FUNCTION: In epithelial cells, the heterodimer gE/gI is required for the cell-to-cell spread of the virus, by sorting nascent virions to cell junctions. Once the virus reaches the cell junctions, virus particles can spread to adjacent cells extremely rapidly through interactions with cellular receptors that accumulate at these junctions. Implicated in basolateral spread in polarized cells. In neuronal cells, gE/gI is essential for the anterograde spread of the infection throughout the host nervous system. Together with US9, the heterodimer gE/gI is involved in the sorting and transport of viral structural components toward axon tips. SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane protein Host cell membrane; Single-pass type I membrane protein Host cell junction Host Golgi apparatus membrane; Single-pass type I membrane protein Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). The heterodimer gE/gI then redistribute to cell junctions to promote cell-cell spread later in the infection (By similarity). SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein I family.


SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the alliinase family.


FUNCTION: The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the variable large protein (Vlp) family. Beta subfamily.


FUNCTION: Small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import. SIMILARITY: Belongs to the GPN-loop GTPase family.


FUNCTION: Glucuronyl hydrolase involved in ulvan degradation. 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). Unsaturated 3S- rhamnoglycuronyl hydrolase works together with ulvan lyases to fully degrade the ulvan polymer, catalyzing specifically the cleavage of the unsaturated 4-deoxy-L-threo-hex-4-enopyranosiduronic acid (deltaUA) of deltaUA-Rha3S disaccharides and deltaUA-Rha3S-Xyl-Rha3S tetrasaccharides, the end products of the ulvan lyase reaction. Also hydrolases deltaUA-Rha3S-IduA-Rha3S and deltaUA-Rha3S-GlcA-Rha3S tetrasaccharidestetrasaccharides. Prefers tetrasaccharides over disaccharides and prefers an uronic residue at subsite +2. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the glycosyl hydrolase 105 family.


FUNCTION: Negative regulator of epidermal growth factor receptor (EGFR) signaling. SIMILARITY: Belongs to the lst-2 family.


FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production). SUBCELLULAR LOCATION: Cytoplasm, cytosol Membrane; Peripheral membrane protein; Cytoplasmic side.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eL40 family.


FUNCTION: Toxin with unknown function in healthy organisms. On glioma cells, inhibits chloride currents in a voltage-dependent manner (when tested on gliomas cells) (PubMed:17166663). Also interacts with MMP2 and significantly inhibits its catalytic activity (PubMed:21424168). May be internalized with chloride channels (probably ClC-3/CLCN3) and MMP2, thus inhibiting the chloride channels necessary for cell shrinkage and tumor propagation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Chloride channel inhibitor family.


FUNCTION: Beta-galactosidase. SIMILARITY: Belongs to the glycosyl hydrolase 2 family.


FUNCTION: Involved in copper transport. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.


FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)- enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Required for normal spermatogenesis and oogenesis (PubMed:16943775). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Chromosome Note=Localizes around sperm chromatids. SIMILARITY: Belongs to the type IB topoisomerase family.


FUNCTION: Catalyzes the conversion of UDP-D-glucuronate to a mixture of UDP-D-apiose and UDP-D-xylose. D-Apiose (3-C-hydroxymethyl-d-erythrose) is the only plant cell wall monosaccharide with a branched carbon skeleton and found in rhamnogalacturonan II (RG-II), apiogalacturonan, and several apioglycosides (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family.


FUNCTION: Possible role in phototransduction. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein.


FUNCTION: ATP-binding subunit of the mitochondrial potassium channel located in the mitochondrial inner membrane. Together with CCDC51/MITOK, forms a protein complex localized in the mitochondria that mediates ATP-dependent potassium currents across the inner membrane (that is, mitoK(ATP) channel) (By similarity). Plays a role in mitochondrial iron transport. Required for maintenance of normal cardiac function, possibly by influencing mitochondrial iron export and regulating the maturation of cytosolic iron sulfur cluster-containing enzymes (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family. Multidrug resistance exporter (TC 3.A.1.201) subfamily.


FUNCTION: Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the hemopexin family.


SIMILARITY: Belongs to the IS21/IS1162 putative ATP-binding protein family.


FUNCTION: Required for proper function of the glomerular filtration barrier. It is involved in the maintenance of a stable podocyte architecture with interdigitating foot processes connected by specialized cell-cell junctions, known as the slit diaphragm (PubMed:11416156). Is a signaling protein that needs the presence of TEC kinases to fully trans-activate the transcription factor AP-1. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Note=Predominantly located at podocyte slit diaphragm. SIMILARITY: Belongs to the immunoglobulin superfamily.


FUNCTION: May sustain the structure of the postsynaptic density (PSD). SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.


FUNCTION: Necessary for flagellar biosynthesis. May be involved in translocation of the flagellum (By similarity). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the GTP-binding SRP family.


SIMILARITY: Belongs to the UPF0523 family.


FUNCTION: Component of a binary toxin active against Culex and some Aedes mosquito larvae (PubMed:1512580, PubMed:8419297). The individual subunits are not toxic. BinAB binds to the gastric caecum and posterior midgut of C.quinquefasciatus larvae; this subunit alone binds the entire larval gut. Binary toxin internalization into host gut cells requires both proteins (PubMed:1512580). Toxic to Aedes atropalpus mosquito larvae; mortality towards both C.quinquefasciatus and A.atropalpus is maximal by 48 hours. A.aegypti is not very susceptible to this toxin (PubMed:8419297). SUBCELLULAR LOCATION: Spore, perispore. SIMILARITY: Belongs to the toxin_10 family.


SIMILARITY: Belongs to the varicellovirus ORF57 protein family.


FUNCTION: Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both RAS/MAPK and PI3K/AKT/TOR signaling cascades downstream of EGFR. Required for the RAS/MAPK signaling cascade activation upon EGFR stimulation, it also activates both signaling cascades independently of EGFR activation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FAM83 family.


SIMILARITY: Belongs to the succinylarginine dihydrolase family.


FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity). SIMILARITY: Belongs to the GatC family.


FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family.


FUNCTION: Catalyzes the incorporation of amino acid(s) into the interchain peptide bridge of peptidoglycan, using aminoacyl-tRNA as amino acid donor. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FemABX family.


FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the eukaryotic ATPase B chain family.


FUNCTION: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. May play a role in the association of MAD1 with the NPC (By similarity). SUBCELLULAR LOCATION: Nucleus, nuclear pore complex Nucleus membrane; Peripheral membrane protein Note=Tightly associated with the nuclear membrane and lamina. SIMILARITY: Belongs to the Nup35 family.


SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the MG067/MG068/MG395 family.


FUNCTION: Promotes the expression of genes involved in photosynthesis at least in dedifferentiated calli. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


FUNCTION: Converts HMG-CoA to mevalonate. SIMILARITY: Belongs to the HMG-CoA reductase family.


FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin (H2Neo) to 6-hydroxymethyl-7,8-dihydropterin (6-HMD). SIMILARITY: Belongs to the archaeal dihydroneopterin aldolase family.


SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily.


