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


SIMILARITY: Belongs to the xanthine dehydrogenase family.


SIMILARITY: Belongs to the UPF0263 family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 3 family.


FUNCTION: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase A chain family.


FUNCTION: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines. SIMILARITY: Belongs to the Dus family. DusB subfamily.


FUNCTION: Histone binding-protein that regulates chromatin dynamics and minichromosome maintenance (MCM) loading at replication origins, possibly by promoting chromatin openness (PubMed:25990725). SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus Chromosome Note=Present in the nucleus throughout interphase and is detached from chromatin at the onset of mitosis and rebinds at telophase when the pre-replication complexes (pre-RC) is formed (PubMed:25990725).


FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. Plays an important role in the assembly of the N-DRC linker (By similarity). Plays dual roles at both the primary (or non-motile) cilia to regulate hedgehog signaling and in motile cilia to coordinate cilia movement. Required for proper motile cilia functioning. Positively regulates ciliary smoothened (SMO)-dependent Hedgehog (Hh) signaling pathway by facilitating the trafficking of SMO into the cilium and the stimulation of SMO activity in a GRK2-dependent manner (PubMed:17366626, PubMed:21659505, PubMed:27472056). May play a role in the spermatozoa motility (PubMed:11751847). SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Cell projection, cilium, flagellum Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, cilium basal body Golgi apparatus Cell projection, cilium Cytoplasm, cytoskeleton, flagellum axoneme Note=Associates with microtubules (PubMed:17366626). Localized to the cytoplasm of round spermatids, the tails of elongating spermatids, and mature spermatid tail bundles protruding into the lumen, and in the flagellum of epididymal spermatozoa (PubMed:11751847). SIMILARITY: Belongs to the DRC4 family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldehyde dehydrogenase family.


FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family. TyrS type 2 subfamily.


FUNCTION: Part of an ABC transporter complex involved in the uptake of all common nucleosides (PubMed:20595258). Responsible for the translocation of the substrate across the membrane (Probable). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family.


FUNCTION: [Assembly protein]: Plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging. FUNCTION: [Assemblin]: Protease that plays an essential role in virion assembly within the nucleus. Catalyzes the cleavage of the assembly protein after formation of the spherical procapsid. By that cleavage, the capsid matures and gains its icosahedral shape. The cleavage sites seem to include -Ala-Ser-, -Ala-Ala-, as well as Ala-Thr bonds. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging. FUNCTION: [Capsid scaffolding protein]: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein. Cleavages products are evicted from the capsid before or during DNA packaging. SUBCELLULAR LOCATION: [Assembly protein]: Host nucleus. SUBCELLULAR LOCATION: [Capsid scaffolding protein]: Host cytoplasm. SUBCELLULAR LOCATION: [Assemblin]: Host nucleus. SIMILARITY: Belongs to the herpesviridae capsid scaffolding protein family.


FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression through mitosis. Acts by initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates, leading to the degradation of APC/C substrates by the proteasome and promoting mitotic exit. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.


FUNCTION: ATP-dependent RNA helicase. SIMILARITY: Belongs to the DEAD box helicase family. DDX24/MAK5 subfamily.


FUNCTION: Catalyzes the NADPH-dependent reduction of 1,5-anhydro-D- fructose (AF) to 1,5-anhydro-D-glucitol. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldo/keto reductase family.


FUNCTION: Involved in non-homologous end joining (NHEJ) in the repair of double-strand DNA breaks (DSB). Has a role in meiosis. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the XRCC4-XLF family. XLF subfamily.


FUNCTION: Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein. SIMILARITY: Belongs to the Ycf3 family.


FUNCTION: Contributes to modulation of the type III secretion system (T3SS) in response to host cells via the regulation of the OprB transport system. FUNCTION: Member of the two-component regulatory system GtrS/GltR involved in the regulation of glucose metabolism and transport, as well as regulation of the exotoxin A gene expression (PubMed:24920832). GltR controls the transcription of genes involved in glucose metabolism (glk and edd/gap-1) and transport (oprB) as well as the expression of toxA that encodes exotoxin A, the primary virulence factor (PubMed:8830708, PubMed:24920832). Acts as a repressor that is released from its target operators upon phosphorylation (PubMed:24920832). SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Positive regulator of sigma-B activity. Non-phosphorylated RsbV binds to RsbW, preventing its association with sigma-B. When phosphorylated, releases RsbW, which is then free to complex with and inactivate sigma-B (By similarity). SIMILARITY: Belongs to the anti-sigma-factor antagonist family.


FUNCTION: Involved in DNA damage tolerance by regulating translesion synthesis (TLS) of templates carrying DNA damage lesions such as 8oxoG and abasic sites (PubMed:24191025). May act by stimulating activity of DNA polymerases involved in TLS, such as PRIMPOL and polymerase delta (POLD1) (PubMed:24191025, PubMed:26984527). SUBCELLULAR LOCATION: Mitochondrion matrix Nucleus Note=Mainly localizes to the mitochondrial matrix; a small fraction localizes in the nucleus.


FUNCTION: Alkaline phosphatase that metabolizes various phosphate compounds and plays a key role in skeletal mineralization and adaptive thermogenesis. Has broad substrate specificity and can hydrolyze a considerable variety of compounds: however, only a few substrates, such as diphosphate (inorganic pyrophosphate; PPi), pyridoxal 5'-phosphate (PLP) and N-phosphocreatine are natural substrates. Plays an essential role in skeletal and dental mineralization via its ability to hydrolyze extracellular diphosphate, a potent mineralization inhibitor, to phosphate: it thereby promotes hydroxyapatite crystal formation and increases inorganic phosphate concentration. Acts in a non-redundant manner with PHOSPHO1 in skeletal mineralization: while PHOSPHO1 mediates the initiation of hydroxyapatite crystallization in the matrix vesicles (MVs), ALPL/TNAP catalyzes the spread of hydroxyapatite crystallization in the extracellular matrix. Also promotes dephosphorylation of osteopontin (SSP1), an inhibitor of hydroxyapatite crystallization in its phosphorylated state; it is however unclear whether ALPL/TNAP mediates SSP1 dephosphorylation via a direct or indirect manner. Catalyzes dephosphorylation of PLP to pyridoxal (PL), the transportable form of vitamin B6, in order to provide a sufficient amount of PLP in the brain, an essential cofactor for enzymes catalyzing the synthesis of diverse neurotransmitters. Additionally, also able to mediate ATP degradation in a stepwise manner to adenosine, thereby regulating the availability of ligands for purinergic receptors (By similarity). Also capable of dephosphorylating microbial products, such as lipopolysaccharides (LPS) as well as other phosphorylated small-molecules, such as poly-inosine:cytosine (poly I:C) (By similarity). Acts as a key regulator of adaptive thermogenesis as part of the futile creatine cycle: localizes to the mitochondria of thermogenic fat cells and acts by mediating hydrolysis of N- phosphocreatine to initiate a futile cycle of creatine dephosphorylation and phosphorylation. During the futile creatine cycle, creatine and N-phosphocreatine are in a futile cycle, which dissipates the high energy charge of N-phosphocreatine as heat without performing any mechanical or chemical work (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Extracellular vesicle membrane; Lipid-anchor, GPI- anchor Mitochondrion membrane; Lipid-anchor, GPI-anchor Mitochondrion intermembrane space Note=Localizes to special class of extracellular vesicles, named matrix vesicles (MVs), which are released by osteogenic cells (PubMed:32710882). Localizes to the mitochondria of thermogenic fat cells: tethered to mitochondrial membranes via a GPI- anchor and probably resides in the mitochondrion intermembrane space (By similarity). SIMILARITY: Belongs to the alkaline phosphatase family.


