNCTION: Transcription factor. Binds to the DNA sequence 5'-AACAAT-3'. Acts downstream of vegt and upstream of nodal signaling to promote endodermal and mesodermal differentiation by promoting vegt-induced expression of both endodermal genes (including endodermin) and mesodermal genes (including snai1/snail and snai2/slug). Induces expression of multiple nodal genes (including nodal, nodal2, nodal4, nodal5 and nodal6) and binds directly to sites within the promoter of the nodal5 gene. The endodermal and mesodermal specification pathways then interact to initiate cardiogenesis. Acts partially redundantly with sox18 during cardiogenesis. Also acts as an antagonist of beta- catenin signaling. Regulates (possibly indirectly) development of the pronephros, the functional larval kidney. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Binds to human plasminogen (and plasmin) via its kringle repeats. Also binds to albumin, immunoglobulin G and fibrinogen. Could provide the bacteria with a mechanism for invasion, as streptococcal- bound plasmin could permit tissue penetration. SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor. SIMILARITY: Belongs to the M protein family.


SUBCELLULAR LOCATION: Secreted Note=Secreted via the ESX-3 / type VII secretion system (T7SS). SIMILARITY: Belongs to the WXG100 family. CFP-10 subfamily.


FUNCTION: Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and subsequent activation of ERN1/IRE1 (By similarity). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen Melanosome Cytoplasm Cell surface. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (By similarity). Localizes to the cell surface in epithelial cells; high levels of free iron promotes cell surface localization (By similarity). SIMILARITY: Belongs to the heat shock protein 70 family.


FUNCTION: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit of the SDH catalytic dimer. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the SDHAF2 family.


FUNCTION: Lysozymes have primarily a bacteriolytic function. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 22 family.


FUNCTION: Required for pre-mRNA splicing as component of the spliceosome (PubMed:11991638). Plays a redundant role with MAGOHB as core component of the exon junction complex (EJC) and in the nonsense- mediated decay (NMD) pathway (PubMed:23917022). The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense- mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the function is different from the established EJC assembly. FUNCTION: Required for pre-mRNA splicing as component of the spliceosome. Plays a redundant role with MAGOHB as core component of the exon junction complex (EJC) and in the nonsense-mediated decay (NMD) pathway. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). The MAGOH-RBM8A heterodimer inhibits the ATPase activity of EIF4A3, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The MAGOH-RBM8A heterodimer interacts with the EJC key regulator PYM1 leading to EJC disassembly in the cytoplasm and translation enhancement of EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S preinitiation complex. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms; the function is different from the established EJC assembly. SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm Note=Detected in granule-like structures in the dendroplasm (By similarity). Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles (PubMed:19324961). SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm Note=Detected in granule-like structures in the dendroplasm (PubMed:16275927). Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm Note=Detected in granule-like structures in the dendroplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles. SIMILARITY: Belongs to the mago nashi family.


FUNCTION: Receptor for relaxins. The activity of this receptor is mediated by G proteins leading to stimulation of adenylate cyclase and an increase of cAMP. Binding of the ligand may also activate a tyrosine kinase pathway that inhibits the activity of a phosphodiesterase that degrades cAMP (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Probable endonuclease involved in intron homing. Encoded in the group-I intron of the subunit rRNA-encoding gene (rrnL), it generates a staggered cut with 4-nt (CTCG) 3'-OH overhangs 2 bp downstream from the intron insertion site. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the LAGLIDADG endonuclease family.


FUNCTION: May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly (By similarity). Binds to membranes enriched in phosphatidylinositol 3- phosphate (PtdIns(3)P). Plays an important role in protein trafficking. SUBCELLULAR LOCATION: Golgi apparatus Cytoplasmic vesicle, clathrin-coated vesicle Note=Localizes also to a novel cellular compartment, the 'delta compartment', characterized by colocalization of EPSIN2 and DELTA-ADR. SIMILARITY: Belongs to the epsin family.


FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the antibiotic 2,4-dihydroxy-3-methyl-6- (2-oxopropyl)benzaldehyde (DHMBA) and its derivatives (PubMed:22510154, PubMed:23001671). The direct non-reducing polyketide synthase dbaI product is 2,4-dihydroxy-3-methyl-6-(2-oxopropyl)benzaldehyde (DHMBA), produced by condensation of one acetyl-CoA starter unit with 4 malonyl- CoA units and one methylation step (PubMed:22510154). The FAD-dependent monooxygenase dbaH is responsible for the synthesis of yellow pigments derived from the oxidation of DHMBA (PubMed:23001671). The roles of dbaB, C, E and F have still to be determined (Probable). SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.


FUNCTION: Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post- translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Note=Secreted into the extracellular matrix as a chondroitin sulfate proteoglycan (CSPG). SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum. SIMILARITY: Belongs to the leprecan family.