FUNCTION: Torulene dioxygenase; part of pathway that mediates the biosynthesis of neurosporaxanthin, a carboxylic apocarotenoid acting as an essential protective pigments and leading to orange pigmentation (PubMed:17493127). CarT mediates the cleavage of torulene into beta- apo-4'-carotenal, the aldehyde corresponding to the acidic neurosporaxanthin (PubMed:17493127). Is also active on other monocyclic synthetic substrates such as beta-apo-8'-carotenal and beta-apo-10'- carotenal to produce beta-apo-14'-carotenal and retinal(beta-apo-15'- carotenal), respectively (PubMed:17493127). Neurosporaxanthin is synthesized from geranyl-geranyl pyrophosphate (GGPP) through several enzymatic activities. Phytoene synthase activity performed by the bifunctional enzyme carAR first produces phytoene from geranyl-geranyl pyrophosphate (GGPP). The phytoene dehydrogenase carB then introduces 4 desaturations to lead to lycopene which is substrate of the carotene cyclase activity of carAR that leads to the production of gamma- carotene. CarB then performs a 5th desaturation reaction to yield torulene. Torulene is the substrate of the dioxidase carT that breaks the molecule, removing five carbon atoms to yield beta-apo-4'- carotenal, whereas the aldehyde dehydrogenase carD mediates the last step by converting beta-apo-4'-carotenal into neurosporaxanthin (Probable). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the carotenoid oxygenase family.


FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of flavoglaucin and congeners (including aspergin, dihydroauroglaucin and auroglaucin), prenylated salicylaldehyde derivatives carrying a saturated or an unsaturated C-7 side chain (PubMed:32134669). The PKS fogA releases the carboxylic acid (8E,10E,12E)-3,5,7-trihydroxytetradeca-8,10,12-trienoic acid as its product, as well as derivatives with one and two double bonds (PubMed:32134669). FogA is indeed able to reduce the initial triketide, thus being at least partially responsible for the differently saturated heptyl side chains of flavoglaucin congeners (PubMed:32134669). The oxidoreductases fogB, fogC and fogD modify the nascent polyketide in fogA-bound form and, together, fogA, fogB, fogC and fogD are necessary for the formation of the aromatic core and the cyclized PKS products are released as salicyl alcohols (PubMed:32134669). In particular, fogB is responsible for oxidation of a hydroxyl group or reduction of remaining double bond(s) at the C-7 residue whereas fogD is probably involved in the reductive release of the modified PKS products (PubMed:32134669). The cytochrome P450 monooxygenase fogE is then responsible for the hydroxylation at C-3 of the benzene ring (PubMed:32134669). The fogE products are substrates of the prenyltransferase fogH and the prenylated benzyl alcohols are subsequently oxidized by the fogF to produce the final aryl aldehydes flavoglaucin and congeners (PubMed:32134669). The short-chain dehydrogenase fogG does not seem to be involved in the biosynthesis of the prenylated salicylaldehyde derivatives (PubMed:32134669). SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family.


FUNCTION: The METTL3-METTL14 heterodimer forms a N6-methyltransferase complex that methylates adenosine residues at the N(6) position of some mRNAs and regulates the circadian clock, differentiation of embryonic stem cells and cortical neurogenesis. In the heterodimer formed with mettl3, mettl14 constitutes the RNA-binding scaffold that recognizes the substrate rather than the catalytic core. N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in mRNA stability and processing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the MT-A70-like family.


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


FUNCTION: Postsynaptic neurotoxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 12 (Hwtx-2) family. 02 (Hwtx-2) subfamily.


FUNCTION: Possible role in chlorophyll and/or carotenoid binding. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ELIP/psbS family.


SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the FlgA 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 spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA) (By similarity). SIMILARITY: Belongs to the CRISPR-associated protein Cas7/Cst2/DevR family. Subtype I-a/Apern subfamily.


FUNCTION: Decapping enzyme required for the removal of the 5'-end m7GpppN cap tethered to viral and host mRNAs to allow their decay in cells. May therefore accelerate viral and cellular mRNA turnover to eliminate competing host mRNAs and allow stage-specific synthesis of viral proteins. Acceleration of the turnover of cellular transcripts may even promote the shutoff of host protein synthesis. In addition to the mRNA cap, g5R also efficiently hydrolyzes diphosphoinositol polyphosphates. Down-regulation of the level of PP-InsP5 (diphosphoinositol pentakisphosphate) may play a role in viral manipulation of the cellular secretory pathway, a step necessary for the formation of virions. Binds viral and cellular poly(A) mRNAs, thereby decreasing both types of mRNAs. SUBCELLULAR LOCATION: Host rough endoplasmic reticulum Note=Accumulates at the periphery of the viral factories. SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.


FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Does not show detyrosinase or deglycylase activities from the carboxy-terminus of tubulin. FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of tubulin protein. Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of non-tubulin proteins. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, cilium basal body Note=Colocalizes with gamma- tubulin in the centrioles and with glutamylated tubulin in the basal bodies of ciliated cells. SIMILARITY: Belongs to the peptidase M14 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 (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 25 family.


FUNCTION: Catalyzes the synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) with pyridoxal 5'-phosphate as cofactor. SIMILARITY: Belongs to the group II decarboxylase family.


FUNCTION: Catalyzes the second step of the urea cycle, the condensation of carbamoyl phosphate with L-ornithine to form L-citrulline. The urea cycle ensures the detoxification of ammonia by converting it to urea for excretion. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.


FUNCTION: DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit at low temperature. Exhibits RNA-stimulated ATP hydrolysis and RNA unwinding activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DEAD box helicase family. SrmB subfamily.


SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the PP3/GlyCAM-1 family.


FUNCTION: May play a role in cell differentiation in the intestinal epithelium. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.


FUNCTION: Catalyzes the insertion of Co(2+) into sirohydrochlorin as part of the anaerobic pathway to cobalamin biosynthesis. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the insertion of Ni(2+) into sirohydrochlorin to yield Ni- sirohydrochlorin. SIMILARITY: Belongs to the CbiX family. CbiXS subfamily.


FUNCTION: It is likely that the major role of L-chain is to prevent the retention of H-chain in ER by forming the disulfide linkage. SUBCELLULAR LOCATION: Secreted.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eS21 family.


FUNCTION: Member of the two-component regulatory system WalK/WalR. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Thioesterase that has relatively broad substrate specificity, hydrolyzing primarily medium- and long-chain acyl-CoA substrates to free fatty acids and CoA. Functions in the thioesterase-dependent pathway of beta-oxidation of oleate and conjugated linoleate ((9Z,11E)- octadecadienoate or CLA), which provides all energy and carbon precursors required for the growth of E.coli. Thus, supports growth on oleate or conjugated linoleate as the sole source of carbon by hydrolyzing 3,5-tetradecadienoyl-CoA, the terminal metabolite of oleate beta-oxidation via the alternative thioesterase-dependent pathway, and 3,5-dodecadienoyl-CoA, the end product of CLA beta-oxidation, respectively. Seems to be involved in 3-hydroxyalkanoate production in E.coli. FUNCTION: Thioesterase that has relatively broad substrate specificity, hydrolyzing primarily medium- and long-chain acyl-CoA substrates to free fatty acids and CoA (PubMed:1645722, PubMed:24271180, PubMed:20547355). Functions in the thioesterase-dependent pathway of beta-oxidation of oleate and conjugated linoleate ((9Z,11E)- octadecadienoate or CLA), which provides all energy and carbon precursors required for the growth of E.coli. Thus, supports growth on oleate or conjugated linoleate as the sole source of carbon by hydrolyzing 3,5-tetradecadienoyl-CoA, the terminal metabolite of oleate beta-oxidation via the alternative thioesterase-dependent pathway, and 3,5-dodecadienoyl-CoA, the end product of CLA beta-oxidation, respectively (PubMed:18702504, PubMed:14707139). Seems to be involved in 3-hydroxyalkanoate production in E.coli (PubMed:20547355). SIMILARITY: Belongs to the C/M/P thioester hydrolase family.


