FUNCTION: Interferon-inducible antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon. Catalyzes the conversion of cytidine triphosphate (CTP) to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP) via a SAM-dependent radical mechanism. In turn, ddhCTP acts as a chain terminator for the RNA- dependent RNA polymerases from multiple viruses and directly inhibits viral replication. Therefore, inhibits a wide range of DNA and RNA viruses (PubMed:32719955, PubMed:31517388). Promotes also TLR7 and TLR9-dependent production of IFN-beta production in plasmacytoid dendritic cells (pDCs) by facilitating 'Lys-63'-linked ubiquitination of IRAK1 by TRAF6. Plays a role in CD4+ T-cells activation and differentiation. Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB activities. Can inhibit secretion of soluble proteins (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Golgi apparatus Endoplasmic reticulum Lipid droplet Mitochondrion Mitochondrion inner membrane Mitochondrion outer membrane. SIMILARITY: Belongs to the radical SAM superfamily. RSAD2 family.


FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth. Together with TBC1D13 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes. FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth. Together with TBC1D13 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes (By similarity). FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth. Together with TBC1D13 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Membrane, clathrin-coated pit Cytoplasmic vesicle, clathrin-coated vesicle Endosome Melanosome Note=Present on sorting endosomes and recycling endosome tubules (PubMed:16950109). Tends to be enriched in PIP2-positive cell membrane domains (PubMed:16950109). During mitosis, associated with the plasma membrane and present at the ingressing furrow during early cytokinesis as well as at the intercellular bridge later during cytokinesis (PubMed:16950109). Identified in stage I to stage IV melanosomes (PubMed:17081065). SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Membrane, clathrin-coated pit Cytoplasmic vesicle, clathrin-coated vesicle Endosome Melanosome Note=Present on sorting endosomes and recycling endosome tubules. Tends to be enriched in PIP2-positive cell membrane domains. During mitosis, associated with the plasma membrane and present at the ingressing furrow during early cytokinesis as well as at the intercellular bridge later during cytokinesis. Identified in stage I to stage IV melanosomes. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Membrane, clathrin-coated pit Cytoplasmic vesicle, clathrin-coated vesicle Endosome Melanosome Note=Present on sorting endosomes and recycling endosome tubules. Tends to be enriched in PIP2-positive cell membrane domains. During mitosis, associated with the plasma membrane and present at the ingressing furrow during early cytokinesis as well as at the intercellular bridge later during cytokinesis. Identified in stage I to stage IV melanosomes. SIMILARITY: Belongs to the small GTPase superfamily. Rab family.


FUNCTION: Catalyzes the last irreversible step in the biosynthesis of L-serine from carbohydrates, the dephosphorylation of O-phospho-L- serine to L-serine. L-serine can then be used in protein synthesis, to produce other amino acids, in nucleotide metabolism or in glutathione synthesis, or can be racemized to D-serine, a neuromodulator. May also act on O-phospho-D-serine. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. SerB family.


FUNCTION: Probable component of a transcriptional corepressor complex that acts specifically in the karrikin pathway (PubMed:26754282). Controls seedling growth redundantly with SMAX1, but is not involved in leaf morphology, shoot branching or germination control (PubMed:26754282). SIMILARITY: Belongs to the ClpA/ClpB family.


FUNCTION: Plays a role in regulating magnetite crystal size (PubMed:17965152). The lumenal domain may bind the magnetite crystals, affecting crystal size and shape (By similarity). SUBCELLULAR LOCATION: Magnetosome membrane; Multi-pass membrane protein Note=Purified magnetosomes remain attached to each other (PubMed:11571158). Resistant to trypsin digestion in isolated magnetosomes (PubMed:14766587). Localizes as a filament-like structure in a straight line running through the center of the cell, in a position that corresponds to magnetosomes (PubMed:18539817, PubMed:22007638). SIMILARITY: Belongs to the magnetosome MamC family.


FUNCTION: Stabilizes the structure of photosystem II oxygen-evolving complex (OEC), the ion environment of oxygen evolution and protects the OEC against heat-induced inactivation. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Lumenal side Note=Associated with photosystem II at the lumenal side of the thylakoid membrane. SIMILARITY: Belongs to the PsbU family.


FUNCTION: Functions as a negative regulator of actin polymerization. Modulates actin/myosin II at cortex actinomyosins to prevent excessive F-actin polymerization around the cell periphery, thereby maintaining proper cell shape during phagocytosis and chemotaxis.


FUNCTION: Involved in the induction of apoptosis, through both caspase- dependent and caspase-independent pathways. May act as a Ras effector protein. May suppress the serum-induced basal levels of NF-kappa-B (By similarity).


FUNCTION: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. FUNCTION: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. Has a preference for oxidized pyrimidines, such as thymine glycol (prefers 5S isomers) 5,6-dihydrouracil:G, 5-hydroxyuracil:G, 5- hydroxycytosine:G and urea:A. Cleaves ssDNA containing an AP site. SIMILARITY: Belongs to the Nth/MutY family.