FUNCTION: Dioxygenase that catalyzes the first step of DNA base J (beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5- hydroxymethyluracil (HOMedU). DNA base J is a hypermodified thymidine residue found in the genome of kinetoplastid parasites, which is localized primarily to repetitive DNA, namely the telomeres, and is implicated in the regulation of antigenic variation. Also specifically binds to base J-containing DNA (J-DNA). Involved in propagation and maintenance of DNA base J synthesis initiated by JBP2 by specifically binding already synthesized DNA base J and propagating J synthesis. Thymine dioxygenase activity and J-DNA-binding are independent functions (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TET family. JBP1 subfamily.


FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. FUNCTION: The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites. FUNCTION: Lactotransferrin is a major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity. Antimicrobial properties may include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. The most effective inhibitory activity is seen against E.coli and P.aeruginosa. Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. Interferes with the lipopolysaccharide (LPS)-stimulated TLR4 signaling, but cannot directly stimulate the TLR4 signaling pathway and subsequent NF-kappa-B activation. FUNCTION: Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria. SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule Note=Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils (By similarity). SIMILARITY: Belongs to the transferrin family.


FUNCTION: Catalyzes a proton abstraction reaction that results in 2,5- elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3- cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6- hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC). SIMILARITY: Belongs to the AB hydrolase superfamily. MenH family.


FUNCTION: Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins (PubMed:27292798). Binds to polyubiquitin chains of different linkage types, including 'Lys-6', 'Lys-11', 'Lys- 29', 'Lys-33', 'Lys-48' and 'Lys-63' (PubMed:28082312). May play a regulatory role at the level of protein turnover (PubMed:27292798). SIMILARITY: Belongs to the MINDY deubiquitinase family. FAM63 subfamily.


FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL15 family.


FUNCTION: Plays an essential role in the proliferation of yeast cells. Involved in a signaling pathway, required for optimal cell wall integrity, that acts in parallel with the PKC1-SLT2-dependent pathway. Downstream kinase in the sphingolipid-mediated signaling pathway. Its phosphorylation is regulated by the intracellular sphingolipid concentration. Cooperates with SLI1 in mediating resistance to the sphingolipid biosynthesis inhibitor drug myriocin (ISP-1). Its kinase activity is essential for the resistance. Required for both receptor- mediated and fluid-phase endocytosis, but is not necessary for receptor phosphorylation or ubiquitination. Necessary for the internalization of plasma membrane proteins carrying different types of internalization signals. Acts downstream of the PKH kinases to control endocytosis by phosphorylating components of the endocytic machinery. Phosphorylation of residue Thr-504 in the activation loop is essential for activity. phosphorylates and down-regulates flippase activator FPK1. SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side Note=Intracellular localization is regulated by the intracellular sphingolipid levels. During the yeast cell cycle, distributed both on the plasma membrane and in the cytosol. Greater accumulation was detected on the plasma membrane, such as in the budding area, a daughter cell and the neck region of the mother cell in the S phase, and the septum between a mother cell and a daughter cell in the G2 phase. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.


FUNCTION: Catalyzes the dehydrogenation of morphine to morphinone. Uses both NAD and NADP, but the activity is much greater with NAD than with NADP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldo/keto reductase family.


FUNCTION: Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. SIMILARITY: Belongs to the troponin C family.


FUNCTION: Reversible inhibitor of voltage-gated sodium channels (Nav). Delays the fast inactivation kinetics of neuronal-type sodium channels. In vivo, it induces rat penile erection (PubMed:15246765). This effect may be due to the neuronal nitric oxide synthase (NOS1), since one of its selective inhibitor completely abolishes all the toxic effects of the toxin (PubMed:15246765). This toxin also causes scratching, lacrimation, hypersalivation, sweating and agitation followed by spastic paralysis of the anterior and posterior extremities and death at dose levels of 0.24 mg/mouse (PubMed:1397265, PubMed:16278100, PubMed:15246765). It is also insecticidal to the larval and adult forms of the house fly (PubMed:1397265). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 03 (Tx2) family. 06 subfamily.


FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the acetokinase family.


FUNCTION: One of at least two accessory proteins for anaerobic nitric oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.


FUNCTION: Catalyzes the cross-linking of a glutamate residue and a tyrosine residue in the PqqA protein as part of the biosynthesis of pyrroloquinoline quinone (PQQ). SIMILARITY: Belongs to the radical SAM superfamily. PqqE family.


FUNCTION: Catalyzes the conversion of cobalt-precorrin-8 to cobyrinate. SIMILARITY: Belongs to the CobH/CbiC family.


FUNCTION: Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily.


FUNCTION: Hirudin is a potent thrombin-specific protease inhibitor. It forms a stable non-covalent complex with alpha-thrombin, thereby abolishing its ability to cleave fibrinogen. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I14 (hirudin) family.


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


FUNCTION: Essential component of the cytosolic iron-sulfur (Fe/S) protein assembly machinery. Required for the maturation of extramitochondrial Fe/S proteins. SIMILARITY: Belongs to the WD repeat CIA1 family.


SIMILARITY: Belongs to the UPF0502 family.


FUNCTION: Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Controls sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor (By similarity). SIMILARITY: Belongs to the SKP1 family.


SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


FUNCTION: May play a role in angiogenesis, synapse formation, cellular migration and adhesion. SUBCELLULAR LOCATION: Secreted Cytoplasm Cell surface Synapse.


FUNCTION: Transfers 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A on a serine residue to the apo-acyl carrier protein (gamma chain) of the citrate lyase to yield holo-acyl carrier protein. SIMILARITY: Belongs to the CitX family.


FUNCTION: Synthesizes selenophosphate from selenide and ATP. SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class I subfamily.


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 (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the protamine P1 family.


FUNCTION: Transmembrane transporter; part of the Fusarium detoxification of benzoxazolinone cluster involved in the degradation of benzoxazolinones produced by the host plant (PubMed:25727347, PubMed:26828593). Maize, wheat, and rye produce the 2 benzoxazinone phytoanticipins 2,4-dihy-droxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA) and 2,4-dihydroxy-1,4-benzoxazin-3-one (DIBOA) that, due to their inherent instability once released, spontaneously degrade to the more stable corresponding benzoxazolinones, 6-methoxy-2-benzoxazolinone (MBOA) and 2-benzoxazolinone (BOA), respectively (By similarity). FPSE_08127 is proposed to shuttle metabolites of benzoxazolinone degradation (Probable). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.


FUNCTION: This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. SIMILARITY: Belongs to the bacterial ribosomal protein bL25 family.


FUNCTION: Catalyzes the transfer of the 2-phospholactate moiety from (2S)-lactyl-2-diphospho-5'-guanosine to 7,8-didemethyl-8-hydroxy-5- deazariboflavin (FO) with the formation of oxidized coenzyme F420-0 and GMP. SIMILARITY: Belongs to the CofD family.


FUNCTION: Vacuolar carboxypeptidase involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (By similarity). SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the peptidase S10 family.


SIMILARITY: Belongs to the MQO family.


FUNCTION: Required for activity of HDA1 histone deacetylase complex. The HDA1 histone deacetylase complex is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HDA2/3 family. HDA3 subfamily.


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. FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family.


FUNCTION: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ThiI family.


FUNCTION: Multifunctional enzyme that catalyzes a series of post- translational modifications on Lys residues in procollagen. Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (By similarity). Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine (By similarity). Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues. Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen-like domain, giving rise to hydroxylysine and 1,2- glucosylgalactosyl-5-hydroxylysine residues. Catalyzes hydroxylation and glycosylation of Lys residues in the ADIPOQ collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues. Essential for normal biosynthesis and secretion of type IV collagens. Essential for normal formation of basement membranes (By similarity). SUBCELLULAR LOCATION: Rough endoplasmic reticulum Endoplasmic reticulum lumen Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side Secreted Secreted, extracellular space Note=The majority of the secreted protein is associated with the extracellular matrix.


