FUNCTION: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily.


FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. This is the largest subunit of complex I and it is a component of the iron- sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized. SUBCELLULAR LOCATION: Mitochondrion inner membrane. SIMILARITY: Belongs to the complex I 75 kDa subunit family.


FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D- fructose 6-phosphate, respectively) (PubMed:23185017, PubMed:26985301, PubMed:29298880). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:29298880). Plays a key role in maintaining the integrity of the outer mitochondrial membrane by preventing the release of apoptogenic molecules from the intermembrane space and subsequent apoptosis (PubMed:18350175). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein Cytoplasm, cytosol Note=The mitochondrial-binding peptide (MBP) region promotes association with the mitochondrial outer membrane (PubMed:29298880). The interaction with the mitochondrial outer membrane via the mitochondrial-binding peptide (MBP) region promotes higher stability of the protein (PubMed:29298880). Release from the mitochondrial outer membrane into the cytosol induces permeability transition pore (PTP) opening and apoptosis (PubMed:18350175). SIMILARITY: Belongs to the hexokinase family.


FUNCTION: Negatively regulates RAC1 signaling and RAC1-driven cytoskeletal remodeling (PubMed:31285585). Regulates chemotaxis, cell migration and epithelial polarization by controlling the polarity, plasticity, duration and extent of protrusions. Limits Rac1 mediated activation of the Scar/WAVE complex, focuses protrusion signals and regulates pseudopod complexity by inhibiting Scar/WAVE-induced actin polymerization (By similarity). Protects against Salmonella bacterial infection. Attenuates processes such as macropinocytosis, phagocytosis and cell migration and restrict sopE-mediated bacterial entry (PubMed:31285585). Restricts also infection mediated by Mycobacterium tuberculosis and Listeria monocytogenes (PubMed:31285585). Involved in the regulation of mitochondrial dynamics and oxidative stress (PubMed:29059164). SUBCELLULAR LOCATION: Membrane; Lipid- anchor Mitochondrion. SIMILARITY: Belongs to the CYRI family.


FUNCTION: Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits. SIMILARITY: Belongs to the eIF-1A family.


FUNCTION: Participates in the biosynthesis of capsaicinoids in pungent cultivars of Capsicum annuum (PubMed:15918882, PubMed:25884984, PubMed:36296471). Capsaicinoids, the alkaloids responsible for the heat or pungency of chili pepper, are synthesized from phenylpropanoid intermediates in the placental tissue of chili peper fruit (Probable). Can transfer an acyl from (6E)-8-methylnon-6-enoyl-CoA to vanillylamine forming capsaicin and CoA (PubMed:15918882, PubMed:25884984, PubMed:36296471). SIMILARITY: Belongs to the plant acyltransferase family.


FUNCTION: Oxidoreductase required for tumor suppression. NADPH-bound form inhibits nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors. May act as a redox sensor linked to transcription through regulation of nuclear import. SUBCELLULAR LOCATION: Cytoplasm Nucleus envelope.


FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase A chain family.


FUNCTION: Catalyzes the trans-addition of the 3 molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. May be involved in vesicle trafficking and protein sorting (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FPP/GGPP synthase family.


FUNCTION: Contributes to the regulation of secretory and vacuolar transport pathways in the post-Golgi network, and to the maintenance of the Golgi apparatus and trans-Golgi network (TGN) morphologies (PubMed:22307646). Together with VTI12, required for membrane fusion (PubMed:15919093). Vesicle trafficking protein that functions in the secretory pathway and mediates liposome fusion; the fusion of phospholipid vesicles containing SYP41 and VTI12 is triggered by YKT61 and YKT62 (PubMed:15919093, PubMed:24021022). Required for extracellular resistance responses to a fungal pathogen (PubMed:22307646). Also involved in the protection of chloroplasts from salicylic acid-dependent biotic stress (PubMed:22307646). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Single-pass type IV membrane protein Note=SYP41 is found in a different region of the TGN than SYP42. SIMILARITY: Belongs to the syntaxin family.


FUNCTION: Mitochondrial ribosomal protein required for central cell maturation. May work together with PIA2 in controlling female gametophyte development, possibly by regulating the expression of some mitochondrial proteins. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS9 family.


FUNCTION: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (PubMed:16118314, PubMed:17646546, PubMed:19340006, PubMed:24076655). Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-5-RING ubiquitin ligase complex (ECS complex, also named CRL5 complex) and initiating ubiquitination of ECS substrates: associates with ECS complex and specifically mediates addition of the first ubiquitin on ECS targets (By similarity). The initial ubiquitin is then elongated (By similarity). E3 ubiquitin-protein ligase activity is activated upon binding to neddylated form of the ECS complex (PubMed:24076655). Mediates 'Lys-6', 'Lys-48'- and 'Lys-63'-linked polyubiquitination (PubMed:16118314, PubMed:17646546, PubMed:19340006). May play a role in myelopoiesis (PubMed:19340006). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the RBR family. Ariadne subfamily.


FUNCTION: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the GST superfamily. Phi family.


FUNCTION: Unusual broad substrate spectrum amino acid:sodium cotransporter that promotes absorption of the D isomers of essential amino acids. Neutral amino acids are the preferred substrates, especially methionine and phenylalanine (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family.


FUNCTION: Enhances DNA synthesis and may play a role in cell proliferation. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. Forms with the glucose-6-phosphate transporter (SLC37A4/G6PT) the complex responsible for glucose production in the terminal step of glycogenolysis and gluconeogenesis. Hence, it is the key enzyme in homeostatic regulation of blood glucose levels. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glucose-6-phosphatase family.


FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the bacteriostatic effect of cognate toxin ParT by inserting into its active site. SIMILARITY: Belongs to the MbcA/ParS/Xre antitoxin family.


FUNCTION: Terpene cyclase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes nodulisporic acids (NA). Nodulisporic acid A (NAA) and its chemically modified derivatives are of particular significance because of their highly potent insecticidal activity against blood-feeding arthropods and lack of observable adverse effects on mammals, in particular the tremogenicity associated with the paspaline-derived IDTs is not observed (PubMed:29283570). The geranylgeranyl diphosphate (GGPP) synthase ggs1, localized outside of the cluster, is proposed to catalyze the first step in nodulisporic acid biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (PubMed:29283570). Condensation of indole-3-glycerol phosphate with GGPP by the prenyl transferase nodC then forms 3-geranylgeranylindole (3-GGI) (PubMed:29283570). Epoxidation by the FAD-dependent monooxygenase nodM leads to a single-epoxidized-GGI that is substrate of the terpene cyclase nodB for cyclization to yield emindole SB (PubMed:29283570). The terminal methyl carbon, C28, of emindole SB is then oxidized by the cytochrome P450 monooxygenase nodW to produce nodulisporic acid F (NAF), the pentacyclic core of NAA (PubMed:29283570). NAF is converted to nodulisporic acid E (NAE) via prenylation. This step is probably performed by one of the indole diterpene prenyltransferases nodD1 or nodD2 (Probable). Several oxidation steps performed by the FAD-linked oxidoreductase nodO and one of the cytochrome P450 monooxygenase nodR, nodX or nodZ further convert NAE to nodulisporic acid D (NAD) (Probable). NAD is substrate of cytochrome P450 monooxygenase nodJ to produce the precursor of nodulisporic acid C (NAC), converted to NAC by one of the indole diterpene prenyltransferases nodD1 or nodD2 (Probable). The FAD- dependent monooxygenase nodY2 then oxidizes NAC to nodulisporic acid B (NAB) (Probable). Finally NAB is converted to NAA by one of the cytochrome P450 monooxygenases nodR, nodX or nodZ (Probable). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the paxB family.