FUNCTION: Negative regulator of the carB operon in the dark. Binds specifically to the CarA operator, in the region around the carB promoter, which blocks access to the RNA polymerase. SIMILARITY: Belongs to the CarA/CarH B12-binding photoregulator family.


FUNCTION: Transcriptional repressor that plays a role in various developmental processes. Specifically binds the consensus DNA sequence 5'-[AC]ACATCTG[GT][AC]-3' which contains the E box core, and acts by recruiting chromatin remodeling multiprotein complexes (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family. ZBTB18 subfamily.


FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.


FUNCTION: Potential protease involved in virion morphogenesis. SIMILARITY: Belongs to the peptidase U35 family.


FUNCTION: Antimicrobial peptide active against fungi, Gram-positive and Gram-negative bacteria. Inhibits growth of hyphae in the fungi A.niger (IC(50)=3.5 ug/ml), B.sorokiniana (IC(50)=3.0 ug/ml), F.oxysporum (IC(50)=9.5 ug/ml), F.graminearum (IC(50)=6.9 ug/ml), F.culmorum (IC(50)=6.9 ug/ml) and B.cinerea (IC(50)=27.4 ug/ml). Has no effect on spore germination. Destroys spores in germinated conidia by disruption of cell walls and membranes in A.niger and B.sorokiniana. Causes vacuolization of germinated macro- and microconidia in F.oxysporum, F.graminearum and F.culmorum. Strongly inhibits growth of P.infestans on potato tubers above concentrations of 13.6 ug/ml. Inhibits growth of Gram-positive bacteria C.michiganensis and B.subtilis and of Gram- negative bacteria P.syringae, E.carotovora and E.coli. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the DEFL family.


FUNCTION: Mitochondrial S-adenosyl-L-methionine/S-adenosyl-L- homocysteine antiporter. Mediates the exchange of cytosolic S-adenosyl- L-methionine, the predominant methyl-group donor for macromolecule methylation processes, for mitochondrial S-adenosylhomocysteine(SAH), a by-product of methylation reactions. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.


FUNCTION: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the binding-protein-dependent transport system permease family. CysTW subfamily.


FUNCTION: Component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. Controls particularly membrane and organelle development genes. SUBCELLULAR LOCATION: Nucleus Note=Localizes to centromeric and flanking chromatin. SIMILARITY: Belongs to the RSC1 family.


SIMILARITY: Belongs to the UPF0200 family.


FUNCTION: Involved in cytokinesis and septation where it has a role in the localization of F-actin. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.


FUNCTION: Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. AstC subfamily.


FUNCTION: Catalyzes the reduction of phosphonoacetaldehyde to 2- hydroxyethylphosphonate, a step in the biosynthesis of phosphinothricin tripeptide. Phosphinothricin tripeptide is both a natural-product antibiotic and potent herbicide. Can use both NAD and NADP but the preferred substrate is NAD. SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase family.


FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used during anaerobic growth, and succinate dehydrogenase is used during aerobic growth. The QFR enzyme complex binds 2 quinones in or near the membrane; 1 near the [3Fe-4S] cluster (QP is proximal to the [3Fe-4S] cluster, on the cytoplasmic side of the membrane) while QD (the distal cluster) is on the other side of the membrane. It is not clear if both of the quinol- binding sites are functionally relevant (PubMed:10373108, PubMed:11850430). SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.


FUNCTION: Repressor of translation initiation that regulates eIF4E1 activity by preventing its assembly into the eIF4F complex (PubMed:11389445, PubMed:19804760, PubMed:25702871). Hypophosphorylated form competes with eIF4G1 and strongly binds to eIF4E1, leading to repress translation (PubMed:25702871). In contrast, hyperphosphorylated form dissociates from eIF4E1, allowing interaction between eIF4G1 and eIF4E1, leading to initiation of translation (PubMed:25702871). Acts as a regulator of various biological processes, such as innate immunity, cell growth or synaptic transmission (PubMed:10811906, PubMed:11389445, PubMed:27525480). Acts downstream of phosphoinositide-3-kinase (PI3K) to regulate cell growth (PubMed:11389445). Extends lifespan upon dietary restriction by regulating the mitochondrial translation (PubMed:19804760). Acts as a regulator of lifespan in response to cold by regulating the mitochondrial translation (PubMed:28827349). Acts as a negative regulator of presynaptic release of neurotransmitter in motor neurons: Thor expression is induced in response to insulin signaling, leading to prevent of translation of complexin (cpx), a protein known to regulate the exocytosis of synaptic vesicles (PubMed:27525480). Acts as a negative regulator of synaptic strength at the neuromuscular junction: Thor expression in response to acute fasting prevents translation, thereby suppressing retrograde synaptic enhancement (PubMed:27916456). SIMILARITY: Belongs to the eIF4E-binding protein family.