SIMILARITY: Belongs to the phosphoglycerate kinase family.


FUNCTION: Transcriptional coactivator that specifically associates with POU2F3 (PubMed:35576971). This complex drives the development of tuft cells, a rare a rare chemosensory cells that coordinate immune and neural functions within mucosal epithelial tissues (PubMed:35576971). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the POU2AF family.


FUNCTION: Catalyzes the formation of flavonols from dihydroflavonols. It can act on dihydrokaempferol to produce kaempferol, on dihydroquercetin to produce quercitin and on dihydromyricetin to produce myricetin (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family.


FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in the tryptophan catabolic pathway which is also a broad spectrum antagonist of the three ionotropic excitatory amino acid receptors among others. May catalyze the beta-elimination of S-conjugates and Se- conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond. Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro). SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Acts as a calcium sensor. CBL proteins interact with CIPK serine-threonine protein kinases. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the calcineurin regulatory subunit family.


FUNCTION: The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein Host endosome membrane; Single-pass type I membrane protein Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). SIMILARITY: Belongs to the herpesviridae glycoprotein H family.


FUNCTION: Involved in defense responses (PubMed:19696351, PubMed:26740780). Contributes to slowing defense responses toward Magnaporthe oryzae (PubMed:19696351).


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 13 family.


FUNCTION: Necessary for protein translocation in the endoplasmic reticulum. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SecE/SEC61-gamma 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 21 family.


FUNCTION: Functions as a nucleotide exchange factor (NEF) for Hsp70 chaperones which accelerates the release of ADP. Required for fully efficient Hsp70-mediated folding of proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FES1 family.


FUNCTION: May play an important role in centriole assembly and/or stability and ciliogenesis. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Note=Colocalizes with mitochondria in cortical germ plasm islands. The mitochondrial localization may be microtubule-dependent. SIMILARITY: Belongs to the WD repeat POC1 family.


FUNCTION: Histone demethylase that demethylates di-methylated 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor (PubMed:34329293). Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed (By similarity). Plays a role in the mitotic development of the germline (PubMed:34329293). May be involved in H3 demethylation in mitotic cells including gut and embryonic cells (PubMed:34329293). Plays a role in sensitivity upon interstrand cross- link DNA damage, probably by positively regulating the expression of mlh-1 (PubMed:34329293). Plays a role in developmental growth and lifespan regulation in response to ultraviolet-induced damage (PubMed:33046905). No obvious role in larval development, sex chromosome segregation or for regulating meiotic crossover frequency (PubMed:34329293). SUBCELLULAR LOCATION: Nucleus Note=Only localizes to 5% of premeiotic tip and pachytene nuclei. SIMILARITY: Belongs to the flavin monoamine oxidase family.


FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase subfamily.


FUNCTION: Catalyzes the isomerization of D-erythrulose-4P to L- erythrulose-1P. FUNCTION: Catalyzes the isomerization of D-erythrulose-4P to L- erythrulose-1P. Involved in the degradation pathway of erythritol, that allows B.abortus to grow on this compound as the sole carbon source. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the triosephosphate isomerase family.


FUNCTION: Putative FAD-dependent oxidoreductase involved in the resistance to cercosporin and other singlet oxygen-generating photosensitizers. Translocates from mitochondria to the nucleus under apoptotic conditions, where it degrades DNA and induces apoptosis. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein Nucleus Note=Translocates from mitochondrion to the nucleus upon apoptosis induction. SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.


FUNCTION: Might take part in the signal recognition particle (SRP) pathway. This is inferred from the conservation of its genetic proximity to ftsY/ffh. May be a regulatory protein. SIMILARITY: Belongs to the UPF0122 family.


FUNCTION: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Translocation stops specifically at Xer-dif sites, where FtsK interacts with the Xer recombinase, allowing activation of chromosome unlinking by recombination. FtsK orienting polar sequences (KOPS) guide the direction of DNA translocation. FtsK can remove proteins from DNA as it translocates, but translocation stops specifically at XerCD-dif site, thereby preventing removal of XerC and XerD from dif (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein Note=Located at the septum. SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.


FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Prokaryotic type I sub-subfamily.


FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D- fructose 6-phosphate, respectively) (PubMed:5871820). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:5871820). SIMILARITY: Belongs to the hexokinase family.


FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity). Binds plasminogen when expressed on the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity, which in turn contributes to tissue invasion and virulence. FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. SUBCELLULAR LOCATION: Cytoplasm Secreted Cell surface Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface. SUBCELLULAR LOCATION: Cytoplasm Secreted Cell surface Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface. SIMILARITY: Belongs to the enolase family.


SIMILARITY: Belongs to the Ves family.


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


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TPP enzyme family.


FUNCTION: Transcription factor required for normal development of thymus, parathyroid glands, ultimobranchial bodies, teeth, skeletal elements of skull and larynx as well as distal limbs. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Plays an important role in the physiology of adrenergic neurons. SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Cell projection, axon Note=Expressed in dopaminergic axons and axon terminals. SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.


FUNCTION: Mediates the uptake of pyruvate into mitochondria. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial pyruvate carrier (MPC) (TC 2.A.105) family.


FUNCTION: ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the DEAD box helicase family. DDX52/ROK1 subfamily.


FUNCTION: Probably involved in the RNA silencing pathway. May bind to short RNAs such as microRNAs (miRNAs) or short interfering RNAs (siRNAs), and represses the translation of mRNAs which are complementary to them (By similarity). SIMILARITY: Belongs to the argonaute family. Ago subfamily.


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


FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Positively regulates the expression of the sigY-yxlCDEFG operon upon nitrogen starvation. Also positively regulates ybgB. SIMILARITY: Belongs to the sigma-70 factor family. ECF subfamily.


FUNCTION: Binds directly to 16S ribosomal RNA. FUNCTION: Binds directly to 16S ribosomal RNA. SIMILARITY: Belongs to the bacterial ribosomal protein bS20 family. SIMILARITY: Belongs to the bacterial ribosomal protein bS20 family.


FUNCTION: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1A (PBP1a). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor; Periplasmic side. SIMILARITY: Belongs to the LpoA family.


FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family. SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.


FUNCTION: Reductase component of a two-component system that degrades 2,4,5-trichlorophenol. TftC provides the FADH(2) required by TftD. TftD oxidizes 2,4,5-trichlorophenol (2,4,5-TCP) to 2,5-dichloro-p- benzoquinone, which is chemically reduced to 2,5-dichloro-p- hydroquinone (2,5-DiCHQ). Then, TftD oxidizes the latter to 5-chloro-2- hydroxy-p-benzoquinone. SIMILARITY: Belongs to the non-flavoprotein flavin reductase family.


FUNCTION: Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as nitrogen source. SIMILARITY: Belongs to the ureidoglycolate lyase family.


FUNCTION: One of the proteins required for the normal export of preproteins out of the cell cytoplasm. It is a molecular chaperone that binds to a subset of precursor proteins, maintaining them in a translocation-competent state. It also specifically binds to its receptor SecA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SecB family.


FUNCTION: Component of TORC2, which regulates cell cycle-dependent polarization of the actin-cytoskeleton and cell wall integrity. TORC2 controls polarity of the actin cytoskeleton, which is required for orienting the secretory pathway toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity pathway. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Vacuole membrane; Peripheral membrane protein; Cytoplasmic side.