FUNCTION: Nuclear export factor for BMP-specific SMAD1/5/8 that plays a critical role in terminating BMP signaling and regulating mesenchymal stem cell differentiation by blocking osteoblast differentiation to promote myogenic differention. Directly recognizes dephosphorylated SMAD1/5/8 and mediates their nuclear export in a Ran-dependent manner. SUBCELLULAR LOCATION: Nucleus Cytoplasm.


FUNCTION: Ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the motilin family.


FUNCTION: Protein-histidine N-methyltransferase that specifically mediates 3-methylhistidine (tele-methylhistidine) methylation of actin at 'His-73'. Histidine methylation of actin is required for smooth muscle contraction of the laboring uterus during delivery. Does not have protein-lysine N-methyltransferase activity and probably only catalyzes histidine methylation of actin. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Localizes mainly in the cytoplasm. SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase superfamily. SETD3 actin-histidine methyltransferase family.


FUNCTION: Plays a role in cytoplasmic trafficking of RNA. Binds to the cis-acting response element, A2RE. May be involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus Note=Component of ribonucleosomes.


FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function (By similarity). Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (By similarity). The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCTN1 (PubMed:27474409). Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes (PubMed:27474409). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm Note=Detected in the cytoplasm of pachytene spermatocytes. Localizes to the manchette in elongating spermatids. SIMILARITY: Belongs to the dynein intermediate chain family.


FUNCTION: Cytokine that acts as a regulator of the activity of Nodal/BMP pathways during the establishment of bilateral asymmetry in the head and trunk of the embryo. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the DAN family.


FUNCTION: Component of the larval cuticle.


FUNCTION: Catalyzes the transfer of the gamma-phosphate of ATP to D- galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). FUNCTION: Catalyzes the transfer of the gamma-phosphate of ATP to D- galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). To a lesser extent, is also able to phosphorylate 2-deoxy-D-galactose and D- galactosamine. Is not able to use D-galacturonic acid, D-talose, L- altrose, and L-glucose as substrates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GHMP kinase family. GalK subfamily.


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


FUNCTION: Has a dual role in the assembly of cytochrome oxidase subunit 1 (cox1). It has a regulative function on cox1 synthesis, acting as a translational activator specific for the cox1 mRNA, and it also binds to newly synthesized cox1 protein (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the MSS51 family.


FUNCTION: Involved in protein N-glycosylation. Essential for the second step of the dolichol-linked oligosaccharide pathway. Anchors the catalytic subunit ALG13 to the ER (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Nucleus membrane; Single- pass membrane protein. SIMILARITY: Belongs to the ALG14 family.


FUNCTION: May be involved in the regulation of spermatogenesis and sperm maturation. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase C chain family.


FUNCTION: May have the capacity to recognize and bind specific classes of odorants. May act as a carrier molecule, transporting odorants across the mucus layer to access receptor sites. May serve as a primary defense mechanism by recognizing and removing potentially harmful odorants or pathogenic microorganisms from the mucosa or clearing excess odorant from mucus to enable new odorant stimuli to be received (By similarity). SUBCELLULAR LOCATION: Secreted Cytoplasm. SIMILARITY: Belongs to the BPI/LBP/Plunc superfamily. BPI/LBP family.


FUNCTION: Part of an energy-coupled inorganic carbon pump; its substrate may be carbon dioxide. Expression of both dabA2 and dabB2 (DAB2) restores growth in ambient air to E.coli deleted of its carbonic anhydrase genes (called CAfree, deletion of 'can' and 'cynT'); neither dabA2 or dabB2 alone is sufficient. Rescue is pH-independent, suggesting it transports CO(2) and not carbonate ions. Together the genes allow greater than normal uptake of inorganic carbon by E.coli (PubMed:31406332). Uptake of carbon dioxide rather than bicarbonate has been suggested based on kinetic calculations (Probable). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the inorganic carbon transporter (TC 9.A.2) DabB family.


FUNCTION: Involved in transcriptional activation. Component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Involved in the accumulation of the PSII complex. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen. SIMILARITY: Belongs to the FKBP-type PPIase family.


FUNCTION: Binds nucleotic acids in vitro. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall biosynthesis and morphogenesis. Plays a key role in virulence. SUBCELLULAR LOCATION: Secreted, cell wall Membrane; Lipid-anchor, GPI-anchor Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP). SIMILARITY: Belongs to the glycosyl hydrolase 72 family.


FUNCTION: Binds to 23S rRNA. SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the universal ribosomal protein uL23 family.


FUNCTION: Binds 16S rRNA, required for the assembly of 30S particles. SUBCELLULAR LOCATION: Plastid, cyanelle. SIMILARITY: Belongs to the universal ribosomal protein uS14 family.


FUNCTION: May be a novel gestational hormone required to compensate for absence of other members of the GH/CS cluster during gestation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the somatotropin/prolactin family.


FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL20 family.


FUNCTION: ATP-dependent RNA helicase. 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). Its RNA-dependent ATPase and RNA-helicase activities are induced by MLN51/CASC3, but abolished in presence of the MAGO-Y14 heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGO-Y14 heterodimer increases the RNA-binding affinity of the EJC (By similarity). EJC core proteins play essential roles in rice development, growth and reproduction. Regulates the splicing of UDT1 (UNDEVELOPED TAPETUM 1) pre-mRNA transcript. UDT1 is a key regulator in stamen development (PubMed:27071313). 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 DEAD box helicase family. DDX48/FAL1 subfamily.


FUNCTION: Phosphatase which catalyzes the conversion of NADP(+) to NAD(+) and of NADPH to NADH (By similarity). Shows a small preference for NADPH over NADP(+) (By similarity). Represses translation and promotes degradation of target mRNA molecules (By similarity). Plays an important role in post-transcriptional regulation of metabolic genes under circadian control (By similarity). Exerts a rhythmic post- transcriptional control of genes necessary for metabolic functions including nutrient absorption, glucose/insulin sensitivity, lipid metabolism, adipogenesis, inflammation and osteogenesis (By similarity). Plays an important role in favoring adipogenesis over osteoblastogenesis and acts as a key regulator of the adipogenesis/osteogenesis balance (By similarity). Promotes adipogenesis by facilitating PPARG nuclear translocation which activates its transcriptional activity (By similarity). Regulates circadian expression of NOS2 in the liver and negatively regulates the circadian expression of IGF1 in the bone (By similarity). Critical for proper development of early embryos (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, perinuclear region Mitochondrion. SIMILARITY: Belongs to the CCR4/nocturin family.


FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J- domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Substrate recognition component in chaperone- mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2. KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co- chaperones and the E3 ligase STUB1. Interacts with VGF-derived peptide TLQP-21. SUBCELLULAR LOCATION: Cytoplasm Melanosome Nucleus, nucleolus Cell membrane Lysosome membrane; Peripheral membrane protein; Cytoplasmic side Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock. SIMILARITY: Belongs to the heat shock protein 70 family.


