FUNCTION: Participates in bacterial attachment to several surfaces, including various extracellular matrix (ECM) components and a hydrophobic abiotic surface. Involved in adhesion to host epithelial cells and is required for full virulence in mice. Also implicated in the resistance to porcine serum. SUBCELLULAR LOCATION: Cell surface Cell outer membrane Note=The C-terminal translocator domain is localized in the outer membrane and the passenger domain is at the cell surface (By similarity). Localizes at the new cell pole generated after cell division (PubMed:24236157). SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.


FUNCTION: Part of the ABC transporter complex CntABCDF (Opp1) involved in the uptake of metal in complex with the metallophore staphylopine (StP). Involved in the import of divalent metals ions such as nickel, cobalt and zinc. Binds the metal via the metallophore StP, and transfers the StP-metal complex to the membrane-bound permease (PubMed:23279021, PubMed:29581261). Binds one molecule of StP/metal. Binds StP/Co(2+) and StP/Ni(2+) tighter than StP/Zn(2+) (PubMed:29581261). Plays a major role in nickel/cobalt import in zinc- depleted conditions. Contributes to virulence. Required for full urease activity in vitro (PubMed:23279021). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.


FUNCTION: Involved in the production of the root hair deformation (HAD) factor specifically on medicago. SIMILARITY: To the R.leguminosarum biovar viciae counterpart.


FUNCTION: May play a role in the defense system against pathogens. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Calcium-dependent lectin that acts as a pattern recognition receptor (PRR) of the innate immune system: recognizes damage- associated molecular patterns (DAMPs) of abnormal self and pathogen- associated molecular patterns (PAMPs) of bacteria and fungi. The PAMPs notably include mycobacterial trehalose 6,6'-dimycolate (TDM), a cell wall glycolipid with potent adjuvant immunomodulatory functions. Interacts with signaling adapter Fc receptor gamma chain/FCER1G to form a functional complex in myeloid cells. Binding of mycobacterial trehalose 6,6'-dimycolate (TDM) to this receptor complex leads to phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 (Th1) and T-helper 17 (Th17) cell subtypes. Also recognizes alpha-mannose residues on pathogenic fungi of the genus Malassezia and mediates macrophage activation. Through recognition of DAMPs released upon nonhomeostatic cell death, enables immune sensing of damaged self and promotes inflammatory cell infiltration into the damaged tissue. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Cell projection, phagocytic cup.


FUNCTION: Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of BRI1. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor Note=Plasma membrane localization is required for its function in the regulation of brassinosteroid signaling.


FUNCTION: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the ExbD/TolR family.


FUNCTION: Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins. SUBCELLULAR LOCATION: Secreted Host cell membrane. SIMILARITY: Belongs to the RxLR effector family.


FUNCTION: Molecular adapter that acts as a bridge between proteins, and which is involved skeletal muscle development (By similarity). Functions as signal transducer for MSTN during skeletal muscle regeneration and myogenesis (By similarity). May regulate chemotaxis of both macrophages and myoblasts by reorganising actin cytoskeleton, leading to more efficient lamellipodia formation via a PI3 kinase dependent pathway (By similarity). In contrast to AKIRIN2, not involved in nuclear import of proteasomes (PubMed:34711951). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the akirin family.


FUNCTION: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking (By similarity). May associate with nucleic acids and regulate gene expression at the transcriptional or post- transcriptional level (By similarity). SUBCELLULAR LOCATION: Nucleus Cell membrane Note=Recruits calmodulin (CaM2) at plasma membrane subdomains. SIMILARITY: Belongs to the IQD family.


FUNCTION: Inhibitor of trypsin and chymotrypsin. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Catalyzes the ATP-dependent addition of one alpha-linked L- glutamate molecule to coenzyme gamma-F420-2, producing coenzyme alpha- F420-3. Thus, caps the gamma-polyglutamate tail of coenzyme F420 with a terminal alpha-linked glutamate (By similarity). SIMILARITY: Belongs to the RimK family. CofF subfamily.


FUNCTION: Catalyzes the reduction of nitrite to nitric oxide (NO), probably with azurin as electron donor. Essential for growth and survival in oxygen-depleted environments. Can also provide protection against killing by normal human sera. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the multicopper oxidase family.


FUNCTION: Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 1 subfamily.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the two pore domain potassium channel (TC 1.A.1.8) family.


FUNCTION: Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells (PubMed:23851396, PubMed:23934049, PubMed:2527252, PubMed:8033114, PubMed:8567728, PubMed:19074442). Has high affinity for folate and folic acid analogs at neutral pH (PubMed:23851396, PubMed:23934049, PubMed:2527252, PubMed:8033114, PubMed:8567728). Exposure to slightly acidic pH after receptor endocytosis triggers a conformation change that strongly reduces its affinity for folates and mediates their release (PubMed:8567728). Required for normal embryonic development and normal cell proliferation (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor Apical cell membrane; Lipid-anchor, GPI- anchor Basolateral cell membrane; Lipid-anchor, GPI-like-anchor Secreted Cytoplasmic vesicle Cytoplasmic vesicle, clathrin-coated vesicle Endosome Note=Endocytosed into cytoplasmic vesicles and then recycled to the cell membrane. SIMILARITY: Belongs to the folate receptor family.


FUNCTION: Has a role in chromosome segregation. May provide a dynamic connection between kinetochore microtubules and kinetochore chromatin. Negatively regulates mis12. SUBCELLULAR LOCATION: Nucleus Note=Associated with chromatin. SIMILARITY: Belongs to the PPP phosphatase family. PP-6 (PP-V) subfamily.


FUNCTION: Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of type I collagen. By acting on collagen glycosylation, facilitates the formation of collagen triple helix. Also involved in the biosynthesis of collagen type IV. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen Note=Colocalized with PLOD3 and mannose binding lectin. SIMILARITY: Belongs to the glycosyltransferase 25 family.


FUNCTION: Catalyzes the first step of diphthamide biosynthesis, a post- translational modification of histidine which occurs in elongation factor 2. Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase, predominantly cbr1. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DPH1/DPH2 family. DPH1 subfamily.


FUNCTION: Was first identified based on its probable role in the regulation of pituitary gene transcription. Binds to the prolactin gene (PRL) promoter and seems to activate transcription. FUNCTION: Guanine nucleotide exchange factor that specifically activates the small GTPase SAR1B. Mediates the recruitment of SAR1B and other COPII coat components to endoplasmic reticulum membranes and is therefore required for the formation of COPII transport vesicles from the ER. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Nucleus Note=Concentrates at endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER).


FUNCTION: Involved in chromosome segregation. Facilitates nuclear oscillation during meiotic prophase I, the 'horsetail' phase, by acting as a dynein anchor. Essential for anchoring dhc1 to the cortex. Required for proper sliding of the microtubules along the cell cortex, which leads to the proper U-turn movement of the nucleus. SUBCELLULAR LOCATION: Cytoplasm, cell cortex Note=Localizes to the cell cortex during the 'horsetail' phase of mitosis.