FUNCTION: Catalyzes the formation of 2'-nucleotide products from 2',3'- cyclic substrates (PubMed:6272743). May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin (By similarity). SUBCELLULAR LOCATION: Membrane; Lipid- anchor Melanosome Note=Firmly bound to membrane structures of brain white matter. SIMILARITY: Belongs to the 2H phosphoesterase superfamily. CNPase family.


FUNCTION: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA), formerly called psiRNA (prokaryotic silencing) in this organism. Part of the Cmr ribonucleoprotein complex which has divalent cation- dependent endoribonuclease activity specific for ssRNA complementary to the crRNA (target RNA), generating 5' hydroxy- and 3' phosphate or 2'- 3' cyclic phosphate termini (PubMed:19945378). Cmr4 is probably the subunit that cleaves target RNA. Cmr complex does not cleave ssDNA complementary to the crRNA. Cleavage of invading RNA is guided by the crRNA; substrate cleavage occurs a fixed distance (14 nt) from the 3' end of the crRNA. In vitro reconstitution shows Cmr1-2 and Cmr5 are not absolutely necessary for target cleavage. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the CRISPR system Cmr1 family.


FUNCTION: Involved in viral RNA replication.


FUNCTION: Required for pre-mRNA splicing and maintenance of stable U6 small nuclear RNA levels. Implicated in the formation of stable and biologically active snRNP structures. As part of the U4/U6.U5 tri-snRNP particle, dispensible for spliceosome assembly, but required for conformational changes, which result in U4 snRNA release and the subsequent catalytic activation of the spliceosome (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the PRP38 family.


FUNCTION: Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon. KdpD may function as a membrane-associated protein kinase that phosphorylates KdpE in response to environmental signals (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: In the central section; belongs to the universal stress protein A family.


FUNCTION: This recombinant serine protease inhibitor inhibits both trypsin (Ki=2.4 nM) and chymotrypsin (Ki=23 nM) (PubMed:17447883). It may also inhibit the TRPV1 receptor, a receptor of the pain pathway (By similarity). In vivo, shows anti-histamine activity, since it dose- dependently weakens the clinical manifestation of the allergic reaction induced by histamine injection. In vivo, does not show toxicity to mice by intraperitoneal injection (PubMed:17447883). SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the venom Kunitz-type family. Sea anemone type 2 potassium channel toxin subfamily.


FUNCTION: Part of the binding-protein-dependent transport system for L- arabinose. Probably responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily.


FUNCTION: Required for the production of circadian rhythms. The biological cycle depends on the rhythmic formation and nuclear localization of the TIM-PER complex. Light induces the degradation of TIM, which promotes elimination of PER. Nuclear activity of the heterodimer coordinatively regulates PER and TIM transcription through a negative feedback loop. Behaves as a negative element in circadian transcriptional loop. Does not appear to bind DNA, suggesting indirect transcriptional inhibition (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm, perinuclear region Note=Nuclear at specific periods of the day. First accumulates in the perinuclear region about one hour before translocation into the nucleus. Interaction with per is required for nuclear localization. SIMILARITY: Belongs to the timeless family.


SUBCELLULAR LOCATION: Secreted Note=Secreted by the lacrimal gland into tears. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.


FUNCTION: Required for preprotein translocation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SEC62 family.


FUNCTION: May be required for disulfide bond formation in some proteins. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.


FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Probable component of kinase complex containing smg-1 and recruited to stalled ribosomes. SIMILARITY: Belongs to the SMG9 family.


FUNCTION: May be involved in the formation or repair of [Fe-S] clusters present in iron-sulfur proteins. SIMILARITY: Belongs to the NifU family.


FUNCTION: Regulatory transcriptional protein, which trans-activates gene expression from early baculovirus promoters. Can also trans- activate its own promoter, suggesting that it is autoregulated during normal infection of insect cells. SIMILARITY: Belongs to the nucleopolyhedrovirus IE-1 protein family.


FUNCTION: Transcriptional factor involved in regulation of membrane lipid biosynthesis by repressing genes involved in fatty acid and phospholipid metabolism. SIMILARITY: Belongs to the FapR family.


FUNCTION: S-adenosyl-L-methionine-dependent protein-lysine N- methyltransferase that trimethylates 60S ribosomal protein L12 (rpl1201 and rpl1202) at 'Lys-4' and may dimethylate L12 also at 'Lys-40' and 'Lys-41'. Overexpression causes a severe growth defect. Has a role in meiosis. SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. RKM2 family.


FUNCTION: Capsid polyprotein VP90: self-assembles to form an icosahedral T=3 capsid. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the astroviridae capsid polyprotein family.