SIMILARITY: Belongs to the isochorismatase family.


FUNCTION: Major component of the virion core that undergoes proteolytic processing during the immature virion (IV) to mature virion (MV) transition. Essential for the formation of a structurally normal core. SUBCELLULAR LOCATION: Virion Note=Localizes to the virion core wall, the mature protein accounts for 11% of the dry mass of the virion. SIMILARITY: Belongs to the orthopoxvirus OPG129 family.


FUNCTION: Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptidoglycans. Host outer membrane disruption is possibly due to local fusion between the inner and outer membrane performed by the spanin complex (By similarity). SUBCELLULAR LOCATION: Host cell outer membrane; Lipid- anchor; Periplasmic side.


FUNCTION: Tyrosine phosphatase thought to play a role in transcription regulation during organogenesis through its intrinsic protein phosphatase activity (PubMed:14628052, PubMed:14628053). The phosphatase activity was shown in vitro. Appears to function together with So and Dac in eye development (PubMed:9428512, PubMed:9428513). Required for the survival of eye progenitor cells at a critical stage in morphogenesis (PubMed:8431945). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HAD-like hydrolase superfamily. EYA family.


FUNCTION: Plays a role as an inducible effector molecule that mediates Fas resistance produced by surface Ig engagement in B cells. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FAIM1 family.


FUNCTION: Member of the two-component regulatory system GlrR/GlrK that up-regulates transcription of the glmY sRNA when cells enter the stationary growth phase. Activates GlrR by phosphorylation. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.


FUNCTION: Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the transglycosylase Slt family.


FUNCTION: Involved in cell wall metabolism and required for the separation of the mother and daughter cells. SIMILARITY: Belongs to the WD repeat DSE1 family.


FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side. Note=Forms the periphery of the phycobilisome rod. SIMILARITY: Belongs to the phycobiliprotein family.


FUNCTION: Zinc finger protein that functions as a cofactor for steroid hormone receptors, such as NR3C1/GR (PubMed:28139699). Directs NR3C1/GR transcriptional activity toward specific biologic pathways by changing NR3C1/GR binding and transcriptional activity on the glucocorticoid- responsive genes (PubMed:28139699). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.


FUNCTION: MFS-type transporter; part of the gene cluster that mediates the biosynthesis of calbistrin A and related compounds. Calbistrin A is a secondary metabolite with an interesting structure that was recently found to have bioactivity against leukemia cells. It consists of two polyketides linked by an ester bond: a bicyclic decalin containing polyketide and a linear 12 carbon dioic acid structure (PubMed:30598828). Required for the secretion of calbistrin A and calbistrin C, as well as of related compounds decumbenone A, B and C (PubMed:30598828). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet family.


FUNCTION: Probable serine protease inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the protease inhibitor I19 family.


FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATPase B chain family.


FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long subfamily.


FUNCTION: General regulator of phagocytosis. Required to uptake Gram negative bacterium by macrophages. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein Golgi apparatus Mitochondrion.


FUNCTION: Possibly acts as a regulatory protein and not as a calcium buffer or transport protein.


FUNCTION: Has a role in spermatogenesis and oogenesis. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the cueball family.


FUNCTION: Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks with regressed leading strands and nicked Holliday junctions. Cleavage probably occurs approximately half a helical turn upstream of the free 5'-end in these structures. May be required in mitosis for the processing of stalled replication fork intermediates arising spontaneously or subsequent to treatment with DNA damaging agents such as methylmethane sulfonate (MMS), camptothecin (CPT) or UV. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI). This involves consecutive cleavage of D-loops and nicked Holliday junctions leading to sister chromatid crossover. In contrast to MSH4-MSH5 dependent crossover, double Holliday junctions do not seem to be involved. Spore formation and viability are severely impaired in deletion strains. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the EME1/MMS4 family.


SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.


FUNCTION: Microtubule-dependent motor that is involved in microtubule organization in the mitotic spindle. SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. NCD subfamily.


FUNCTION: Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds. SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.


FUNCTION: Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ERD2 family.


SIMILARITY: Belongs to the peptidase M4 family.


FUNCTION: Centrosomal protein which may be required for microtubule attachment to centrosomes. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. SIMILARITY: Belongs to the translokin family.


FUNCTION: Mitochondrial aminoacyl-tRNA synthetase that catalyzes the ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (His-AMP). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.


FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system; overexpression in wild-type temporarily inhibits cell growth, overexpression in a hipAB deletion leads to acute growth inhibition. The toxic effect of HipA is neutralized by its cognate antitoxin HipB. In the ternary phosphoserine-HipA-HipB-DNA complex the DNA is bent about 125 degrees; all HipA in the crystallized ternary complex is phosphorylated. In E.coli phosphorylation of HipA is thought to release HipB from the HipA-HipB-DNA complex, suggesting the complex functions differently in the 2 bacteria (PubMed:25056321). Phosphorylates Glu- tRNA-ligase (GltX, on 'Ser-239') in vivo, with HipB probably acts as a corepressor for transcription of the hipBA promoter (By similarity). SIMILARITY: Belongs to the HipA Ser/Thr kinase family.