FUNCTION: Nucleotide pyrophosphatase that generates diphosphate (PPi) and functions in bone mineralization and soft tissue calcification by regulating pyrophosphate levels (PubMed:9662402, PubMed:10352096, PubMed:11004006, PubMed:12082181, PubMed:22510396, PubMed:25260930). PPi inhibits bone mineralization and soft tissue calcification by binding to nascent hydroxyapatite crystals, thereby preventing further growth of these crystals (PubMed:9662402, PubMed:10352096, PubMed:11004006, PubMed:12082181, PubMed:19419305, PubMed:22510396, PubMed:25260930, PubMed:25479107, PubMed:26910915, PubMed:30111653). Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP and UTP to their corresponding monophosphates with release of pyrophosphate, as well as diadenosine polyphosphates, and also 3',5'-cAMP to AMP (PubMed:11027689, PubMed:1647027, PubMed:23027977, PubMed:8223581). May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling (PubMed:1647027). Inhibits ectopic joint calcification and maintains articular chondrocytes by repressing hedgehog signaling; it is however unclear whether hedgehog inhibition is direct or indirect (PubMed:30111653). Appears to modulate insulin sensitivity (By similarity). Also involved in melanogenesis (By similarity). Also able to hydrolyze 2',3'-cGAMP (cyclic GMP-AMP), a second messenger that activates TMEM173/STING and triggers type-I interferon production (PubMed:25344812). 2',3'-cGAMP degradation takes place in the lumen or extracellular space, and not in the cytosol where it is produced; the role of 2',3'-cGAMP hydrolysis is therefore unclear (By similarity). Not able to hydrolyze the 2',3'-cGAMP linkage isomer 3',3'-cGAMP (By similarity). SUBCELLULAR LOCATION: [Ectonucleotide pyrophosphatase/phosphodiesterase family member 1]: Cell membrane; Single-pass type II membrane protein. Basolateral cell membrane; Single-pass type II membrane protein. Note=Targeted to the basolateral membrane in polarized epithelial cells and in hepatocytes, and to matrix vesicles in osteoblasts. SUBCELLULAR LOCATION: [Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, secreted form]: Secreted Note=Secreted following proteolytic cleavage. SIMILARITY: Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.


FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major phycobiliprotein in the PBS rod. SUBCELLULAR LOCATION: Plastid, cyanelle thylakoid membrane; Peripheral membrane protein; Stromal side Note=Part of the phycobilisome rod. SIMILARITY: Belongs to the phycobiliprotein family.


FUNCTION: May play a role in floral meristem development and maintenance of stamens, rather than in determining polarity in floral organs. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the YABBY family.


FUNCTION: Catalytic component of METTL1-WDR4 methyltransferase complex that mediates the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs). Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in a large subset of tRNAs that contain the 5'-RAGGU-3' motif within the variable loop. M7G46 interacts with C13-G22 in the D-loop to stabilize tRNA tertiary structure and protect tRNAs from decay. Also acts as a methyltransferase for a subset of internal N(7)-methylguanine in mRNAs. Internal N(7)-methylguanine methylation of mRNAs regulates translation. Also methylates a specific subset of miRNAs. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.


FUNCTION: Secreted growth factor that mediates its signal through cell- surface proteoglycan and non-proteoglycan receptors (PubMed:16814777, PubMed:11278720, PubMed:19141530). Binds cell-surface proteoglycan receptor via their chondroitin sulfate (CS) groups (PubMed:26896299, PubMed:27445335). Thereby regulates many processes like cell proliferation, cell survival, cell growth, cell differentiation and cell migration in several tissues namely neuron and bone (PubMed:1733956, PubMed:1768439, PubMed:11278720, PubMed:19141530, PubMed:27445335, PubMed:30667096, PubMed:19442624). Also plays a role in synaptic plasticity and learning-related behavior by inhibiting long-term synaptic potentiation (By similarity). Binds PTPRZ1, leading to neutralization of the negative charges of the CS chains of PTPRZ1, inducing PTPRZ1 clustering, thereby causing the dimerization and inactivation of its phosphatase activity leading to increased tyrosine phosphorylation of each of the PTPRZ1 substrates like ALK, CTNNB1 or AFAP1L2 in order to activate the PI3K-AKT pathway (PubMed:17681947, PubMed:27445335, PubMed:30667096, PubMed:16814777, PubMed:10706604). Through PTPRZ1 binding controls oligodendrocyte precursor cell differentiation by enhancing the phosphorylation of AFAP1L2 in order to activate the PI3K-AKT pathway (PubMed:27445335, PubMed:30667096). Forms a complex with PTPRZ1 and integrin alpha-V/beta-3 (ITGAV:ITGB3) that stimulates endothelial cell migration through SRC dephosphorylation and activation that consequently leads to ITGB3 'Tyr-773' phosphorylation (PubMed:19141530). In adult hippocampus promotes dendritic arborization, spine development, and functional integration and connectivity of newborn granule neurons through ALK by activating AKT signaling pathway (By similarity). Binds GPC2 and chondroitin sulfate proteoglycans (CSPGs) at the neuron surface, leading to abrogation of binding between PTPRS and CSPGs and neurite outgrowth promotion (By similarity). Binds SDC3 and mediates bone formation by recruiting and attaching osteoblasts/osteoblast precursors to the sites for new bone deposition (By similarity). Binds ALK and promotes cell survival and cell proliferation through MAPK pathway activation (PubMed:11278720). Inhibits proliferation and enhances differentiation of neural stem cells by inhibiting FGF2-induced fibroblast growth factor receptor signaling pathway (By similarity). Mediates regulatory mechanisms in normal hemostasis and in hematopoietic regeneration and in maintaining the balance of myeloid and lymphoid regeneration (By similarity). In addition may play a role in the female reproductive system, auditory response and the progesterone-induced decidualization pathway (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pleiotrophin family.


FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG) (By similarity). Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate effector cell activation in the absence of antigenic trigger. Mediates IgG effector functions on natural killer (NK) cells. Binds antigen-IgG complexes generated upon infection and triggers NK cell-dependent cytokine production and degranulation to limit viral load and propagation (By similarity). Fc-binding subunit that associates with FCER1G adapters to form functional signaling complexes. Following the engagement of antigen-IgG complexes, triggers phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapters with subsequent activation of phosphatidylinositol 3-kinase signaling and sustained elevation of intracellular calcium that ultimately drive NK cell activation (By similarity). Mediates enhanced ADCC in response to afucosylated IgGs (PubMed:34485821). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.


FUNCTION: During mitosis, may play a role in the metaphase-to-anaphase transition. SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Note=Partially localizes to the nucleolus.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the UPF0499 family.


FUNCTION: Adapter protein that functions as clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. May act as a tumor suppressor. SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Membrane, clathrin-coated pit. Note=Colocalizes with large insert-containing isoforms of MYO6 at clathrin-coated pits/vesicles. During mitosis is progressively displaced from the membrane and translocated to the cytoplasm.


FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. Contributes probably to the adaptation to inorganic phosphate (Pi) deprivation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PEPCase type 1 family.


FUNCTION: Mitochondrial transporter that mediates uptake of thiamine pyrophosphate (ThPP) into mitochondria. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.


FUNCTION: The replicase large subunit is an RNA-dependent RNA polymerase active in viral RNA replication. SIMILARITY: Belongs to the tobamovirus RNA-directed RNA polymerase family.


FUNCTION: Adapter protein able to interact with different proteins and involved in different biological processes (PubMed:11459825, PubMed:11459826, PubMed:17719540, PubMed:17296730, PubMed:19443654, PubMed:29656893). Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis (PubMed:20164194). Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions (PubMed:20164194). Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs) (PubMed:29656893). During G1 and S phase of the cell cycle, the complex functions downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and suppress DNA end resection (PubMed:29656893). Mediates various NHEJ-dependent processes including immunoglobulin class-switch recombination, and fusion of unprotected telomeres (PubMed:29656893). May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1 (PubMed:17296730). Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle (PubMed:11459825, PubMed:17719540). Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation (PubMed:19443654). SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, spindle Cytoplasm Chromosome Note=Recruited to sites of chromosomal double-stranded breaks during G1 and S phase of the cell cycle.


FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ketopantoate reductase family.


FUNCTION: HCNP may be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Seems to be mediated by a specific receptor (By similarity). FUNCTION: Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the phosphatidylethanolamine-binding protein family.


FUNCTION: Snake venom natriuretic peptide that exhibits hypotensive and vasorelaxant effects. Produces a dose-dependent hypotension in rats, followed by significant increases in concentrations of markers of nitric oxide (NO) formation measured in the plasma and vasorelaxation in a thoracic aortic ring bath. The peptide may exert its hypotensive action, at least in part, through stimulation of NO production. The vasorelaxant effect is endothelium-dependent and does not appear to be mediated by the natriuretic peptide receptor-A, as its action is not modified by isatin (a potent NPR1 antagonist). May act by activating the natriuretic peptide receptor-B (NPR2). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the natriuretic peptide family. Snake NP subfamily.