FUNCTION: Transcriptional activator of the Yersinia virulence regulon.


SIMILARITY: Belongs to the TTC38 family.


FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATPase alpha/beta chains family.


SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.


FUNCTION: Cell surface receptor that plays a functionally redundant role in the inhibition of neurite outgrowth mediated by MAG (By similarity). Plays a functionally redundant role in postnatal brain development (PubMed:27339102). Contributes to normal axon migration across the brain midline and normal formation of the corpus callosum (PubMed:27339102). Does not seem to play a significant role in regulating axon regeneration in the adult central nervous system (PubMed:22406547). Protects motoneurons against apoptosis; protection against apoptosis is probably mediated by MAG (PubMed:26335717). Like other family members, plays a role in restricting the number dendritic spines and the number of synapses that are formed during brain development (PubMed:22325200). Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton (PubMed:22325200). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Membrane raft Cell projection, dendrite Cell projection, axon Perikaryon Note=Localized to the surface of neurons, including axons. Detected close to synapses, but is excluded from synapses. SIMILARITY: Belongs to the Nogo receptor family.


FUNCTION: Glycosyltransferase that mediates the glucosylation of anthocyanidin 3-O-glucosides to yield anthocyanidin 3-O-sophorosides. 3-O-sophoroside derivatives are required for the color of flowers. SIMILARITY: Belongs to the UDP-glycosyltransferase family.


FUNCTION: Binds to the sigma-S subunit of RNA polymerase, activating expression of sigma-S-regulated genes. Stimulates RNA polymerase holoenzyme formation and may bind to several other sigma factors, such as sigma-70 and sigma-32. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Crl family.


FUNCTION: Transcriptional regulator of the pepQ gene for prolidase.


FUNCTION: Serine protease inhibitor. Inhibits trypsin, elastase, plasmin and kallikrein.


FUNCTION: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5- phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family.


FUNCTION: Catalyzes the transamination of phenylalanine, tyrosine and tryptophan. Shows virtually no activity towards aspartic acid, alanine, valine or isoleucine. SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: May play a role in fatty acid biosynthesis and insulin sensitivity. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.


SIMILARITY: Belongs to the CSN12 family.


FUNCTION: This vanadium-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family.


FUNCTION: Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3- ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane during regulated or polarized secretion. Involved in polarized cell growth and organ morphogenesis. During cytokinesis, involved in cell plate initiation, cell plate maturation and formation of new primary cell wall. SUBCELLULAR LOCATION: Cytoplasm, cytosol Note=Localized to globular structures in the perinuclear region. SIMILARITY: Belongs to the SEC15 family.


SIMILARITY: Belongs to the peptidase S16 family.


FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Required for activated transcription of the MtnA gene. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 31 family.


SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: To yeast YML093w.


FUNCTION: Component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (PubMed:29911972). Required for internalization of the GABA receptor GABRA1 from the cell membrane via endosomes and subsequent GABRA1 degradation (By similarity). Acts as a mediator of cell spreading and cytoskeletal responses to the extracellular matrix component THBS1 (PubMed:18710924). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytosol Nucleus, nucleoplasm Cell projection, ruffle Cytoplasm, cell cortex Synapse Postsynapse Note=Colocalizes with GABRA1 at synapses and in postsynaptic regions. Colocalizes with actin fibers in the cell cortex.


FUNCTION: A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit has ssDNA-dependent ATPase and 5'-3' helicase activity. When added to pre- assembled RecBC greatly stimulates nuclease activity and augments holoenzyme processivity. Negatively regulates the RecA-loading ability of RecBCD. SIMILARITY: Belongs to the RecD family.


FUNCTION: Acts as a positive regulator of ciliary hedgehog signaling (By similarity). Plays a role in ciliogenesis (By similarity). Plays an important role in the mitochondrial function and is essential for maintaining mitochondrial morphology and inner membrane ultrastructure (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Nucleus Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the CIBAR family.


FUNCTION: One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Acts to efflux copper or a copper complex. It is possible that YfmO could contribute to copper resistance. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily.


FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. Displays trypsin-like substrate specificity and shows activity towards casein, gelatin, fibronectin and IGFBP3. SIMILARITY: Belongs to the peptidase S1 family. Kallikrein subfamily.


FUNCTION: Mating ciliate pheromones (or gamones) are diffusible extracellular communication signals that distinguish different intraspecific classes of cells commonly referred to as 'mating types'. They prepare the latter for conjugation by changing their cell surface properties. SUBCELLULAR LOCATION: Secreted.


FUNCTION: This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family.


FUNCTION: Acts as a GTPase activator for the Rac-type GTPase by converting it to an inactive GDP-bound state.


FUNCTION: The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase. SIMILARITY: Belongs to the enterotoxin A family.