FUNCTION: Interferes with TCR signaling from the cell membrane. Interacts with CD247/TCRZ (TCR zeta chain) and exert potent down- regulation of cell surface TCR/CD3 complexes. FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates cell surface expression of CD4, CD28, CD3, and MHC-I or MHC-II molecules. FUNCTION: Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike (By similarity). FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. One of the earliest and most abundantly expressed viral proteins (By similarity). SUBCELLULAR LOCATION: Host cell membrane; Lipid-anchor; Cytoplasmic side Note=Associates with the inner plasma membrane through its N-terminal domain. SIMILARITY: Belongs to the lentivirus primate group Nef protein family.


FUNCTION: Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC, CEP250 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGO1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates CEP68 and CNTLN directly or indirectly (PubMed:24554434). NEK2-mediated phosphorylation of CEP68 promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis (PubMed:25704143). Involved in the regulation of centrosome disjunction (PubMed:26220856). Phosphorylates CCDC102B either directly or indirectly which causes CCDC102B to dissociate from the centrosome and allows for centrosome separation (PubMed:30404835). FUNCTION: [Isoform 2]: Not present in the nucleolus and, in contrast to isoform 1, does not phosphorylate and activate NEK11 in G1/S-arrested cells. FUNCTION: [Isoform 1]: Phosphorylates and activates NEK11 in G1/S- arrested cells. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Note=Predominantly cytoplasmic. SUBCELLULAR LOCATION: [Isoform 4]: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Predominantly nuclear. SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. Nucleus, nucleolus Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle pole. Chromosome, centromere, kinetochore. Chromosome, centromere Note=STK3/MST2 and SAV1 are required for its targeting to the centrosome. Colocalizes with SGO1 and MAD1L1 at the kinetochore. Not associated with kinetochore in the interphase but becomes associated with it upon the breakdown of the nuclear envelope. Has a nucleolar targeting/ retention activity via a coiled-coil domain at the C-terminal end. SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily.


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


FUNCTION: The small GTPases Rab are key regulators in vesicle trafficking (PubMed:24788816). Essential for maintaining the integrity of the endosome-trans-Golgi network structure (By similarity). Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (PubMed:24788816). Recruits LRRK2 to the Golgi complex and stimulates LRRK2 kinase activity (PubMed:29212815). Regulates neuronal process morphology in the intact central nervous system (CNS) (By similarity). May play a role in the formation of typhoid toxin transport intermediates during Salmonella enterica serovar Typhi (S.Typhi) epithelial cell infection (PubMed:22042847). FUNCTION: The small GTPases Rab are key regulators in vesicle trafficking (By similarity). Essential for maintaining the integrity of endosome-trans-Golgi network structure (By similarity). Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (By similarity). Recruits LRRK2 to the Golgi apparatus and stimulates LRRK2 kinase activity (By similarity). Regulates also neuronal process morphology in the intact central nervous system (CNS) (By similarity). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Cytoplasm Cytoplasm, perinuclear region Golgi apparatus Golgi apparatus, trans-Golgi network Vacuole Cytoplasm, cytoskeleton Note=Colocalizes with LRRK2 along tubular structures emerging from Golgi apparatus (PubMed:29212815). Colocalizes with GM130 at the Golgi apparatus (PubMed:22042847). Colocalizes with dynamic tubules emerging from and retracting to the Golgi apparatus (PubMed:22042847). Colocalizes with TGN46 at the trans- Golgi network (TGN) (PubMed:24788816). In Salmonella enterica serovar Typhi (S.Typhi) infected epithelial cells, is recruited and colocalized with both S.Typhi-containing vacuoles and dynamic tubules as well as those emerging from the vacuole toward the cell periphery (PubMed:22042847). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Cytoplasm Cytoplasm, perinuclear region Golgi apparatus Golgi apparatus, trans-Golgi network Cytoplasm, cytoskeleton Note=Colocalizes with GM130 at the Golgi apparatus (By similarity). Colocalizes with LRRK2 at dynamic tubules emerging from and retracting to the Golgi apparatus (By similarity). Colocalizes with TGN46 at the trans-Golgi network (TGN) (By similarity). SIMILARITY: Belongs to the small GTPase superfamily. Rab family.


FUNCTION: Catalyzes the phosphorylation of the dietary vitamin B6 vitamers pyridoxal (PL), pyridoxine (PN) and pyridoxamine (PM) to form pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), respectively (By similarity). PLP is the active form of vitamin B6, and acts as a cofactor for over 140 different enzymatic reactions (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the pyridoxine kinase family.


FUNCTION: [Ninjurin-1]: Homophilic transmembrane adhesion molecule involved in various processes such as inflammation, cell death, axonal growth, cell chemotaxis and angiogenesis (By similarity). Promotes cell adhesion by mediating homophilic interactions via its extracellular N- terminal adhesion motif (N-NAM) (PubMed:19595672). Involved in the progression of the inflammatory stress by promoting cell-to-cell interactions between immune cells and endothelial cells (By similarity). Involved in leukocyte migration during inflammation by promoting transendothelial migration of macrophages via homotypic binding (By similarity). Promotes the migration of monocytes across the brain endothelium to central nervous system inflammatory lesions (By similarity). Acts as a regulator of Toll-like receptor 4 (TLR4) signaling triggered by lipopolysaccharide (LPS) during systemic inflammation; directly binds LPS (By similarity). Acts as a mediator of both programmed and necrotic cell death (By similarity). Plays a key role in the induction of plasma membrane rupture during programmed and necrotic cell death: oligomerizes in response to death stimuli to mediate plasma membrane rupture (cytolysis), leading to release intracellular molecules named damage-associated molecular patterns (DAMPs) that propagate the inflammatory response (By similarity). Plays a role in nerve regeneration by promoting maturation of Schwann cells (By similarity). Acts as a regulator of angiogenesis (PubMed:33028854). Promotes the formation of new vessels by mediating the interaction between capillary pericyte cells and endothelial cells (By similarity). Promotes osteoclasts development by enhancing the survival of prefusion osteoclasts (By similarity). Also involved in striated muscle growth and differentiation (By similarity). FUNCTION: [Secreted ninjurin-1]: Secreted form generated by cleavage, which has chemotactic activity. Acts as an anti-inflammatory mediator by promoting monocyte recruitment, thereby ameliorating atherosclerosis. SUBCELLULAR LOCATION: [Secreted ninjurin-1]: Secreted. SUBCELLULAR LOCATION: [Ninjurin-1]: Cell membrane; Multi-pass membrane protein Synaptic cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ninjurin family.


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


FUNCTION: Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes low production of type I interferon (IFN-alpha and IFN-beta) (PubMed:29478775). Compared to other mammals, STING1-dependent type I interferon induction is strongly reduced in bats, suggesting that the cGAS-STING pathway promotes a limited inflammatory response (PubMed:29478775). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (By similarity). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di- GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (By similarity). Upon binding of c-di-GMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state (By similarity). In addition to promote the production of type I interferons, plays a direct role in autophagy (By similarity). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (By similarity). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (By similarity). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Cytoplasm, perinuclear region Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Cytoplasmic vesicle, autophagosome membrane; Multi-pass membrane protein Mitochondrion outer membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Note=In response to double-stranded DNA stimulation, translocates from the endoplasmic reticulum through the endoplasmic reticulum-Golgi intermediate compartment and Golgi to post- Golgi vesicles, where the kinase TBK1 is recruited (By similarity). Upon cGAMP-binding, translocates to the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) in a process that is dependent on COPII vesicles; STING1-containing ERGIC serves as a membrane source for LC3 lipidation, which is a key step in autophagosome biogenesis (By similarity). SIMILARITY: Belongs to the STING family.