FUNCTION: Involved in the 3'-end formation of mRNA precursors (pre- mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length. Increases the affinity of poly(A) polymerase for RNA. Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between the nucleus and the cytoplasm but predominantly found in the nucleus.


FUNCTION: Has alpha-ketoglutarate-dependent dioxygenase activity. Does not show detectable activity towards fatty acid CoA thioesters. Is not expected to be active with phytanoyl CoA (By similarity). SIMILARITY: Belongs to the PhyH family. PHYHD1 subfamily.


FUNCTION: May play a role in the development of the central system. SIMILARITY: Belongs to the PHYHIP family.


FUNCTION: Plays a dual, essential role in magnetosome formation; required for magnetosome vesicle formation as well as biomineralization (PubMed:20212111) (Probable). Probably binds and transports iron (By similarity). Requires heterodimerization with MamM for stability (By similarity). SUBCELLULAR LOCATION: Magnetosome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family.


FUNCTION: Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Mediates the cis and medial Golgi localization of mannosyltransferases through direct binding of their cytosolic domains. Involved in vacuolar protein sorting (By similarity). SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Peripheral membrane protein; Cytoplasmic side Note=Phosphatidylinositol 4-phosphate-binding and oligomerization participate in the recruitment onto Golgi membranes. SIMILARITY: Belongs to the GOLPH3/VPS74 family.


FUNCTION: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA in the 40S particle. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family.


FUNCTION: Probable transcription factor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the NK-2 homeobox family.


SIMILARITY: Belongs to the costars family.


FUNCTION: Component of the ska-1 complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. Required for timely anaphase onset during mitosis, when chromosomes undergo bipolar attachment on spindle microtubules leading to silencing of the spindle checkpoint. The ska-1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. Affinity for microtubules is synergistically enhanced in the presence of the ndc-80 complex and may allow the ndc-80 complex to track depolymerizing microtubules. In the complex, it mediates the interaction with microtubules. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle Chromosome, centromere, kinetochore. SIMILARITY: Belongs to the SKA1 family.


SIMILARITY: Belongs to the asfivirus I267L family.


FUNCTION: Hydrolyzes alpha-ketoglutaramate (a-KGM) to alpha- ketoglutarate (alpha-KG) and ammonia (specific activity 21 umol/min/mg), has very weak activity on L-glutamine, and no activity on deaminated glutathione (dGSH) or glutathione. May function as a metabolite repair enzyme. SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family.


FUNCTION: With S4 and S5 plays an important role in translational accuracy. FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit (By similarity). FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit. FUNCTION: With S4 and S5 plays an important role in translational accuracy. SIMILARITY: Belongs to the universal ribosomal protein uS12 family. SIMILARITY: Belongs to the universal ribosomal protein uS12 family.


FUNCTION: Involved in the formation of nucleus-vacuole (NV) junctions during piecemeal microautophagy of the nucleus (PMN). NV junctions are interorganelle interfaces mediated by NVJ1 in the nuclear envelope and VAC8 on the vacuole membrane. Together, NVJ1 and VAC8 form Velcro-like patches through which teardrop-like portions of the nucleus are pinched off into the vacuolar lumen and degraded by the PMN process. Acts also as an outer-nuclear membrane receptor for OSH1 and TSC13 (By similarity). SUBCELLULAR LOCATION: Nucleus outer membrane; Single-pass membrane protein.


SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily.


FUNCTION: Palmitoyl acyltransferase. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase subfamily.


FUNCTION: Snake venom phospholipase A2 (PLA2) that lacks enzymatic activity. Displays myotoxic activities (By similarity). A model of myotoxic mechanism has been proposed: an apo Lys49-PLA2 is activated by the entrance of a hydrophobic molecule (e.g. fatty acid) at the hydrophobic channel of the protein leading to a reorientation of a monomer (By similarity). This reorientation causes a transition between 'inactive' to 'active' states, causing alignment of C-terminal and membrane-docking sites (MDoS) side-by-side and putting the membrane- disruption sites (MDiS) in the same plane, exposed to solvent and in a symmetric position for both monomers (By similarity). The MDoS region stabilizes the toxin on membrane by the interaction of charged residues with phospholipid head groups (By similarity). Subsequently, the MDiS region destabilizes the membrane with penetration of hydrophobic residues (By similarity). This insertion causes a disorganization of the membrane, allowing an uncontrolled influx of ions (i.e. calcium and sodium), and eventually triggering irreversible intracellular alterations and cell death (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily. K49 sub-subfamily.