FUNCTION: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily.


FUNCTION: Catalyzes the sequential release of Tyr-Pro, Phe-Pro and Gly- Pro from the N-terminus of peptides and proteins. Is able to cleaves bioactive peptide beta-casomorphin. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. SUBCELLULAR LOCATION: [Isoform 1]: Periplasm. SIMILARITY: Belongs to the peptidase S9B family.


FUNCTION: Mediates visceral muscle contractile activity (myotropic activity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the kinin family.


FUNCTION: Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:17327425, PubMed:17068142, PubMed:17268472, PubMed:24742672). Required for normal body fat and glucose homeostasis (PubMed:17327425, PubMed:17068142, PubMed:17268472, PubMed:24742672). ADIPOQ-binding activates a signaling cascade that leads to increased PPARA activity, and ultimately to increased fatty acid oxidation and glucose uptake (PubMed:12802337, PubMed:17268472, PubMed:24742672). Has intermediate affinity for globular and full-length adiponectin (PubMed:12802337). Required for normal revascularization after chronic ischemia caused by severing of blood vessels (PubMed:24742672). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Localized to the cell membrane and intracellular organelles. SIMILARITY: Belongs to the ADIPOR family.


FUNCTION: Involved in the cross-linking of microtubules and microfilaments (PubMed:12584248, PubMed:24706950). Regulates microtubule dynamics and stability by interacting with microtubule plus-end tracking proteins, such as MAPRE1, to regulate microtubule growth along actin stress fibers (PubMed:24706950). Enhances ADORA2- mediated adenylyl cyclase activation by acting as a scaffold to recruit trimeric G-protein complexes to ADORA2A (By similarity). Regulates ciliary orientation and performance in cells located in the airway (PubMed:30665704). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell membrane Cytoplasm, cytoskeleton, stress fiber Cytoplasm, cytoskeleton, cilium basal body Note=Colocalizes with ADORA2A at neuronal processes (By similarity). Colocalizes with and tracks the tips of microtubule plus ends (PubMed:24706950). SIMILARITY: Belongs to the GAS2 family.


FUNCTION: Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. Phosphorylates NEDD9/HEF1 (By similarity). EIF6 phosphorylation promotes its nuclear export. Triggers down- regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate (By similarity). Interacts with DDX3X; this interaction enhances CSNK1D kinase activity in vitro, but it is unclear whether this interaction is physiologically relevant (By similarity). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. Casein kinase I subfamily.


FUNCTION: Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. SIMILARITY: Belongs to the heat shock protein 70 family.


FUNCTION: [Envelope protein E]: Binds to host cell surface receptor and mediates fusion between viral and cellular membranes. Envelope protein is synthesized in the endoplasmic reticulum in the form of heterodimer with protein prM. They play a role in virion budding in the ER, and the newly formed immature particle is covered with 60 spikes composed of heterodimer between precursor prM and envelope protein E. The virion is transported to the Golgi apparatus where the low pH causes dissociation of PrM-E heterodimers and formation of E homodimers. prM-E cleavage is ineficient, and many virions are only partially matured. These uncleaved prM would play a role in immune evasion. SUBCELLULAR LOCATION: [Envelope protein E]: Virion membrane; Multi-pass membrane protein Host endoplasmic reticulum membrane; Multi-pass membrane protein.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: To U.parvum UU008, UU041 and UU042.


FUNCTION: Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells. Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR. The VDR-RXR heterodimers bind to specific response elements on DNA and activate the transcription of vitamin D3- responsive target genes (By similarity). Plays a central role in calcium homeostasis (By similarity). Also functions as a receptor for the secondary bile acid lithocholic acid (LCA) and its metabolites (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Localizes mainly to the nucleus. Translocated into the nucleus via both ligand-dependent and ligand- independent pathways; ligand-independent nuclear translocation is mediated by IPO4. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily.


FUNCTION: NmrA-like family domain-containing oxidoreductase; part of the lna gene cluster that mediates the biosynthesis of diastereomeric piperazines. Lna and lnb clusters encode sets of enzymes that produce overlapping sets of previously undescribed metabolites such as piperazinomycin-like metabolites or morpholine (PubMed:23281040). The lna and lnb biosynthetic pathways appear to be part of a signaling network that controls the formation of sclerotia, a resilient overwintering structure (PubMed:23281040). One primary function of the non-canonical nonribosomal peptide synthetases lnaA and lnbA consists in the reduction of L-tyrosine (PubMed:23281040). The presence in the clusters of tailoring enzymes such as the oxidoreductases lnaB, lnbB, lnaE or lnbE, as well as of the cytochrome P450 monooxygenases lnaC, lnaD, or lnbC, might explain formation of various diastereomeric piperazines (PubMed:23281040). SIMILARITY: Belongs to the NmrA-type oxidoreductase family.


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. SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X' sub-subfamily.


FUNCTION: Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity. SIMILARITY: Belongs to the troponin I family.


FUNCTION: Lipid droplet-associated protein that maintains the balance between lipogenesis and lipolysis and also regulates fatty acid oxidation in oxidative tissues. Recruits mitochondria to the surface of lipid droplets and is involved in lipid droplet homeostasis by regulating both the storage of fatty acids in the form of triglycerides and the release of fatty acids for mitochondrial fatty acid oxidation. In lipid droplet triacylglycerol hydrolysis, plays a role as a scaffolding protein for three major key lipolytic players: ABHD5, PNPLA2 and LIPE. Reduces the triacylglycerol hydrolase activity of PNPLA2 by recruiting and sequestering PNPLA2 to lipid droplets. Phosphorylation by PKA enables lipolysis probably by promoting release of ABHD5 from the perilipin scaffold and by facilitating interaction of ABHD5 with PNPLA2. Also increases lipolysis through interaction with LIPE and upon PKA-mediated phosphorylation of LIPE (By similarity). SUBCELLULAR LOCATION: Lipid droplet Cytoplasm Mitochondrion Note=Lipid droplet surface-associated. Exchanges between lipid droplets and the cytoplasm. SIMILARITY: Belongs to the perilipin family.


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


FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6- phosphogluconolactone. Can utilize either NADP(+) or NAD(+). SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase family.


FUNCTION: Involved in UV protection and mutation. Essential for induced (or SOS) mutagenesis. May modify the DNA replication machinery to allow bypass synthesis across a damaged template (By similarity). FUNCTION: Involved in UV protection and mutation. Poorly processive, error-prone DNA polymerase involved in translesion repair (PubMed:10801133). Essential for induced (or SOS) mutagenesis. Able to replicate DNA across DNA lesions (thymine photodimers and abasic sites, called translesion synthesis) in the presence of activated RecA; efficiency is maximal in the presence of the beta sliding-clamp and clamp-loading complex of DNA polymerase III plus single-stranded binding protein (SSB) (PubMed:10801133). RecA and to a lesser extent the beta clamp-complex may target Pol V to replication complexes stalled at DNA template lesions (PubMed:10801133). SIMILARITY: Belongs to the peptidase S24 family.


FUNCTION: Required for the transposition of the insertion element. SIMILARITY: Belongs to the transposase IS30 family.


FUNCTION: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in FASLG, ITM2B and TNF processing (PubMed:16829952, PubMed:16829951, PubMed:17557115, PubMed:17965014). Catalyzes the intramembrane cleavage of the anchored fragment of shed TNF-alpha (TNF), which promotes the release of the intracellular domain (ICD) for signaling to the nucleus (PubMed:16829952). Also responsible for the intramembrane cleavage of Fas antigen ligand FASLG, which promotes the release of the intracellular FasL domain (FasL ICD) (PubMed:17557115). Essential for degradation of the invariant chain CD74 that plays a central role in the function of antigen-presenting cells in the immune system (By similarity). Plays a role in the regulation of innate and adaptive immunity (PubMed:16829952). Catalyzes the intramembrane cleavage of the simian foamy virus envelope glycoprotein gp130 independently of prior ectodomain shedding by furin or furin-like proprotein convertase (PC)-mediated cleavage proteolysis (PubMed:23132852). SUBCELLULAR LOCATION: Late endosome membrane; Multi-pass membrane protein Lysosome membrane; Multi- pass membrane protein Membrane; Multi-pass membrane protein; Lumenal side Note=Colocalizes with palmitoylated and myristoylated proteins at the plasma membrane. SIMILARITY: Belongs to the peptidase A22B family.