FUNCTION: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of the bibenzoquinone oosporein, a metabolite required for fungal virulence that acts by evading host immunity to facilitate fungal multiplication in insects (PubMed:26305932). The non-reducing polyketide synthase OpS1 produces orsellinic acid by condensing acetyl- CoA with 3 malonyl-CoA units (PubMed:26305932). Orsellinic acid is then hydroxylated to benzenetriol by the hydroxylase OpS4 (PubMed:26305932). The intermediate is oxidized either nonenzymatically to 5,5'-dideoxy- oosporein or enzymatically to benzenetetrol by the oxidoreductase OpS7 (PubMed:26305932). The latter is further dimerized to oosporein by the catalase OpS5 (PubMed:26305932). OpS6 probably functions en route for protecting cells against oxidative stress by scavenging any leaked free radical form of benzenetetrol by activating the thiol group of glutathione (PubMed:26305932). SIMILARITY: Belongs to the oxidoreductase OpS7 family.


FUNCTION: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. Mdm34 is required for the interaction of the ER-resident membrane protein mmm1 and the outer mitochondrial membrane-resident beta-barrel protein mdm10. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria- endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids. SIMILARITY: Belongs to the MDM34 family.


FUNCTION: Constituent of viral factories. SUBCELLULAR LOCATION: Host cytoplasm Note=Constituent of spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. SIMILARITY: Belongs to the phytoreovirus non-structural protein Pns12A family.


FUNCTION: Involved in the biosynthesis of ADP-glucose, a building block, required in the biosynthesis of maltose-1-phosphate (M1P) and in the elongation reactions to produce linear alpha-1,4-glucans. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc. SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family.


FUNCTION: Responsible for the hydrolysis of cyanuric acid, an intermediate formed during catabolism of s-triazine based compounds in herbicides such as atrazine and polymers such as melamine. Catalyzes the hydrolytic opening of the s-triazine ring of cyanuric acid (2,4,6- trihydroxy-s-triazine) to yield carbon dioxide and carboxybiuret, which spontaneously decarboxylates to biuret. Only active on cyanuric acid and N-methylisocyanuric acid. SIMILARITY: Belongs to the cyclic amide hydrolase (CyAH) family.


FUNCTION: Negative regulator of the mitochondrial respiratory chain. Prevents mitochondrial hyperpolarization state and restricts mitochondrial generation of ATP. Acts as an import component of the TIM23 translocase complex. Stimulates the ATPase activity of HSPA9 (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein.


FUNCTION: Involved in the regulation of melanogenesis. The binding of ASP to MC1R precludes alpha-MSH initiated signaling and thus blocks production of cAMP, leading to a down-regulation of eumelanogenesis (brown/black pigment) and thus increasing synthesis of pheomelanin (yellow/red pigment) (By similarity). SUBCELLULAR LOCATION: Secreted.


FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that catalyzes the synthesis of very long chain saturated (VLC-SFA) and polyunsaturated (PUFA) fatty acids that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May play a critical role in early brain and skin development. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ELO family. ELOVL4 subfamily.


FUNCTION: May be involved in the regulation of spermatogenesis. Stimulates CREM transcriptional activity in a phosphorylation- independent manner (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Nuclei of round and elongated spermatids.


FUNCTION: With S4 and S12 plays an important role in translational accuracy. SIMILARITY: Belongs to the universal ribosomal protein uS5 family.


FUNCTION: Calcium, potassium:sodium antiporter that transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+) (PubMed:22057188). Controls the rapid response termination and proper regulation of adaptation in olfactory sensory neurons (OSNs) which subsequently influences how odor information is encoded and perceived (PubMed:22057188). May play a role in calcium transport during amelogenesis (PubMed:23375655). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cytoplasm. SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. SLC24A subfamily.


FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.


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


FUNCTION: Serine/threonine-protein kinase that may function as a signaling receptor of extracellular matrix component. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


FUNCTION: Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the granulin family.


FUNCTION: May act as an adapter to facilitate the interaction of SnRK1 complex with effector proteins, conferring tissue- and stimulus-type specific differences in the SnRK1 regulation pathway (PubMed:24600465). Involved in seed dormancy control (PubMed:15159630). SUBCELLULAR LOCATION: Cytoplasm, Stress granule Cytoplasm, P-body. SIMILARITY: Belongs to the FLZ family.


FUNCTION: Functions as an E3 ubiquitin ligase.


FUNCTION: Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-thiolated protein (GSSPs). Likely acts synergistically with glutaredoxin to regulate the redox environment of E.coli and defend against oxidative damage. In vitro, the amidase active site also catalyzes hydrolysis of amide and ester derivatives of glutathione (e.g. glutathione ethyl ester and glutathione amide) but lacks activity toward acetylspermidine (N1 and N8) and acetylspermine (N1). FUNCTION: Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. May act synergistically with glutaredoxin to regulate the redox environment and defend against oxidative damage. SIMILARITY: In the C-terminal section; belongs to the glutathionylspermidine synthase preATP-grasp family.


FUNCTION: Low-affinity inorganic phosphate transporter. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family. Pit subfamily.


FUNCTION: Protein disulfide isomerase (Probable). Might play a role in the unfolded protein response (Probable). May regulate transport of alpha4-beta2 neuronal acetylcholine receptor (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum. SIMILARITY: Belongs to the CRELD family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the OCA5 family.


FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small chain family.


FUNCTION: Hydroxysteroid dehydrogenase involved in the biosynthesis of dafrachonic acids (PubMed:18495818, PubMed:20178781, PubMed:24411940). Catalyzes the dehydrogenation of cholesterol or its derivatives and the isomerization of the double carbon bond on the sterol ring. Modifies sterols into a Delta(4)-3-keto-sterols such as cholest-4-en-3-one, precursor of Delta(4)-dafachronic acid (PubMed:18495818). Contributes to the production of Delta(7)-dafachronic acid in the XXX cells (PubMed:24411940). Dafachronic acids act as ligands and bind directly to the nuclear hormone receptor (NHR) daf-12 suppressing dauer formation and inducing reproductive growth (PubMed:18495818, PubMed:24411940). Acts in parallel to AKT-1 to promote reproductive development via DAF-16/FoxO and DAF-12 (PubMed:20178781). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the 3-beta-HSD family.


SIMILARITY: Belongs to the UPF0201 family.


FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.


FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose on both O- and N- linked glycans chains of cell surface glycoproteins and glycolipids and the resulting epitope regulates several processes such as cell-cell interaction including host-microbe interaction, cell surface expression and cell proliferation. Preferentially fucosylates gangliosides GA1 and GM1 in the antrum, cecum and colon and in the female reproductive organs. Fucosylated host glycoproteins or glycolipids mediate interaction with intestinal microbiota influencing its composition. Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble ABO blood group antigen synthesis pathway. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein Note=Membrane-bound form in trans cisternae of Golgi. SIMILARITY: Belongs to the glycosyltransferase 11 family.


FUNCTION: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. Bind to single-stranded DNA (ssDNA) and has DNA-dependent ATPase activity. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. Involved in telomere maintenance. The BCDX2 subcomplex XRCC2:RAD51D can stimulate Holliday junction resolution by BLM (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome, telomere. SIMILARITY: Belongs to the RecA family. RAD51 subfamily.


SIMILARITY: Belongs to the LOG family.