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


FUNCTION: Catalyzes the first step of the osmoprotectant glycine betaine synthesis. SUBCELLULAR LOCATION: Plastid, chloroplast stroma. SIMILARITY: Belongs to the choline monooxygenase family.


FUNCTION: Plays a role in the recycling mechanism in neurons of multiple receptors, including AMPAR, APP and L1CAM and acts at the level of early endosomes to promote sorting of receptors toward a recycling pathway (PubMed:18299352, PubMed:15911354). Regulates sorting and recycling of GRIA2 through interaction with GRIP1 and then contributes to the regulation of synaptic transmission and plasticity by affecting the recycling and targeting of AMPA receptors to the synapse (PubMed:15911354). Is required for faithful sorting of L1CAM to axons by facilitating trafficking from somatodendritic early endosome or the recycling endosome (PubMed:18299352). In an other hand, induces apoptosis via the activation of CASP3 in response to DNA damage (By similarity). SUBCELLULAR LOCATION: Membrane; Single- pass type II membrane protein Golgi apparatus, trans-Golgi network membrane Endosome membrane Cell projection, dendrite Early endosome membrane Late endosome membrane Lysosome lumen Recycling endosome membrane Cytoplasmic vesicle membrane Golgi apparatus, Golgi stack membrane Endosome, multivesicular body membrane Endoplasmic reticulum membrane Note=Endocytosed from the cell surface, thus enters into early endosomes, trafficks to late endosomes and degradates in lysosomes (PubMed:28874679). Endoplasmic reticulum targeting is essential for apoptosis (By similarity). Found in both stationary and motile endosomes. A previous study supports a type I membrane protein topology (By similarity). SIMILARITY: Belongs to the NSG family.


FUNCTION: Essential regulatory subunit of the mitochondrial calcium uniporter complex (uniplex), a complex that mediates calcium uptake into mitochondria. Plays a central role in regulating the uniplex complex response to intracellular calcium signaling. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SMDT1/EMRE family.


FUNCTION: Heavy-metal-binding protein. SIMILARITY: Belongs to the HIPP family.


FUNCTION: Predominantly fucosylates the innermost N-acetyl glucosamine (GlcNAc) residue in biantennary N-glycan acceptors. Postulated to generate core alpha(1->3)-fucose epitope within the chitobiose unit of biantennary N-glycans, providing for a recognition signal to reorient aberrantly folded glycoproteins for degradation (By similarity). Involved in biosynthesis of Lewis X-carrying biantennary N-glycans that regulate neuron stem cell self-renewal during brain development (PubMed:23986452). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 10 family.


FUNCTION: Major facilitator-type transporter, part of the hnx cluster involved in the purine degradation (PubMed:29212709). The nicotinate hydroxylase hnxS accepts nicotinate as a substrate and catalyzes the first step of nicotinate catabolism (PubMed:29212709). The major facilitator-type transporters hxnP and hxnZ are probably involved in the uptake of nicotinate-derived metabolites, and the oxidoreductases hxnT and hxnY in the further metabolism of 6-OH nicotinic acid (PubMed:29212709). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily.


FUNCTION: Plays a role in processing of mitochondrial RNA precursors and in stabilization of a subset of mature mitochondrial RNA species, such as MT-CO1, MT-CO2, MT-CYB, MT-CO3, MT-ND3, MT-ND5 and MT-ATP8/6. May play a role in cell cycle progression. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the FAST kinase family.


FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. These substrates include FILIP1, p53/TP53, CDKN1A and TERT. Keeps cells alive by suppressing p53/TP53 under normal conditions, but stimulates apoptosis by repressing CDKN1A under stress conditions. Acts as a negative regulator of telomerase. Has negative and positive effects on RNA polymerase II- dependent transcription.


FUNCTION: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and in RNA transcription by RNA polymerase II (By similarity). In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment (By similarity). In transcription, TFIIH has an essential role in transcription initiation (By similarity). When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape (By similarity). Necessary for the stability of the TFIIH complex and for the presence of normal levels of TFIIH in the cell (PubMed:34824371). Required for efficient binding of TFIIH to damaged DNA (PubMed:34824371). Dispensable for normal development, but required when transcription is challenged (PubMed:34824371). SUBCELLULAR LOCATION: Nucleus Chromosome Note=Localized to paired homologous chromosomes (bivalents) about 10 minutes after UV irradiation, but localization is lost after 35 minutes, probably as a result of successful DNA damage repair as part of the TFIIH complex. SIMILARITY: Belongs to the TFB5 family.


FUNCTION: Microtubule-binding protein that negatively regulates centriole duplication. Binds to and stabilizes microtubules. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Note=Localizes to the centriole lumen. SIMILARITY: Belongs to the MDM1 family.