FUNCTION: Moderately inhibits voltage-gated sodium channels and weakly inhibits voltage-gated potassium channel (PubMed:17150181, PubMed:17618665, PubMed:23246579, PubMed:26721415). Inhibits the inactivation of rat Nav1.2/SCN2A (IC(50)=870 nM), rat Nav1.3/SCN3A (IC(50)=845 nM), rat Nav1.4/SCN4A (IC(50)=339 nM), human Nav1.5/SCN5A (IC(50)=335 nM) and human Nav1.7/SCN9A sodium channels (IC(50)=348 nM) (PubMed:26721415). The toxin delays the inactivation of sodium channels without affecting the activation and steady-state inactivation kinetics in the physiological range of voltages (PubMed:26721415). Site-directed mutagenesis of the sodium channel indicates that the toxin interacts with site 3 located at the extracellular S3-S4 linker of domain IV (PubMed:26721415). On potassium channels, it inhibits activation of channels with an IC(50) of 8.05 uM through a voltage sensor-trapping mechanism (PubMed:23246579). It increases muscle contraction in several assays (mouse phrenic nerve-diaphragm, toad heart, rat vas deferens) and is suggested to act both presynaptically and postsynaptically (PubMed:17618665). FUNCTION: Moderately inhibits voltage-gated sodium channels and weakly inhibits voltage-gated potassium channel (PubMed:17150181, PubMed:17618665, PubMed:23246579, PubMed:26721415). Inhibits the inactivation of rat Nav1.2/SCN2A (IC(50)=870 nM), rat Nav1.3/SCN3A (IC(50)=845 nM), rat Nav1.4/SCN4A (IC(50)=339 nM), human Nav1.5/SCN5A (IC(50)=335 nM) and human Nav1.7/SCN9A sodium channels (IC(50)=348 nM) (PubMed:26721415). The toxin delays the inactivation of sodium channels without affecting the activation and steady-state inactivation kinetics in the physiological range of voltages (PubMed:26721415). Site-directed mutagenesis of the sodium channel indicates that the toxin interacts with site 3 located at the extracellular S3-S4 linker of domain IV (PubMed:26721415). On potassium channels, it inhibits activation of channels with an IC(50) of 8.05 uM through a voltage sensor-trapping mechanism (PubMed:23246579). It increases muscle contraction in several assays (mouse phrenic nerve-diaphragm, toad heart, rat vas deferens) and is suggested to act both presynaptically and postsynaptically (PubMed:17618665). FUNCTION: Inhibits voltage-gated sodium channels, preferentially subtype Nav1.5/SCN5A (in cardiac myocytes), but also Nav1.6/SCN8A and Nav1.7/SCN9A (TTX-sensitive Nav in rat DRG neurons) and invertebrate Nav (in insect neurons) as well as voltage-gated potassium channels of the subtype Kv2.1/KCNB1. Is suggested to bind to site 3 of the sodium channels and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission. On potassium channels, inhibits activation of channels with an IC(50) of 8.05 uM through a voltage sensor-trapping mechanism (PubMed:23246579). Increases muscle contraction in several assays (mouse phrenic nerve-diaphragm, toad heart, rat vas deferens) and is suggested to act both presynaptically and postsynaptically. SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 33 (Jztx-1) subfamily.


FUNCTION: Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs). SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the OpgD/OpgG family.


FUNCTION: Catalyzes the cleavage of beta-carotene at its central double bond (15,15') to yield two molecules of all-trans-retinal. FUNCTION: Is required for retinal production and bacteriorhodopsin biogenesis. Probably catalyzes the cleavage of beta-carotene at its central double bond (15,15') to yield two molecules of all-trans- retinal. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the Brp/Blh beta-carotene diooxygenase family.


FUNCTION: Putative magnesium transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35.5) family.


FUNCTION: Di-iron-containing protein involved in the repair of iron- sulfur clusters damaged by oxidative and nitrosative stress conditions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RIC family. YtfE subfamily.


FUNCTION: Probable transcription factor. Binds to the consensus DNA sequence 5'-AACAAT-3'. Also binds 5'-CACAAT-3' and 5'-AATAAT-3' with similar affinity. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. Plays a role in the regulation of many virulence factors, motility, quorum sensing, mucoidy, a general mechanism for maintaining lytic phage in populations of bacteria, and biofilm formation. Positively controls the T6 secretion system by directly binding to the promoter regions of hcpA and hcpB, leading to their expression (By similarity). Thereby, allows to colonize several hosts efficiently including mammals, insects, nematodes and plants (PubMed:11717271). FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released (PubMed:9595661). Plays a role in the regulation of many virulence factors, motility, quorum sensing, mucoidy, a general mechanism for maintaining lytic phage in populations of bacteria, and biofilm formation (PubMed:2152909, PubMed:12644493, PubMed:10792721, PubMed:26633362, PubMed:29760208). Positively controls the T6 secretion system by directly binding to the promoter regions of hcpA and hcpB genes, leading to their expression (PubMed:29760208). Thereby, allows to colonize several hosts efficiently including mammals, insects, nematodes and plants (By similarity) (PubMed:2152909, PubMed:9595661, PubMed:12644493, PubMed:10792721, PubMed:26633362, PubMed:29760208). SIMILARITY: Belongs to the sigma-54 factor family.


FUNCTION: In vitro, in the presence of excess copper ions, exhibits ferroxidase and phenoloxidase activities (PubMed:11466290, PubMed:11527384, PubMed:11867755, PubMed:15317788, PubMed:15516598, PubMed:17804014, PubMed:25679350). Fe(2+) is an excellent substrate in the presence of excess Cu(2+), but is inactive in the absence of Cu(2+) (PubMed:15516598, PubMed:17804014). Oxidizes the phenolate iron siderophores enterobactin, 2,3-dihydroxybenzoate (2,3-DHB) and 3- hydroxyanthranilate (3-HAA) (PubMed:11466290, PubMed:15317788). Oxidation and thus inactivation of enterobactin could protect cells from the interaction of enterobactin with copper and play a central role as an interface between copper detoxification and iron homeostasis (PubMed:11466290, PubMed:15317788). Also oxidizes a variety of phenolic model substrates, including 2,2'-azinobis(3-ethylbenzthiazolinesulfonic acid) (ABTS), p-phenylenediamine (pPD), 2,6-dimethoxyphenol (2,6-DMP) and 3,4-dihydroxybenzoic acid (3,4-DHB) (PubMed:11466290, PubMed:11527384, PubMed:17804014, PubMed:25679350). FUNCTION: Multicopper oxidase involved in copper homeostasis and copper tolerance under aerobic conditions (PubMed:11222619, PubMed:11399769, PubMed:11527384, PubMed:15516598). Is responsible for the oxidation of Cu(+) to the less harmful Cu(2+) in the periplasm, thereby preventing Cu(+) from entering the cytoplasm (PubMed:15516598, PubMed:20088522, PubMed:25679350). Probably primarily functions as a cuprous oxidase in vivo (PubMed:20088522). SUBCELLULAR LOCATION: Periplasm Note=Exported via the Tat pathway (PubMed:10766774, PubMed:17218314, PubMed:27129241). Cytoplasmic CueO does not contain copper, even under copper stress conditions, and is transported as an apo-protein to the periplasm. Periplasmic CueO is readily activated by the addition of copper ions in vitro or under copper stress conditions in vivo (PubMed:27129241). Can also be exported by the Sec system (PubMed:17218314). SIMILARITY: Belongs to the multicopper oxidase family.


FUNCTION: Thought to be a regulatory component of the ATP-synthesizing complex in the mitochondria. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the ATPase inhibitor family.