FUNCTION: Actin-binding protein that contains 2 major actin binding sites (By similarity). Organizes filamentous actin into parallel bundles (PubMed:7738015). Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers (By similarity). Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration (PubMed:21685497). Mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to NGF (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm, cell cortex Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, stress fiber Cell projection, growth cone Cell projection, filopodium Cell projection, invadopodium Cell projection, microvillus Cell junction Note=Colocalized with RUFY3 and F-actin at filipodia of the axonal growth cone (PubMed:24720729). Colocalized with DBN1 and F-actin at the transitional domain of the axonal growth cone (PubMed:24720729). SIMILARITY: Belongs to the fascin family.


FUNCTION: Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EAF5 family.


FUNCTION: Probable sodium-dependent amino acid/proton antiporter, could be a neuronal transporter for glutamate. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Colocalizes with synaptotagmins and SNAP25. SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.


SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PRPH2/ROM1 family.


FUNCTION: Component of a transport pathway that contributes to membrane integrity. FUNCTION: Component of a transport pathway that contributes to membrane integrity. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PqiA family.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.


FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CWC25 family.


FUNCTION: Transcriptional coactivator for creb1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of creb1 'Ser-119' phosphorylation. Enhances the interaction of creb1 with taf4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of ppargc1a and inducer of mitochondrial biogenesis in muscle cells (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Appears to be mainly nuclear. SIMILARITY: Belongs to the TORC family.


FUNCTION: Component of the AfsK/AfsR system involved in the response of aerial mycelium formation to glucose. SIMILARITY: Belongs to the AfsR/DnrI/RedD regulatory family.


FUNCTION: Catalyzes the condensation of two molecules of acetyl-CoA to produce acetoacetyl-CoA. SUBCELLULAR LOCATION: Cytoplasm Peroxisome. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the serine/threonine dehydratase family.


FUNCTION: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the cornifin (SPRR) family.


FUNCTION: Probable ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 14 (magi-1) family. OAIP-1 subfamily.


FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:23287728). Shows activity on L-Leu (PubMed:23287728). Damages cell membranes of the Gram-positive bacteria S.aureus (MIC=8 ug/ml and MBC=16 ug/ml) and the Gram-negative bacteria A.baumannii (MIC=16 ug/ml and MBC=32 ug/ml). This antimicrobial activity is dependent on the production of hydrogen peroxyde, since it is inhibited by catalase, a hydrogen peroxyde scavenger. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1 subfamily.


FUNCTION: Transcriptional regulator. Activates E box-dependent transcription in collaboration with TCF3/E47, but the activity is completely antagonized by the negative regulator of neurogenesis HES1. Plays a role in the differentiation of subsets of neural cells by activating E box-dependent transcription (By similarity). SUBCELLULAR LOCATION: Nucleus.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eL6 family.


FUNCTION: Acts as a methyl group carrier between MtbB and MtbA. SIMILARITY: Belongs to the methylamine corrinoid protein family.


FUNCTION: Probable transcription factor that may function in the maintenance of the proper function of the central cell in pollen tube attraction. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the type IB topoisomerase family.


SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite.


FUNCTION: May play a role in protection or detoxification. SUBCELLULAR LOCATION: Secreted.


FUNCTION: BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation (By similarity). They act individually and together to regulate their own expression and that of numerous other sporulation-specific genes (By similarity). Binds promoters of target genes at brlA response elements (BREs) containing the conserved sequence 5'-(C/A)(A/G)AGGG(G/A)-3' (By similarity). Required for conidiophores formation (PubMed:17213655). Controls expression of abaA (PubMed:19850144). SUBCELLULAR LOCATION: Nucleus.


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


FUNCTION: Antitoxin component of a type V toxin-antitoxin (TA) system. Neutralizes the toxic effects of toxin GhoT by digesting ghoT transcripts in a sequence-specific manner (PubMed:22941047). In concert with GhoT is involved in reducing cell growth during antibacterial stress (PubMed:24373067). Overexpression leads to transcript level reduction of 20 other mRNAs involved in purine or pyrimidine synthesis and transport. Not seen to bind its own promoter DNA (PubMed:22941047). FUNCTION: Antitoxin component of a type V toxin-antitoxin (TA) system. Neutralizes the toxic effects of toxin GhoT by digesting ghoT transcripts in a sequence-specific manner. In concert with GhoT is involved in reducing cell growth during antibacterial stress.


FUNCTION: Isoform 1 does not display proton-gated cation channel activity. FUNCTION: Isoform 2 and isoform 3 function as proton-gated sodium channels; they are activated by a drop of the extracellular pH and then become rapidly desensitized. The channel generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Isoform 2 can also transport potassium, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions. Isoform 3 can also transport calcium ions. Mediates glutamate- independent Ca(2+) entry into neurons upon acidosis. This Ca(2+) overloading is toxic for cortical neurons and may be in part responsible for ischemic brain injury. Heteromeric channel assembly seems to modulate channel properties. Functions as a postsynaptic proton receptor that influences intracellular Ca(2+) concentration and calmodulin-dependent protein kinase II phosphorylation and thereby the density of dendritic spines. Modulates activity in the circuits underlying innate fear. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Localizes in synaptosomes at dendritic synapses of neurons. Colocalizes with DLG4 (By similarity). SIMILARITY: Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. ASIC1 subfamily.


FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response which coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp. The second messengers ppGpp and c-di-GMP together control biofilm formation in response to translational stress; ppGpp represses biofilm formation while c-di-GMP induces it. ppGpp activates transcription of CsrA-antagonistic small RNAs CsrB and CsrC, which down-regulate CsrA's action on translation during the stringent response (PubMed:21488981). FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp (By similarity). SIMILARITY: Belongs to the RelA/SpoT family.


FUNCTION: ATPase required for the post-translational delivery of tail- anchored (TA) proteins to the endoplasmic reticulum. Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1/WRB and CAMLG/GET2, where the tail- anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-CAMLG receptor, and returning it to the cytosol to initiate a new round of targeting. SUBCELLULAR LOCATION: Cytoplasm Endoplasmic reticulum. SIMILARITY: Belongs to the arsA ATPase family.


FUNCTION: May promote cell proliferation and inhibition of apoptosis of preadipocytes. SIMILARITY: Belongs to the complex I LYR family.


FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and with PAB1. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. PAN3 family.


FUNCTION: Role in flagellar biosynthesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Bacterial flagellum basal body. SIMILARITY: Belongs to the FliQ/MopD/SpaQ family.


FUNCTION: Required for morphogenesis under gluconeogenic growth conditions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the gluconeogenesis factor family.


FUNCTION: Component of the high affinity leucine, isoleucine, valine, transport system (LIV-I), which is operative without Na(+) and is specific for alanine and threonine, in addition to branched-chain amino acids. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. LivHM subfamily.


FUNCTION: Peroxisomal 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner (By similarity). Involved in the degradation of 3-methyl-branched fatty acids like phytanic acid and the shortening of 2-hydroxy long-chain fatty acids (By similarity). Plays a significant role in the biosynthesis of heptadecanal in the liver (PubMed:29027957). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the TPP enzyme family.


FUNCTION: Responsible for methylating the 5'-cap structure of mRNAs. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family.


FUNCTION: In the nucleus, enhances stability of the PCAF histone acetyltransferase (HAT) complex member TADA2A and thus promotes PCAF- mediated H3K14 and H4K8 HAT activity. May inhibit TADA2A-mediated TP53/p53 'Lys-321' acetylation, leading to reduced TP53 stability and transcriptional activity. May also promote TADA2A-mediated XRCC6 acetylation thus facilitating cell apoptosis in response to DNA damage. FUNCTION: In extracellular secreted form, promotes proliferation and activation of CD8(+) T cells, suggesting a cytokine-like function. Enhances cytotoxic anti-tumor activity of CD8(+) T cells. May inhibit ERK and JNK signaling activity. May suppress cell migration and invasion activity, via its effects on ERK and JNK signaling. Has a critical role in the regulation of osteogenesis and bone development. SUBCELLULAR LOCATION: Nucleus Cytoplasm Secreted Endoplasmic reticulum Note=Accumulates in the nucleus in response to UV irradiation. SIMILARITY: Belongs to the CCDC134 family.