FUNCTION: Plays a crucial role in the maintenance of the structure of mitochondrial cristae and the proper assembly of the mitochondrial respiratory chain complexes. Required for the assembly of TOMM40 into the TOM complex. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein Cytoplasm Mitochondrion. SIMILARITY: Belongs to the SAM50/omp85 family.


FUNCTION: Part of the H1 type VI secretion system (H1-T6SS) specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection (PubMed:21325275, PubMed:24794869). Forms the spike at the tip of the elongating tube formed by haemolysin co-regulated protein 1/Hcp1 (PubMed:26894531). Allows the delivery of the Tse6 toxin to target cells where it exerts its toxicity (PubMed:30177742). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the VgrG protein family.


FUNCTION: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ16 may be involved in the regulation of fluid and pH balance (By similarity). In the kidney, together with KCNJ10, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules. SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein Basolateral cell membrane Note=In kidney distal convoluted tubules, located in the basolateral membrane in the presence of KCNJ10. SIMILARITY: Belongs to the inward rectifier-type potassium channel (TC 1.A.2.1) family. KCNJ16 subfamily.


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


FUNCTION: Lipoamide dehydrogenase is an essential component of the pyruvate dehydrogenase (PDH) and 2-oxoglutarate dehydrogenase (ODH) complexes. Catalyzes the reoxidation of dihydrolipoyl groups which are covalently attached to the lipoate acyltransferase components (E2) of the complexes. Also catalyzes a reversible NADH:NAD(+) transhydrogenation, and is able to transfer electrons from NADH to various redox-active compounds and quinones. May be involved in quinone redox cycling in C.glutamicum. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.


FUNCTION: Component of the DNA-directed RNA polymerase (RNAP) that catalyzes the transcription in the cytoplasm of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Host cytoplasm. SIMILARITY: Belongs to the archaeal RpoN/eukaryotic RPB10 RNA polymerase subunit family.


FUNCTION: Forms a polymeric layer at the periphery of the spindle pole body (SPB) central plaque which has an essential function during SPB duplication and may facilitate attachment of the SPB to the nuclear membrane. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. SIMILARITY: Belongs to the SPC42 family.


FUNCTION: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Catalyzes Na(+) transport, most probably coupled to electron transfer from reduced ferredoxin to methanophenazine and heterodisulfide reductase. Involved in heterodisulfide reduction during methanogenesis from acetate. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily.


FUNCTION: Part of a complex that provides reducing equivalents for heterodisulfide reductase. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family.


FUNCTION: Involved in pre-mRNA splicing and cell cycle control. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CEF1 family.


FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to the formation of s(2)U34, the first step of tRNA-mnm(5)s(2)U34 synthesis. Sulfur is provided by IscS, via a sulfur-relay system. Binds ATP and its substrate tRNAs. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MnmA/TRMU family.


FUNCTION: Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements (PubMed:11809897, PubMed:22570490, PubMed:24164894, PubMed:25623890, PubMed:26051023). Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts (PubMed:2687284). Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter (PubMed:11809897). As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPK and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (PubMed:33174841). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Cytoplasm Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. These granules are not identical with P bodies or stress granules.


FUNCTION: Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity). SIMILARITY: Belongs to the ferritin family.


FUNCTION: Involved in GDP-mannose biosynthesis which serves as the activated sugar nucleotide precursor for mannose residues in cell surface polysaccharides. This enzyme participates in synthesis of the LPS O antigen. SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 2 family.


FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non- coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. RNA polymerases are composed of mobile elements that move relative to each other. In Pol II, RPB6 is part of the clamp element and together with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family.


FUNCTION: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis- acting element (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the WRKY group II-e family.


FUNCTION: Has a calcium-dependent calmodulin-binding activity. SIMILARITY: Belongs to the heat shock protein 70 family.


FUNCTION: IMP-specific 5'-nucleotidase involved in IMP (inositol monophosphate) degradation. SIMILARITY: Belongs to the ISN1 family.


FUNCTION: Required for the synthesis of the quorum-sensing autoinducer CAI-1 ((S)-3-hydroxytridecan-4-one) which probably functions as an intragenus signal. SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.


FUNCTION: Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 'phage' integrase family.


FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1 subfamily.


FUNCTION: Enhances the promotion of guanine-nucleotide exchange by PSCD2 on ARF6 in a concentration-dependent manner. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Translocated with PSCD2 to the plasma membrane upon epidermal growth factor (EGF) stimulation.


SIMILARITY: Belongs to the WD repeat WDR53 family.


FUNCTION: Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.


FUNCTION: Part of the operon norEFCBQD encoding nitric oxide reductase. Essential virulence factor, probably involved in the detoxification of nitric oxide (NO) produced in the macrophages during the innate response against infection (By similarity).


