FUNCTION: Inhibitor of serine proteases. The primary target is elastase, but also has a moderate affinity for plasmin and thrombin (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the serpin family.


FUNCTION: Involved in DNA conjugation, at least in the recipient strain (PubMed:18554329). SUBCELLULAR LOCATION: Secreted Note=Secreted via the ESX-1 / type VII secretion system (T7SS) (By similarity). SIMILARITY: Belongs to the EspB family.


FUNCTION: One of the components of the core complex of photosystem II (PSII). 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. This subunit is found at the monomer-monomer interface (By similarity). Involved in assembly of monomeric PSII from the CP43-less intermediate. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PsbM family.


FUNCTION: Transcription factor involved in specification of neuronal cell types and which is required for inner ear and hypothalamus development. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HMX homeobox family.


FUNCTION: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the tropolone class of fungal maleic anhydrides (PubMed:22508998, PubMed:24863423). The pathway begins with the synthesis of 3-methylorcinaldehyde by the non-reducing polyketide synthase (PKS) tropA (PubMed:22508998). 3-methylorcinaldehyde is the substrate for the FAD-dependent monooxygenase tropB to yield a dearomatized hydroxycyclohexadione (PubMed:22508998, PubMed:24863423). The 2-oxoglutarate-dependent dioxygenase tropC then performs the oxidative ring expansion to provide the first tropolone metabolite stipitaldehyde (PubMed:22508998, PubMed:24863423). Trop D converts stipitaldehyde into stipitacetal which is in turn converted to stipitalide by the short-chain dehydrogenase/reductase tropE (PubMed:24863423). The next steps involve tropF, tropG, tropH, tropI and tropJ to form successive tropolone maleic anhydrides including stipitaldehydic, stipitatonic and stipitatic acids (PubMed:24863423). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family.


FUNCTION: Probable RNA helicase. Required for RNA-mediated gene silencing by the RNA-induced silencing complex (RISC). Required for both miRNA-mediated translational repression and miRNA-mediated cleavage of complementary mRNAs by RISC (By similarity). SUBCELLULAR LOCATION: Cytoplasm, P-body. SIMILARITY: Belongs to the DNA2/NAM7 helicase family. SDE3 subfamily.


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


FUNCTION: Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane Note=In or around the basement membrane. SIMILARITY: Belongs to the SPARC family.


FUNCTION: Putative taste receptor. TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 3 family. TAS1R subfamily.


FUNCTION: Catalyzes the reversible reduction of methylene-H(4)MPT to methyl-H(4)MPT. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the mer family.


FUNCTION: Transcription regulator that can specifically activate or repress expression of target genes. Required for expression of the virulence gene inv. FUNCTION: Transcription regulator that can specifically activate or repress expression of target genes. SIMILARITY: Belongs to the SlyA family.


FUNCTION: Oxygen-binding protein. May be involved in a storage mechanism or for delivery to oxygen-requiring enzymes. The oxygen- binding site contains two iron atoms. SIMILARITY: Belongs to the hemerythrin family.


FUNCTION: Represses adpA expression by binding to the promoter region in the absence of A-factor, causing repression of streptomycin production and of sporulation. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Catalyzes the cleavage of the cysteine-S bond in various cysteine-S-conjugates (PubMed:17191898, PubMed:18515361). Cleaves L- cystathionine, as well as S-substituted cysteine conjugates S-benzyl-L- cysteine and S-ethyl-L-cysteine (PubMed:17191898). Releases four human body odoriferous sulfanylalkanols: 3-methyl-3-sulfanylhexan-1-ol (3M3SH), 3-sulfanylhexan-1-ol, 2-methyl-3-sulfanylbutan-1-ol and 3- sulfanylpentan-1-ol; the release is obtained after the sequential hydrolysis of the Cys-Gly bond of the odorless Cys-Gly-S-conjugate precursors by the dipeptidase TpdA, then the cleavage of the resulting Cys-S-conjugates by MetC (PubMed:17191898, PubMed:18515361). SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. MalY/PatB cystathionine beta-lyase subfamily.


FUNCTION: Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins. Able to activate GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for free GTP. Involved in regulation of microtubule pulling forces during mitotic movement of chromosomes by stimulating G(i)-alpha protein, possibly leading to release G(i)-alpha-GTP and NuMA proteins from the NuMA-GPSM2-G(i)- alpha-GDP complex. Also acts as an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-coupled receptor-mediated ERK activation (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Colocalizes with GNAI1 and RGS14 at the plasma membrane (By similarity). Colocalizes with RIC8A in CA2 hippocampal neurons. SIMILARITY: Belongs to the synembryn family.


FUNCTION: Binds to TEK/TIE2, modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2. Promotes endothelial cell survival, migration and angiogenesis. SUBCELLULAR LOCATION: Secreted.


SIMILARITY: Belongs to the peptidase G1 family.


FUNCTION: Rod linker protein, associated with phycocyanin. Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side Note=This protein occurs in the rod, it is associated with phycocyanin. SIMILARITY: Belongs to the phycobilisome linker protein family.


FUNCTION: Has antibacterial activity against a variety of bacteria including S.aureus, P.aeruginosa and M.tuberculosis. Acts by inducing bacterial membrane breakage (By similarity). FUNCTION: Induces production of reactive oxygen species (ROS) which are necessary for cell proliferation. May play a role in inducing oxidative DNA damage and replicative senescence. May play a role in the coordination of mitochondrial morphology and cell proliferation (By similarity). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the MGR2 family.


FUNCTION: Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. SIMILARITY: Belongs to the bacterioferritin family.


FUNCTION: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A. SIMILARITY: Belongs to the protein prenyltransferase subunit beta family.


FUNCTION: Probably involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.


FUNCTION: Converts tyramine into octopamine, a neurotransmitter involved in pharyngeal pumping and egg laying. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. SIMILARITY: Belongs to the copper type II ascorbate-dependent monooxygenase family.


FUNCTION: Binds estrogens with an affinity similar to that of ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the nuclear hormone receptor family. NR3 subfamily.


FUNCTION: Binds specifically to the plant telomeric double-stranded DNA sequences 5'-GGTTTAG-3'. At least 4 repeats of telomeric sequences are required for binding. Induces DNA bending. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine nucleotides such as inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) or xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HAM1 NTPase family.


FUNCTION: Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs and play a central role in ribosomal RNA processing. The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs. Catalyzes pseudouridylation at position 93 in U2 snRNA. Also catalyzes pseudouridylation of mRNAs; H/ACA-type snoRNAs probably guide pseudouridylation of mRNAs. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the pseudouridine synthase TruB family.


FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of pyranterreones, a family of antioxidative compounds (PubMed:32077283). The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase pytA that condenses 4 malonyl-CoA units ato the acetyl starter unit by the modular PKS of pytA (PubMed:32077283). The acyl chain is then connected to an L-serine through the amide bond by the modular NRPS of pytA (PubMed:32077283). A tetramic acid is formed and released from the PKS- NRPS pytA to give pyranterreone 5 with the help of the thioesterase pytI (PubMed:32077283). Pyranterreone 5 could be methylated by pytC to afford pyranterreone 6 (Probable). Both pyranterreones 5 and 6 are subsequently oxidized by the FAD-linked oxidoreductase pytB and the cytochrome P450 monooxygenase pytD to form the fused gamma-pyrone core, resulting in pyranterreones 7 and 11, respectively (PubMed:32077283). The hydroxy group at C-8 of pyranterreones 7 and 11 are dehydrated by the aspartyl protease pytH to form a delta-7 double bond to give pyranterreones 3 and 1, 2 accordingly (PubMed:32077283). The exo- methylene of pyranterreone 3 could be reduced into a pendant methyl by reductase pytE to provide pyranterreone 4, also known as cordylactam (Probable). Pyranterreone 4 can be reconverted to pyranterreone 3 through pytB-catalyzed dehydrogenation or further oxidized to pyranterreones 9 and 10 (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.