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


FUNCTION: Regulates G protein-coupled receptor signaling cascades, including signaling via muscarinic acetylcholine receptors and dopamine receptors. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Modulates the activity of potassium channels that are activated in response to G protein-coupled receptor signaling. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Membrane; Peripheral membrane protein; Cytoplasmic side Perikaryon Cell projection, dendrite Nucleus Note=Detected in Purkinje cell soma and dendrites. Associated with Purkinje cell membranes. Not detected in Purkinje cell nuclei. Detected in the nucleus after heterologous expression. Recruited to the cell membrane in the presence of GNAO1.


FUNCTION: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state.


FUNCTION: Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA- DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together with the P protein, and reverse-transcribed inside the nucleocapsid. Initiation of reverse-transcription occurs first by binding the epsilon loop on the pgRNA genome, and is initiated by protein priming, thereby the 5'-end of (-)DNA is covalently linked to P protein. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA). The activity of P protein does not seem to be necessary for cccDNA generation, and is presumably released from (+)DNA by host nuclear DNA repair machinery. SIMILARITY: Belongs to the hepadnaviridae P protein family.


FUNCTION: Involved in a membrane generated redox signal; required to maintain repression of photosynthesis gene expression in the presence of oxygen. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.


FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 1 family.


FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IA subfamily.


SUBCELLULAR LOCATION: Protein storage vacuole.


FUNCTION: Involved in the mineralization and structural organization of enamel. SUBCELLULAR LOCATION: Secreted Note=Secreted at a very early stage of enamel formation, and tightly bound to the surface of the growing crystallites. SIMILARITY: Belongs to the tuftelin family.


FUNCTION: A calcium channel that regulates synaptic endocytosis and hence couples exo- with endocytosis. Required in the nervous system and necessary in photoreceptor cells (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein Note=Upon fusion of the synaptic vesicle with the presynaptic membrane, protein is present in the periactive zones, where endocytosis is known to occur. SIMILARITY: Belongs to the calcium channel flower family.


SIMILARITY: Belongs to the universal ribosomal protein uL16 family.


FUNCTION: Specifically dephosphorylates sphingosine 1-phosphate (S1P), dihydro-S1P, and phyto-S1P. Does not act on ceramide 1-phosphate, lysophosphatidic acid or phosphatidic acid. Sphingosine-1-phosphate phosphatase activity is needed for efficient recycling of sphingosine into the sphingolipid synthesis pathway. Regulates the intracellular levels of the bioactive sphingolipid metabolite S1P that regulates diverse biological processes acting both as an extracellular receptor ligand or as an intracellular second messenger (By similarity). Involved in efficient ceramide synthesis from exogenous sphingoid bases. Converts S1P to sphingosine, which is readily metabolized to ceramide via ceramide synthase. In concert with sphingosine kinase 2 (SphK2), recycles sphingosine into ceramide through a phosphorylation/dephosphorylation cycle (By similarity). Regulates endoplasmic-to-Golgi trafficking of ceramides, resulting in the regulation of ceramide levels in the endoplasmic reticulum, preferentially long-chain ceramide species, and influences the anterograde membrane transport of both ceramide and proteins from the endoplasmic reticulum to the Golgi apparatus (By similarity). The modulation of intracellular ceramide levels in turn regulates apoptosis (By similarity). Via S1P levels, modulates resting tone, intracellular Ca(2+) and myogenic vasoconstriction in resistance arteries. Also involved in unfolded protein response (UPR) and ER stress-induced autophagy via regulation of intracellular S1P levels (By similarity). Involved in the regulation of epidermal homeostasis and keratinocyte differentiation (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the type 2 lipid phosphate phosphatase family.


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


FUNCTION: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:33795473, PubMed:27193682, PubMed:2194289, PubMed:2363050, PubMed:2374612). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473, PubMed:27007846). The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C (PubMed:33795473). TBP forms the TFIID-A module together with TAF3 and TAF5 (PubMed:33795473). TBP is a general transcription factor that functions at the core of the TFIID complex (PubMed:33795473, PubMed:27193682, PubMed:2194289, PubMed:2363050, PubMed:2374612, PubMed:9836642). During assembly of the core PIC on the promoter, as part of TFIID, TBP binds to and also bends promoter DNA, irrespective of whether the promoter contains a TATA box (PubMed:33795473). Component of a BRF2-containing transcription factor complex that regulates transcription mediated by RNA polymerase III (PubMed:26638071). Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC during RNA polymerase I-dependent transcription (PubMed:15970593). The rate of PIC formation probably is primarily dependent on the rate of association of SL1 with the rDNA promoter (PubMed:15970593). SL1 is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA (PubMed:15970593). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TBP family.


FUNCTION: May act as a carrier of hyaluronan in serum or as a binding protein between hyaluronan and other matrix protein, including those on cell surfaces in tissues to regulate the localization, synthesis and degradation of hyaluronan which are essential to cells undergoing biological processes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ITIH family.


FUNCTION: May suppress myogenic differentiation by modulating MYOG expression and Erk1/2 signaling. SIMILARITY: Belongs to the LRRC75 family.


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


FUNCTION: Receptor for gonadotropin releasing hormone (GnRH) that mediates the action of GnRH to stimulate the secretion of the gonadotropic hormones luteinizing hormone (LH) and follicle-stimulating hormone (FSH). This receptor mediates its action by association with G- proteins that activate a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Receptor to interleukin-8, which is a powerful neutrophils chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Encapsidates the viral DNA into characteristic twinned ('geminate') particles. Binds the genomic viral ssDNA and shuttles it into and out of the cell nucleus. The CP of bipartite geminiviruses is not required for cell-to-cell or systemic movement. SUBCELLULAR LOCATION: Virion Host nucleus Note=It is actively transported into the host cell nucleus. It may be exported out of the nucleus through a nuclear export signal for cell- to-cell movement and spread (By similarity). SIMILARITY: Belongs to the geminiviridae capsid protein family.


FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4 family.


FUNCTION: Orphan receptor. May bind to a neuropeptide and may regulate nociceptor function and/or development, including the sensation or modulation of pain. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Mas subfamily.


SIMILARITY: Belongs to the transposase 11 family.


FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. SUBCELLULAR LOCATION: Cytoplasm, cytosol Mitochondrion intermembrane space Note=Predominantly mitochondrial. SIMILARITY: Belongs to the adenylate kinase family. AK2 subfamily.


FUNCTION: Might be involved in the expression of prgA, but is not required for activation of the expression of prgB.


FUNCTION: Polyol dehydrogenase that catalyzes the reversible NAD(+)- dependent oxidation of various sugar alcohols. Is mostly active with xylitol, L-iditol and D-sorbitol (D-glucitol) as substrates, leading to the C2-oxidized products D-xylulose, L-sorbose and D-fructose, respectively (PubMed:1459146). Is a key enzyme in the polyol pathway that interconverts glucose and fructose via sorbitol, which constitutes an important alternate route for glucose metabolism (By similarity). May play a role in sperm motility by using sorbitol as an alternative energy source for sperm motility (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane; Peripheral membrane protein Cell projection, cilium, flagellum Note=Associated with mitochondria of the midpiece and near the plasma membrane in the principal piece of the flagellum. Also found in the epididymosome, secreted by the epididymal epithelium and that transfers proteins from the epididymal fluid to the sperm surface. SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family.


SIMILARITY: Belongs to the bacterial solute-binding protein 1 family. WtpA subfamily.


SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Phosphotriesterase family.


FUNCTION: Catalyzes the isomerization of L-ribulose 5-phosphate to D- xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate utilization. SIMILARITY: Belongs to the aldolase class II family. AraD/FucA subfamily.