FUNCTION: Chromatin-associated factor that regulates transcription (PubMed:29065309). Regulates Pol I-mediated rRNA biogenesis and, probably, Pol III-mediated transcription (PubMed:29065309). Regulates the epigenetic status of rDNA (PubMed:29065309). SUBCELLULAR LOCATION: Nucleus Nucleus, nucleolus Chromosome Note=Associates with chromatin regions of rDNA. SIMILARITY: Belongs to the WD repeat PWP1 family.


FUNCTION: May regulate DNA damage response and cell proliferation. SUBCELLULAR LOCATION: Nucleus, nucleoplasm. SIMILARITY: Belongs to the CARF family.


FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'- processing endonuclease activity. Specifically involved in tRNA repair: acts downstream of the ribosome-associated quality control (RQC) pathway by removing a 2',3'-cyclic phosphate from tRNAs following cleavage by ANKZF1. tRNAs are then processed by TRNT1. SUBCELLULAR LOCATION: Cytoplasm, cytosol Nucleus Note=Mainly cytosolic. SIMILARITY: Belongs to the RNase Z 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. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein; Matrix side. SIMILARITY: Belongs to the complex I NDUFB1 subunit family.


SIMILARITY: Belongs to the gamma-glutamyltransferase family.


FUNCTION: Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Considered to have intrinsic transcriptional activity, have some natural ligands such as all-trans retinoic acid (ATRA) and other retinoids which act as inverse agonists repressing the transcriptional activity. Required for normal postnatal development of rod and cone photoreceptor cells. Modulates rod photoreceptors differentiation at least by inducing the transcription factor NRL-mediated pathway. In cone photoreceptor cells, regulates transcription of OPN1SW. Involved in the regulation of the period length and stability of the circadian rhythm. May control cytoarchitectural patterning of neocortical neurons during development. May act in a dose-dependent manner to regulate barrel formation upon innervation of layer IV neurons by thalamocortical axons. May play a role in the suppression of osteoblastic differentiation through the inhibition of RUNX2 transcriptional activity. FUNCTION: Isoform 1 is critical for hindlimb motor control and for the differentiation of amacrine and horizontal cells in the retina. Regulates the expression of PTF1A synergistically with FOXN4. SUBCELLULAR LOCATION: Nucleus Nucleus, nucleoplasm. SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 subfamily.


FUNCTION: Involved in regulation of mitochondrial protein translation and respiration. Plays a role in mitochondria-mediated cell death. May act as a scaffolding protein or stabilizer of respiratory chain supercomplexes. Binds GTP. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. NOA1 subfamily.


SIMILARITY: Belongs to the UPF0587 family.


FUNCTION: ATP-binding protein that negatively regulates activity of the tripartite ATP-independent periplasmic (TRAP) ectoine transport system TeaABC. May regulate uptake according to the ATP status of the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal stress protein A family.


FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity). FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (By similarity). Functions as upstream regulator of FGF10 expression. Plays an important role in embryonic lung development. May contribute to embryonic brain development by regulating the proliferation of dopaminergic precursors and neurons (By similarity). SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the Wnt family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.


SIMILARITY: Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.


FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D- ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. SUBCELLULAR LOCATION: Carboxysome. SIMILARITY: Belongs to the RuBisCO large chain family. Type I subfamily.


FUNCTION: GTPase that associates with pre-60S ribosomal subunits in the nucleolus and is required for their nuclear export and maturation. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. NOG2 subfamily.


FUNCTION: Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule for a long distance without falling off the track). Predominantly recruits 2 dyneins, which increases both the force and speed of the microtubule motor. Component of the FTS/Hook/FHIP complex (FHF complex). The FHF complex may function to promote vesicle trafficking and/or fusion via the homotypic vesicular protein sorting complex (the HOPS complex). May regulate clearance of endocytosed receptors such as MSR1. Participates in defining the architecture and localization of the Golgi complex. FHF complex promotes the distribution of AP-4 complex to the perinuclear area of the cell. FUNCTION: (Microbial infection) Serves as a target for the spiC protein from Salmonella typhimurium, which inactivates it, leading to a strong alteration in cellular trafficking. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Golgi apparatus Note=Enriched at the cis-face of the Golgi complex (By similarity). Localizes to microtubule asters in prophase (By similarity). Localizes to the manchette in elongating spermatids (PubMed:28003339). SIMILARITY: Belongs to the hook family.


FUNCTION: Catalyzes the strictly specific dephosphorylation of 2'- deoxyribonucleoside 5'-monophosphates. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the 5DNU family.


FUNCTION: May be involved in transcriptional regulation as a repressor of ESR1/ER-alpha signaling. Plays a role during development and organogenesis as well as in the function of the adult central nervous system (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.