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


FUNCTION: May activate NF-kappa-B signaling pathways. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.


FUNCTION: In presence of calcium ions, it binds to surfactant phospholipids and contributes to lower the surface tension at the air- liquid interface in the alveoli of the mammalian lung and is essential for normal respiration. Enhances the expression of MYO18A/SP-R210 on alveolar macrophages. SUBCELLULAR LOCATION: Secreted Secreted, extracellular space, extracellular matrix Secreted, extracellular space, surface film. SIMILARITY: Belongs to the SFTPA family.


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.


FUNCTION: Water channel required to facilitate the transport of water across cell membrane. Active as heteromers with PIP1-1, PIP2-1, PIP2-4 or PIP2-5, but not as homomers. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. PIP (TC 1.A.8.11) subfamily.


FUNCTION: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments (By similarity). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.


SIMILARITY: Belongs to the GASA family.


FUNCTION: Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the serpin family.


FUNCTION: Tick salivary platelet aggregation inhibitor that plays an important part in the anti-hemostatic strategy of ticks (Probable). Inhibits platelet aggregation induced by ADP, thrombin and thromboxane A2 (TXA2) (PubMed:25152502). Blocks platelet adhesion to soluble collagen (most probably through the binding to alpha-2/beta-1 integrin (ITGA2/ITGB1)) and binds to purified glycoprotein IIb/IIIa (ITGA2B/ITGB3) in a dose-dependent manner (PubMed:25152502). In vivo, reduces thrombus weight effectively in a rat arteriovenous shunt model and inhibits thrombosis in a carrageenan-induced mouse tail thrombosis model (PubMed:25152502). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ixodegrin family.


FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. 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 NDUFA12 subunit family.


FUNCTION: Exact function not known. Involved in copper resistance. Appears to be involved in copper uptake in conjunction with CopC. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the CopD family.


FUNCTION: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the sigma-70 factor family. RpoH subfamily.


FUNCTION: Component of the type IV secretion system ptl required for secretion of assembled pertussis toxin (PTX) through the outer membrane. Could possess peptidoglycanase activity. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the virB8 family.


SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the WD repeat WDR55 family.


FUNCTION: In nitrogen-limiting conditions, when the ratio of Gln to 2- ketoglutarate decreases, P-II is uridylylated to P-II-UMP. P-II-UMP allows the deadenylation of glutamine synthetase (GS), thus activating the enzyme. Conversely, in nitrogen excess P-II is deuridylated and promotes the adenylation of GS. P-II indirectly controls the transcription of the GS gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of glnA. When P-II is uridylylated to P-II-UMP, these events are reversed. SIMILARITY: Belongs to the P(II) protein family.


FUNCTION: This protein binds directly to 23S ribosomal RNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL1 family.


SIMILARITY: Belongs to the chlamydial CPn_0808/CT_579/TC_0868 family.


FUNCTION: Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen (By similarity). SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily.


FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.


FUNCTION: component of the regulatory network controlling carbon source utilization through ubiquitination and deubiquitination involving creA, creB, creC, creD and acrB. Involved in resistance to acriflavine, and required for normal growth on a range of sole carbon sources, including fructose, cellobiose, raffinose, and starch, and reduced utilization of amino acids, including GABA and beta-alanine, as sole carbon and nitrogen sources. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the acrB family.


FUNCTION: [GLV6p]: Signaling peptide (root growth factor) required during root gravitropism in a PIN2-traffic dependent manner (PubMed:23370719). May be involved in maintaining the postembryonic root stem cell niche (PubMed:20798316). Root growth factor that regulates the pattern of root growth and lateral root development by modulating the length and the number of cortical cells in the root apical meristem (RAM), and the anticlinal asymmetric cell divisions in lateral root initiation cells (By similarity). SUBCELLULAR LOCATION: [GLV6p]: Secreted. SIMILARITY: Belongs to the RGF family.


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


FUNCTION: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in xyloglucan with retention of the beta-configuration of the glycosyl residues in xyloglucan degradation. Cleaves the backbone of the 3 major types of natural xyloglucans (seed galactoxyloglucan from tamarind kernel, dicot fucogalactoxyloglucan from lettuce leaves, and solanaceous arabinogalactoxyloglucan from tomato fruit), to produce xyloglucan oligosaccharides. May be superfluous in xyloglucan degradation compared to BoGH5A (AC A7LXT7), the other Xyloglucan- specific endo-beta-1,4-glucanase. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor Note=Cell outer membrane localization is predicted by analogy with the archetypal sus locus. SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family.


FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. Component of RNA polymerases IV and V which mediate short-interfering RNAs (siRNA) accumulation and subsequent RNA-directed DNA methylation-dependent (RdDM) transcriptional gene silencing (TGS) of endogenous repeated sequences, including transposable elements. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family.


FUNCTION: Actin-binding protein that regulates actin polymerization, filopodia dynamics and increases the branching of proximal dendrites of developing neurons. SUBCELLULAR LOCATION: Nucleus speckle Cell projection, lamellipodium Nucleus Cell projection, growth cone Cell projection, dendrite Note=Localizes to somata and dendrites in cortical neurons. Colocalizes with G- and F-actin in growth cones and proximal dendrites (PubMed:24782708). Colocalizes in the nucleus with PTK2 (PubMed:24782708). SIMILARITY: Belongs to the ABITRAM family.


FUNCTION: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine- rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Phosphorylates SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre- mRNA in endothelial cells (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Cytoplasmic vesicle, secretory vesicle, acrosome. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily.


FUNCTION: Catalyzes the condensation of ribulose 5-phosphate with formaldehyde to form 3-hexulose 6-phosphate. SIMILARITY: Belongs to the HPS/KGPDC family. HPS subfamily.


FUNCTION: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. SIMILARITY: Belongs to the AdoMet synthase 2 family.


FUNCTION: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA. Rad50 controls the balance between DNA end bridging and DNA resection via ATP-dependent structural rearrangements of the Rad50/Mre11 complex. SIMILARITY: Belongs to the SMC family. RAD50 subfamily.


FUNCTION: Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the anaerobic utilization of allantoin as sole nitrogen source. Reinforces the induction of genes involved in the degradation of allantoin and glyoxylate by producing glyoxylate. SIMILARITY: Belongs to the ureidoglycolate lyase family.


FUNCTION: Multifunctional sorting protein that controls the endoplasmic reticulum (ER)-mitochondria communication, including the apposition of mitochondria with the ER and ER homeostasis. In addition, in response to apoptotic inducer, translocates BIB to mitochondria, which initiates a sequence of events including the formation of mitochondrial truncated BID, the release of cytochrome c, the activation of caspase-3 thereby causing cell death. May also be involved in ion channel trafficking, directing acidic cluster-containing ion channels to distinct subcellular compartments. SUBCELLULAR LOCATION: Endoplasmic reticulum Mitochondrion. SIMILARITY: Belongs to the PACS family.