FUNCTION: Serine/threonine-protein kinase likely to be involved in many cellular processes. SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic vesicle, secretory vesicle, microneme Secreted Host cell surface. SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily.


FUNCTION: Microtubule-binding protein required to ensure proper cell division and nuclear envelope reassembly by sequestering the endoplasmic reticulum away from chromosomes during mitosis. Probably acts by clearing the endoplasmic reticulum membrane from metaphase chromosomes. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DP1 family.


FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose. SIMILARITY: Belongs to the arabinose isomerase family.


FUNCTION: Necessary for the formation of a functional phosphodiesterase holoenzyme (By similarity). Involved in retinal circadian rhythm photoentrainment via modulation of UVA and orange light-induced phase- shift of the retina clock (By similarity). May participate in processes of transmission and amplification of the visual signal (By similarity). FUNCTION: Rod-specific cGMP phosphodiesterase that catalyzes the hydrolysis of 3',5'-cyclic GMP (By similarity). Necessary for the formation of a functional phosphodiesterase holoenzyme (By similarity). Involved in retinal circadian rhythm photoentrainment via modulation of UVA and orange light-induced phase-shift of the retina clock (By similarity). May participate in processes of transmission and amplification of the visual signal (By similarity). SUBCELLULAR LOCATION: Membrane; Lipid- anchor Cell projection, cilium, photoreceptor outer segment. SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.


FUNCTION: Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family.


FUNCTION: Major component of the transverse central element of synaptonemal complexes (SCS), formed between homologous chromosomes during meiotic prophase. Requires SYCP1 in order to be incorporated into the central element. May have a role in the synaptonemal complex assembly, stabilization and recombination. SUBCELLULAR LOCATION: Nucleus Chromosome Note=Associates with chromatin. In prophase I stage of meiosis, localizes in the transverse central elements of the central region between lateral elements of the synaptonemal complexes. Found only where the chromosome cores are synapsed. Colocalizes with SYCE2 in the central elements. SIMILARITY: Belongs to the SYCE family.


FUNCTION: Specifically catalyzes the dephosphorylation of N- acetylmuramate 6-phosphate (MurNAc-6P) to MurNac. Is involved in peptidoglycan recycling as part of a cell wall recycling pathway that bypasses de novo biosynthesis of the peptidoglycan precursor UDP- MurNAc. Plays a role in intrinsic resistance to fosfomycin, which targets the de novo synthesis of UDP-MurNAc. Shows a very low activity on GlcNAc-6P, and neither alpha-1-phosphorylated MurNAc, GlcNAc, or glucose nor glucosamine-6P or glucose-6P can be used as a substrate. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family. Phosphatase MupP subfamily.


FUNCTION: Catalyzing the conversion of tetracenomycin F2 to tetracenomycin F1.


FUNCTION: May be involved in follicular development. Oocyte-specific growth/differentiation factor that stimulates folliculogenesis and granulosa cell (GC) growth. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the TGF-beta family.


FUNCTION: DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA. APN1 accounts for > 97% of both apurinic/apyrimidinic (AP) endonuclease and DNA 3'-repair diesterase activities. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the AP endonuclease 2 family.


FUNCTION: Prolyl hydroxylase that mediates hydroxylation of proline residues in target proteins, such as PKM, TELO2, ATF4 and HIF1A (PubMed:24809345). Target proteins are preferentially recognized via a LXXLAP motif (By similarity). Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4- hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins (By similarity). Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C- terminal, CODD) of HIF1A (By similarity). Also hydroxylates HIF2A (By similarity). Has a preference for the CODD site for both HIF1A and HIF2A (By similarity). Hydroxylation on the NODD site by EGLN3 appears to require prior hydroxylation on the CODD site (By similarity). Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex (By similarity). Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy- inducible genes (By similarity). ELGN3 is the most important isozyme in limiting physiological activation of HIFs (particularly HIF2A) in hypoxia (By similarity). Also hydroxylates PKM in hypoxia, limiting glycolysis (By similarity). Under normoxia, hydroxylates and regulates the stability of ADRB2. Regulator of cardiomyocyte and neuronal apoptosis (By similarity). In cardiomyocytes, inhibits the anti- apoptotic effect of BCL2 by disrupting the BAX-BCL2 complex (By similarity). In neurons, has a NGF-induced proapoptotic effect, probably through regulating CASP3 activity (By similarity). Also essential for hypoxic regulation of neutrophilic inflammation (PubMed:21317538). Plays a crucial role in DNA damage response (DDR) by hydroxylating TELO2, promoting its interaction with ATR which is required for activation of the ATR/CHK1/p53 pathway (By similarity). Also mediates hydroxylation of ATF4, leading to decreased protein stability of ATF4 (PubMed:24809345). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Colocalizes with WDR83 in the cytoplasm.