FUNCTION: Recognizes base lesions in the genome and initiates base excision DNA repair. Acts as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA with a preference for single-stranded DNA substrates. The activity is greater toward mismatches (U/G) compared to matches (U/A). Excises uracil (U), 5-formyluracil (fU) and uracil derivatives bearing an oxidized group at C5 [5-hydroxyuracil (hoU) and 5-hydroxymethyluracil (hmU)] in ssDNA and dsDNA, but not analogous cytosine derivatives (5-hydroxycytosine and 5- formylcytosine), nor other oxidized bases. The activity is damage- specific and salt-dependent. The substrate preference is the following: ssDNA > dsDNA (G pair) = dsDNA (A pair) at low salt concentration, and dsDNA (G pair) > dsDNA (A pair) > ssDNA at high salt concentration. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily. SMUG1 family.


FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2A subfamily.


FUNCTION: May play a role in the degradation of type I rhamnogalacturonan derived from plant cell walls. SIMILARITY: Belongs to the Gfo/Idh/MocA family.


FUNCTION: Required for conjugation with F-type plasmids; probably serves as the mating receptor on recipient cells. FUNCTION: With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the outer membrane OOP (TC 1.B.6) superfamily. OmpA family.


FUNCTION: Involved in the degradation of 3,6-anhydro-L-galactose, which is the major monomeric sugar of red macroalgae. Catalyzes the isomerization of 3,6-anhydrogalactonate (AHGA) to 2-keto-3-deoxy- galactonate (KDGal). SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family.


SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family.


FUNCTION: Cytidine deaminase catalyzing the cytidine to uridine postranscriptional editing of a variety of mRNAs. Form complexes with cofactors that confer differential editing activity and selectivity. Responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in the apolipoprotein B mRNA. Also involved in CGA (Arg) to UGA (Stop) editing in the NF1 mRNA (By similarity). May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation (PubMed:21496894). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family.


FUNCTION: Expressed in gonadotrope cells, acts as an inhibin B coreceptor and regulates follicle-stimulating hormone (FSH) levels and female fertility. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.


FUNCTION: Required for hemolysin production. SIMILARITY: Belongs to the CvfC family.


FUNCTION: Required for processing of 5.8S rRNA (short form) at site A3 and for 5'- and 3'-processing of pre-tRNA. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the POP3 family.


FUNCTION: May be involved in transcriptional regulation as a repressor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.


FUNCTION: Formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr). SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP mutase family.


FUNCTION: Catalyzes the reduction of NADP in the presence of molecular H(2) to yield NADPH. SIMILARITY: Belongs to the complex I 24 kDa subunit family.


FUNCTION: The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly- ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'- linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1- UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'- linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes. Together with RNF135 and UB2V1, catalyzes the viral RNA-dependent 'Lys-63'-linked polyubiquitination of RIGI to activate the downstream signaling pathway that leads to interferon beta production (By similarity). UBE2V1-UBE2N together with TRAF3IP2 E3 ubiquitin ligase mediate 'Lys-63'-linked polyubiquitination of TRAF6, a component of IL17A-mediated signaling pathway. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.


FUNCTION: Catalyzes the excretion of spermidine. FUNCTION: Catalyzes the excretion of spermidine. Can also confer resistance to deoxycholate and SDS. FUNCTION: Catalyzes the excretion of spermidine. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family. MdtI subfamily. SIMILARITY: Belongs to the drug/metabolite transporter (DMT) superfamily. Small multidrug resistance (SMR) (TC 2.A.7.1) family. MdtI subfamily.


FUNCTION: Catalyzes the first oxidative step of the phenylpropanoid pathway in higher plants by transforming trans-cinnamate into p- coumarate (By similarity). The compounds formed by this pathway are essential components for lignification, pollination, and defense against ultraviolet light, predators and pathogens (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Mediates the exchange of one Ca(2+) ion against three to four Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes (PubMed:1374913, PubMed:11241183, PubMed:1476165). Contributes to Ca(2+) transport during excitation-contraction coupling in muscle (PubMed:1374913, PubMed:11241183, PubMed:1476165). In a first phase, voltage-gated channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic reticulum (PubMed:1374913, PubMed:11241183, PubMed:1476165). SLC8A1 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline (PubMed:1374913, PubMed:11241183, PubMed:1476165). Required for normal embryonic heart development and the onset of heart contractions (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. SLC8 subfamily.


FUNCTION: 3-hydroxy-3-methylglutaryl coenzyme A reductase; part of the gene cluster that mediates the biosynthesis of the diterpene ent- pimara-8(14),15-diene (PD) (PubMed:22506079, PubMed:27098256). Within the cluster, the HMG-CoA reductase AN1593 functions in the mevalonate pathway, which produces isoprenoid precursors (PubMed:22506079, PubMed:27098256). The geranylgeranyl pyrophosphate (GGPP) synthase AN1592 is needed in the formation of GGPP, the precursor for diterpenes (PubMed:22506079, PubMed:27098256). Lastly, the pimaradiene synthase pbcA performs the 2 cyclization steps that convert GGPP to ent-pimara- 8(14),15-diene (PubMed:22506079, PubMed:27098256). The putative roles of the remaining cluster enzymes in ent-pimara-8(14),15-diene biosynthesis is unclear (Probable). The cytochrome P450 monooxygenase AN1598, the glutathione S-transferase AN1595, the oxidoreductases AN1596 and AN1597 probably function as decorative enzymes (Probable). It is possible that in biological conditions the compound is oxidized to ent-pimara-8(14),15-dien-19-oic acid, which is a bioactive diterpene compound predominant in many plant extracts (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the HMG-CoA reductase family.


FUNCTION: Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization (By similarity). SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum. SIMILARITY: Belongs to the PSMG1 family.


FUNCTION: Glycosyltransferase that catalyzes the transfer of an N- acetylglucosamine (GlcNAc) moiety in beta1-6 linkage from UDP-GlcNAc onto mucin-type core 1 O-glycan to form the branched mucin-type core 2 O-glycan (PubMed:1329093, PubMed:23027862). The catalysis is metal ion- independent and occurs with inversion of the anomeric configuration of sugar donor (By similarity). Selectively involved in synthesis of mucin-type core 2 O-glycans that serve as scaffolds for the display of selectin ligand sialyl Lewis X epitope by myeloid cells, with an impact on homeostasis and recruitment to inflammatory sites (By similarity). Can also act on glycolipid substrates. Transfers GlcNAc moiety to GalGb4Cer globosides in a reaction step to the synthesis of stage- specific embryonic antigen 1 (SSEA-1) determinant (By similarity). Can use Galbeta1-3GalNAcalpha1- and Galbeta1-3GalNAcbeta1- oligosaccharide derivatives as acceptor substrates (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein Note=Also detected in the trans-Golgi network. SIMILARITY: Belongs to the glycosyltransferase 14 family.


FUNCTION: Receptor for granulocyte colony-stimulating factor (CSF3), essential for granulocytic maturation. Plays a crucial role in the proliferation, differientation and survival of cells along the neutrophilic lineage. In addition it may function in some adhesion or recognition events at the cell surface. SUBCELLULAR LOCATION: [Isoform 2]: Secreted. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the type I cytokine receptor family. Type 2 subfamily.


FUNCTION: Cytotoxin and helminthotoxin. MBP also induces non-cytolytic histamine release from basophils. It is involved in antiparasitic defense mechanisms and immune hypersensitivity reactions (By similarity). SUBCELLULAR LOCATION: Secreted.