FUNCTION: Cysteine protease that acts as a key streptococcal virulence factor by cleaving host proteins involved in immune response (PubMed:7516997, PubMed:10456871, PubMed:11406581, PubMed:11598100, PubMed:12438337, PubMed:12621045, PubMed:24331465, PubMed:23532847, PubMed:19237546, PubMed:35008838, PubMed:35110732, PubMed:35545676). Triggers inflammation by mediating cleavage of host proteins, which can both promote host pathogenesis by triggering sterile inflammation and/or restrict streptococcal infection, depending on host immune statue and infection site (PubMed:35110732, PubMed:35545676, PubMed:35008838). Cleaves host gasdermin-A (GSDMA) in epithelial cells, promoting GSDMA activation and formation of gasdermin pores, triggering pyroptosis (PubMed:35110732, PubMed:35545676). Pyroptosis triggers the elimination of the infected skin cell, depriving the pathogen of its protective niche, while inducing an inflammatory response (PubMed:35110732, PubMed:35545676). This ultimately prevents bacterial penetration of the epithelial barrier and a subsequent systemic dissemination of the pathogen (PubMed:35110732, PubMed:35545676). Also mediates cleavage of the cytokine precursor interleukin-1 beta (IL1B) to its mature form, resulting in inflammation and septic shock (PubMed:28331908, PubMed:32719155). SpeB-mediated maturation of IL1B plays a dual role depending on infection site: while IL1B inflammatory response prevents bacterial growth during invasive skin infections, it promotes streptococcal infection of the nasopharynx by disrupting colonization resistance mediated by the microbiota (PubMed:28331908, PubMed:32719155). Inhibits host autophagy be catalyzing cleavage and inactivation of key autophagy factors, such as CALCOCO2, NBR1 and SQSTM1 (PubMed:24331465). Cleaves and inhibits a number of complement factors, such as C2, C3-beta chain of C3, C4, C5 or SERPING1, thereby promoting evasion of host immunity (PubMed:18160402, PubMed:23532847, PubMed:35008838). May also impair adaptive immunity by catalyzing cleavage and degradation of host immunoglobulins to promote immune system evasion; the relevance of this activity is however unsure in vivo (PubMed:11406581, PubMed:11598100, PubMed:12438337, PubMed:12496168, PubMed:23569114, PubMed:35008838). Catalyzes maturation and release of the peptide hormone bradykinin from the precursor Kininogen-1 (KNG1) to produce hypotension during septic shock (PubMed:8760820). Also involved in bacterial translocation across the host epithelial barrier by mediating cleavage and degradation of host epithelial junction proteins, such as CDH1 and OCLN (PubMed:23532847). Additionally, has been involved in degradation of fibronectin and vitronectin, two host extracellular matrix proteins involved in tissue integrity (PubMed:7516997). Also able to catalyze cleavage and degradation of streptococcal proteins, such as C5a peptidase, EndoS or SmeZ (PubMed:7730368, PubMed:16980693, PubMed:18182097, PubMed:24799625). Degradation of streptococcal proteins is however strictly regulated to preserve integrity of other virulence factors (PubMed:24799625). SUBCELLULAR LOCATION: Secreted Host extracellular space Host cytoplasm. SIMILARITY: Belongs to the peptidase C10 family.


FUNCTION: Microtubule-associated protein which regulates cell division and neuronal migration during cortical development. Necessary for mitotic spindle organization. Necessary for radial and tangential cell migration during brain development, possibly acting as a regulator of cell morphology and process formation during migration. May enhance calcium influx through CACNA1E and stimulate programmed cell death (By similarity). Microtubule inner protein (MIP) part of the dynein- decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (PubMed:34715025). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, spindle pole Cytoplasm, cytoskeleton, cilium axoneme.


SIMILARITY: Belongs to the NAC-alpha family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0056 (MarC) family.


FUNCTION: Chloroplast omega-3 fatty acid desaturase introduces the third double bond in the biosynthesis of 18:3, and probably also 16:3 fatty acids, important constituents of plant membranes. It is thought to use ferredoxin as an electron donor and to act on fatty acids esterified to galactolipids, sulfolipids and phosphatidylglycerol. SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fatty acid desaturase type 1 family.


SIMILARITY: Belongs to the AIM6 family.


FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium- binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regulates the release of lumenal Ca(2+) via the calcium release channel RYR2; this plays an important role in triggering muscle contraction. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats. SUBCELLULAR LOCATION: Sarcoplasmic reticulum lumen Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells. SIMILARITY: Belongs to the calsequestrin family.


FUNCTION: Manganese-dependent repressor that controls a regulon of oxidative stress resistance and iron-storage proteins. Regulates expression of genes encoding antioxidant proteins, such as katA, ahpCF, bcp and trxB. Also regulates expression of the iron-storage protein ftn, the ferritin-like protein mrgA, the ferric uptake regulator fur, the manganese transporter operon mntABC, and its own expression. May act as a hydrogen peroxide and organic hydroperoxide sensor. Required for full virulence in a murine skin abscess model of infection. FUNCTION: Manganese-dependent repressor that controls a regulon of oxidative stress resistance and iron-storage proteins. May act as a hydrogen peroxide and organic hydroperoxide sensor (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Fur family.


FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Macronuclei. SIMILARITY: Belongs to the histone H2B family.


FUNCTION: Thiol-disulfide oxidoreductase which is required in disulfide reduction during c-type cytochrome synthesis. May accept reducing equivalents from CcdA, leading to breakage of disulfide bonds in apocytochrome c; following this reduction heme can be covalently attached. SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein Note=The thioredoxin-like motif is exposed on the outside of the membrane. SIMILARITY: Belongs to the thioredoxin family. ResA subfamily.


FUNCTION: Metallothioneins have a high content of cysteine residues that bind various heavy metals. SIMILARITY: Belongs to the metallothionein superfamily. Type 1 family.


FUNCTION: TAP is a slow, tight-binding inhibitor of blood coagulation, specific for factor Xa.


SIMILARITY: Belongs to the adenoviridae E1B 19 kDa protein family.


FUNCTION: Neisseria acquires iron by extracting it from serum transferrin (TF) in its human host. Acts as a TF receptor and is required for TF utilization. Binds both apo- and holo-TF, via the TF C- terminus. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TonB-dependent receptor family.


FUNCTION: Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Does not oxidize all pdi related proteins, suggesting that it can discriminate between PDI1 and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. SIMILARITY: Belongs to the EROs family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 4-oxalocrotonate tautomerase family. PptA subfamily.


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


FUNCTION: Calcium-sensitive protein which reversibly blocks the barbed ends of actin filaments but does not sever preformed actin filaments. May play an important role in macrophage function. May play a role in regulating cytoplasmic and/or nuclear structures through potential interactions with actin. May bind DNA. Uncapping occurs either when Ca(2+) falls or when the concentration of polyphosphoinositide rises, both at low and high Ca(2+). SUBCELLULAR LOCATION: Nucleus Cytoplasm Melanosome Cell projection, lamellipodium. Cell projection, ruffle. Note=In macrophages, may be predominantly cytoplasmic. Nuclear localization was observed in fibroblasts. In macrophages, present at the membrane-cytoplasm interface. In activated macrophages, concentrated in the ruffles of the leading lamellipodia. SIMILARITY: Belongs to the villin/gelsolin family.


FUNCTION: Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif (PubMed:18713856). Mediates processing of TGFB1, an essential step in TGF-beta-1 activation (By similarity). Converts through proteolytic cleavage the non-functional Brain natriuretic factor prohormone into its active hormone BNP(1-45) (By similarity). By mediating processing of accessory subunit ATP6AP1/Ac45 of the V-ATPase, regulates the acidification of dense-core secretory granules in islets of Langerhans cells (PubMed:18713856). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein Cell membrane; Single- pass type I membrane protein Secreted Endosome membrane; Single-pass type I membrane protein Note=Shuttles between the trans-Golgi network and the cell surface. Propeptide cleavage is a prerequisite for exit of furin molecules out of the endoplasmic reticulum (ER). A second cleavage within the propeptide occurs in the trans Golgi network (TGN), followed by the release of the propeptide and the activation of furin. SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.