FUNCTION: DNA glycosylase with broad substrate specificity. Can remove uracil from double-stranded DNA containing either a U/G, U/A, U/C or U/T base pair (PubMed:12000829, PubMed:17870091, PubMed:24838246). Can also excise hypoxanthine from double-stranded DNA containing G/I, T/I, and A/I base pairs, xanthine from both double-stranded and single stranded DNA, thymine from G/T mismatched DNA, 5'-hydroxymethyluracil and 5'-fluorouracil (PubMed:17870091, PubMed:24838246). SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily. Type 5 (UDGb) family.


FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1. SIMILARITY: Belongs to the thiamine-monophosphate kinase family.


FUNCTION: The H2 subclass of histamine receptors mediates gastric acid secretion. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Transcription factor that binds GC and GT boxes in the D1A, D2 and D3 dopamine receptor promoters and displaces Sp1 and Sp3 from these sequences. It modulates dopaminergic transmission in the brain by repressing or activating transcription from several different promoters depending on cellular context. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.


FUNCTION: Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur donor by being thiocarboxylated (-COSH) at its C-terminus by uba4. After interaction with MOCS2B, the sulfur is then transferred to precursor Z to form molybdopterin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MoaD family. MOCS2A subfamily.


FUNCTION: This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B. FUNCTION: This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the cystatin family.


FUNCTION: Required for production of the bacteriocin subtilosin. Could catalyze some step in the processing of presubtilosin (By similarity). SIMILARITY: Belongs to the peptidase M16 family.


FUNCTION: Major facilitator transporter involved in extracellular siderophore uptake (PubMed:20507510). Gibberella zeae produces extracellular coprogen-type siderophores as well as the intracellular siderophore ferricrocin (PubMed:17056706). The role of extracellular siderophores is to supply iron to the fungus during plant infection, and the intracellular ferricrocin is required for intracellular iron distribution and storage with a crucial role in ascus and ascospore development (PubMed:17056706, PubMed:17043871, PubMed:17601875). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily.


FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. SIMILARITY: Belongs to the SEC15 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 a 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. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 49 kDa subunit family.


FUNCTION: Promotes leaf senescence mediated by abscisic acid (ABA), salicylic acid (SA) and jasmonic acid (MeJA), probably though the induction of expression of senescence-associated genes (SAGs) and defense-related genes. SUBCELLULAR LOCATION: Cytoplasm Note=Present in cytoplasmic foci. SIMILARITY: Belongs to the LARP family.


FUNCTION: Probable DNA helicase that may play a role in DNA repair during meiosis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MCM family.


FUNCTION: Might contribute to the loading of the ESCRT machinery. SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the TOM1 family.


FUNCTION: Part of the ABC transporter complex GsiABCD involved in glutathione import. Responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Glutathione importer (TC 3.A.1.5.11) family.


FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the universal ribosomal protein uS7 family.


FUNCTION: HMG-CoA synthase; part of the gene cluster that mediates the biosynthesis of 1233A, a natural compound known as an inhibitor of HMG- CoA synthase in the mevalonate pathway and with antibacterial and antifungal activities (PubMed:32139880). This enzyme condenses acetyl- CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase (By similarity). As part of the 1233A biosynthesis cluster, is involved in conferring self-resistance to 1233A (PubMed:32139880). SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase family.


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


FUNCTION: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane. SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the VPS27 family.


FUNCTION: Heterodimer with SLC3A2, that functions as an antiporter by mediating the exchange of extracellular anionic L-cystine and intracellular L-glutamate across the cellular plasma membrane (By similarity). Provides L-cystine for the maintenance of the redox balance between extracellular L-cystine and L-cysteine and for the maintenance of the intracellular levels of glutathione that is essential for cells protection from oxidative stress (By similarity). The transport is sodium-independent, electroneutral with a stoichiometry of 1:1, and is drove by the high intracellular concentration of L-glutamate and the intracellular reduction of L- cystine. In addition, mediates the import of L-kynurenine leading to anti-ferroptotic signaling propagation required to maintain L-cystine and glutathione homeostasis. Moreover, mediates N-acetyl-L-cysteine uptake into the placenta leading to subsequently down-regulation of pathways associated with oxidative stress, inflammation and apoptosis. In vitro can also transport L-aspartate (By similarity). May participate in astrocyte and meningeal cell proliferation during development and can provide neuroprotection by promoting glutathione synthesis and delivery from non-neuronal cells such as astrocytes and meningeal cells to immature neurons. Controls the production of pheomelanin pigment directly (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell projection, microvillus membrane; Multi- pass membrane protein Note=Localized to the microvillous membrane of the placental syncytiotrophoblast. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family.