FUNCTION: Putative pheromone receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Major component of the eye of elephant shrews, which in contrast to other mammals, possesses both a lens- and a non-lens class- 1 aldehyde dehydrogenase 1. This eye-specific form is a structural protein of the lens and, in other part of the eye, serves as the major form of ALDH1. Can convert/oxidize retinaldehyde to retinoic acid. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aldehyde dehydrogenase family.


SIMILARITY: Belongs to the phage O protein family.


FUNCTION: Involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the MnmG family.


FUNCTION: Involved in the early part of the secretory pathway. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type I membrane protein Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the KISH family.


FUNCTION: Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1- diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'- monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine. FUNCTION: Acts on guanine, xanthine and to a lesser extent hypoxanthine. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. XGPT subfamily.


FUNCTION: Bacteriocin active against Listeria monocytogenes. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bacteriocin class IIA/YGNGV family.


FUNCTION: Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also plays an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, myofibril Cytoplasm, cytoskeleton, stress fiber Note=On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle). SIMILARITY: Belongs to the caldesmon family.


FUNCTION: Ceramide-binding protein that may transfer ceramides from the endoplasmic reticulum membrane to the cis-Golgi network membrane, and is thereby required for the biosynthesis of complex sphingolipids. SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane; Peripheral membrane protein Endoplasmic reticulum membrane; Peripheral membrane protein Cytoplasm Nucleus Note=Localizes to the interface between the cis-Golgi network and endoplasmic reticulum exit sites. SIMILARITY: Belongs to the SVF1 family.


FUNCTION: Endonuclease which resolves Holliday junctions (HJs) by the introduction of symmetrically related cuts across the junction point, to produce nicked duplex products in which the nicks can be readily ligated. Four-way DNA intermediates, also known as Holliday junctions, are formed during homologous recombination and DNA repair, and their resolution is necessary for proper chromosome segregation (PubMed:19020614, PubMed:26682650). Cleaves HJs by a nick and counter- nick mechanism involving dual coordinated incisions that lead to the formation of ligatable nicked duplex products. Cleavage of the first strand is rate limiting, while second strand cleavage is rapid. Largely monomeric, dimerizes on the HJ and the first nick occurs upon dimerization at the junction (PubMed:26578604). Efficiently cleaves both single and double HJs contained within large recombination intermediates. Exhibits a weak sequence preference for incision between two G residues that reside in a T-rich region of DNA (PubMed:28049850). Has also endonuclease activity on 5'-flap and replication fork (RF) DNA substrates (PubMed:26578604). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. GEN subfamily.


FUNCTION: This is a base non-specific ribonuclease. SIMILARITY: Belongs to the RNase T2 family.


FUNCTION: One of the components of the bacteriochlorophyll-protein complex in the chromatophore membrane.


FUNCTION: Antimicrobial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Caerin subfamily.


FUNCTION: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b family.


FUNCTION: Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone and D-glyceraldehyde 3-phosphate via an aldolization reaction. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the transaldolase family. Type 3A subfamily.


FUNCTION: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the transfer of the acetyl group from acetyl-CoA to the hydroxyl group of L-serine to yield the activated serine, O-acetyl-L-serine. It prefers L-serine over L-homoserine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.


FUNCTION: Acts as an anti-FlhC(2)FlhD(4) factor by binding to FlhD, decreasing its ability to bind DNA, and thus negatively regulates expression of flagellar class II operons, decreasing motility in nutrient-poor medium. Required for resistance to host phagocyte oxidase. Suppresses killing of macrophages, while promoting resistance to hydrogen peroxide. Data regarding c-di-GMP is controversial; suppresses bacterial c-di-GMP levels (PubMed:15882417) but neither synthesizes nor degrades c-di-GMP (PubMed:19376870). FUNCTION: Acts as an anti-FlhC(2)FlhD(4) factor by binding to FlhD, decreasing its ability to bind DNA, and thus negatively regulates expression of flagellar class II operons, decreasing motility in nutrient-poor medium. Positively regulates expression of the multicellular rdar morphotype behavior, its major regulator CsgD and suppresses motility. Regulates the rdar morphotype and motility indirectly by affecting the expression of the c-di-GMP-dependent phosphodiesterases YciZ and YhjH. Required for resistance to host phagocyte oxidase. Suppresses killing of macrophages, while promoting resistance to hydrogen peroxide. Data regarding c-di-GMP is controversial; suppresses bacterial c-di-GMP levels (PubMed:15882417) but neither synthesizes nor degrades c-di-GMP (PubMed:19376870). FUNCTION: Acts as an anti-FlhC(2)FlhD(4) factor by binding to FlhD, decreasing its ability to bind DNA, and thus negatively regulates expression of flagellar class II operons, decreasing motility in nutrient-poor medium. Required for resistance to host phagocyte oxidase (By similarity). SIMILARITY: Belongs to the YdiV family.


FUNCTION: Isopenicillin-N N-acyltransferase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic (PubMed:2120195, PubMed:2110531, PubMed:1368505). AatA catalyzes the exchange of the alpha-aminoadipyl side chain of isopenicillin N for phenylacetic acid to yield penicillin (PubMed:2120195, PubMed:2110531, PubMed:1368505). This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively (PubMed:23053082). The penicillin biosynthesis occurs via 3 enzymatic steps, the first corresponding to the production of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D- valine (LLD-ACV or ACV) by the NRPS acvA. The tripeptide ACV is then cyclized to isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin in the peroxisomal matrix (PubMed:1368505) (Probable). FUNCTION: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic (PubMed:1368505, PubMed:2120195, PubMed:2110531). The first step of the pathway is performed by the trimodular NRPS acvA that produces the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L- cysteinyl-D-valine (LLD-ACV or ACV) via condensation of the 3 residues L-2-aminoadipate, L-cysteine and L-valine (PubMed:9266851, PubMed:9355751, PubMed:19686863, PubMed:21889568). The precursor amino acids for penicillin biosynthesis are withdrawn from the vacuolar amino acid pool by the MFS-type transporter penV (PubMed:8416970, PubMed:22777282). Each of the constituent amino acids of the tripeptide acv are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates (PubMed:9266851, PubMed:21889568). The tripeptide ACV is then cyclized to form isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus (PubMed:1368505, PubMed:1369045, PubMed:1588566). Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin (PubMed:2120195, PubMed:2110531, PubMed:1368505). This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively (PubMed:23053082). SUBCELLULAR LOCATION: Peroxisome matrix Note=The unprocessed preprotein is translocated inside peroxisomes and regulates its self-processing. SIMILARITY: Belongs to the peptidase C45 family.


FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Is specific for tRNA(Asp) since it aspartylates tRNA(Asn) 3 orders of magnitude less efficiently than tRNA(Asp). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.


FUNCTION: Guanine-nucleotide exchange factor (GEF) that acts as an activator of Rop (Rho of plants) GTPases by promoting the exchange of GDP for GTP. In postembryonic roots, modulates root stem cell maintenance by regulating the expression of PLT1 and PLT2, which are key transcription factors that mediate the patterning of the root stem cell niche. May connect RopGEF-regulated Rac/Rop signaling and auxin- dependent PLT-regulated root pattern formation. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Interacts with ARAC1/ROP3 on plasma membrane.