FUNCTION: Responsible for glycerol-3-phosphate uptake. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Organophosphate:Pi antiporter (OPA) (TC 2.A.1.4) family.


FUNCTION: One of the primary rRNA binding proteins, it binds directly to 18S rRNA where it nucleates assembly of the head domain of the small subunit. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uS7 family.


FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase T1B family.


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


FUNCTION: Induces the expression of gadE and mdtEF. Could also regulate the expression of other genes involved in acid resistance (By similarity).


FUNCTION: Acts as a modulator of nicotinic acetylcholine receptors (nAChRs) function in the brain (PubMed:27344019). Inhibits nicotine- induced Ca(2+) influx through nAChRs (By similarity). In vitro, specifically inhibits alpha-3:beta-4 and alpha-7 nAChR currents in an allosteric manner (By similarity). Acts as a positive regulator of Wnt/beta-catenin signaling (By similarity). SUBCELLULAR LOCATION: Secreted Cytoplasm Cell membrane; Lipid-anchor, GPI-anchor Synapse, synaptosome Membrane raft Cell projection, dendrite Perikaryon Note=Colocalizes with alpha-3:beta- 4- and alpha-7- nicotinic acetylcholine receptors (nAChRs) in the primary cortex and hippocampus.


FUNCTION: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion intermembrane space. SIMILARITY: Belongs to the anamorsin family.


FUNCTION: Required for maximal expression of sirC, not required to invade host cells. FUNCTION: Required for maximal expression of sirC, not required to invade host cells. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SirB2 family.


FUNCTION: Could play a role in taste reception. Could be necessary for the concentration and delivery of sapid molecules in the gustatory system. Can bind various ligands, with chemical structures ranging from lipids and retinoids to the macrocyclic antibiotic rifampicin and even to microbial siderophores. Exhibits an extremely wide ligand pocket (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.


FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol- pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (By similarity). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). Required for the assembly of both SST3A- and SS3B-containing OST complexes (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the DDOST 48 kDa subunit family.


FUNCTION: Receptor for ADP. Coupled to G(i)-proteins. May play a role in hematopoiesis and the immune system (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity). SIMILARITY: In the N-terminal section; belongs to the MsrA Met sulfoxide reductase family. SIMILARITY: In the C-terminal section; belongs to the MsrB Met sulfoxide reductase family.


SIMILARITY: Belongs to the BetVI family.


FUNCTION: [Frataxin mature form]: Functions as an activator of persulfide transfer to the scaffoding protein ISCU as component of the core iron-sulfur cluster (ISC) assembly complex and participates to the [2Fe-2S] cluster assembly. Accelerates sulfur transfer from NFS1 persulfide intermediate to ISCU and to small thiols such as L-cysteine and glutathione leading to persulfuration of these thiols and ultimately sulfide release. Binds ferrous ion and is released from FXN upon the addition of both L-cysteine and reduced FDX2 during [2Fe-2S] cluster assembly (By similarity). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity). May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. May function as an iron chaperone protein that protects the aconitase [4Fe-4S]2+ cluster from disassembly and promotes enzyme reactivation. May play a role as a high affinity iron binding partner for FECH that is capable of both delivering iron to ferrochelatase and mediating the terminal step in mitochondrial heme biosynthesis (By similarity). FUNCTION: [Extramitochondrial frataxin]: Modulates the RNA-binding activity of ACO1. May be involved in the cytoplasmic iron-sulfur protein biogenesis. May contribute to oxidative stress resistance and overall cell survival. SUBCELLULAR LOCATION: [Extramitochondrial frataxin]: Cytoplasm, cytosol. SUBCELLULAR LOCATION: [Frataxin mature form]: Mitochondrion. SIMILARITY: Belongs to the frataxin family.


FUNCTION: It is not clear if the 2 type A proteins in this organism are functionally redundant (PubMed:9573198). FUNCTION: When a minimal gvp locus (gvpA2-gvpR-gvpN-gvpF-gvpG-gvpL- gvpS-gvpK-gvpJ-gvpT-gvpU, called pNL29) is expressed in E.coli gas vesicles are made. FUNCTION: Gas vesicles are hollow, gas filled proteinaceous nanostructures found in some microorganisms. During planktonic growth they allow positioning of the organism at a favorable depth for light or nutrient acquisition. GvpA forms the protein shell. SUBCELLULAR LOCATION: Gas vesicle shell. SIMILARITY: Belongs to the gas vesicle protein type A family.


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


FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.


FUNCTION: Single-stranded DNA-specific cytidine deaminase. Involved in somatic hypermutation (SHM), gene conversion, and class-switch recombination (CSR) in B-lymphocytes by deaminating C to U during transcription of Ig-variable (V) and Ig-switch (S) region DNA. Required for several crucial steps of B-cell terminal differentiation necessary for efficient antibody responses. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Predominantly cytoplasmic. In the presence of MCM3AP/GANP, relocalizes to the nucleus. SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL55 family.


FUNCTION: Chromatin-associated, histone tail-binding protein that represses transcription via recruitment of HDAC3 and nuclear hormone receptor corepressors. SUBCELLULAR LOCATION: Nucleus Chromosome.


FUNCTION: Component of the ribosomal small subunit processome for the biogenesis of ribosomes, functions in pre-ribosomal RNA (pre-rRNA) processing (By similarity). Essential for embryonic development in part through the regulation of p53 pathway. Controls the expansion growth of digestive organs and liver (By similarity). Also involved in the sympathetic neuronal development (By similarity). Mediates, with CAPN3, the proteasome-independent degradation of p53/TP53 (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the UTP25 family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the autoinducer-2 exporter (AI-2E) (TC 2.A.86) family.


FUNCTION: Part of the ABC transporter complex DdpABCDF, which is probably involved in D,D-dipeptide transport. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.


FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine phosphate. SIMILARITY: Belongs to the thiamine kinase family.


FUNCTION: Has very low affinity for the DHPS substrate 6-hydroxymethyl- 7,8-dihydropterin-pyrophosphate, but can bind the inhibitor dapsone. Seems to lack dihydropteroate synthase activity, and does probably not function in folate metabolism (By similarity). FUNCTION: Has very low affinity for the DHPS substrate 6-hydroxymethyl- 7,8-dihydropterin-pyrophosphate, but can bind the inhibitor dapsone. Seems to lack dihydropteroate synthase activity, and does probably not function in folate metabolism. SIMILARITY: Belongs to the DHPS family.


FUNCTION: Accessory component of the DNA polymerase epsilon complex (By similarity). Participates in DNA repair and in chromosomal DNA replication (By similarity). Forms a complex with CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome-remodeling activity of ISWI/SNF2H and ACF1 (By similarity). Does not enhance nucleosome sliding activity of the ACF-5 ISWI chromatin remodeling complex (By similarity). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Contractile protein that plays a role in heart development and function (By similarity). Following phosphorylation, plays a role in cross-bridge cycling kinetics and cardiac muscle contraction by increasing myosin lever arm stiffness and promoting myosin head diffusion; as a consequence of the increase in maximum contraction force and calcium sensitivity of contraction force. These events altogether slow down myosin kinetics and prolong duty cycle resulting in accumulated myosins being cooperatively recruited to actin binding sites to sustain thin filament activation as a means to fine-tune myofilament calcium sensitivity to force (PubMed:15331360). During cardiogenesis plays an early role in cardiac contractility by promoting cardiac myofibril assembly (By similarity). SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, A band.