SUBCELLULAR LOCATION: Host cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Together with FL/APO2, involved in the temporal regulation of meristem identity during both vegetative and reproductive developments in an APO2- dependent manner (By similarity). Promotes spikelet formation by suppressing the precocious conversion of inflorescence meristems to spikelet meristems, probably via a positive regulation of class-C floral homeotic genes, but not of class-B genes, and through the control of cell proliferation in meristems (PubMed:21119645). Mediates culm development and strength/diameter enhancement at internodes (PubMed:21119645). Required for the regulation of the plastochron, floral organ identity, and floral determinacy (By similarity). Controls the number of primary rachis branches (PRBs) (PubMed:20151298). May trigger the formation of vascular bundle systems which, consequently, promote carbohydrate translocation to panicles (PubMed:20151298). Involved in ozone-induced grain yield regulation (PubMed:25923431). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.


FUNCTION: Agglucetin specifically causes platelet aggregation and surface exposure of integrin alpha-IIb/beta-3 with a GPIb-(GP1BA-) dependent manner in washed platelets. It binds to human platelets in a saturable manner, and its binding is specifically blocked by anti-GP Ib mAb. It regulates endothelial cell survival and promotes angiogenesis by activating integrin alpha-v/beta-3 signaling through FAK/phosphatidylinositol 3-kinase (PI3K)/Akt pathway. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family.


FUNCTION: Mitochondrial transporter of arginine, lysine, homoarginine, methylarginine (By similarity). Transports with a much lesser extent, ornithine and histidine (PubMed:19287344). Does not transport carnitine nor acylcarnitines. Functions by both counter-exchange and uniport mechanisms. Plays a physiolocical role in the import of basic amino acids into mitochondria for mitochondrial protein synthesis and amino acid degradation (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.


FUNCTION: Neurotoxin that produces dose-dependent hypolocomotion and hyperalgesia in mice. May directly act on the central nervous system, as it is 6500-fold more potent when administered intracerebroventricularly than intraperitoneal. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ohanin/vespryn family.


FUNCTION: Acts as a specific nuclear import carrier for hsp70 proteins following heat-shock stress: acts by mediating the nucleoporin- dependent translocation of ATP-bound hsp70 proteins into the nucleus. hsp70 proteins import is required to protect cells from heat shock damages (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus. SIMILARITY: Belongs to the OPI10 family.


FUNCTION: Required for anaerobic carnitine reduction. May bring reductant to CaiA. SIMILARITY: Belongs to the ETF beta-subunit/FixA family.


FUNCTION: Has a role in meiosis. SUBCELLULAR LOCATION: Mitochondrion.


FUNCTION: Arginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in target proteins (PubMed:21531333, PubMed:24140420, PubMed:27994012, PubMed:28158808). Catalyzes the formation of monomethylarginine and asymmetric dimethylarginine on histones H2A and H4, a specific tag for epigenetic transcriptional activation (PubMed:21531333). Catalyzes asymmetric arginine dimethylation of mitochondrial proteins necessary for mitochondrial oxidative phosphorylation activity and thus aerobic respiration and ATP synthesis, and the mitochondrial stress response (PubMed:27994012). Methylates arginine residues in P-granule components pgl-1 and pgl-3 to promote P-granule degradation by autophagy in somatic cells to ensure exclusive localization of the P-granules in germ cells (PubMed:24140420). Modulates the interaction of P-granule proteins epg- 2 and sepa-1 (PubMed:24140420). Methylates arginine residues in daf-16, which blocks ftt-2 binding to daf-16, prevents akt-mediated phosphorylation and allows for daf-16 to translocate to the nucleus (PubMed:21531333). In turn, association with daf-16 therefore allows for the transcriptional activation of daf-16 and regulation of longevity-related genes (PubMed:21531333). Maintains lifespan by modulating daf-16 activity downstream of the daf-2 signaling pathway (PubMed:21531333, PubMed:28158808). Plays a role in heat and oxidative stress resistance (PubMed:21531333, PubMed:28158808). Role in stress resistance and also fat storage may be in association with the daf-2 signaling pathway (PubMed:21531333). Required for normal feeding behavior (PubMed:27994012). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Diffuse cytoplasmic localization during embryogenesis. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family.


FUNCTION: Anchors the catalytic components of the fumarate reductase complex to the cell membrane, binds quinones. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the FrdD family.


SIMILARITY: Belongs to the asparagine synthetase family.


FUNCTION: Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MtrE family.


FUNCTION: Regulatory protein of the TOL plasmid xyl operons. In the presence of m-xylene or m-methylbenzyl alcohol XylR activates both the xylCMABN operon and the regulatory gene xylS; xylS itself activates the xylXYZLTEGFJQKIH operon. XylR interacts with sigma-54.


FUNCTION: Adds the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation. Transfers glucose from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ALG10 glucosyltransferase family.


FUNCTION: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 family.


FUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein component 4 family.


FUNCTION: Proton-selective channel that specifically transports protons into cells (PubMed:29371428). Proton channel activity is only weakly- sensitive to voltage (PubMed:29371428). Proton-selective channel activity is probably required in cell types that use changes in intracellular pH for cell signaling or to regulate biochemical or developmental processes (PubMed:29371428). In the vestibular system of the inner ear, required for the formation and function of otoconia, which are calcium carbonate crystals that sense gravity and acceleration (PubMed:12651873). Probably acts by maintaining the pH appropriate for formation of otoconia (PubMed:29371428). Regulates purinergic control of intracellular calcium in vestibular supporting cells (PubMed:17606897, PubMed:20554841). May be involved in sour taste perception in sour taste cells by mediating entry of protons within the cytosol (PubMed:29371428). Also involved in energy metabolism, by reducing adipose tissue inflammation and protecting from obesity- induced metabolic dysfunction (PubMed:24379350). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Detected in the gelatinous membrane overlying the inner ear macular epithelium. SIMILARITY: Belongs to the otopetrin family.


FUNCTION: May play a role in microtubule deacetylation by negatively regulating the SIRT2 deacetylase activity toward alpha-tubulin and thereby participate in the control of cell cycle progression and genomic stability. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle pole Nucleus Cytoplasm Note=Also localizes to microtubules. SIMILARITY: Belongs to the BEX family.


FUNCTION: Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. TolB occupies a key intermediary position in the Tol-Pal system because it communicates directly with both membrane-embedded components, Pal in the outer membrane and TolA in the inner membrane. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the TolB family.


FUNCTION: Catalyzes the reversible phosphorolysis of chitobiose (N,N'- diacetylchitobiose or (GlcNAc)(2)) into alpha-GlcNAc-1-phosphate and GlcNAc with inversion of the anomeric configuration. SIMILARITY: Belongs to the glycosyl hydrolase 94 family.


FUNCTION: Contracts smooth muscle of the gastrointestinal and genitourinary tract, regulates growth hormone release, modulates insulin release, and may be involved in the control of adrenal secretion. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the galanin family.


FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. SUBCELLULAR LOCATION: Nucleus. Chromosome.


FUNCTION: Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including neurogenesis, vascular development, angiogenesis and osteogenesis (PubMed:14973287, PubMed:15206957, PubMed:10049358). Acts in concert with PTHLH/PTHRP to stimulate ductal outgrowth during embryonic mammary development and to inhibit hair follicle induction (PubMed:17301089). Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. Once all three components are bound together in a complex at the cell surface, BMPR2 phosphorylates and activates BMPR1A. In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Can also signal through non-canonical BMP pathways such as ERK/MAP kinase, PI3K/Akt or SRC cascades. For example, induces SRC phosphorylation which, in turn, activates VEGFR2, leading to an angiogenic response (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the TGF-beta family.