FUNCTION: Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (DXXLL) motif. Mediates export of the GPCR receptor ADRA2B to the cell surface. Involved in BACE1 transport and sorting as well as regulation of BACE1 protein levels. Regulates retrograde transport of BACE1 from endosomes to the trans-Golgi network via interaction through the VHS motif and dependent of BACE1 phosphorylation. Modulates BACE1 protein levels independently of the interaction between VHS domain and DXXLL motif through recognition of ubiquitination (By similarity). Key player in a novel DXXLL-mediated endosomal sorting machinery to the recycling pathway that targets NTRK1 to the plasma membrane (PubMed:26446845). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein Endosome membrane; Peripheral membrane protein Early endosome membrane; Peripheral membrane protein Recycling endosome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the GGA protein family.


SIMILARITY: Belongs to the asfivirus C84L family.


FUNCTION: Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as microRNAs (miRNAs) and represses the translation of mRNAs which are complementary to them. Lacks endonuclease activity and does not appear to cleave target mRNAs. Also required for RNA-directed transcription and replication of the human hapatitis delta virus (HDV). SUBCELLULAR LOCATION: Cytoplasm, P-body. SIMILARITY: Belongs to the argonaute family. Ago subfamily.


SIMILARITY: Belongs to the TMA7 family.


FUNCTION: Probably part of the binding-protein-dependent transport system y4mIJK. This system probably transports a sugar. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.


FUNCTION: Involved in the biosynthesis of forosamine ((4- dimethylamino)-2,3,4,6-tetradeoxy-alpha-D-threo-hexopyranose), a highly deoxygenated sugar component of several bioactive natural products such as the insecticidal spinosyns A and D (PubMed:11358695, PubMed:18345667). Catalyzes C-3 deoxygenation of dTDP-4-keto-2,6- dideoxy-alpha-D-glucose to yield dTDP-4-keto-2,3,6-trideoxy-D-glucose via a combined transamination-deoxygenation reaction (PubMed:18345667). The catalysis is initiated by a transamination step in which pyridoxal 5'-phosphate (PLP) is converted to pyridoxamine 5'-phosphate (PMP) in the presence of L-glutamate (PubMed:18345667). This coenzyme then forms a Schiff base with dTDP-4-keto-2,6-dideoxy-alpha-D-glucose and the resulting adduct undergoes a PMP-mediated beta-dehydration reaction to give a sugar enamine intermediate, which after a 2 electrons reduction and hydrolysis yields dTDP-4-keto-2,3,6-trideoxy-D-glucose as a product (PubMed:18345667). Requires cellular reductase (ferredoxin or flavodoxin reductase) rather than a specific partner reductase (PubMed:18345667). L-glutamate is 20-fold more efficient than L- aspartate as an amino donor (PubMed:18345667). In the absence of an electron source and in the presence of L-glutamate, catalyzes a transamination reaction, converting dTDP-4-keto-2,6-dideoxy-alpha-D- glucose to dTDP-4-amino-2,4,6-trideoxy-D-glucose (PubMed:18345667). SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.


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


FUNCTION: E3 ubiquitin-protein ligase that cooperates with the microRNAs (miRNAs) machinery and promotes embryonic stem cells proliferation and maintenance (Probable). Binds to miRNAs and associates with AGO2, participating in post-transcriptional repression of transcripts such as CDKN1A (By similarity). In addition, participates in post-transcriptional mRNA repression in a miRNA independent mechanism (PubMed:23125361). Facilitates the G1-S transition to promote rapid embryonic stem cell self-renewal by repressing CDKN1A expression. Required to maintain proliferation and prevent premature differentiation of neural progenitor cells during early neural development: positively regulates FGF signaling by controlling the stability of SHCBP1 (By similarity). Specific regulator of miRNA biogenesis. Binds to miRNA MIR29A hairpin and postranscriptionally modulates MIR29A levels, which indirectly regulates TET proteins expression (PubMed:28431233). SUBCELLULAR LOCATION: Cytoplasm, P-body. SIMILARITY: Belongs to the TRIM/RBCC family.


FUNCTION: Binds zinc. Could be an important component of the zinc- balancing mechanism (By similarity). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the ZraP family.


FUNCTION: May regulate plasma membrane ATPase activity. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the plant proton pump-interactor protein family.


SIMILARITY: Belongs to the LovG family.


FUNCTION: Inhibits voltage-gated potassium channels (IC(50)=14.42 nM for rKCNA1/Kv1.1, IC(50)=80.4 nM for rKCNA2/Kv1.2, IC(50)=7.76 nM for rKCNA6/Kv1.6, IC(50)=13.12 nM for hKCNA3/Kv1.3, and IC(50)=49.14 nM for insect Shaker IR). Binds the Shaker IR channels in a voltage- independent manner. SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the sea anemone type 1 potassium channel toxin family. Type 1b subfamily.