FUNCTION: Protein with chaperone functions important for the control of protein folding, processing, stability and localization as well as for the reduction of misfolded protein aggregates. Involved in the regulation of synaptic vesicle recycling, controls STON2 protein stability in collaboration with the COP9 signalosome complex (CSN). In the nucleus, may link the cytoskeleton with the nuclear envelope, this mechanism seems to be crucial for the control of nuclear polarity, cell movement and, specifically in neurons, nuclear envelope integrity. Participates in the cellular trafficking and may regulate the subcellular location of multipass membrane proteins such as the dopamine transporter SLC6A3, leading to the modulation of dopamine neurotransmission. In the endoplasmic reticulum, plays a role in the quality control of protein folding by increasing clearance of misfolded proteins such as SGCE variants or holding them in an intermediate state for proper refolding. May have a redundant function with TOR1B in non- neural tissues (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum lumen Nucleus inner membrane; Peripheral membrane protein Cell projection, growth cone. Cytoplasmic vesicle membrane. Cytoplasmic vesicle, secretory vesicle. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Note=Peripherally associated with the inner face of the ER membrane, probably mediated by the interaction with TOR1AIP1. The association with nucleus envelope is mediated by the interaction with TOR1AIP2. Upon oxidative stress, redistributes to protusions from the cell surface. SIMILARITY: Belongs to the ClpA/ClpB family. Torsin subfamily.


FUNCTION: Transcription factor that plays a role of repressor of filamentous growth and flocculation. Antagonizes functions of SFL2 and FLO8. Plays a role in the hyphal repression induced by secreted factors like dodecanol by competitors such as Pseudomonas aeruginosa and Burkholderia cenocepacia. SUBCELLULAR LOCATION: Nucleus Note=Localizes to the nucleus in both yeast and hyphal cells. SIMILARITY: Belongs to the HSF family.


FUNCTION: Involved in endoplasmic reticulum (ER) stress response. Senses unfolded proteins in the lumen of the ER via its N-terminal domain which leads to enzyme auto-activation. The active endoribonuclease domain splices bZIP50 mRNA to generate a new C- terminus, converting it into a potent unfolded-protein response (UPR) transcriptional activator, which then induces transcription of UPR target genes, such as luminal-binding protein (BiP) chaperones. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


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


FUNCTION: Produces green light with a wavelength of 544 nm. SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.


FUNCTION: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism (By similarity). SIMILARITY: Belongs to the GlnD family.


FUNCTION: Receptor for the hormone galanin (PubMed:24517231). Receptor for the hormones spexin-1 and spexin-2 (PubMed:24517231, PubMed:31474838). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 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 Nucleus. SIMILARITY: Belongs to the universal ribosomal protein uL18 family.


FUNCTION: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. mL61 is not essential in cells grown at 30 degree Celsius but is required for mitochondrial translation in cells grown at 18 degree Celsius. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein mL61 family.


SIMILARITY: Belongs to the opioid growth factor receptor family.


FUNCTION: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not been identified so far. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ORC1 family.


FUNCTION: Required for replication of the leading DNA strand and for completion of lagging strand synthesis. It is essential for cell cycle progression. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DNA polymerase delta/II small subunit family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the intermediate filament family.


FUNCTION: Positive regulatory protein for the occ operon involved in octopine catabolism and uptake. Also acts as a negative regulator of its expression. SIMILARITY: Belongs to the LysR transcriptional regulatory family.


FUNCTION: May bind to RNA. SUBCELLULAR LOCATION: Nucleus speckle Note=Colocalizes with poly(A) RNA in nuclear speckles. SIMILARITY: Belongs to the ZC3H14 family.


FUNCTION: An outer membrane protein that may participate in pathogenesis. Some human Lyme disease patients have antibodies against this protein (PubMed:10948116). The Mlp proteins probably undergo intragenic recombination, generating new alleles (Probable). SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the Multicopy lipoprotein (Mlp) family.


FUNCTION: Acts as a sulfur carrier required for molybdopterin biosynthesis. Component of the molybdopterin synthase complex that catalyzes the conversion of precursor Z into molybdopterin by mediating the incorporation of 2 sulfur atoms into precursor Z to generate a dithiolene group. In the complex, serves as sulfur donor by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. After interaction with MOCS2B, the sulfur is then transferred to precursor Z to form molybdopterin. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MoaD family. MOCS2A subfamily.


FUNCTION: Probable lipase required downstream of MPK4 for accumulation of the plant defense-potentiating molecule, salicylic acid, thus contributing to the plant innate immunity against invasive biotrophic pathogens and to defense mechanisms upon recognition of microbe- associated molecular patterns (MAMPs). Participates in the regulation of various molecular and physiological processes that influence fitness. Together with SG101, required for programmed cell death (PCD) triggered by NBS-LRR resistance proteins (e.g. RPS4, RPW8.1 and RPW8.2) in response to the fungal toxin fumonisin B1 (FB1) and avirulent pathogens (e.g. P.syringae pv. tomato strain DC3000 avrRps4 and pv. maculicola, turnip crinkle virus (TCV), and H.arabidopsidis isolates CALA2, EMOY2, EMWA1 and HIND4). Together with EDS1, confers a basal resistance by restricting the growth of virulent pathogens (e.g. H.arabidopsidis isolates NOCO2 and EMCO5, E.orontii isolate MGH, and P.syringae pv. tomato strain DC3000 or expressing HopW1-1 (HopPmaA)). Necessary for the salicylic acid-(SA-) dependent systemic acquired resistance (SAR) response that involves expression of multiple defense responses, including synthesis of the phytoalexin camalexin and expression of pathogenesis-related genes (e.g. PR1, ALD1, BGL2 and PR5) in response to pathogens, triggering a signal amplification loop that increases SA levels via EDS5 and SID2, but, together with EDS1, seems to repress the ethylene/jasmonic acid (ET/JA) defense pathway. May also function in response to abiotic stresses such as UV-C light and LSD1- dependent acclimatization to light conditions that promote excess excitation energy (EEE), probably by transducing redox signals and modulating stomatal conductance. Regulates the formation of lysigenous aerenchyma in hypocotyls in response to hypoxia, maybe via hydrogen peroxide production. Modulates leaf senescence in insect-infested tissue and triggers a phloem-based defense mechanism including antibiosis (e.g. green peach aphid (GPA), M.persicae) to limit phloem sap uptake and insect growth, thus providing an EDS1-independent basal resistance to insects. Also involved in regulation of root meristematic zone-targeted growth arrest together with EDS1 and in a VICTR-dependent manner. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Can move to the cytoplasm when in complex with EDS1. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.


FUNCTION: Involved in the export and assembly of PMF fimbrial subunits across the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fimbrial export usher family.


FUNCTION: Essential transmembrane GTPase, which mediates mitochondrial fusion during spermatogenesis (PubMed:9230308, PubMed:18799731). In early spermatocytes, fusion of mitochondria give rise to two organelles named Nebenkern and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission (PubMed:9230308, PubMed:18799731). Essential for fertility (PubMed:9230308). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily.


FUNCTION: DNA replication licensing factor, required for pre- replication complex assembly. Cooperates with cdc6 to promote the loading of the mini-chromosome maintenance complex onto chromatin to form the pre-replication complex necessary to initiate DNA replication. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Cdt1 family.


FUNCTION: RNA-dependent RNA polymerase that plays an essential role in the virus replication. SUBCELLULAR LOCATION: Host membrane. SIMILARITY: Belongs to the tombusviridae RNA polymerase family.