FUNCTION: Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). SIMILARITY: Belongs to the GGGP/HepGP synthase family. Group II subfamily.


FUNCTION: Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. SUBCELLULAR LOCATION: Secreted. Bacterial flagellum. SIMILARITY: Belongs to the FliD family.


FUNCTION: Plays a role in vesicular protein sorting. Required for the endosome-to-Golgi retrieval of the vacuolar protein sorting receptor vps10. Required to form proper forespore membranes. SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the VPS35 family.


FUNCTION: Up-regulated in CNS of active, non-hibernating snails suggesting involvement in the regulation of hibernation and maintenance of the active state.


FUNCTION: Receptor for angiotensin II, a vasoconstricting peptide, which acts as a key regulator of blood pressure and sodium retention by the kidney. The activated receptor in turn couples to G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and thus activates phospholipase C and increases the cytosolic Ca(2+) concentrations, which in turn triggers cellular responses such as stimulation of protein kinase C. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L- selenocysteine. Selenocysteine lyase activity is however unsure in vivo. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily.


FUNCTION: Ligand-activated transcription factor that enables cells to adapt to changing conditions by sensing compounds from the environment, diet, microbiome and cellular metabolism, and which plays important roles in development, immunity and cancer (PubMed:7812217). Upon ligand binding, translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE). Regulates a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation. Xenobiotics can act as ligands: upon xenobiotic- binding, activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons. Next to xenobiotics, natural ligands derived from plants, microbiota, and endogenous metabolism are potent AHR agonists. Tryptophan (Trp) derivatives constitute an important class of endogenous AHR ligands. Acts as a negative regulator of anti-tumor immunity: indoles and kynurenic acid generated by Trp catabolism act as ligand and activate AHR, thereby promoting AHR-driven cancer cell motility and suppressing adaptive immunity. Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1. Inhibits PER1 by repressing the CLOCK-BMAL1 heterodimer mediated transcriptional activation of PER1. The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=Initially cytoplasmic; upon binding with ligand and interaction with a HSP90, it translocates to the nucleus.


FUNCTION: [Disintegrin mojastin-2]: Inhibits ADP-induced platelet aggregation (IC(50) = 13.8 nM) probably by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) located on the platelet surface. FUNCTION: [Disintegrin mojastin-1]: Inhibits the three processes involved in platelet function (adhesion, activation and aggregation). It inhibits platelet adhesion to fibronectin with an IC(50) of 58.6 nM. It inhibits ATP release from platelet induced by ADP with an IC(50) of 19.5 nM on platelet-rich plasma, probably by binding to ADP receptors (P2RY1 and P2RY12). Finally, it inhibits ADP-induced platelet aggregation with IC(50) of 44.7 nM on platelet-rich plasma and 19.3 nM on whole blood, probably by binding to alpha-IIb/beta-3 (ITGA2B/ITGB3) (PubMed:20598348). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-II subfamily. P-IIa sub-subfamily.


FUNCTION: Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (By similarity). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (By similarity). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (By similarity). Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5 (By similarity). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (By similarity). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Membrane Nucleus Synapse Secreted Cell projection, axon Note=Membrane-bound in dopaminergic neurons (By similarity). Expressed and colocalized with SEPTIN4 in dopaminergic axon terminals, especially at the varicosities (By similarity). SIMILARITY: Belongs to the synuclein family.


FUNCTION: Catalyzes the transfer of a methyl group to L-homocysteine resulting in methionine formation. Can use methylcobalamin and methylcobinamide as methyl donors, but methylcobalamin is not considered to be the physiological substrate. SIMILARITY: Belongs to the archaeal MetE family.


FUNCTION: N-methyltransferase; part of the gene cluster that mediates the biosynthesis of benzomalvin A and D (PubMed:28604695). The pathway begins with the loading of amino acid precursors onto the A domains of the non ribosomal peptide synthetases benY and benZ (PubMed:28604695). BenY and the A1 domain of benZ are loaded with anthranilate (Anth), while the A2 domain of benZ is loaded with phenylalanine (Phe) (PubMed:28604695). N-methylation of Phe by the methyltransferase benX may happen before loading of Phe onto benZ, after loading of Phe, or after dipeptide formation (PubMed:28604695). Condensation of Anth with the secondary amine of NmPhe or Phe is catalyzed by the C1 domain of benZ, forming a dipeptide intermediate (PubMed:28604695). This is followed by in trans condensation of the Anth-NmPhe dipeptide with Anth bound to the T domain of benY by the C2 domain of benZ to form the linear tripeptide Anth-NmPhe-Anth (PubMed:28604695). Cyclization and release of the tripeptide is then catalyzed by the C-terminal C domain of benY and the resulting 11-member macrocyclic intermediate is expected to spontaneously collapse to form the benzodiazepine core (PubMed:28604695). Benzomalvin A is in conformational equilibrium with its atropisomer, benzomalvin D (PubMed:28604695). SIMILARITY: Belongs to the methyltransferase superfamily.


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


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0299 family.


FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Required for proper complex I assembly. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Required for proper complex I assembly (PubMed:30245030). Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the complex I LYR family.


FUNCTION: Cell membrane receptor of natural killer/NK cells that is activated by binding of extracellular ligands including BAG6 and NCR3LG1. Stimulates NK cells cytotoxicity toward neighboring cells producing these ligands. It controls, for instance, NK cells cytotoxicity against tumor cells. Engagement of NCR3 by BAG6 also promotes myeloid dendritic cells (DC) maturation, both through killing DCs that did not acquire a mature phenotype, and inducing the release by NK cells of TNFA and IFNG that promote DC maturation. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the natural cytotoxicity receptor (NCR) family.


FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the eukaryotic ATPase epsilon family.


FUNCTION: Ribosyldihydronicotinamide dehydrogenase-like protein; part of the tra gene cluster that produces terrestric acid (PubMed:30811183). The clavatol biosynthesis cluster cla and the terrestric acid cluster tra are both involved in the production of peniphenones and penilactones (PubMed:30811183). The non-reducing PKS claF is responsible for the formation of clavatol from successive condensations of 3 malonyl-CoA units, presumably with a simple acetyl- CoA starter unit, and 2 methylation steps (PubMed:30811183). The esterase claE probably collaborates with claF by catalyzing the hydrolysis of ACP-bound acyl intermediates to free the ACP from stalled intermediates (By similarity). The clavatol oxidase claD then converts clavatol to hydroxyclavatol (PubMed:30811183). Spontaneous dehydration of hydroxyclavatol leads to the accumulation of the highly active ortho-quinone methide (PubMed:30811183, PubMed:31860310). On the other hand, the PKS-NRPS hybrid traA is involved in the formation of crustosic acid, with the help of traB and traD (PubMed:30811183). The polyketide synthase module (PKS) of traA is responsible for the synthesis of the polyketide backbone via the condensation of an acetyl- CoA starter unit with 3 malonyl-CoA units (PubMed:30811183). The downstream nonribosomal peptide synthetase (NRPS) module then amidates the carboxyl end of the polyketide with L-malic acid (PubMed:30811183). Because traA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase traG (By similarity). Crustosic acid undergoes decarboxylation and isomerization to the terrestric acid, catalyzed by the 2-oxoglutarate-dependent dioxygenase traH (PubMed:30811183). Both acids are further converted to the 2 gamma-butyrolactones (R)-5-methyltetronic acid and (S)-5- carboxylmethyltetronic acid, with involvement of the cytochrome P450 monooxygenase claJ (PubMed:30811183). Spontaneous addition of the methide to these gamma-butyrolactones leads to peniphenone D and penilactone D, which undergo again stereospecific attacking by methide to give penilactones A and B (PubMed:30811183, PubMed:31860310). SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family.