FUNCTION: Membrane component of antiviral defense system Retron Ec48, composed of a non-coding RNA (ncRNA), a reverse transcriptase (RT) and this membrane protein. Expression of this retron confers protection against bacteriophages lambda, T2, T4, T5 and T7. At multiplicity of infection (MOI) of 0.02 cultures grow normally when infected with lambda without collapsing, at MOI 2 cultures enter growth stasis. At MOI 3 cell membranes are permeabilized within 15 minutes of infection but do not lyse, suggesting the phage are not able to finish a replication cycle. Antiviral defense is suppressed by mutations that knockout the lambda gam expression or phage T7 gp5.9 expression; both viral genes inhibit host RecBCD (PubMed:33157039). The Ec48 retron may sense the integrity of the RecBCD enzyme; when RecBCD is perturbed by viral proteins the Ec48 effector (the membrane protein) is activated, leading to abortive infection and bacterial growth arrest (Probable). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily. D49 sub-subfamily.


FUNCTION: Seed storage protein. Has a protein kinase activity. Binds leginsulin. SIMILARITY: Belongs to the peptidase A1 family.


FUNCTION: Alpha-mannosidase involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 47 family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS10 family.


FUNCTION: Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane (By similarity). SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the vesiculovirus glycoprotein family.


FUNCTION: Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia. SIMILARITY: Belongs to the anthranilate synthase component I family.


FUNCTION: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-272 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (By similarity). Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ALB/AFP/VDB family.


FUNCTION: Inhibits potassium channels. May be active towards small conductance calcium-activated potassium channels (KCNN, SK), and less active towards voltage-gated potassium channels (Kv/KCN). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 14 subfamily.


FUNCTION: [Isoform Crk-II]: Regulates cell adhesion, spreading and migration (PubMed:31311869). Mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4 (PubMed:19004829). May regulate the EFNA5-EPHA3 signaling (By similarity). FUNCTION: Involved in cell branching and adhesion mediated by BCAR1- CRK-RAPGEF1 signaling and activation of RAP1. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Translocated to the plasma membrane upon cell adhesion. SIMILARITY: Belongs to the CRK family.


FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine- induced inhibition of adenylate cyclase through the action of G proteins. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Interaction with RAB26, GGA1, GGA2 and GGA3 mediates transport from the Golgi to the cell membrane. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA2B sub-subfamily.


FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. Together with RAB11A, RAB3IP, RAB8A, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, perinuclear region Cell projection, growth cone Midbody, Midbody ring Note=Perinuclear in undifferentiated cells. Redistributes to growing neurites and growth cones during neuronal differentiation (By similarity). Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). SIMILARITY: Belongs to the SEC15 family.


FUNCTION: Involved in ABA and stress responses and acts as a positive component of glucose signal transduction. Functions as transcriptional activator in the ABA-inducible expression of rd29B. Binds specifically to the ABA-responsive element (ABRE) of the rd29B gene promoter. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the bZIP family. ABI5 subfamily.


FUNCTION: A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-GGWCC-3' and cleaves after G-1. SIMILARITY: Belongs to the TdeIII type II restriction endonuclease family.


FUNCTION: Probable transcription factor that binds to the DNA sequence 5'-GCATTAAATGC-3' (PubMed:16778018). Seems to promote cell differentiation (PubMed:25564655). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HD-ZIP homeobox family. Class IV subfamily.


FUNCTION: Transaminase that degrades gamma-amino butyric acid (GABA). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. Reduces ethyl 4-chloro-3- oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. SIMILARITY: Belongs to the aldo/keto reductase family.


FUNCTION: ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA, used for the elongation of fatty acids and biosynthesis of isoprenoids, flavonoids and malonated derivatives. May supply substrate to the cytosolic acetyl-CoA carboxylase, which generates the malonyl-CoA used for the synthesis of a multitude of compounds, including very long chain fatty acids and flavonoids. Required for normal growth and development and elongation of C18 fatty acids to C20 to C24 fatty acids in seeds. In contrast to all known animal ACL enzymes having a homomeric structure, plant ACLs are composed of alpha and beta chains (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 02 (plectoxin) family. 05 (U19- lycotoxin) subfamily.


FUNCTION: Involved in the induction of apoptosis. May act as a Ras effector protein. May suppress the serum-induced basal levels of NF- kappa-B.


FUNCTION: Bifunctional terpene synthase that converts dimethylallyl diphosphate (DMAPP) and isopentenyl diphosphate (IPP) into astellifadiene (PubMed:27038368). The C-terminal prenyltransferase (PT) domain of EvAS catalyzes formation of geranylfarnesyl pyrophosphate (GFPP), whereas the N-terminal terpene cyclase (TC) domain catalyzes the cyclization of GFPP to astellifadiene (PubMed:27038368). SIMILARITY: In the N-terminal section; belongs to the terpene synthase family. SIMILARITY: In the C-terminal section; belongs to the FPP/GGPP synthase family.


FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen (PubMed:15296735). Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (By similarity). SIMILARITY: Belongs to the CTP synthase family.


SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the synaptobrevin family.


SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid.


FUNCTION: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N- exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors. By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the EMC1 family.


SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family. ARP1 subfamily.


FUNCTION: May be involved in intracellular signaling through interaction with PtdInsPs and calmodulin (CaM); may keep PtdInsPs attached to the plasma membrane until Ca(2+)-CaM reaches a competitive concentration subsequent to an increase triggered by a stimulus, thus leading to PtdInsPs release and subsequent activation of InsPs- dependent signaling cascade. Interacts competitively at the N-terminus with calcium ions and CaM (in a calcium-dependent manner), and with the phosphatidylinositol phosphates PtdIns(3,4,5)P(3), PtdIns(3,4)P(2), PtdIns(4,5)P(2) and PtdIns(3,5)P(2). Binds also weakly to PtdIns(3)P, PtdIns(4)P and PtdIns(5)P. Negative regulator of hypocotyl cell elongation by destabilizing cortical microtubules in a calcium- dependent manner. Binds directly to and destabilized microtubules to enhance microtubule depolymerization when cytoplasmic calcium increases. In case of Turnip mosaic virus (TuMV) infection, confers sensitivity by promoting viral cell-to-cell movement through interaction with viral P3N-PIPO. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cytoplasm. Cytoplasm, cytoskeleton. Cell junction, plasmodesma. Note=Shuttles from plasma membrane to cytoplasm (e.g. colocalizes with cortical microtubules) upon calcium levels increase. Co-localizes with Turnip mosaic virus (TuMV) P3N-PIPO at the plasmodesmata. SIMILARITY: Belongs to the DREPP family.


FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF- 2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit L family.


FUNCTION: Catalyzes the last step in the trans-sulfuration pathway from L-methionine to L-cysteine in a pyridoxal-5'-phosphate (PLP)-dependent manner, which consists on cleaving the L,L-cystathionine molecule into L-cysteine, ammonia and 2-oxobutanoate (Probable) (PubMed:13525371). Part of the L-cysteine derived from the trans-sulfuration pathway is utilized for biosynthesis of the ubiquitous antioxidant glutathione. Besides its role in the conversion of L-cystathionine into L-cysteine, it utilizes L-cysteine and L-homocysteine as substrates (at much lower rates than L,L-cystathionine) to produce hydrogen sulfide (H2S). In vitro, it converts two L-cysteine molecules into lanthionine and H2S, and two L-homocysteine molecules to homolanthionine and H2S, which can be particularly relevant under conditions of severe hyperhomocysteinemia. Lanthionine and homolanthionine are structural homologs of L,L-cystathionine that differ by the absence or presence of an extra methylene group, respectively. Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target proteins: sulfhydration consists of converting -SH groups into -SSH on specific cysteine residues of target proteins such as GAPDH, PTPN1 and NF-kappa- B subunit RELA, thereby regulating their function. By generating the gasotransmitter H2S, it participates in a number of physiological processes such as vasodilation, bone protection, and inflammation (By similarity). Plays an essential role in myogenesis by contributing to the biogenesis of H2S in skeletal muscle tissue (By similarity). Can also accept homoserine as substrate (PubMed:13525371). Catalyzes the elimination of selenocystathionine (which can be derived from the diet) to yield selenocysteine, ammonia and 2-oxobutanoate (Probable). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the trans-sulfuration enzymes family.