FUNCTION: Involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2) (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle lumen. SIMILARITY: Belongs to the glycosyl hydrolase 47 family.


FUNCTION: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere, kinetochore. Note=Localized at the central region, but not at the outer repeats, of the centromere and remains at the centromere during mitosis and meiosis. SIMILARITY: Belongs to the NKP2 family.


FUNCTION: Acts on the G1 phase of the cell cycle to control cell division rate in both shoot and root meristems. The complex formed with CDKA-1 phosphorylates plant retinoblastoma protein. SIMILARITY: Belongs to the cyclin family. Cyclin D subfamily.


FUNCTION: Required for the transposition of the insertion element. SIMILARITY: Belongs to the transposase IS21/IS408/IS1162 family.


FUNCTION: Contributes to the assembly of the acentrosomal spindle and phragmoplast microtubule arrays as part of the augmin complex. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle Cytoplasm, cytoskeleton, phragmoplast Note=Preferentially localizes to microtubules minus ends. SIMILARITY: Belongs to the HAUS6 family.


FUNCTION: Has a role in meiosis. SUBCELLULAR LOCATION: Cytoplasm. Nucleus membrane; Multi-pass membrane protein.


FUNCTION: Required for stress adaptation, morphogenesis and virulence.


FUNCTION: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin- responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Aux/IAA family.


FUNCTION: May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49) family. Rh subfamily.


FUNCTION: Transcriptional activator that binds the same DNA consensus sequence as p53 (PubMed:11696333, PubMed:15242600, PubMed:28560849). Has a role in normal development to ensure proper meiotic chromosome segregation (PubMed:11557844, PubMed:12445383). Promotes apoptosis under conditions of cellular and genotoxic stress in response to DNA damage, hypoxia, or starvation (PubMed:11696333, PubMed:11557844, PubMed:12445383, PubMed:15273685, PubMed:17186023, PubMed:18836529, PubMed:21901106). Regulates germline apoptosis in response to DNA damage (PubMed:11696333, PubMed:15273685, PubMed:15707894, PubMed:16319925, PubMed:17276923, PubMed:17186023, PubMed:17347667, PubMed:19015549, PubMed:26598553). Its pro-apoptotic activity is inhibited when bound to ape-1 in vitro (PubMed:12524540). Plays a role in cell cycle arrest in the germline in response to DNA damage by UV-C light (PubMed:17347667). However, not required for survival in response to DNA damage induced by UV-C light, indicating that it is unlikely to be involved in DNA repair (PubMed:17347667). Required for induction of ced-13 in response to DNA damage (PubMed:15605074). Regulates DNA damage-induced apoptosis by inducing transcription of the programmed cell death activator egl-1 (PubMed:12445383, PubMed:19521535). Regulates germline proliferation by activating phg-1 (PubMed:17186023). Modulates lifespan (PubMed:17895432, PubMed:18836529, PubMed:28560849). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the p53 family.


FUNCTION: Olfactory receptor specific for 2-phenylethylamine, a trace amine present at high concentration in the urine of carnivore species, playing a key role in fear and avoidance responses. 2-phenylethylamine acts as a kairomone in the chemical detection of carnivore odor and triggers fear in mice. This receptor is probably mediated by the G(s)- class of G-proteins which activate adenylate cyclase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Binds medium- and long-chain acyl-CoA esters. SIMILARITY: Belongs to the ACBD7 family.


FUNCTION: Has antibacterial activity against M.luteus and E.coli. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the invertebrate defensin family. Type 2 subfamily.


FUNCTION: Promotes differentiation and/or maintenance of the vascular procambium, the initial cells of the developing vasculature (PubMed:20044450). Part of the TDIF-TDR-WOX4 signaling pathway that plays a crucial role in the maintenance of the vascular meristem organization during secondary growth (PubMed:20729381). Is required for promoting the proliferation of procambial/cambial stem cells but not for repressing their commitment to xylem differentiation in response to the TDIF signal (PubMed:20729381). Acts redundantly with WOX14 downstream of the TDR/PXY receptor kinase to regulate procambial cell proliferation and differentiation in vascular tissue, independently of any role in vascular (PubMed:23578929). Acts as a cambium regulator in the inflorescence stem (PubMed:21926336). Is required for auxin- dependent cambium stimulation in the inflorescence stem (PubMed:21926336). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WUS homeobox family.


SUBCELLULAR LOCATION: Host membrane; Single-pass membrane protein Virion. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1B family.


FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. May play a critical role against oxidative stress, affecting both the survival and the virulence of S.pneumoniae. FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. May play a critical role against oxidative stress, affecting both the survival and the virulence of S.pneumoniae (By similarity). SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.


FUNCTION: Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing, translation regulation, nonsense-mediated mRNA decay, RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC complex is involved in mRNA export from the nucleus, leading to the recruitment of the mRNA export machinery to the 5'-end of mRNA and to mRNA export in a 5' to 3' direction through the nuclear pore. The CBC complex is also involved in mediating U snRNA and intronless mRNAs export from the nucleus. The CBC complex is essential for a pioneer round of mRNA translation, before steady state translation when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer round of mRNA translation mediated by the CBC complex plays a central role in nonsense-mediated mRNA decay (NMD), NMD only taking place in mRNAs bound to the CBC complex, but not on eIF4E-bound mRNAs. The CBC complex enhances NMD in mRNAs containing at least one exon-junction complex (EJC), promoting the interaction between UPF1 and UPF2. The CBC complex is also involved in 'failsafe' NMD, which is independent of the EJC complex, while it does not participate in Staufen-mediated mRNA decay (SMD). During cell proliferation, the CBC complex is also involved in microRNAs (miRNAs) biogenesis via its interaction with SRRT/ARS2 and is required for miRNA-mediated RNA interference. The CBC complex also acts as a negative regulator of parn, thereby acting as an inhibitor of mRNA deadenylation. In the CBC complex, NCBP1/CBP80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high affinity cap-binding state with the cap structure. Associates with NCBP3 to form an alternative cap-binding complex (CBC) which plays a key role in mRNA export. The conventional CBC with NCBP2 binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus whereas the alternative CBC with NCBP3 does not bind snRNA and associates only with mRNA thereby playing a role only in mRNA export (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the NCBP1 family.


FUNCTION: Acts catalytically in the formation of tail protein dimers. SIMILARITY: Belongs to the tfa family.


FUNCTION: Galactose-binding lectin that binds to and agglutinates erythrocytes in a calcium-dependent manner. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the true venom lectin family.


FUNCTION: Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P- TEFb), which facilitates the transition from abortive to production elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II), SUPT5H and RDBP. The CDK9/cyclin-K complex has also a kinase activity toward CTD of RNAP II and can substitute for P-TEFb in vitro (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.


FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.


FUNCTION: Plays a role in the regulation of membrane potential. Could mediate a proton leak (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0057 (PMP3) family.


FUNCTION: Cell surface adhesion protein that plays a key role in virulence by allowing adherence to the insect host surface (PubMed:17337634). Required to orientate the cytoskeleton and stimulate the expression of genes involved in the cell cycle (PubMed:17337634). Is also involved in achieving the septin hourglass shape and subsequent separation of cells (PubMed:17337634). SUBCELLULAR LOCATION: Secreted, cell wall Cell membrane; Lipid-anchor, GPI-anchor Note=Found anchored in the cell membrane as well as a covalently-linked GPI-modified cell wall protein (GPI-CWP) (By similarity). Heterogeneously and randomly distributed within the cell wall structure (PubMed:17337634). SIMILARITY: Belongs to the RBT5 family.