FUNCTION: ATP-binding RNA helicase which may be involved in the ribosome biogenesis. SUBCELLULAR LOCATION: Nucleus, nucleolus Chromosome. SIMILARITY: Belongs to the DEAD box helicase family. DDX18/HAS1 subfamily.


FUNCTION: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA- precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Required during oogenesis and imaginal development. FUNCTION: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA- precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Required during oogenesis and imaginal development. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=May associate with nascent RNP complexes within the nucleus. SUBCELLULAR LOCATION: Cytoplasm Nucleus Note=May associate with nascent RNP complexes within the nucleus. SIMILARITY: Belongs to the universal ribosomal protein uS2 family.


FUNCTION: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). SUBCELLULAR LOCATION: Cytoplasm, perinuclear region Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Nucleus membrane; Peripheral membrane protein; Cytoplasmic side Note=Localizes mainly at the nuclear periphery and the endoplasmic reticulum membrane. SIMILARITY: Belongs to the NPL4 family.


FUNCTION: Protein that can both mediate the addition of adenosine 5'- monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-273 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Adenylyltransferase that mediates the addition of adenosine 5'- monophosphate (AMP) to specific residues of target proteins. In vivo target proteins include the heat-shock 70 family proteins hsp-1 and hsp-3 and the translation elongation factors eef-1A, eef-1G and eef-2. Can AMPylate core histone H3 in vitro (By similarity). Can also act as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from target proteins (By similarity). Decreases susceptibility to P.aeruginosa-mediated killing and might therefore play a role in the innate immune response (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein Nucleus membrane; Single-pass membrane protein Note=Predominantly localized to the endoplasmic reticulum and to the nucleus. SIMILARITY: Belongs to the fic family.


FUNCTION: Metalloaminopeptidase that catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg- Pro-Pro (PubMed:10095056). Contributes to the degradation of bradykinin (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase M24B family.


FUNCTION: Highly potent toxin against both insect and some mammalian sodium channels (Nav) (PubMed:34445875). It potently inhibits inactivation of insect sodium channels of B.germanica (BgNav1) (EC(50)=2.6 nM) and also delays the inactivation of mammalian Nav with potent activity on Nav1.1/SCN1A (hNav1.1/SCN1A; EC(50)=7.9 nM, rNav1.2/SCN2A; EC(50)=24.3 nM, rNav1.3/SCN3A; EC(50)=105.6 nM, rNav1.4/SCN4A; EC(50)=46.4 nM, hNav1.5/SCN5A; EC(50)=215.2 nM, mNav1.6/SCN8A; EC(50)=36.3 nM, hNav1.9/SCN9A; EC(50)=97.2 nM) (PubMed:34445875). 1 uM is enough to completely inhibits the inactivation, resulting in sustained non-inactivating currents (By similarity). In addition, the toxin significantly enhances the recovery from inactivation, and the open state is not required for the toxin to interact with the channel (By similarity). In vivo, injection into brine shrimp (Artemia salina) stops movement or causes death after 24 hours (EC(50)=2.8 uM) (PubMed:34445875). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the nemertide family.


FUNCTION: Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Has an essential role in mediating growth by negatively regulating insulin signaling. It also has a role in maintaining presynaptic function in the neuromuscular junction synapses of third-instar larvae. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CRBN family.


FUNCTION: Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs, the first step in 5- carboxymethoxyuridine (cmo5U) biosynthesis. May be part of an alternate pathway, which is able to bypass cmo5U biogenesis in a subset of tRNAs under aerobic conditions. SIMILARITY: Belongs to the TrhO family.


FUNCTION: ATP-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the pointed end of the daughter actin filament. In podocytes, required for the formation of lamellipodia downstream of AVIL and PLCE1 regulation. In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs). Plays a role in ciliogenesis. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection Nucleus Note=In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cell projection Nucleus Note=In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes). SIMILARITY: Belongs to the actin family. ARP3 subfamily.


SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase family.


FUNCTION: Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. SIMILARITY: Belongs to the prokaryotic molybdopterin-containing oxidoreductase family.


FUNCTION: Cleaves thioester-linked long fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides. SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the palmitoyl-protein thioesterase family.


FUNCTION: Probable neurotoxin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin D superfamily.


SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.


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


FUNCTION: Transcription activator that binds to DNA in promoters of target genes on a specific bipartite motif 5'-[ACG][CA]GT[AG](5- 6n)[CT]AC[AG]-3' (PubMed:23340744). Promotes lateral root development (PubMed:16359384). Triggers the expression of senescence-associated genes during age-, salt- and dark-induced senescence through a regulatory network that may involve cross-talk with salt- and H(2)O(2)- dependent signaling pathways (PubMed:9351240, PubMed:15295076, PubMed:20113437, PubMed:21303842). Regulates also genes during seed germination (PubMed:20113437). Regulates positively aging-induced cell death (PubMed:19229035). Involved in age-related resistance (ARR) against Pseudomonas syringae pv. tomato and Hyaloperonospora arabidopsidis (PubMed:19694953). Antagonizes GLK1 and GLK2 transcriptional activity, shifting the balance from chloroplast maintenance towards deterioration during leaf senescence (PubMed:23459204). Promotes the expression of senescence-associated genes, including ENDO1/BFN1, SWEET15/SAG29 and SINA1/At3g13672, during senescence onset (PubMed:23340744). SUBCELLULAR LOCATION: Nucleus Note=Localizes in the nucleus, where it interacts with NLA.


FUNCTION: Catalyzes the reduction of both Delta(1)-pyrroline-2- carboxylate (Pyr2C) and Delta(1)-piperideine-2-carboxylate (Pip2C) to L-proline and L-pipecolate, respectively, using NADPH as the electron donor. Can use NADH instead of NADPH, although with much less efficiency. Plays an essential role in the catabolism of D-proline and D-lysine, which allows P.putida to grow on each of these amino-acids as a sole carbon source; D-lysine appears to be catabolized only through the pipecolate pathway. Can also catalyze the reverse oxidation reactions, albeit at a much lower rate. To a lesser extent, is able to catalyze in vitro the NADPH-dependent formation of N-alkyl-L-amino acids from the corresponding alpha-oxo acids and alkylamines, e.g. the formation of N-methylalanine from pyruvate and N-methylamine; cannot use ammonia as substrate for these reductive amination reactions. Shows neither malate dehydrogenase nor lactate dehydrogenase activity. SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.


FUNCTION: Capsid protein (CA) is the structural component of the virus- like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid- like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity). SUBCELLULAR LOCATION: Cytoplasm.


SUBCELLULAR LOCATION: Cytoplasm, cytosol Cytoplasm Rough endoplasmic reticulum Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). SIMILARITY: Belongs to the eukaryotic ribosomal protein eS21 family.


FUNCTION: Might be efficient in the degradation of transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the peptidase S1C family.


FUNCTION: This enzyme hydrolyzes cefotaxime, ceftazidime and other broad spectrum cephalosporins. SIMILARITY: Belongs to the class-A beta-lactamase family.