FUNCTION: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ3 subfamily.


SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene synthases family.


FUNCTION: Produces in vitro relaxation of rat arterial smooth muscle and constriction of intestinal smooth muscle (By similarity). May target bradykinin receptors (BDKRB). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bradykinin-related peptide family.


FUNCTION: Has a large extracellular domain which may be involved in the recognition of an extracellular signal present during germination, leading to activation or inhibition of cAMP synthesis by the cytoplasmic domain. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.


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


FUNCTION: Part of the ABC transporter complex TcyABC involved in L- cystine import. Responsible for energy coupling to the transport system (Probable). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. L-cystine importer (TC 3.A.1.3.14) family.


SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HMGB family.


FUNCTION: Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cytolysis. Pore formation is a multi- step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of monomers. SUBCELLULAR LOCATION: Secreted Nematocyst Target cell membrane Note=Forms an alpha-helical membrane channel in the prey. SIMILARITY: Belongs to the actinoporin family. Sea anemone subfamily.


FUNCTION: Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the 5'-nucleotidase family.


FUNCTION: Acts as a transcriptional activator or repressor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. Maf subfamily.


FUNCTION: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. This subunit may be involved in the elongation of the multiprimed DNA template. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the activator 1 small subunits family.


FUNCTION: Catalyzes the deamination of 5-methylthioadenosine and S- adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L- homocysteine, respectively. Is also able to deaminate adenosine. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.


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


FUNCTION: RNA demethylase that mediates oxidative demethylation of different RNA species, such as mRNAs, tRNAs and snRNAs, and acts as a regulator of fat mass, adipogenesis and energy homeostasis. Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. M6A demethylation by FTO affects mRNA expression and stability. Also able to demethylate m6A in U6 small nuclear RNA (snRNA). Mediates demethylation of N(6),2'-O-dimethyladenosine cap (m6A(m)), by demethylating the N(6)-methyladenosine at the second transcribed position of mRNAs and U6 snRNA. Demethylation of m6A(m) in the 5'-cap by FTO affects mRNA stability by promoting susceptibility to decapping. Also acts as a tRNA demethylase by removing N(1)- methyladenine from various tRNAs. Has no activity towards 1- methylguanine. Has no detectable activity towards double-stranded DNA. Also able to repair alkylated DNA and RNA by oxidative demethylation: demethylates single-stranded RNA containing 3-methyluracil, single- stranded DNA containing 3-methylthymine and has low demethylase activity towards single-stranded DNA containing 1-methyladenine or 3- methylcytosine. Ability to repair alkylated DNA and RNA is however unsure in vivo. Involved in the regulation of fat mass, adipogenesis and body weight, thereby contributing to the regulation of body size and body fat accumulation. Involved in the regulation of thermogenesis and the control of adipocyte differentiation into brown or white fat cells (By similarity). Regulates activity of the dopaminergic midbrain circuitry via its ability to demethylate m6A in mRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm Note=Localizes mainly in the nucleus, where it is able to demethylate N(6)-methyladenosine (m6A) and N(6),2'- O-dimethyladenosine cap (m6A(m)) in U6 small nuclear RNA (snRNA), N(1)- methyladenine from tRNAs and internal m6A in mRNAs. In the cytoplasm, mediates demethylation of m6A and m6A(m) in mRNAs and N(1)- methyladenine from tRNAs. SIMILARITY: Belongs to the fto family.


FUNCTION: May act as a scaffolding protein within caveolar membranes. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (By similarity). Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (By similarity). Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (By similarity). Negatively regulates TGFB1- mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein Cell membrane; Peripheral membrane protein Membrane, caveola; Peripheral membrane protein Membrane raft Note=Colocalized with DPP4 in membrane rafts. Potential hairpin-like structure in the membrane. Membrane protein of caveolae (By similarity). SIMILARITY: Belongs to the caveolin family.


FUNCTION: Catalyzes the N-acetylation of the amino acid thialysine (S- (2-aminoethyl)-L-cysteine), a L-lysine analog with the 4-methylene group substituted with a sulfur. May also catalyze acetylation of polyamines, such as norspermidine, spermidine or spermine. However, ability to acetylate polyamines is weak, suggesting that it does not act as a diamine acetyltransferase in vivo. SUBCELLULAR LOCATION: Cytoplasm Note=Intracellular organelles. SIMILARITY: Belongs to the acetyltransferase family.


FUNCTION: Nuclear transcriptional activator of viral gene expression, that is essential for viral transcription from the LTR promoter and replication. Acts as a sequence-specific molecular adapter, directing components of the cellular transcription machinery to the viral RNA to promote processive transcription elongation by the RNA polymerase II (RNA pol II) complex, thereby increasing the level of full-length transcripts. In the absence of Tat, the RNA Pol II generates short or non-processive transcripts that terminate at approximately 60 bp from the initiation site. Tat associates with the CCNT1/cyclin-T1 component of the P-TEFb complex (CDK9 and CCNT1), which promotes RNA chain elongation. This binding increases Tat's affinity for a hairpin structure at the 5'-end of all nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR RNA) and allows Tat/P-TEFb complex to bind cooperatively to TAR RNA. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs. FUNCTION: Extracellular circulating Tat can be endocytosed by surrounding uninfected cells via the binding to several surface receptors such as CD26, CXCR4, heparan sulfate proteoglycans (HSPG) or LDLR. Neurons are rarely infected, but they internalize Tat via their LDLR. Through its interaction with nuclear HATs, Tat is potentially able to control the acetylation-dependent cellular gene expression. Modulates the expression of many cellular genes involved in cell survival, proliferation or in coding for cytokines or cytokine receptors. Tat plays a role in T-cell and neurons apoptosis. Tat induced neurotoxicity and apoptosis probably contribute to neuroAIDS. Circulating Tat also acts as a chemokine-like and/or growth factor-like molecule that binds to specific receptors on the surface of the cells, affecting many cellular pathways. In the vascular system, Tat binds to ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of endothelial cells and competes with bFGF for heparin-binding sites, leading to an excess of soluble bFGF. SUBCELLULAR LOCATION: Host nucleus, host nucleolus Host cytoplasm Secreted Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type. SIMILARITY: Belongs to the lentiviruses Tat family.


FUNCTION: Possesses E3 ubiquitin-protein ligase activity in vitro when associated with the E2 enzyme UBC8 in vitro (PubMed:20884812, PubMed:15644464). Plays combinatory roles with AIRP2 in the positive regulation of the abscisic acid-mediated drought stress response (PubMed:20884812). SUBCELLULAR LOCATION: Cytoplasm, cytosol.


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


FUNCTION: Binds phosphatidic acid. Protein tyrosine phosphatase that exhibits also lipid phosphatase activity. Hydrolyzed poorly p- nitrophenyl phosphate (p-NPP). Can use PtdIns isomers as substrates. Removes efficiently phosphate from the D3 position of the inositol ring, less from the D4 position and not at all from the D5 position on monophosphorylated PtdIns isomers (PIPs). The presence of a phosphate group in the D5 position on PIP(2) isomers reduces lipid phosphatase activity. Mostly active on PtdIns(3)P and PtdIns(3,4)P(2), to a lower extent, on PtdIns(4)P and PtdIns(3,5)P(2), but barely against PtdIns(3,4,5)P(3) as substrate. SIMILARITY: Belongs to the PTEN phosphatase protein family.