FUNCTION: Major reticulophagy (also called ER-phagy) receptor that acts independently of other candidate reticulophagy receptors to remodel subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover. The ATG8-containing isolation membrane (IM) cradles a tubular segment of TEX264-positive ER near a three-way junction, allowing the formation of a synapse of 2 juxtaposed membranes with trans interaction between the TEX264 and ATG8 proteins. Expansion of the IM would extend the capture of ER, possibly through a 'zipper-like' process involving continued trans TEX264-ATG8 interactions, until poorly understood mechanisms lead to the fission of relevant membranes and, ultimately, autophagosomal membrane closure. Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: acts by bridging VCP/p97 to covalent DNA-protein cross-links (DPCs) and initiating resolution of DPCs by SPRTN. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type III membrane protein Cytoplasmic vesicle, autophagosome Cytoplasm, cytosol Nucleus Chromosome Note=Is trafficked from tubular ER to growing autophagosomes via its cytosolic LIR motif. Also found in the cytosol, nucleus and chromatin. In response to formation of covalent DNA-protein cross-links (DPCs), localizes to the nuclear periphery, and associates with DNA replication forks.


FUNCTION: Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of BMAL1 in the blood vessels. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. NOCT enhances its nuclear translocation (By similarity). SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily.


FUNCTION: May bind amino acids.


FUNCTION: Assembly factor required for Rieske Fe-S protein RIP1 incorporation into the cytochrome b-c1 (CIII) complex. Functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane. Modulates the mitochondrial matrix zinc pool (By similarity). FUNCTION: Assembly factor required for Rieske Fe-S protein RIP1 incorporation into the cytochrome b-c1 (CIII) complex. Functions as a chaperone, binding to this subunit within the mitochondrial matrix and stabilizing it prior to its translocation and insertion into the late CIII dimeric intermediate within the mitochondrial inner membrane. Modulates the mitochondrial matrix zinc pool. SUBCELLULAR LOCATION: Mitochondrion matrix. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the complex I LYR family. MZM1 subfamily.


FUNCTION: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for calcitonin-gene-related peptide (CGRP) together with CALCRL (By similarity). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the RAMP family.


SUBCELLULAR LOCATION: Virion tegument Note=Also found in dense bodies. SIMILARITY: Belongs to the herpesviridae large structural phosphoprotein family.


FUNCTION: Has acyl-CoA thioesterase activity towards medium and long- chain (C14 to C18) fatty acyl-CoA substrates, and probably plays a role in mitochondrial fatty acid metabolism. Plays a role in the apoptotic process, possibly via its regulation of AKT1 activity. According to PubMed:11598301, inhibits AKT1 phosphorylation and activity. According to PubMed:17615157, enhances AKT1 activity by favoring its phosphorylation and translocation to plasma membrane. SUBCELLULAR LOCATION: Cell membrane Cell projection, ruffle membrane Cytoplasm Mitochondrion Mitochondrion inner membrane; Peripheral membrane protein Mitochondrion intermembrane space Note=Released from the mitochondria into the cytosol in response to apoptotic stimuli. SIMILARITY: Belongs to the THEM4/THEM5 thioesterase family.


FUNCTION: Transcriptional coactivator; part of the gene cluster that mediates the biosynthesis of an emodin derivative that may be involved in black Sigatoka disease of banana (PubMed:30735556). With MYCFIDRAFT_198930, coregulates the production of the PKS8-1 cluster product (Probable). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Catalyzes the irreversible beta-carboxylation of phosphoenolpyruvate (PEP) to form oxaloacetate (OAA), a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. SIMILARITY: Belongs to the PEPCase type 2 family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family.


FUNCTION: Involved in the planar cell polarity (PCP) pathway that is essential for the polarization of epithelial cells during morphogenetic processes, including gastrulation and neurulation (By similarity). PCP is maintained by two molecular modules, the global and the core modules (PubMed:23140624). Proteins of the core module include the proteins Frizzled (Fz), Disheveled (Dsh), Van Gogh (Vang), Prickle (Pk), Flamingo (Fmi, Celsr) and Diego (Dgo) (PubMed:23140624). The core module proteins develop subcellular asymmetry, accumulating in two groups on opposite sides of epithelial cells (PubMed:23140624). Distinct proximal (Vang, Pk and Fmi) and distal (Fz, Dsh, Dgo and Fmi) complexes segregate to opposite sides of the cell, where they interact with the opposite complex in the neighboring cell at or near the adherents junctions (PubMed:23140624). Directional information to orient polarization with respect to the tissue axes is provided by the global module which involves Wnt proteins (PubMed:23140624). Involved in the organization of the basal body (By similarity). Involved in cilia growth and positioning (By similarity). Required for proper assembly, stability, and function of mitochondrial membrane ATP synthase (mitochondrial complex V) (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell membrane; Peripheral membrane protein; Cytoplasmic side Mitochondrion Note=Recruited by vangl2 to anterior cell borders. This polarity is controlled by wnt proteins (By similarity). Wtip is involved in the recruitment of prickle3 to the basal body (By similarity). SIMILARITY: Belongs to the prickle / espinas / testin family.


FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. FUNCTION: Is also involved in protein lipoylation via its role as an octanoyl/lipoyl carrier protein intermediate. SIMILARITY: Belongs to the GcvH family.


FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). May play a role in the regulation of the timing of gene expression during the development and in the definition aspects of the phenotype that mediate social behavior in genetically heterogeneous groups. SUBCELLULAR LOCATION: Nucleus Cytoplasm. SIMILARITY: Belongs to the histone deacetylase family. HD type 1 subfamily.


FUNCTION: Required for mRNA export from the nucleus to the cytoplasm. Acts as an adapter that uses the DDX39B/UAP56-NFX1 pathway to ensure efficient mRNA export and delivering to the nuclear pore. Associates with spliced and unspliced mRNAs simultaneously with ALYREF/THOC4 (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Nucleus speckle. SIMILARITY: Belongs to the UIF family.


FUNCTION: Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway (Probable). The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans- signaling'. Alternatively, 'cluster signaling' occurs when membrane- bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells (Probable). FUNCTION: IL6 is a potent inducer of the acute phase response. Rapid production of IL6 contributes to host defense during infection and tissue injury, but excessive IL6 synthesis is involved in disease pathology. In the innate immune response, is synthesized by myeloid cells, such as macrophages and dendritic cells, upon recognition of pathogens through toll-like receptors (TLRs) at the site of infection or tissue injury (Probable). In the adaptive immune response, is required for the differentiation of B cells into immunoglobulin- secreting cells. Plays a major role in the differentiation of CD4(+) T cell subsets. Essential factor for the development of T follicular helper (Tfh) cells that are required for the induction of germinal- center formation. Required to drive naive CD4(+) T cells to the Th17 lineage. Also required for proliferation of myeloma cells and the survival of plasmablast cells (By similarity). FUNCTION: Acts as an essential factor in bone homeostasis and on vessels directly or indirectly by induction of VEGF, resulting in increased angiogenesis activity and vascular permeability (PubMed:17075861, PubMed:12794819). Induces, through 'trans-signaling' and synergistically with IL1B and TNF, the production of VEGF (PubMed:12794819). Involved in metabolic controls, is discharged into the bloodstream after muscle contraction increasing lipolysis and improving insulin resistance (PubMed:20823453). 'Trans-signaling' in central nervous system also regulates energy and glucose homeostasis (By similarity). Mediates, through GLP-1, crosstalk between insulin- sensitive tissues, intestinal L cells and pancreatic islets to adapt to changes in insulin demand (By similarity). Also acts as a myokine (Probable). Plays a protective role during liver injury, being required for maintenance of tissue regeneration (By similarity). Also has a pivotal role in iron metabolism by regulating HAMP/hepcidin expression upon inflammation or bacterial infection (PubMed:15124018). Through activation of IL6ST-YAP-NOTCH pathway, induces inflammation-induced epithelial regeneration (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-6 superfamily.