FUNCTION: Cytochrome b subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of menaquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome b family.


FUNCTION: Required for the assembly of yeast cytochrome oxidase. Involved in the biosynthesis of heme A and the initial step in this pathway, the hydroxylation of heme O, is thought to be catalyzed by a three-component mono-oxygenase consisting of COX15, ferredoxin YAH1 and ferredoxin reductase ARH1. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the COX15/CtaA family.


FUNCTION: Has bactericidal activity. SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule. SIMILARITY: Belongs to the beta-defensin family.


FUNCTION: Member of the yiaKLX1X2PQRS operon; however YiaX1 is not required for L-ascorbate utilization under aerobic conditions. SIMILARITY: Belongs to the YiaX1 family.


FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulates the genomic RNA and VP2 proteins. Attaches virion to target cells. Once attached, the virion is endocytosed. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the caliciviridae capsid protein family.


FUNCTION: Mediates voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. The channel activity is up-regulated by cAMP. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.8/KCNA10 sub-subfamily.


FUNCTION: Possesses hydroxyproline O-galactosyltransferase activity. Transfers galactose from UDP-galactose to hydroxyproline residues in the arabinogalactan proteins (AGPs). Is specific for AGPs containing non-contiguous peptidyl hydroxyproline residues. The addition of galactose onto the peptidyl hydroxyproline residues in AGP core proteins represents the first committed step in arabinogalactan polysaccharide addition. AGP glycans play essential roles in both vegetative and reproductive plant growth. SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 31 family.


FUNCTION: Probable chloride channel. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the tweety family.


FUNCTION: Potential disease resistance protein. SIMILARITY: Belongs to the disease resistance NB-LRR family. RPP8/HRT subfamily.


FUNCTION: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin- associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.


FUNCTION: Snake venom zinc metalloprotease that possesses high hemorrhagic activity. It inhibits collagen-induced platelet aggregation and activates prothrombin (F2). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom metalloproteinase (M12B) family. P-III subfamily. P-IIIa sub-subfamily.


FUNCTION: Can phosphorylate the myelin basic protein in vitro (PubMed:14720124). Required for endosperm development in embryos (PubMed:15634699). Maybe involved in auxin and osmotic stress responses (PubMed:21431781). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate, the first step in the de novo biosynthesis of NAD(+). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. NadB subfamily.


FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication in an ATP-dependent manner (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ORC1 family.


FUNCTION: Involved in nuclear movement during fibroblast polarization and migration. Proposed to be involved in actin-dependent nuclear movement via association with transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow (By similarity). Overexpression can recruit Ran GTPase to the nuclear periphery (PubMed:27541860). FUNCTION: [Isoform 2]: May define a distinct membrane domain in the vicinity of the mitotic spindle (PubMed:19494128). Involved in the organization of the nuclear envelope implicating EMD, SUN1 and A-type lamina (PubMed:21610090). SUBCELLULAR LOCATION: [Isoform 2]: Nucleus inner membrane; Multi-pass membrane protein Cytoplasm, cytoskeleton, spindle pole Note=The C- terminal of isoform 2 is located on the nucleoplasmic side. During interphase, isoform 2 is distributed in the inner nuclear membrane in distinct micro-domains and during mitosis, it is found in the ER but it also localizes to the polar regions of the mitotic spindle. SIMILARITY: Belongs to the TMEM201 family.


FUNCTION: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. Acts as a ligand for integrin which is required for IGF2 signaling. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insulin family.


FUNCTION: Catalyzes the transport of dicarboxylates, such as oxoglutarate, oxaloacetate, malate, and succinate, and of tricarboxylates, such as citrate, isocitrate, cis-aconitate, and trans- aconitate by a counter-exchange mechanism across the inner mitochondrial membrane. Substrate preference in reconstituted proteoliposomes is oxaloacetate > malonate > malate > maleate > succinate > oxoglutarate > citrate > trans-aconitate > cis-aconitate > sulfate > isocitrate. May be important for plant metabolic functions requiring organic acid flux to or from the mitochondria, such as nitrogen assimilation, export of reducing equivalents from the mitochondria, and fatty acid elongation. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.


FUNCTION: Cell-counting factor that limits the maximum size of the multicellular structure. Does not possess acid phosphatase activity. Cells with decreased levels of this protein form large groups while cells overexpressing this protein form small groups. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the histidine acid phosphatase family.


SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.


FUNCTION: One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. This subunit is directly involved in the binding to pre-mRNAs (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Localized with DDX1 in cleavage bodies.


FUNCTION: Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PDX1. Involved in the indirect resistance to singlet oxygen-generating photosensitizers. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutaminase PdxT/SNO family.


FUNCTION: Catalyzes the epoxidation of physiological unsaturated fatty acids in vitro. Can use laurate, oleate, linoleate, linolenate and vernolate as substrate. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. FUNCTION: Plays a crucial role in the lysogenic life cycle of bacteriophage lambda, as it is required not only in the recombination reaction, which inserts lambda DNA into the E.coli chromosome, but also for the synthesis of int and cI repressor, two phage proteins necessary for DNA insertion and repression, respectively. The synthesis of int and cI proteins is regulated indirectly by IHF via translational control of the lambda cII protein. FUNCTION: This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. FUNCTION: One of the 2 subunits of integration host factor (IHF), a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. Binds to hundreds of transcriptionally inactive, AT-rich DNA sites, approximately half its binding sites are in non-coding DNA, which only accounts for about 10% of the genome (PubMed:16963779). FUNCTION: Has an essential role in conjugative DNA transfer (CDT), the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut in the origin of transfer by TraI, at the nic site. Relaxosome formation requires binding of IHF and TraY to the oriT region, which then facilitates binding of TraI. SUBCELLULAR LOCATION: Cytoplasm, nucleoid Note=Scattered throughout the nucleoid (PubMed:21903814). SIMILARITY: Belongs to the bacterial histone-like protein family. SIMILARITY: Belongs to the bacterial histone-like protein family.


FUNCTION: Binds to sodium channels (Nav) and affects the channel activation process. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily. Sodium channel inhibitor family. Beta subfamily.


FUNCTION: Component of a hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4- tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4- tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1- hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)- aconitate. These reactions are part of the biosynthesis pathway of coenzyme B. SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC type 2 subfamily.


FUNCTION: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT (By similarity). SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsaA/PsaB family.


FUNCTION: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood (PubMed:16317684). Modulates SLC51A glycosylation, membrane trafficking and stability activities (PubMed:16317684). The Ost-alpha/Ost-beta complex efficiently transports the major species of bile acids (taurocholate) (PubMed:16317684). Taurine conjugates are transported more efficiently across the basolateral membrane than glycine- conjugated bile acids (By similarity). Can also transport steroids such as estrone 3-sulfate and dehydroepiandrosterone 3-sulfate, therefore playing a role in the enterohepatic circulation of sterols (PubMed:16317684). Able to transport eicosanoids such as prostaglandin E2 (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Note=Mainly restricted to the lateral and basal membranes of ileal enterocytes. SIMILARITY: Belongs to the OST-beta family.


SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family.


SIMILARITY: Belongs to the peptidase C69 family.


FUNCTION: Possesses antimicrobial activity against both Gram-negative (MIC between 23.8 and 51.2 uM) and Gram-positive (MIC between 11.8 and 46.5 uM) bacteria, as well as against the fungus C.tropicalis (MIC of 48.6 uM). Also possesses a relatively high hemolytic activity. SUBCELLULAR LOCATION: Secreted Target cell membrane Note=Forms a helical membrane channel in the prey. SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP) superfamily. Medium-length antimicrobial peptide (group 3) family.