FUNCTION: Required for proper spore morphogenesis. Important for spore germination (By similarity). SUBCELLULAR LOCATION: Spore membrane; Multi-pass membrane protein Spore outer membrane; Multi-pass membrane protein Cell membrane. SIMILARITY: Belongs to the YwcE family.


SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein. SIMILARITY: Belongs to the asfivirus B475L family.


SIMILARITY: Belongs to the cycloisomerase 2 family.


FUNCTION: Involved in nuclear pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus, Cajal body Nucleus, nucleoplasm Cytoplasm Note=Present in coiled bodies and an interchromatin network. Redistributed throughout the cytoplasm upon entry into mitosis. Also detected in central nucleolar vacuole. SIMILARITY: Belongs to the RRM U1 A/B'' family.


FUNCTION: Probably transports organic cations. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily. Organic cation transporter (TC 2.A.1.19) family.


FUNCTION: Enhances the ATPase activity of DHX15 in vitro. SUBCELLULAR LOCATION: Nucleus speckle Nucleus, nucleolus.


FUNCTION: Involved in maintenance of ploidy through proteasome dependent degradation of CDK inhibitor rum1 and S-phase initiator cdc18. Functions as a recognition factor for rum1 and cdc18, which are subsequently ubiquitinated and targeted to the 26S proteasome for degradation. Together with pop2, required for cig2 instability during G2 and M phase and cig2 degradation in exponentially growing cells. Regulates cell-cycle progression under starvation through the rum1 protein. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Induces filopodia formation and promotes neurite growth in a CDC42-independent manner; impedes neurite growth inhibitory-mediated axonal retraction. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase family.


FUNCTION: Hydrolyzes the 1,4-alpha-glycoside bonds in oligomeric and polymeric 1,4-alpha-glucans and transfers oligosaccharides (maltotriose being the shortest one) to acceptor maltodextrins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glycosyl hydrolase 13 family.


FUNCTION: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). FUNCTION: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm Note=Colocalizes with CheA chemoreceptor patches near the cell poles, which requires CheA(short). SIMILARITY: Belongs to the CheZ family.


FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. May play a role in axon guidance during nervous system development. May also play an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and synapse formation. More generally, may play a role in targeted cell migration and adhesion. Upon activation by ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Early endosome membrane; Single-pass type I membrane protein Cell projection, dendrite. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.


FUNCTION: May play an immunoevasive role in the pathogenesis of Marek's disease. It is a candidate for causing the early-stage immunosuppression that occurs after MDHV infection. SUBCELLULAR LOCATION: Secreted. Host cell membrane; Single-pass membrane protein. Note=Predominantly secreted. Secreted, but a small amount of mature GP57-65 is anchored in the plasma membrane or held by other interactions. SIMILARITY: Belongs to the herpesviridae glycoprotein C family.


FUNCTION: Male determiner protein (M-factor) that controls male somatic sexual differentiation. Acts as a dominant factor that regulates the mRNA splicing of doublesex (dsx) or fruitless (fru) transcripts and promotes expression of male splice forms of dsx and fru.


FUNCTION: Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR) (PubMed:18417535, PubMed:20348101, PubMed:12205100, PubMed:20231364, PubMed:23754376, PubMed:23509288, PubMed:28575658, PubMed:26681308). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange (PubMed:18417535, PubMed:20348101, PubMed:12205100, PubMed:20231364, PubMed:23754376, PubMed:23509288, PubMed:28575658, PubMed:26681308). Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template (PubMed:18417535, PubMed:20348101, PubMed:12205100, PubMed:20231364, PubMed:23754376, PubMed:23509288, PubMed:28575658, PubMed:26681308). Recruited to resolve stalled replication forks during replication stress (PubMed:27797818, PubMed:31844045). Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR (PubMed:24141787, PubMed:12442171). Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3 (PubMed:20413593). Also involved in interstrand cross-link repair (PubMed:26253028). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasm, perinuclear region. Mitochondrion matrix Chromosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Colocalizes with RAD51AP1 and RPA2 to multiple nuclear foci upon induction of DNA damage (PubMed:20154705). DNA damage induces an increase in nuclear levels (PubMed:20154705). Together with FIGNL1, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) or camptothecin (CPT) treatment (PubMed:23754376). Accumulated at sites of DNA damage in a SPIDR- dependent manner (PubMed:23509288). Recruited at sites of DNA damage in a MCM9-MCM8-dependent manner (PubMed:23401855). Colocalizes with ERCC5/XPG to nuclear foci in S phase (PubMed:26833090). Recruited to stalled replication forks during replication stress by the TONSL-MMS22L complex, as well as ATAD5 and WDR48 in an ATR-dependent manner (PubMed:27797818, PubMed:31844045). SIMILARITY: Belongs to the RecA family. RAD51 subfamily.


FUNCTION: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones (PubMed:30468448). Component of the parthenolide biosynthetic pathway; parthenolide and conjugates are promising anti- cancer drugs highly active against colon cancer cells (PubMed:30468448). Catalyzes the conversion of costunolide and parthenolide to 3-beta-hydroxycostunolide and 3-beta- hydroxyparthenolide, respectively (PubMed:24704560). SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Multifunctional serine/threonine kinase that plays a role in several processes including egress of virus particles from the nucleus, modulation of the actin cytoskeleton and regulation of viral and cellular gene expression. Regulates the nuclear localization of viral envelopment factor proteins 24 and 27, by phosphorylating the protein kinase ORF66, indicating a role in nuclear egress. Disrupts host nuclear lamins, including LMNA and LMNB1. Phosphorylates the viral Fc receptor composed of glycoproteins E (gE) and I (gI) (By similarity). Phosphorylation of glycoprotein E (gE) by UL13 alters its subcellular localization, from the host early endosome to the plasma membrane. Participates in the transcriptional regulation of cellular and viral mRNAs mainly by phosphorylating the viral transcriptional regulator IE63. FUNCTION: Multifunctional serine/threonine kinase that plays a role in several processes including egress of virus particles from the nucleus, modulation of the actin cytoskeleton and regulation of viral and cellular gene expression. Regulates the nuclear localization of viral envelopment factor proteins 24 and 27, by phosphorylating the protein kinase ORF66, indicating a role in nuclear egress. Disrupts host nuclear lamins, including LMNA and LMNB1. Phosphorylates the viral Fc receptor composed of glycoproteins E (gE) and I (gI). Phosphorylation of glycoprotein E (gE) by UL13 alters its subcellular localization, from the host early endosome to the plasma membrane. Participates in the transcriptional regulation of cellular and viral mRNAs mainly by phosphorylating the viral transcriptional regulator IE63 (By similarity). SUBCELLULAR LOCATION: Virion tegument Host nucleus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


FUNCTION: Found in condensed chromomeres. Binds preferentially to AT- rich DNA. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the HMGB family.


FUNCTION: The soluble form (GHBP) acts as a reservoir of growth hormone in plasma and may be a modulator/inhibitor of GH signaling. FUNCTION: Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to, and activates the JAK2/STAT5 pathway. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Note=On growth hormone binding, GHR is ubiquitinated, internalized, down-regulated and transported into a degradative or non-degradative pathway. SUBCELLULAR LOCATION: [Growth hormone-binding protein]: Secreted Note=Complexed to a substantial fraction of circulating GH. SIMILARITY: Belongs to the type I cytokine receptor family. Type 1 subfamily.