FUNCTION: Promotes sorting of SMDT1/EMRE in mitochondria by ensuring its maturation. Interacts with the transit peptide region of SMDT1/EMRE precursor protein in the mitochondrial matrix, leading to protect it against protein degradation by YME1L1, thereby ensuring SMDT1/EMRE maturation by the mitochondrial processing peptidase (PMPCA and PMPCB). SUBCELLULAR LOCATION: Mitochondrion matrix.


FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that is essential for the transition from metaphase to anaphase in mitosis. Involved in both degradation of proteins responsible for maintaining sister chromatid cohesion at the onset of anaphase and of mitotic cyclins A and B at the exit of mitosis. Acts by initiating polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.


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


FUNCTION: NADPH oxidase which constitutively produces superoxide upon formation of a complex with CYBA/p22phox. Plays a role in the biogenesis of otoconia/otolith, which are crystalline structures of the inner ear involved in the perception of gravity (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.


FUNCTION: Required for transport of secretory proteins from the Golgi complex. Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes in vitro (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the SFH family.


FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids. This isoform may play a role in regulating the transport, accumulation, and compartmentation of zinc in the hippocampus. SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family.


FUNCTION: Component of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form the 43S pre-initiation complex (43S PIC). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF-2B. SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family.


FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). SIMILARITY: Belongs to the ALAD family.


SUBCELLULAR LOCATION: Endoplasmic reticulum Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily.


FUNCTION: Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein.


FUNCTION: Putative tyrosine recombinase. Not involved in the cutting and rejoining of the recombining DNA molecules on dif(SL) site. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'phage' integrase family. XerD-like subfamily.


FUNCTION: Regulates voltage-gated potassium channels assembled from KCNA1, KCNA4 and KCNAB1. It slows down channel inactivation by precluding channel closure mediated by the KCNAB1 subunit. Ligand for ADAM22 that positively regulates synaptic transmission mediated by AMPA-type glutamate receptors. Plays a role in suppressing the production of MMP1/3 through the phosphatidylinositol 3-kinase/ERK pathway (By similarity). SUBCELLULAR LOCATION: Secreted Synapse Cytoplasm.


FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in trehalose transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.


FUNCTION: Very long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (PubMed:7668252, PubMed:9461620, PubMed:18227065, PubMed:9839948, PubMed:9599005). The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl- CoA (PubMed:7668252, PubMed:9461620, PubMed:18227065, PubMed:9839948). Among the different mitochondrial acyl-CoA dehydrogenases, very long- chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 12 to 24 carbons long primary chains (PubMed:21237683, PubMed:9839948). SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion inner membrane; Peripheral membrane protein. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.


FUNCTION: Potentially involved in docking of synaptic vesicles at presynaptic active zones (PubMed:7901002). May mediate Ca(2+)- regulation of exocytosis acrosomal reaction in sperm (By similarity). FUNCTION: Potentially involved in docking of synaptic vesicles at presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm (By similarity). FUNCTION: Potentially involved in docking of synaptic vesicles at presynaptic active zones (By similarity). May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Note=Colocalizes with Lamin A/C and NuMA in interphasic nuclei, and with NuMA and gamma- tubulin in the pericentrosomal region of the mitotic spindle in dividing cells. SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Single-pass type IV membrane protein. SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the syntaxin family.


FUNCTION: Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Plays a role in the complex assembly and recruits GspL resulting in a stable complex in the inner membrane. Provides thus a link between the energy-providing GspE protein in the cytoplasm and the rest of the T2SS machinery. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the GSP M family.


SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the peptidase C1 family.


FUNCTION: Serine protease inhibitor which displays weak inhibitory activity against trypsin (By similarity). May play a role in facial patterning during embryonic development (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family.


FUNCTION: Is able to bind two actin monomers at high concentrations of G-actin. Inhibits actin polymerization by sequestering G-actin and stabilizing actin dimers (By similarity).


FUNCTION: Specific component of the STT3A-containing form of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:31831667). N- glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. May be involved in N-glycosylation of APP (amyloid-beta precursor protein). Can modulate gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1. SUBCELLULAR LOCATION: Endoplasmic reticulum Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the OSTC family.


FUNCTION: May be involved in ulvan degradation (Probable). Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl) (Probable). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor.


FUNCTION: Essential for natural transformation. Could be a transporter involved in DNA uptake. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: To B.subtilis ComEC, H.influenzae REC2, and E.coli YcaI.


SIMILARITY: Belongs to the MEMO1 family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the scoloptoxin-13 family.


FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients. SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane protein Cell membrane, sarcolemma; Multi-pass membrane protein Cell projection, axon Melanosome. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily.


FUNCTION: Involved in the ethylmalonyl-CoA pathway for acetate assimilation. Catalyzes the reversible condensation of glyoxylate and acetyl-CoA to L-malyl-CoA and the reversible condensation of glyoxylate and propionyl-CoA to beta-methylmalyl-CoA. FUNCTION: Involved in the ethylmalonyl-CoA pathway for acetate assimilation. Catalyzes the reversible condensation of glyoxylate and acetyl-CoA to L-malyl-CoA and the reversible condensation of glyoxylate and propionyl-CoA to yield beta-methylmalyl-CoA. SIMILARITY: Belongs to the HpcH/HpaI aldolase family.


FUNCTION: Possesses beta-glucosidase activity toward 4-methyl- umbelliferyl-beta-D-glucoside in vitro. Possesses myrosinase activity toward indol-3-yl-methylglucosinolate (I3M) and 4-methoxy-indol-3-yl- methylglucosinolate (4MO-I3M) in vivo (PubMed:19095900). Component of an inducible preinvasion resistance mechanism that prevents penetration of the nonhost fungal species B.graminis and E.pisi (PubMed:16293760). Involved in indole glucosinolate (IGS) activation during pattern- triggered immunity (PTI). Functions as myrosinase for the breakdown of flg22-triggered IGS. Required for both callose deposition and glucosinolate activation during pathogen-triggered resistance (PubMed:19095898). During fungal attack, required for IGS activation that mediates broad-spectrum antifungal defense (PubMed:19095900). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the glycosyl hydrolase 1 family.


FUNCTION: Antimicrobial peptide. Active against some Gram-positive and Gram-negative bacterial strains. Active against fungus C.glabrata 090902 but not against C.albicans ATCC 12231. Shows very weak hemolytic activity against human erythrocytes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Temporin subfamily.


FUNCTION: Catalyzes the NAD-dependent oxidation and subsequent decarboxylation of D-threonate 4-phosphate to produce dihydroxyacetone phosphate (DHAP). SIMILARITY: Belongs to the PdxA family. PdxA2 subfamily.


FUNCTION: Increases viral DNA accumulation. Enhances infectivity and symptom expression (By similarity). SIMILARITY: Belongs to the geminiviridae replication enhancer protein family.


FUNCTION: Ubiquitin-like protein involved in cytoplasm to vacuole transport (Cvt), autophagy vesicles formation, mitophagy, and nucleophagy. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate functions as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes (By similarity). SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATG12 family.


FUNCTION: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (PubMed:22723690). SUBCELLULAR LOCATION: Cell projection, axon Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the intermediate filament family.


FUNCTION: Required for late and very late gene expression. May be a component of the novel RNA polymerase activity induced by baculovirus infection. SIMILARITY: Belongs to the RNA polymerase beta chain family.


FUNCTION: Involved in DNA excision repair. Initiates repair by binding to damaged sites with various affinities, depending on the photoproduct and the transcriptional state of the region. Required for UV-induced CHEK1 phosphorylation and the recruitment of CEP164 to cyclobutane pyrimidine dimmers (CPD), sites of DNA damage after UV irradiation (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the XPA family.


FUNCTION: Essential for viral replication in vivo (By similarity). Plays a role in the association of the matrix protein with the nucleocapsid, which initiates assembly and budding (By similarity). SUBCELLULAR LOCATION: Virion Host cytoplasm Host nucleus Note=Localizes in cytoplasmic inclusion bodies substructures called inclusion bodies associated granules (IBAGs). Forms a layer between the matrix and nucleocapsid. SIMILARITY: Belongs to the pneumoviridae M2-1 protein family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family. Amino acid/auxin permease (AAAP) (TC 2.A.18.6) subfamily.


FUNCTION: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (PubMed:15140988). Required for canonical autophagy (macroautophagy), non-canonical autophagy as well as for mitophagy. The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins to reveal a C-terminal glycine. Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy. Protease activity is also required to counteract formation of high- molecular weight conjugates of ATG8 proteins (ATG8ylation): acts as a deubiquitinating-like enzyme that removes ATG8 conjugated to other proteins, such as ATG3. In addition to the protease activity, also mediates delipidation of ATG8 family proteins. Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy. Also involved in non-canonical autophagy, a parallel pathway involving conjugation of ATG8 proteins to single membranes at endolysosomal compartments, by catalyzing delipidation of ATG8 proteins conjugated to phosphatidylserine (PS). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytosol Cytoplasmic vesicle, autophagosome Endoplasmic reticulum Mitochondrion Note=Mainly localizes to the cytoplasm, including cytosol. SIMILARITY: Belongs to the peptidase C54 family.