FUNCTION: Epoxide hydrolase; part of the asc-2 gene cluster that mediates the biosynthesis of ascofuranone, a strong inhibitor of cyanide-insensitive alternative oxidases and a promising drug candidate against African trypanosomiasis (PubMed:30952781, PubMed:35418536). The first step in the pathway is performed by the non-reducing polyketide synthase ascC that produces orsellinic acid by condensing acetyl-CoA with 3 malonyl-CoA units (PubMed:30952781, PubMed:35418536). Orsellinic acid is then prenylated by the prenyltransferase ascA to yield ilicicolinic acid B (PubMed:30952781, PubMed:35418536). Ilicicolinic acid B is further reduced to ilicicolin B by the reductase ascB (PubMed:30952781, PubMed:35418536). The halogenase ascD then chlorinates ilicicolin B to produce ilicicolin A which is converted to ilicicolin A epoxide by the cytochrome P450 monooxygenase ascE that catalyzes stereoselective epoxidation of the terminal double bond of the prenyl group (PubMed:30952781, PubMed:35418536). Ilicicolin A epoxide is the last common precursor for the biosynthesis of ascofuranone and ascochlorin (PubMed:30952781, PubMed:35418536). The terpene cyclase ascF produces a monocyclic terpene, and the cyclization reaction is proposed to be initiated by protonation of the terminal epoxide of ilicicolin A epoxide to generate a monocyclic tertiarycation, which is followed by a series of hydride and methyl shifts with abstraction of proton, leading to the formation of the (14S,15R,19R)-trimethylcyclohexanone ring structure of ilicicolin C, which is finally reduced to ascochlorin by the dehydrogenase ascG (PubMed:30952781). On the other hand, ilicicolin A epoxide is hydroxylated by the cytochrome P450 monooxygenase ascH, and the resultant product is cyclized by the terpene cyclase ascI to ascofuranol via protonation-initiated epoxide ring opening, which facilitates the 6-endo-tet cyclization to form the tetrahy-drofuran ring (PubMed:30952781). Finally, ascofuranol is oxidized into ascofuranone by ascJ (PubMed:30952781, PubMed:35418536). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the membrane-bound ascI terpene cyclase family.


FUNCTION: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (By similarity). Dispensable for SPC enzymatic activity (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SPCS1 family.


FUNCTION: Required for cytoplasmic lattice formation, thereby modulates the distribution of organelles during oocyte maturation and zygote development (PubMed:31575650). Required for preimplantation development in female fertility (PubMed:31575650). May be involved in inflammation and recognition of cytosolic pathogen-associated molecular patterns (PAMPs) not intercepted by membrane-bound receptors (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Expressed and colocalizes with NLRP5 at the oocyte subcortex. SIMILARITY: Belongs to the NLRP family.


FUNCTION: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme. SIMILARITY: Belongs to the DRC10 family.


FUNCTION: Photoreceptor implicated in non-image-forming responses to light. May be able to isomerize covalently bound all-trans retinal back to 11-cis retinal (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.


FUNCTION: inhibits Kv1.3/KCNA3 channel (1 uM of the toxin inhibits currents by 64.1%). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium channel inhibitor family. Alpha-KTx 30 subfamily.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL2 family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the radical SAM superfamily. RlmN family.


FUNCTION: May play a role in cell differentiation, proliferation and apoptosis. Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator of disk morphogenesis (PubMed:19228982). Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner. SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. Cell projection, microvillus membrane; Multi-pass membrane protein. Cell projection, cilium, photoreceptor outer segment. Endoplasmic reticulum Endoplasmic reticulum-Golgi intermediate compartment Note=Found in extracellular membrane particles in various body fluids such as ventricular fluid of the developing brain and urine. SIMILARITY: Belongs to the prominin family.


FUNCTION: RNA-binding factor involved in multiple aspects of cellular processes like alternative splicing of pre-mRNA and translation regulation. Modulates alternative 5'-splice site and exon selection. Acts as a muscle cell differentiation-promoting factor. Activates exon skipping of the PTB pre-mRNA during muscle cell differentiation. Antagonizes the activity of the splicing factor PTBP1 to modulate muscle cell-specific exon selection of alpha tropomyosin. Binds to intronic pyrimidine-rich sequence of the TPM1 and MAPT pre-mRNAs. Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA. Exerts a suppressive activity on Cap-dependent translation via binding to CU- rich responsive elements within the 3'UTR of mRNAs, a process increased under stress conditions or during myocytes differentiation. Recruits EIF4A1 to stimulate IRES-dependent translation initiation in respons to cellular stress. Associates to internal ribosome entry segment (IRES) in target mRNA species under stress conditions. Plays a role for miRNA- guided RNA cleavage and translation suppression by promoting association of AGO2-containing miRNPs with their cognate target mRNAs. Associates with miRNAs during muscle cell differentiation. Binds preferentially to 5'-CGCGCG[GCA]-3' motif in vitro (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Nucleus speckle Cytoplasm Cytoplasmic granule Note=Undergoes continuous nucleocytoplasmic shuttling. Upon nuclear import colocalizes with SR proteins in nuclear speckles. Arsenite stress-induced phosphorylation increases its subcellular relocalization from the nucleus to the cytoplasm and to cytoplasmic stress granules (SG) via a p38 MAPK signaling pathway. Primarily localized in nucleus and nucleoli under cell growth conditions and accumulated in the cytoplasm and cytoplasm perinuclear granules upon muscle cell differentiation (By similarity).


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 19 (CSTX) family. 04 (U1-Lctx) subfamily.


FUNCTION: A terminal oxidase that catalyzes quinol-dependent, Na(+)- independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested (PubMed:8626304). Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 2 family.


FUNCTION: PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro. SUBCELLULAR LOCATION: Cytoplasm Nucleus Endosome Cell membrane; Peripheral membrane protein Cleavage furrow Midbody Note=Associates with chromatin in a ligand-dependent manner. Localization to endosomes is mediated via its interaction with RHOB. Association to the cell membrane is dependent on Ser-377 phosphorylation. Accumulates during telophase at the cleavage furrow and finally concentrates around the midbody in cytokinesis. SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ST7 family.


FUNCTION: Involved in the biosynthesis of carbapenam-3-carboxylate, a beta-lactam antibiotic of the carbapenem class. Catalyzes the ATP- dependent formation of (3S,5S)-carbapenam-3-carboxylate from (2S,5S)-5- carboxymethylproline.


FUNCTION: Catalyzes the formation of the isocyclic ring in chlorophyll biosynthesis. Mediates the cyclase reaction, which results in the formation of divinylprotochlorophyllide (Pchlide) characteristic of all chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester (MgPMME). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the AcsF family.


FUNCTION: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs). Binds an AT-rich DNA sequences in the FLOWERING LOCUS T (FT) promoter (PubMed:22442143). Acts redundantly with AHL18, AHL27 and AHL29 in the regulation of flowering and regulation of the hypocotyl elongation. Plays a role in both photo- and skotomorphogenesis (PubMed:19517252). Acts as a chromatin remodeling factor that modifies the architecture of FLOWERING LOCUS T (FT) chromatin by modulating both H3 acetylation and methylation leading to the regulation of FT expression during flowering induction (PubMed:22442143). SUBCELLULAR LOCATION: Nucleus.