FUNCTION: Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopantetheine adenylyltransferase, coded by the coaD domain; the fifth reaction is catalyzed by the dephospho-CoA kinase, coded by the coaE domain. May act as a point of CoA biosynthesis regulation. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion matrix Note=The protein is mainly present in the mitochondrial matrix, probably anchored to the inner mitochondrial membrane, but is also present in cell lysate. SIMILARITY: In the central section; belongs to the eukaryotic CoaD family.


SIMILARITY: Belongs to the small heat shock protein (HSP20) family.


FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the aromatic-ring hydroxylase family. KMO subfamily.


FUNCTION: [Protein XRCC4, C-terminus]: Acts as an activator of the phospholipid scramblase activity of XKR4 (PubMed:33725486). This form, which is generated upon caspase-3 (CASP3) cleavage, translocates into the cytoplasm and interacts with XKR4, thereby promoting phosphatidylserine scramblase activity of XKR4 and leading to phosphatidylserine exposure on apoptotic cell surface (PubMed:33725486). FUNCTION: [DNA repair protein XRCC4]: DNA non-homologous end joining (NHEJ) core factor, required for double-strand break repair and V(D)J recombination (PubMed:10757784, PubMed:10854421, PubMed:17124166, PubMed:16412978, PubMed:8548796, PubMed:25742519, PubMed:12517771, PubMed:17290226, PubMed:22228831, PubMed:25597996, PubMed:25934149, PubMed:26100018, PubMed:26774286). Acts as a scaffold protein that regulates recruitment of other proteins to DNA double-strand breaks (DSBs) (PubMed:15385968, PubMed:20852255, PubMed:26774286, PubMed:27437582). Associates with NHEJ1/XLF to form alternating helical filaments that bridge DNA and act like a bandage, holding together the broken DNA until it is repaired (PubMed:26100018, PubMed:27437582, PubMed:28500754, PubMed:21775435, PubMed:22287571, PubMed:21768349). The XRCC4-NHEJ1/XLF subcomplex binds to the DNA fragments of a DSB in a highly diffusive manner and robustly bridges two independent DNA molecules, holding the broken DNA fragments in close proximity to one other (PubMed:27437582). The mobility of the bridges ensures that the ends remain accessible for further processing by other repair factors (PubMed:27437582). Plays a key role in the NHEJ ligation step of the broken DNA during DSB repair via direct interaction with DNA ligase IV (LIG4): the LIG4-XRCC4 subcomplex reseals the DNA breaks after the gap filling is completed (PubMed:9242410, PubMed:10757784, PubMed:10854421, PubMed:12517771, PubMed:17290226, PubMed:19837014). XRCC4 stabilizes LIG4, regulates its subcellular localization and enhances LIG4's joining activity (PubMed:9242410, PubMed:10757784, PubMed:10854421, PubMed:12517771, PubMed:17290226, PubMed:21982441, PubMed:22228831). Binding of the LIG4-XRCC4 subcomplex to DNA ends is dependent on the assembly of the DNA-dependent protein kinase complex DNA-PK to these DNA ends (PubMed:10757784, PubMed:10854421). Promotes displacement of PNKP from processed strand break termini (PubMed:20852255, PubMed:28453785). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Localizes to site of double-strand breaks. SUBCELLULAR LOCATION: [Protein XRCC4, C-terminus]: Cytoplasm Note=Translocates from the nucleus to the cytoplasm following cleavage by caspase-3 (CASP3). SIMILARITY: Belongs to the XRCC4-XLF family. XRCC4 subfamily.


FUNCTION: Together with bola2, acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins. Required for hemoglobin maturation. Does not possess any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity. SUBCELLULAR LOCATION: Cytoplasm, cytosol.


FUNCTION: Transcriptional regulator (PubMed:20940257). Recognizes and binds 2 copies of the core DNA sequence motif 5'-GGGGG-3' (PubMed:20940257). Binds to the HMGN1 promoter and may repress HMGN1 expression (By similarity). Regulates SNCA expression in primary cortical neurons (By similarity). Binds to the COL2A1 promoter and activates COL2A1 expression, as part of a complex with SOX9 (PubMed:20940257). Plays a role in chondrocyte differentiation (PubMed:20940257). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.


FUNCTION: Polymerizes as an extended structure around the baseplate- tail tube complex. During ejection, the sheath shifts to a contracted form, thereby making the inner tail tube protrude through the host cell envelope. SUBCELLULAR LOCATION: Virion Host cytoplasm Note=Tail. SIMILARITY: Belongs to the myoviridae tail sheath protein family.


FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic ribosomal protein eS25 family.


FUNCTION: Involved in the asymmetric conversion of racemic 5- substituted hydantoins to the corresponding L-amino acids. Prefers L- carbamoyl-L-tryptophan and N-carbamoyl-L-tyrosine. Has weaker activity with N-carbamoyl-D,L-phenylalanine and N-carbamoyl-L-thienyalanine. Carbamoyl derivatives of beta-alanine and charged aliphatic amino acids are not accepted as substrates. SIMILARITY: Belongs to the peptidase M20 family.


FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators (PubMed:9305900, PubMed:10965849, PubMed:10625675, PubMed:16143298, PubMed:16112079, PubMed:15558016, PubMed:27435673). Catalyzes the peroxidation of arachidonate and linoleate into (8S)-HPETE and (9S)- HPODE respectively (PubMed:9305900, PubMed:10965849, PubMed:10625675, PubMed:16143298, PubMed:16112079, PubMed:15558016, PubMed:27435673). In addition to generate (8S)-HPETE from free arachidonic acid (AA), may produce other HETE isomers from phospholipid-esterified polyunsaturated fatty acids and minor products derived from (8S)-HPETE itself that may include leukotriene A4 and 8,15-diHPETE (PubMed:16143298, PubMed:16112079, PubMed:27435673). With free arachidonate as substrate, has no detectable 15S-lipoxygenase activity and only displays a 8S- lipoxygenase activity (PubMed:10625675, PubMed:16112079, PubMed:16143298, PubMed:15558016, PubMed:10965849, PubMed:9305900). However may have a 15S-lipoxygenase activity with (8S)-HPETE to produce (8S,15S)-diHPETE and when oxidizes directly arachidonic acid esterified to membrane-bound phospholipids to produce a phospholipid-esterified 15-HpETE (PubMed:27435673, PubMed:16112079, PubMed:16143298). May also catalyze (15S)-HPETE peroxidation to produce 8,15-diHPETE (PubMed:16112079). May play a role in keratinocyte differentiation through activation of the peroxisome proliferator activated receptor signaling pathway (PubMed:10965849). SUBCELLULAR LOCATION: Cytoplasm, cytosol Membrane; Peripheral membrane protein Note=Predominantly cytosolic; becomes enriched at membranes upon calcium binding. SIMILARITY: Belongs to the lipoxygenase family.


FUNCTION: Required for autophagic breakdown of peroxisomes, called pexophagy, through linking peroxisomes to the autophagy apparatus. Involved in regulation of the glyoxylate cycle. SUBCELLULAR LOCATION: Peroxisome Note=Recruited to peroxisomes by PEX3.


FUNCTION: Component of the monoterpenoid indole alkaloids (MIAs, e.g. echitovenine, tabersonine, lochnericine, 19-hydroxytabersonine and horhammericine) biosynthetic pathway; MIAs are used in cancer treatment and other medical applications (PubMed:31009114). Cytochrome P450 catalyzing the hydroxylation of (+)-vincadifformine to (+)- minovincinine (PubMed:31009114, PubMed:35660549). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.