FUNCTION: Phospholipase A1 (PLA1) that hydrolyzes ester bonds at the sn-1 position of glycerophospholipids producing a free fatty acid and a lysophospholipid (PubMed:30221923). Prefers phosphatidate (1,2-diacyl- sn-glycero-3-phosphate, PA) as substrate in vitro, but can efficiently hydrolyze phosphatidylinositol (1,2-diacyl-sn-glycero-3-phospho-(1D- myo-inositol), PI), as well as a range of other glycerophospholipid substrates such as phosphatidylcholine (1,2-diacyl-sn-glycero-3- phosphocholine, PC), phosphatidylethanolamine (1,2-diacyl-sn-glycero-3- phosphoethanolamine, PE), phosphatidylserine (1,2-diacyl-sn-glycero-3- phospho-L-serine, PS) and phosphatidylglycerol (1,2-diacyl-sn-glycero- 3-phospho-(1'-sn-glycerol), PG) (PubMed:30221923) (By similarity). Involved in the regulation of the endogenous content of polyunsaturated PI and PS lipids in the nervous system (PubMed:30221923). Changes in these lipids extend to downstream metabolic products like PI phosphates PIP and PIP2, which play fundamental roles in cell biology (PubMed:30221923). Regulates mitochondrial morphology (PubMed:24599962). These dynamic changes may be due to PA hydrolysis at the mitochondrial surface (PubMed:24599962). May play a regulatory role in spermatogenesis or sperm function (PubMed:24599962). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PA-PLA1 family.


FUNCTION: Participates in the degradation of poly-3-hydroxybutyrate (PHB). It works downstream of poly(3-hydroxybutyrate) depolymerase, hydrolyzing D(-)-3-hydroxybutyrate oligomers of various length (3HB- oligomers) into 3HB-monomers. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the D-(-)-3-hydroxybutyrate oligomer hydrolase family.


FUNCTION: Nicotinic acid adenine dinucleotide phosphate (NAADP) binding protein. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the LSM12 family.


FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2- bound GDP for GTP. SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.


FUNCTION: Hydrolyzes nucleotides into nucleosides (By similarity). Snake venom 5'-nucleotidases are widely distributed among venomous snake taxa, but there is a lack of information about their biological activities. They have been shown to inhibit platelet aggregation. This effect may be due to the liberation of inhibitory AMP or adenosine by its action on ADP released upon initiation of aggregation. Venom 5'- nucleotidases are also known to synergistically act in vivo with other toxins like ADPases, phospholipases, and disintegrins to exert a more pronounced anti-coagulant effect. SUBCELLULAR LOCATION: Membrane; Lipid- anchor, GPI-anchor. SIMILARITY: Belongs to the 5'-nucleotidase family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NmrA-type oxidoreductase family. Isoflavone reductase subfamily.


FUNCTION: May be involved in pectin and/or xylans biosynthesis in cell walls. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 8 family.


FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol- phosphate-mannose required for a number of critical mannosyl transfer reactions such as folding and glycosylation of secretory proteins in the ER lumen. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic PMM family.


FUNCTION: Involved in copper homeostasis, could be involved in both copper efflux and the delivery of copper to copper-dependent enzymes (PubMed:7635807). Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation (PubMed:11830644). Functions during envelope stress responses; when overproduced induces degP through the activation of the two-component envelope stress response system CpxA/CpxR (PubMed:7635808, PubMed:15252048). DegP induction seems to require membrane anchoring of this protein (PubMed:15252048). Structural changes and/or interaction of the CXXC motif with its environment may lead to activation of the Cpx stress response (PubMed:17698001). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor.


FUNCTION: Adapter protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Predominantly cytoplasmic, with some expression in the nucleus.


FUNCTION: Enzyme that catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the thermonuclease family.


FUNCTION: Catalyzes the reversible retro-aldol cleavage of both 5-keto- 4-deoxy-D-glucarate and 2-keto-3-deoxy-D-glucarate to pyruvate and tartronic semialdehyde. SIMILARITY: Belongs to the HpcH/HpaI aldolase family. KDGluc aldolase subfamily.


FUNCTION: Error-prone polymerase lacking a proofreading 3'-5' exonuclease which catalyzes the gap-filling reaction during the DNA repair process (By similarity). Specifically binds intermediates in the single-nucleotide base-excision repair process (By similarity). Also catalyzes DNA polymerization with low nucleotide-insertion fidelity (By similarity). Probably acts as a strategic DNA mutase, which gives rise to a rapid emergence of variants (By similarity). Generates mismatched G-G pairs, in that case, the polymerase first binds the deoxynucleotide followed by mismatch formation (By similarity). Together with the viral DNA ligase, fills the single nucleotide gaps generated by the AP endonuclease (Probable). Binds DNA with high affinity via the helix alphaE (By similarity). SUBCELLULAR LOCATION: Virion Note=Found in association with viral nucleoid. SIMILARITY: Belongs to the DNA polymerase type-X family.


FUNCTION: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA (PubMed:11714285). Plays a role in the synthesis of ribosomal RNA in the nucleolus (PubMed:10791971). SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus, nucleolus Note=Localizes to the nucleolus in proliferative cells but disappears in quiescent cells. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.


FUNCTION: Forms a dome thereby closing the central channel at the end of the baseplate. Changes its conformation upon activation by calcium allowing the channel to open at the bottom of the baseplate for DNA ejection. SUBCELLULAR LOCATION: Virion Note=Part of the baseplate. SIMILARITY: Belongs to the skunalikevirus baseplate protein gp16 family.


FUNCTION: The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD or NADP for catalysis, however it has higher catalytic efficiency with NAD. FUNCTION: The actual biological function of YdiB remains unclear, nor is it known whether 3-dehydroshikimate or quinate represents the natural substrate. Catalyzes the reversible NAD-dependent reduction of both 3-dehydroshikimate (DHSA) and 3-dehydroquinate to yield shikimate (SA) and quinate, respectively. It can use both NAD or NADP for catalysis, however it has higher catalytic efficiency with NAD. SIMILARITY: Belongs to the shikimate dehydrogenase family.


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. YcaD (TC 2.A.1.26) family.


FUNCTION: Sugar transporter that specifically mediates the transport of UDP-N-acetylglucosamine (UDP-GlcNAc), GDP-fucose and UDP-xylose. Functions redundantly with nac in the O-fucosylation of Notch, positively regulating Notch signaling. Involved in the biosynthesis of heparan sulfate-glycosaminoglycan (HS-GAG) and in Dpp signaling in the wing imaginal disk. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35B subfamily.


FUNCTION: Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids with implications in host antimicrobial defense, inflammatory response and tissue regeneration (By similarity). 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 (By similarity). Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane. Upon sterile inflammation, targets membrane phospholipids of extracellular mitochondria released from activated platelets, generating free unsaturated fatty acids such as arachidonate that is used by neighboring leukocytes to synthesize inflammatory eicosanoids such as leukotrienes. Simultaneously, by compromising mitochondrial membrane integrity, promotes the release in circulation of potent damage-associated molecular pattern molecules that activate the innate immune response (By similarity). Plays a stem cell regulator role in the intestinal crypt. Within intracellular compartment mediates Paneth cell differentiation and its stem cell supporting functions by inhibiting Wnt signaling pathway in intestinal stem cell (ICS). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates Wnt signaling pathway in ICS cells and tissue regeneration (By similarity). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines. Independent of its catalytic activity, acts as a ligand for integrins. Binds to and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1. Binds to a site (site 2) which is distinct from the classical ligand-binding site (site 1) and induces integrin conformational changes and enhanced ligand binding to site 1. Induces cell proliferation in an integrin- dependent manner (By similarity). SUBCELLULAR LOCATION: Secreted Cell membrane; Peripheral membrane protein Mitochondrion outer membrane; Peripheral membrane protein. SIMILARITY: Belongs to the phospholipase A2 family.


FUNCTION: Transcriptional repressor for the ribose rbsDACBK operon.


SIMILARITY: In the C-terminal section; belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid- beta precursor protein). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels. SUBCELLULAR LOCATION: Membrane; Single- pass type I membrane protein Cytoplasmic vesicle membrane; Single- pass type I membrane protein Melanosome Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. SIMILARITY: Belongs to the nicastrin family.