FUNCTION: Sterol-binding protein that mediates cholesterol transport from the endoplasmic reticulum to endosomes (By similarity). Creates contact site between the endoplasmic reticulum and late endosomes: localizes to late endosome membranes and contacts the endoplasmic reticulum via interaction with VAPA and VAPB (By similarity). Acts as a lipid transfer protein that redirects sterol to the endosome at the expense of the cell membrane and favors membrane formation inside endosomes (By similarity). May also mediate cholesterol transport between other membranes, such as mitochondria membrane or cell membrane (By similarity). However, such results need additional experimental evidences; probably mainly mediates cholesterol transport from the endoplasmic reticulum to endosomes (By similarity). Does not activate transcriptional cholesterol sensing (By similarity). SUBCELLULAR LOCATION: Late endosome membrane; Multi-pass membrane protein Note=Localizes to contact sites between the endoplasmic reticulum and late endosomes: associates with the endoplasmic reticulum membrane via interaction with VAPA, VAPB or MOSPD2. SIMILARITY: Belongs to the STARD3 family.


FUNCTION: Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Cob(I)alamin adenosyltransferase family.


FUNCTION: Negative transcriptional regulator of the glycine cleavage system operon (GCV). Does not autoregulate its own expression. It is not yet known how GcvR acts as a repressor. It does not seem to bind DNA. It could interact with GcvA and suppress its activatory activity. FUNCTION: Possible negative transcriptional regulator of the glycine cleavage system operon (GCV). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5- methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (By similarity). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ELP3 family.


FUNCTION: Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively. SIMILARITY: Belongs to the IUNH family. RihA subfamily.


FUNCTION: Carboxyltransferase subunit of the 3-methylcrotonyl-CoA carboxylase, an enzyme that catalyzes the conversion of 3- methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the AccD/PCCB family.


FUNCTION: Binds preferentially single-stranded DNA and unwinds double- stranded DNA. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the HMGB family.


FUNCTION: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of dibenzodioxocinones such as pestalotiollide B, a novel class of inhibitors against cholesterol ester transfer protein (CEPT) (PubMed:31474098). essential for dibenzodioxocinones biosynthesis and may be involved in the secretion of the cluster products (Probable). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily.


FUNCTION: Small GTPase. Negatively regulates the transcription regulation activity of the APBB1/FE65-APP complex via its interaction with APBB1/FE65 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Cytoplasm, perinuclear region Nucleus. SIMILARITY: Belongs to the small GTPase superfamily. RasD family.


FUNCTION: Trans-Golgi-associated GTPase that regulates protein sorting. Controls the targeting of ARL1 and its effector to the trans-Golgi. Required for the lipidation of chylomicrons in the intestine and required for VLDL lipidation in the liver. FUNCTION: Trans-Golgi-associated GTPase that regulates protein sorting. Controls the targeting of ARL1 and its effector to the trans-Golgi. Required for the lipidation of chylomicrons in the intestine and required for VLDL lipidation in the liver. SUBCELLULAR LOCATION: Golgi apparatus Golgi apparatus, trans-Golgi network Note=Located in the trans-Golgi in the GTP-bound active state. SUBCELLULAR LOCATION: Golgi apparatus. Golgi apparatus, trans-Golgi network Note=Located in the trans-Golgi in the GTP-bound active state. SIMILARITY: Belongs to the small GTPase superfamily. Arf family.


FUNCTION: Involved in cell wall peptidoglycan recycling. Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.


SIMILARITY: Belongs to the LovG family.


FUNCTION: Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein moaD. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the HesA/MoeB/ThiF family.


FUNCTION: Inner capsid protein that self-assembles to form an icosahedral capsid with a T=2 symmetry, which consists of 120 copies of VP2, with channels at each of its five-fold vertices. This capsid constitutes the innermost concentric layer of the viral mature particle. It encapsidates the polymerase VP1, the capping enzyme VP3 and the genomic dsRNA, thereby defining the core. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels formed by VP2 N-termini. VP2 is required for the replicase activity of VP1 polymerase. Probably recruits a copy of a VP1-VP3 complex, potentially along with a segment of plus-strand RNA, as a decamer of VP2 assembles. May activate the autoinhibited VP1/RNA complex to coordinate packaging and genome replication. SUBCELLULAR LOCATION: Virion Note=Inner capsid protein. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. SIMILARITY: Belongs to the rotavirus VP2 family.


FUNCTION: Forms the central cylindrical hub of the baseplate and plays an important role in baseplate and tail assembly (Probable). Core component of the initiator complex that triggers the tail tube polymerization during tail assembly (Probable). Forms a conduit that probably functions as an extension of the tail tube allowing viral DNA release during ejection. Might facilitate the interaction of the virus with the host cell surface through electrostatic interactions during virus entry into host cell. SUBCELLULAR LOCATION: Virion Host cytoplasm Note=Baseplate protein.


FUNCTION: Involved in lignin biosynthesis. Catalyzes the final step specific for the production of lignin monomers, like coniferyl alcohol, sinapyl alcohol and 4-coumaryl alcohol (By similarity). SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.


FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein synthesis by a non-covalent modification of the ribosomes. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. TetM/TetO subfamily.


FUNCTION: Cytochrome b562 is an integral component of the cytochrome b- c1 complex in the cyclic electron transfer system of photosynthetic bacteria. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b561 family.


FUNCTION: Stimulates viral early and late gene expression and thus play a crucial role in the regulation of productive infection. In addition, activates quiescent cells to reenter the cell cycle and up-regulates several E2F-responsive genes, which are responsible for pushing the cell into S phase. In S-phase, inhibits cellular DNA synthesis and blocks further cell cycle progression (By similarity). SUBCELLULAR LOCATION: Host nucleus. Note=Colocalizes with host PML- associated nuclear bodies. SIMILARITY: Belongs to the HHV-5 IE2 protein family.


FUNCTION: Involved with IBR3 and IBR10 in the peroxisomal beta- oxidation of indole-3-butyric acid (IBA) to form indole-3-acetic acid (IAA), a biologically active auxin. May be responsible for catalyzing the dehydrogenation step in the conversion of IBA (PubMed:20562230). May be involved in the peroxisomal activation of 2,4- dichlorophenoxybutyric acid (2,4-DB), a precursor of active auxins that inhibit root growth (PubMed:19043666). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eS25 family.


FUNCTION: Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. FUNCTION: Nucleocapsid protein p15 is involved in the packaging and encapsidation of two copies of the genome. FUNCTION: Matrix protein p19 targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex (By similarity). SUBCELLULAR LOCATION: [Capsid protein p24]: Virion. SUBCELLULAR LOCATION: [Nucleocapsid protein p15-gag]: Virion. SUBCELLULAR LOCATION: [Matrix protein p19]: Virion.


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.


SIMILARITY: Belongs to the universal ribosomal protein uS8 family.


FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins (PubMed:30265660). This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required (PubMed:30265660). Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair (By similarity). Belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides (By similarity). In addition, regulates gene expression in response to bacterial infection (PubMed:30265660). Binds to the GATA transcription factor elt-2 to control its transcriptional activity and thus the expression of elt-2-dependent genes in response to infection by Gram-negative bacteria such as P.aeruginosa (PubMed:30265660). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the AAA ATPase family.