FUNCTION: Probable xylan acetyltransferase required for 2-O- and 3-O- monoacetylation of xylosyl residues in xylan (PubMed:29569182). Possesses extremely low activity in vitro (PubMed:29569182). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.


FUNCTION: Mitochondrial glycine transporter that imports glycine into the mitochondrial matrix. Plays an important role in providing glycine for the first enzymatic step in heme biosynthesis, the condensation of glycine with succinyl-CoA to produce 5-aminolevulinate (ALA) in the mitochondrial matrix. Required during erythropoiesis. FUNCTION: May play a role as pro-apoptotic protein that induces caspase-dependent apoptosis. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family. SLC25A38 subfamily.


FUNCTION: Sesquiterpene synthase that catalyzes the conversion of farnesyl diphosphate to (-)-5-epi-eremophilene. SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.


SIMILARITY: Belongs to the UPF0242 family.


FUNCTION: RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are used as primers by PB1 for transcription of viral mRNAs. During virus replication, PB1 initiates RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn serves as a template for the production of more vRNAs. SUBCELLULAR LOCATION: Host nucleus Host cytoplasm. SIMILARITY: Belongs to the influenza viruses polymerase PB1 family.


FUNCTION: Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpA that pull DNA away from mid-cell into both cell halves. SUBCELLULAR LOCATION: Cytoplasm Note=Associated with two foci at the outer edges of the nucleoid region in young cells, and at four foci within both cell halves in older cells. SIMILARITY: Belongs to the ScpB family.


FUNCTION: May reduce toxic product malonic semialdehyde to 3- hydroxypropionic acid, which is excreted. SIMILARITY: Belongs to the nitroreductase family. HadB/RutE subfamily.


FUNCTION: Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. Involved in bone resorption. SIMILARITY: Belongs to the DEF8 family.


FUNCTION: Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.


FUNCTION: Acts as histone H2A/H2B chaperone in nucleosome assembly. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the nucleosome assembly protein (NAP) family.


FUNCTION: Responsible in a heterologous system for the transport of sucrose into the cell, with the concomitant uptake of protons (symport system). Can also transport biotin, and probably maltose at a lesser rate. In planta, the role of SUC5 for the transport of sucrose seems to be negligible. Plays a role in the nutrition of the filial tissues during early seed development and is probably involved in the import of biotin into the endosperm and the embryo epidermis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycoside-pentoside-hexuronide (GPH) cation symporter transporter (TC 2.A.2.4) family.


FUNCTION: Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Binding of extracellular ligands such as growth factors, cytokines and hormones to their cell-surface receptors activates RAS and this initiates RAF1 activation. RAF1 then further activates the dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK cascade, and catalyze the concomitant phosphorylation of a threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located in the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2, leading to their activation and further transduction of the signal within the MAPK/ERK cascade. Depending on the cellular context, this pathway mediates diverse biological functions such as cell growth, adhesion, survival and differentiation predominantly through the regulation of transcription, metabolism and cytoskeletal rearrangements (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily.


FUNCTION: Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta). SUBCELLULAR LOCATION: Host cytoplasm Host nucleus Note=Predominantly found in the host nucleus. SIMILARITY: Belongs to the papillomaviridae E7 protein family.


FUNCTION: Involved in Beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Beta- (1-->2)glucan exporter (TC 3.A.1.108.1) family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 2 family. Mth subfamily.


FUNCTION: Insecticidal neurotoxin that induces an irreversible spastic paralysis when injected into insects. Modifies presynaptic voltage- gated sodium channels (Nav), causing them to open at the normal resting potential of the nerve. This leads to spontaneous release of neurotransmitter and repetitive action potentials in motor neurons (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 07 (Beta/delta-agtx) family. 03 (aga-4) subfamily. Aga sub-subfamily.


FUNCTION: Plays a role in the catabolism of L-fucose, a sugar that is part of the carbohydrates that are attached to cellular glycoproteins. Catalyzes the dehydration of L-fuconate to 2-keto-3-deoxy-L-fuconate by the abstraction of the 2-proton to generate an enediolate intermediate that is stabilized by the magnesium ion. May down-regulate thymidylate synthase activity, possibly already at the RNA level, by promoting the degradation of TYMS mRNA via an antisense RNA-based mechanism. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mandelate racemase/muconate lactonizing enzyme family. ENOSF1 subfamily.


FUNCTION: Plays a role in the regulation of cell shape and polarity. Plays a role in cellular protein transport, including protein transport away from primary cilia. Neuroprotective protein (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cell projection, cilium. SIMILARITY: Belongs to the RILPL family.


FUNCTION: Required for KRAS signaling regulation and modulation of cell proliferation (By similarity). Regulator of KRAS prenylation, and probably prenylation of other small GTPases (By similarity). Required for lymphocyte development and function (By similarity). Not required for myeloid cell development (By similarity). SIMILARITY: Belongs to the small GTPase superfamily. Rab family.


FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This alternative sigma factor is specific for the flagellin gene (fliC) expression. SIMILARITY: Belongs to the sigma-70 factor family.


FUNCTION: Involved in telomere length regulation and promotes fully efficient non-homologous end-joining (NHEJ) by a mechanism activated in postdiauxic/stationary phase. SUBCELLULAR LOCATION: Nucleus Chromosome, telomere. SIMILARITY: Belongs to the FYV6 family.


FUNCTION: Binds estrogens, fatty acids and metals. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. SUBCELLULAR LOCATION: [Isoform 1]: Secreted. SIMILARITY: Belongs to the ALB/AFP/VDB family.


FUNCTION: Transcriptional repressor of nitrogen fixation and assimilation genes. Binds to two tandem operators in the glnA and nif promoters, thereby blocking transcription of the genes. SIMILARITY: Belongs to the NrpR family.


FUNCTION: Probably functions as a hexose-6-phosphate 1-epimerase. SIMILARITY: Belongs to the glucose-6-phosphate 1-epimerase family.


FUNCTION: Involved in the regulation of cellular calcium homeotasis (PubMed:25996873). Required for spermatogenesis (PubMed:25996873). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein.


FUNCTION: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. SIMILARITY: Belongs to the peptidase M24B family.


FUNCTION: Glycosyltransferase that catalyze the transfer of GlcNAc from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans through a beta1-4 linkage and participates in the production of tri- and tetra-antennary N-linked sugar chains (By similarity). Involved in glucose transport by mediating SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression of SLC2A2 in pancreatic beta cells (By similarity). SUBCELLULAR LOCATION: [Alpha-1,3-mannosyl-glycoprotein 4-beta-N- acetylglucosaminyltransferase A soluble form]: Secreted. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 54 family.


SIMILARITY: Belongs to the CarA family.


FUNCTION: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the KAE1 / TsaD family.


FUNCTION: Serine peptidase whose precise substrate specificity remains unclear (By similarity). Does not cleave peptides after a arginine or lysine residue (By similarity). Regulates trans-Golgi network morphology and sorting by regulating the membrane binding of the AP-1 complex (By similarity). May play a role in the regulation of synaptic vesicle exocytosis (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Golgi apparatus, trans-Golgi network Cytoplasm, cytoskeleton Golgi apparatus Nucleus Note=Co-localizes with AP-1 in the trans-Golgi network (By similarity). Co-localizes with MAP2 and ACTB on the cytoskeleton (By similarity). Co-localizes with STX6 and GOSR2 at the Golgi apparatus (By similarity). SIMILARITY: Belongs to the peptidase S9A family.


FUNCTION: Orphan nuclear receptor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family.


FUNCTION: Removes maltotriose and maltotetraose chains that are attached by 1,6-alpha-linkage to the limit dextrin main chain, generating a debranched limit dextrin. SIMILARITY: Belongs to the glycosyl hydrolase 13 family.


FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.


FUNCTION: Catalyzes the aminotransferase reaction from putrescine to 2- oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline (PubMed:12617754, PubMed:3510672). This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4- aminobutanoate (gamma-aminobutyrate or GABA) via 4-aminobutanal, which allows E.coli to grow on putrescine as the sole nitrogen source (PubMed:3510672, PubMed:22636776). Also functions as a cadaverine transaminase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate (PubMed:12617754, PubMed:30498244). Is also able to transaminate spermidine, in lower extent, but not ornithine. Alpha-ketobutyrate and pyruvate can also act as amino acceptors, although much less efficiently (PubMed:12617754). FUNCTION: Catalyzes the aminotransferase reaction from putrescine to 2- oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate (gamma-aminobutyrate or GABA) via 4- aminobutanal. Also functions as a cadaverine transaminase in a a L- lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. Putrescine aminotransferase subfamily. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. Putrescine aminotransferase subfamily.


FUNCTION: This toxin acts as a voltage-dependent gating-modifier (PubMed:25240294). It inhibits the sodium conductance (IC(50)=124 nM) and slows the fast inactivation (EC(50)=1180 nM) of Nav1.5/SCN5A (PubMed:17176080, PubMed:25240294). It significantly shifts the activation to more depolarized voltages and decreases the deactivation of Nav1.5 currents upon extreme depolarization, but only slightly affects voltage-dependence of steady-state inactivation (PubMed:17176080, PubMed:25240294). In addition, this toxin causes an approximately five-fold decrease in the rate of recovery from inactivation and an approximately 1.9-fold reduction in the closed- state inactivation rate (PubMed:25240294). This toxin integrates the functions of site 3 toxins (alpha-scorpion toxins) with site 4 toxins (beta-scorpion and spider toxins) by targeting multiple sites on Nav1.5 (PubMed:25240294). Also shows inhibition of voltage-gated potassium channels (5 uM completely inhibits Kv2.1/KCNB1, whereas 5 uM moderately inhibits Kv4.2/KCND2 Kv4.1/KCND1 channels) (PubMed:17176080). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 28 (Jztx-11) subfamily.


FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis. SIMILARITY: Belongs to the pyridoxal phosphate-binding protein YggS/PROSC family.


FUNCTION: May be involved in endocytic recycling of growth factor receptors such as EGFR. SUBCELLULAR LOCATION: Cytoplasm, cytosol.


FUNCTION: Plays a role in biomineralization. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the amelogenin family.


FUNCTION: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation. Induces fibroblasts to differentiate into myoblasts. Interacts with and is inhibited by the twist protein. This interaction probably involves the basic domains of both proteins (By similarity). SUBCELLULAR LOCATION: Nucleus.


SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Periplasmic side Note=Has been isolated in association with the inner membrane, suggesting it may be tethered to the membrane. SIMILARITY: To E.coli YihF and H.influenzae HI_1236.


FUNCTION: E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2). SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.


FUNCTION: Could be a NAD-dependent oxidoreductase.


FUNCTION: Involved in succinate export with YjjP. Both proteins are required for export. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ThrE exporter (TC 2.A.79) family.


FUNCTION: Catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D- glucosamine (PGA), a biofilm adhesin polysaccharide. N-deacetylation promotes PGA export through the PgaA porin (By similarity). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor; Periplasmic side. SIMILARITY: Belongs to the polysaccharide deacetylase family.


FUNCTION: Plays an important role in regulating intracellular signaling events associated with erythroid terminal differentiation. SUBCELLULAR LOCATION: Nucleus Cytoplasm Midbody Note=Shuttles between nucleus and cytoplasm during the cell cycle.


FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate. SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate mutase family.


FUNCTION: Essential for respiratory growth and required for mitochondrial protein synthesis. Required for vacuolar acidification (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the RRG1 family.


FUNCTION: Cytochrome P450 hydroxylase catalyzing the conversion of decanoate (capric acid) and dodecanoate (lauric acid) to their corresponding omega-hydroxy metabolites, 10-hydroxydecanoate and 12- hydroxydodecanoate, respectively; these hydroxylated components affect plant growth, including reducing root elongation. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins- secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:22158414, PubMed:20176268). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:20176268, PubMed:17576170). SUBCELLULAR LOCATION: Secreted Cell membrane.


FUNCTION: Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (By similarity). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (By similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (By similarity). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the peptidase M10A family.


FUNCTION: MAP4K component of the MAPK pathway required for the mating pheromone response and the regulation of cell polarity and cell cycle. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. STE20 subfamily.


FUNCTION: Has a major regulatory role in sexual and asexual development. It may bind DNA itself or it may have a role in preventing DNA-binding of another protein. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TALE/M-ATYP homeobox family.


SIMILARITY: Belongs to the SURF2 family.


FUNCTION: Glycosyltransferase involved in the biosynthesis of aurones, plant flavonoids that provide yellow coloration to flowers. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the UDP-glycosyltransferase family.


SIMILARITY: Belongs to the UPF0597 family.


FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets dietary phospholipids in the intestinal tract. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines. May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation in the intestinal tract. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (By similarity). May act in an autocrine and paracrine manner (By similarity). Has anti- helminth activity in a process regulated by gut microbiota. Upon helminth infection of intestinal epithelia, directly affects phosphatidylethanolamine contents in the membrane of helminth larvae, likely controlling an array of phospholipid-mediated cellular processes such as membrane fusion and cell division while providing for better immune recognition, ultimately reducing larvae integrity and infectivity (By similarity). SUBCELLULAR LOCATION: Secreted Note=Secreted from pancreatic acinar cells in its inactive form. SIMILARITY: Belongs to the phospholipase A2 family.


FUNCTION: Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence (By similarity). SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.


FUNCTION: Tyrosine-protein kinase that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, cell attachment and cell spreading. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down-stream of the activated FCER1 receptor and the mast/stem cell growth factor receptor KIT. Plays a role in the regulation of mast cell degranulation. Plays a role in the regulation of cell differentiation and promotes neurite outgrowth in response to NGF signaling. Plays a role in cell scattering and cell migration in response to HGF-induced activation of EZR. Phosphorylates BCR and down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1, PECAM1, STAT3 and TRIM28. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle. Golgi apparatus. Cell junction, focal adhesion. Note=Distributed throughout the cytosol when the kinase is not activated. Association with microtubules requires activation of the kinase activity. Shuttles between focal adhesions and cell-cell contacts in epithelial cells. Recruited to the lateral cell membrane in polarized epithelial cells by interaction with phosphorylated EZR. Detected at tubular membrane structures in the cytoplasm and at the cell periphery. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Fes/fps subfamily.


FUNCTION: Acyl-CoA-dependent lysophosphatidic acid acyltransferase with preference for oleoyl-CoA. Involved in triacylglyceride homeostasis and lipid droplet formation. Involved in vacuolar protein sorting. SUBCELLULAR LOCATION: Lipid droplet Endoplasmic reticulum membrane; Single-pass membrane protein Note=Lipid droplets consist of a surface phospholipid monolayer and a hydrophobic interior. The latter makes embedding of proteins containing transmembrane segments difficult, and these may instead adopt a hairpin or monotonic conformation when associated with lipid droplet membranes. Always localizes to lipid droplets, irrespective of whether cells are grown on glucose or oleate. SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase 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 4 family.


FUNCTION: Inactivates the type B streptogramin antibiotics by linearizing the lactone ring at the ester linkage, generating a free phenylglycine carboxylate and converting the threonyl moiety into 2- amino-butenoic acid. SIMILARITY: Belongs to the Vgb family.