FUNCTION: Mitochondrial mRNA maturase required for splicing of intron 4 of the cytochrome b (COB) gene, containing its own coding sequence, and intron 4 in COX1, coding for the related homing endonuclease aI4. In vivo splicing requires in addition the imported mitochondrial leucyl- tRNA synthetase NAM2. Both proteins seem to stimulate the intrinsic ribozyme activity of intron bI4 through binding to and stabilizing specific secondary and tertiary structure elements in the RNA. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: In the C-terminal section; belongs to the LAGLIDADG endonuclease family.


FUNCTION: Catalyzes xyloglucan endohydrolysis (XEH) and/or endotransglycosylation (XET). Cleaves and religates xyloglucan polymers, an essential constituent of the primary cell wall, and thereby participates in cell wall construction of growing tissues. SUBCELLULAR LOCATION: Secreted, cell wall Secreted, extracellular space, apoplast. SIMILARITY: Belongs to the glycosyl hydrolase 16 family. XTH group 1 subfamily.


FUNCTION: Involved in the uptake of shikimate, an intermediate in the aromatic amino acid biosynthetic pathway. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Metabolite:H+ Symporter (MHS) family (TC 2.A.1.6) family.


FUNCTION: Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)]. Does not constitute the major arsenate reductase in cells: essential only in the absence of ArsC (AC P74313). SIMILARITY: Belongs to the ArsC family.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 3 family.


FUNCTION: Catalyzes the final step of the nicotinamide adenine dinucleotide (NAD) de novo synthesis pathway, the ATP-dependent amidation of deamido-NAD using L-glutamine as a nitrogen source. SIMILARITY: In the C-terminal section; belongs to the NAD synthetase family.


FUNCTION: Transcription factor that specifically regulates the expression of the pgm gene cluster that mediates the biosynthesis of cryptic naphthoquinones derived pigments responsible for the coloration of the fruiting bodies. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: ESCRT-III-like protein required to recruit the ESCRT-III complex to the nuclear envelope (NE) during late anaphase (By similarity). Together with SPAST, the ESCRT-III complex promotes NE sealing and mitotic spindle disassembly during late anaphase (By similarity). Recruited to the reforming NE during anaphase by LEMD2 (By similarity). Plays a role in the endosomal sorting pathway (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus envelope Note=Diffused localization, with some punctate distribution, especially in the perinuclear area. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase. SIMILARITY: Belongs to the SNF7 family.


FUNCTION: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class- switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'- TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'- TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8(+) T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Present in the nucleus and cytoplasm, but shows increased nuclear translocation after activation of T-cells. SIMILARITY: Belongs to the bZIP family.


FUNCTION: Resistance to Hg(2+) in bacteria appears to be governed by a specialized system which includes mercuric reductase. MerA protein is responsible for volatilizing mercury as Hg(0). SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.


FUNCTION: Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cellular enzymes, transcription factors, neuronal excitability, cell growth, proliferation, survival, migration and apoptosis. Plays an important role in cellular stress response. Contributes to regulation of renal Na(+) retention, renal K(+) elimination, salt appetite, gastric acid secretion, intestinal Na(+)/H(+) exchange and nutrient transport, insulin-dependent salt sensitivity of blood pressure, salt sensitivity of peripheral glucose uptake, cardiac repolarization and memory consolidation. Up-regulates Na(+) channels: SCNN1A/ENAC, SCN5A and ASIC1/ACCN2, K(+) channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and KCNE1, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channels: BSND, CLCN2 and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2 /EAAT2, SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, glutamate receptor: GRIK2/GLUR6. Up-regulates carriers: SLC9A3/NHE3, SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT, SLC2A1/GLUT1, SLC5A1/SGLT1 and SLC15A2/PEPT2. Regulates enzymes: GSK3A/B, PMM2 and Na(+)/K(+) ATPase, and transcription factors: CTNNB1 and nuclear factor NF-kappa-B. Stimulates sodium transport into epithelial cells by enhancing the stability and expression of SCNN1A/ENAC. This is achieved by phosphorylating the NEDD4L ubiquitin E3 ligase, promoting its interaction with 14-3-3 proteins, thereby preventing it from binding to SCNN1A/ENAC and targeting it for degradation. Regulates store-operated Ca(+2) entry (SOCE) by stimulating ORAI1 and STIM1. Regulates KCNJ1/ROMK1 directly via its phosphorylation or indirectly via increased interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and activates MDM2-dependent ubiquitination of p53/TP53. Phosphorylates SLC2A4/GLUT4 and up-regulates its activity. Phosphorylates APBB1/FE65 and promotes its localization to the nucleus. Phosphorylates FBXW7 and plays an inhibitory role in the NOTCH1 signaling. Phosphorylates FOXO1 resulting in its relocalization from the nucleus to the cytoplasm. Phosphorylates FOXO3, promoting its exit from the nucleus and interference with FOXO3-dependent transcription. Phosphorylates BRAF and MAP3K3/MEKK3 and inhibits their activity. Phosphorylates SLC9A3/NHE3 in response to dexamethasone, resulting in its activation and increased localization at the cell membrane. Phosphorylates CREB1. Necessary for vascular remodeling during angiogenesis (By similarity). Phosphorylates MAPT/TAU and mediates microtubule depolymerization and neurite formation in hippocampal neurons. Phosphorylates MAPK1/ERK2 and activates it by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. May also play an important role in the development of particular groups of neurons in the postnatal brain. SUBCELLULAR LOCATION: Cytoplasm Nucleus Endoplasmic reticulum membrane Cell membrane Mitochondrion Note=The subcellular localization is controlled by the cell cycle, as well as by exposure to specific hormones and environmental stress stimuli. In proliferating cells, it shuttles between the nucleus and cytoplasm in synchrony with the cell cycle, and in serum/growth factor-stimulated cells it resides in the nucleus. In contrast, after exposure to environmental stress or treatment with glucocorticoids, it is detected in the cytoplasm and with certain stress conditions is associated with the mitochondria. In osmoregulation through the epithelial sodium channel, it can be localized to the cytoplasmic surface of the cell membrane. Nuclear, upon phosphorylation (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family.


FUNCTION: Methyltransferase involved in methanogenesis from methylamines methanol pathway. Catalyzes the transfer of the methyl group from the methylated corrinoid protein MtmC (MtmC1 or MtmC2) to coenzyme M, forming the substrate for coenzyme-B sulfoethylthiotransferase. SIMILARITY: Belongs to the uroporphyrinogen decarboxylase family. MtbA/MtaA subfamily.


FUNCTION: Required for nicotinamide riboside transport across the inner membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the nicotinamide ribonucleoside (NR) uptake permease (TC 4.B.1) family.


FUNCTION: [Centrocin 2, heavy chain]: Has antimicrobial activity against Gram-negative bacteria, Gram-positive bacteria and against fungi with minimum inhibitory concentration (MIC) between 0.78 uM and 50 uM. Shows little hemolytic activity at concentrations up to 12.5 uM but >50% lysis at 100 uM.


FUNCTION: Involved in the bidirectional transport of formate during mixed-acid fermentation. Functions to maintain relatively constant intracellular formate levels during growth, using different mechanisms for efflux and uptake of the anion. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the FNT transporter (TC 2.A.44) family.


FUNCTION: RNA exonuclease that acts as a negative regulator of RNA interference (RNAi) (PubMed:14961122). Probably acts by degrading the 3'-overhangs of short interfering RNAs (siRNAs) (PubMed:14961122). Component of the ERI/DICER complex which is involved in processing amplified double-stranded RNA (dsRNA) intermediates during small-RNA- mediated gene-silencing or RNA interference (RNAi) (Probable). SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Transfers sialic acid from the donor of substrate CMP-sialic acid to galactose containing acceptor substrates. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 29 family.


FUNCTION: Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin-12 and reducing production of interleukin-10 and is essential in the pathway that leads to type I immunity. FUNCTION: Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the osteopontin family.