FUNCTION: Plays a role in the recruitment of the RNA exosome complex to pre-rRNA to mediate the 3'-5' end processing of the 5.8S rRNA; this function may include MPHOSPH6. Can activate PRKDC not only in the presence of linear DNA but also in the presence of supercoiled DNA. Can induce apoptosis in a p53/TP53 dependent manner. May regulate the TRAX/TSN complex formation. Potentiates transcriptional repression by NR1D1 and THRB (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Nucleus, nucleolus Note=EXOSC10 is required for nucleolar localization. Colocalizes with TSNAX in the nucleus. SIMILARITY: Belongs to the C1D family.


FUNCTION: Preferentially hydrolyzes para-nitrophenyl-beta-D- galactoside. Can hydrolyze para-nitrophenyl-beta-D-fucoside with 5 time less efficiency. SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the glycosyl hydrolase 35 family.


SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein Golgi apparatus Note=Associated and found in vesicular structures of Golgi complex. SIMILARITY: Belongs to the CHIC family.


FUNCTION: Essential for normal male fertility and for progressive motility of spermatozoa. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection, cilium, flagellum Cytoplasm, cytoskeleton, flagellum axoneme. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.


FUNCTION: Is involved in the catabolism of quinate. Allows the utilization of quinate as carbon source via the beta-ketoadipate pathway. SIMILARITY: Belongs to the type-II 3-dehydroquinase family.


FUNCTION: Could function as an adhesive molecule and its matrix bound and soluble fragments may play a critical role in vascular biology. SUBCELLULAR LOCATION: Secreted Cell membrane; Peripheral membrane protein.


FUNCTION: In absence of DNA repair, the XPC complex also acts as a transcription coactivator: XPC interacts with the DNA-binding transcription factor E2F1 at a subset of promoters to recruit KAT2A and histone acetyltransferase complexes (HAT). KAT2A recruitment specifically promotes acetylation of histone variant H2A.Z.1/H2A.Z, but not H2A.Z.2/H2A.V, thereby promoting expression of target genes. FUNCTION: Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen- bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts. XPC:RAD23B contacts DNA both 5' and 3' of a cisplatin lesion with a preference for the 5' side. XPC:RAD23B induces a bend in DNA upon binding. XPC:RAD23B stimulates the activity of DNA glycosylases TDG and SMUG1. SUBCELLULAR LOCATION: Nucleus Chromosome Cytoplasm Note=Omnipresent in the nucleus and consistently associates with and dissociates from DNA in the absence of DNA damage. Continuously shuttles between the cytoplasm and the nucleus, which is impeded by the presence of NER lesions. SIMILARITY: Belongs to the XPC family.


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


FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the histone H4 family.


FUNCTION: Involved in DNA double-strand break (DSB) repair and recombination. Promotes the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RAD52 family.


FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNA. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts induce type I interferon and NF- Kappa-B through the RIG-I pathway (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit family.


FUNCTION: Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and UDP-galactose to galactose 1-phosphate and UMP. Preferred substrate is UDP-glucose. SIMILARITY: Belongs to the Nudix hydrolase family.


FUNCTION: Nuclear genome-encoded factor involved in ribosome biogenesis in chloroplasts (PubMed:22576849, PubMed:23227895, PubMed:25043599). Binds specific group II introns in chloroplasts and facilitates their splicing. Is required for rRNA maturation in plastids and may contribute to the assembly of the large (50S) ribosomal subunit (PubMed:22576849). Required for normal development of chloroplasts (PubMed:22576849, PubMed:23227895, PubMed:25043599). Required for the expression of transcripts encoding plastid-localized enzymes involved in abscisic acid (ABA) biosynthesis. Required for maintenance of ABA levels and response to salt stress (PubMed:23227895). Possesses RNA chaperone activity for proper splicing of introns in chloroplasts. Essential for chloroplast function and abiotic stress responses (PubMed:25043599). SUBCELLULAR LOCATION: Plastid, chloroplast Plastid, chloroplast stroma. SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50 subfamily.


FUNCTION: Transcription factor that binds specifically to a 5'-AA[AG]G- 3' consensus core sequence (By similarity). Binds to 5'-TAAAGT-3' motif in REV promoter to triggers its transcription, thus regulating adaxial- abaxial polarity and influencing leaf axial patterning in an auxin transport- and response-dependent manner (e.g. IAA6 and IAA19 genes expression) (PubMed:20807212). Probably involved in early processes for vascular development (PubMed:17583520). The PEAR proteins (e.g. DOF2.4, DOF5.1, DOF3.2, DOF1.1, DOF5.6 and DOF5.3) activate gene expression that promotes radial growth of protophloem sieve elements (PubMed:30626969). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Component of a binary toxin active against Culex and some Aedes mosquito larvae; mortality towards both C.quinquefasciatus and A.atropalpus is maximal by 48 hours. A.aegypti is not very susceptible to this toxin (PubMed:8419297). This subunit is responsible for localized binding to specific regions of the host larval gut. Binary toxin internalization into host gut cells requires both proteins (By similarity). SUBCELLULAR LOCATION: Spore, perispore. SIMILARITY: Belongs to the toxin_10 family.


SIMILARITY: Belongs to the UPF0303 family.


FUNCTION: Specifically catalyzes the removal of N-terminal proline residues from peptides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase S33 family.


FUNCTION: Modulates channel gating kinetics. Causes unique persistent sodium currents. Inactivates the sodium channel opening more slowly than the subunit beta-1. Its association with NFASC may target the sodium channels to the nodes of Ranvier of developing axons and retain these channels at the nodes in mature myelinated axons (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the sodium channel auxiliary subunit SCN3B (TC 8.A.17) family.


FUNCTION: Positively regulates mitochondrial complex assembly and/or stability (PubMed:29949756). Increases mitochondrial membrane potential while decreasing mitochondrial reactive oxygen species (By similarity). Increases mitochondrial respiration rate (PubMed:31296841). Increased mitochondrial respiratory activity promotes myogenic differentiation which facilitates muscle growth and regeneration (PubMed:31296841, PubMed:32393776). Increases mitochondrial calcium retention capacity (PubMed:29949756). Plays a role in maintenance of cellular lipid composition through its interaction with cytochrome b5 reductase CYB5R3 which is required for mitochondrial respiratory complex I activity (PubMed:30796188). Interacts with the mitochondrial trifunctional enzyme complex (MTE) and enhances fatty acid beta-oxidation (PubMed:29949755, PubMed:32243843). Not required for MTE formation or stability (PubMed:29949755). Modulates triglyceride clearance in adipocytes through its role in regulating fatty acid beta-oxidation and lipolysis (PubMed:32243843). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein Note=Preferentially binds to cardiolipin relative to other common cell membrane lipids. SIMILARITY: Belongs to the mitoregulin family.


FUNCTION: Sodium permeable non-voltage-sensitive ion channel inhibited by the diuretic amiloride. Mediates the electrodiffusion of the luminal sodium (and water, which follows osmotically) through the apical membrane of epithelial cells. Plays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid homeostasis, which is important for proper clearance of mucus. SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Cytoplasmic vesicle membrane Note=Apical membrane of epithelial cells. SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. SCNN1B subfamily.