FUNCTION: Copper metallothionein that protects the cell against copper toxicity by tightly chelating copper ions (PubMed:21819456, PubMed:23498952). Required for antioxidant-mediated growth rescue in the presence of fluconazole (PubMed:31694529). Acts as a critical factors for lung colonization and virulence (PubMed:23498952). SUBCELLULAR LOCATION: Cytoplasm, cell cortex. SIMILARITY: Belongs to the metallothionein superfamily.


FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. SIMILARITY: Belongs to the ACBP family.


FUNCTION: Phosphorylates proteins on serine, threonine, and tyrosine (By similarity). Probably associated with cell proliferation (By similarity). Phosphorylates MAD1L1 to promote mitotic checkpoint signaling (By similarity). Essential for chromosome alignment by enhancing AURKB activity (via direct CDCA8 phosphorylation) at the centromere, and for the mitotic checkpoint (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


FUNCTION: RING-type ubiquitin E3 ligase that binds ubiquitin and is required for seed germination and post-germination growth.


FUNCTION: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments. SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PRA1 family.


FUNCTION: Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO. SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. Type 2 subfamily.


FUNCTION: May play a role in neuronal and neurobehavioral development. SIMILARITY: Belongs to the UPF0524 family.


FUNCTION: Transcription factor that binds specifically to the DRE (dual repressor element) and represses HTR1A gene transcription in neuronal cells. The combination of calcium and ATP specifically inactivates the binding with FRE. May play a role in the altered regulation of HTR1A associated with anxiety and major depression. Mediates HDAC-independent repression of HTR1A promoter in neuronal cell. Performs essential function in controlling functional maturation of synapses. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the CC2D1 family.


FUNCTION: Confers immunity to L5 superinfection, required for maintenance of the lysogenic state. Binds to multiple asymmetric DNA sites. Regulates transcription initiation at an early lytic promoter, Pleft, but also affects downstream gene expression at 'stoperator' sites in the phage genome.


FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D- erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily. SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eL32 family.


FUNCTION: Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2- deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway. FUNCTION: Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2- deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway. SIMILARITY: Belongs to the glycosyltransferase group 1 family. MshA subfamily. SIMILARITY: Belongs to the glycosyltransferase group 1 family. MshA subfamily.


FUNCTION: DEAD-box RNA helicase involved in RNA degradation. Has RNA- dependent ATPase activity and unwinds double-stranded RNA. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DEAD box helicase family. RhlB subfamily.


FUNCTION: Required for the assembly and stability of the mitochondrial ribosome (By similarity). Is a positive regulator of mitochondrial protein synthesis (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Mitochondrion inner membrane. SIMILARITY: Belongs to the peroxisomal membrane protein PXMP2/4 family.


SIMILARITY: Belongs to the UPF0434 family.


FUNCTION: Probable methyltransferase.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the drug/metabolite transporter (DMT) superfamily. Plant drug/metabolite exporter (P-DME) (TC 2.A.7.4) family.


FUNCTION: Acts as a neurotoxin by inhibiting voltage-gated potassium channels (Kv). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conopeptide I2-like superfamily.


FUNCTION: Membrane-perturbating peptide with multiple activities (PubMed:34302796). It is insecticidal, since it induces contractile paralysis in insects (L.cuprina) during several hours, and death after 24 hours (PubMed:34302796). It shows antibacterial activity with higher activity against Gram-positive than Gram-negative bacteria (PubMed:34302796). It is also antiparasitic, since it potently inhibits the larval development of the major pathogenic nematode of ruminants (H.contortus, IC(50)=5.1 uM), but fails to reduce the motility of adult males of the other nematode B.malayi (PubMed:34302796). It also shows cytotoxic activity against HEK293 cells (EC(50)=12-14 uM) and induces hemolysis in human erythrocytes (EC(50)=28.6-48.2 uM) (PubMed:34302796). In addition, it causes an important increase in intracellular calcium concentration on neuronal and epithelial cell lines, which supports a non-specific membrane perturbation mechanism of action (PubMed:34302796). In vivo, it induces pain by intraplantar injection into mice, suggesting a defensive function against vertebrate predators (PubMed:34302796). SUBCELLULAR LOCATION: Secreted Target cell membrane Note=Adopts an alpha- helical conformation in membrane-mimetic environments. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Medium-length antimicrobial peptide (group 3) family. Ponericin-W subfamily.


FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: [Isoform 3]: Cell projection, cilium, flagellum Note=Principal piece region of the sperm flagellum. SUBCELLULAR LOCATION: [Isoform 2]: Cell projection, cilium, flagellum Note=Principal piece region of the sperm flagellum. SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily.


FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. VAP cleaves the fusion proteins of Sendai virus, NDV, and influenza virus a at a specific single arginine- containing site, and plays a key role in the viral spreading in the allantoic sac. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family.


FUNCTION: Transcriptional coactivator that specifically associates with POU2F3. This complex drives the development of tuft cells, a rare a rare chemosensory cells that coordinate immune and neural functions within mucosal epithelial tissues. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the POU2AF family.


FUNCTION: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of hydrogenobyrinate, using either L- glutamine or ammonia as the nitrogen source. SIMILARITY: Belongs to the CobB/CbiA family.


FUNCTION: [Truncated CTR1 form]: Mobilizes copper(1+) out of the endosomal compartment, making copper(1+) available for export out of the cells. FUNCTION: [High affinity copper uptake protein 1]: Uniporter that mediates the transport of copper(1+) from the extracellular space to the cytoplasm, across the plasma membrane and delivers directly copper(1+) to specific chaperone such as ATOX1, via a copper(1+)- mediated transient interaction between the C-terminal domain and a copper(1+) chaperone, thus controlling intracellular copper(1+) levels (By similarity). May function in copper(1+) import from the apical membrane thus may drive intestinal copper absorption (By similarity). The copper(1+) transport mechanism is sodium- independent, saturable and of high-affinity. Also mediates the uptake of silver(1+). May function in the influx of the platinum-containing chemotherapeutic agents (By similarity). The platinum-containing chemotherapeutic agents uptake is saturable (By similarity). In vitro, mediates the transport of cadmium(2+) into cells. Also participates in the first step of copper(2+) acquisition by cells through a direct transfer of copper(2+) from copper(2+) carriers in blood, such as ALB to the N-terminal domain of SLC31A1, leading to copper(2+) reduction and probably followed by copper(1+) stabilization. In addition, functions as a redox sensor to promote angiogenesis in endothelial cells, in a copper(1+) transport independent manner, by transmitting the VEGF-induced ROS signal through a sulfenylation at Cys-189 leadin g to a subsequent disulfide bond formation between SLC31A1 and KDR. The SLC31A1-KDR complex is then co-internalized to early endosomes, driving a sustained VEGFR2 signaling (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Early endosome membrane; Multi-pass membrane protein Recycling endosome membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein Late endosome membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Note=The localization is controlled by the intra and extra-cellular copper concentration. Under conditions of elevated extracellular copper concentrations, it is rapidly internalized by endocytosis from the plasma membrane by a clathrin- and dynamin- mediated process and degradated in order to prevent intracellular copper accumulation and to reduce the transport of the copper across the membrane. The internalized SLC31A1 is then localized in early endosomes, and, upon a low extracellular copper concentrations, it is transported back to the plasma membrane in a RAB11A-dependent recycling pathway (By similarity). Localizes to the apical membrane in intestinal epithelial cells (PubMed:20699218). Localizes to the neuronal cell body plasma membranes (By similarity). Mainly localized on the basolateral side of renal tubular cells (By similarity). SIMILARITY: Belongs to the copper transporter (Ctr) (TC 1.A.56) family. SLC31A subfamily.