FUNCTION: Methyltransferase involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine (PubMed:22535422, PubMed:22653730, PubMed:29610307). Catalyzes the conversion of (S)- scoulerine to (S)-tetrahydrocolumbamine (PubMed:22535422, PubMed:22653730). Can convert (S)-tetrahydrocolumbamine to tetrahydropalmatine (PubMed:22535422). Can convert (S)-norreticuline to (S)-norcodamine (PubMed:22535422). Can convert (S)-reticuline to (S)- codamine (PubMed:22535422). Substrate preference is (S)-scoulerine > (S)-tetrahydrocolumbamine > (S)-norreticuline > (S)-reticuline (PubMed:22535422). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family. COMT subfamily.


FUNCTION: Serine protease inhibitor that inhibits plasmin and trypsin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom Kunitz-type family.


SIMILARITY: Belongs to the UPF0358 family.


FUNCTION: Involved in the N-glucosylation of cytokinins. Catalyzes the formation of both the 7-N and the 9-N-glucosides. SIMILARITY: Belongs to the UDP-glycosyltransferase family.


FUNCTION: Inhibitor of cyclin-dependent kinase CDK2 (By similarity). Also acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:20523938, PubMed:16428440, PubMed:28977666). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the CDK2AP family.


FUNCTION: With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits. SIMILARITY: Belongs to the universal ribosomal protein uS12 family.


FUNCTION: Potent agonist for both PKR1/PROKR1 and PKR2/PROKR2, and inducer of a potent and long-lasting hyperalgesia (PubMed:16299550, PubMed:20677202). Shows an EC(50) of 0.264 nM, when tested on neuroblastoma cells (SH-SY5Y) which endogenously express mainly PKR2/PROKR2 (PubMed:20677202). Also potentiates capsaicin-induced TRPV1 current, when tested on DRG neurons (PubMed:16687502, PubMed:20677202). Induces a biphasic hyperalgesia to tactile and thermal stimuli after systemic injection of this protein into rat (PubMed:10422759, PubMed:12466223). The initial phase of hyperalgesia is caused by a local action on nociceptors, because intraplantar injection of this protein causes a strong and localized hyperalgesia with a similar time course to that of the initial phase of hyperalgesia seen with systemic injection. The secondary phase of hyperalgesia is not seen with local intraplantar injection and is therefore probably attributable to a central action of this protein (PubMed:16687502). At subnanomolar concentrations, this protein both induces potent chemotaxis of macrophages and stimulates LPS-induced production of the pro- inflammatory cytokines IL-1 and IL-12 (PubMed:16299550). In vivo, this protein potently stimulates the contraction of the guinea-pig gastrointestinal (GI) smooth muscle (at nanomolar concentration) (PubMed:10422759). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the AVIT (prokineticin) family.


FUNCTION: Interconversion of serine and glycine (PubMed:8505317, PubMed:24698160). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SHMT family.


FUNCTION: May be important in protein trafficking and/or protein folding and stabilization. SUBCELLULAR LOCATION: Cytoplasm Nucleus.


FUNCTION: This is one of the several different receptors for 5- hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. This receptor is a ligand- gated ion channel, which when activated causes fast, depolarizing responses. It is a cation-specific, but otherwise relatively nonselective, ion channel. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Presumably retained within the endoplasmic reticulum unless complexed with HTR3A. SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. 5-hydroxytryptamine receptor (TC 1.A.9.2) subfamily. HTR3C sub- subfamily.


FUNCTION: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6- methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has also a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides (By similarity). Involved in lifespan determination in a ubiquinone-independent manner (PubMed:19478076). Plays a role in modulating mitochondrial stress responses, acting in the nucleus, perhaps via regulating gene expression, independent of its characterized mitochondrial function in ubiquinone biosynthesis. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. SIMILARITY: Belongs to the COQ7 family.


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


FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. FUNCTION: The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity. Shows a preferential cleavage at -Arg-Ser-Arg-Arg-|- and -Arg-Arg-Ser-Arg-|-, and of Z-Phe-Arg-|-aminomethylcoumarin sites. FUNCTION: Lactotransferrin is a major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity. Antimicrobial properties may include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. May have anabolic, differentiating and anti-apoptotic effects on osteoblasts and may also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. May interfere with the lipopolysaccharide (LPS)-stimulated TLR4 signaling (By similarity). SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule Note=Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils (By similarity). SIMILARITY: Belongs to the transferrin family.


FUNCTION: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins (PubMed:29809151). Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed:29809151). Involved in the cotranslational insertion of multi- pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed:29809151). It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N- exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the EMC4 family.


FUNCTION: Immediate-early protein playing a role in various cellular processes including proliferation, adhesion, migration, differentiation and survival (PubMed:15181016, PubMed:15611078, PubMed:12695522, PubMed:21344378, PubMed:12050162). Acts by binding to integrins or membrane receptors such as NOTCH1 (PubMed:12695522, PubMed:21344378, PubMed:15611078). Essential regulator of hematopoietic stem and progenitor cell function (PubMed:17463287). Inhibits myogenic differentiation through the activation of Notch-signaling pathway (PubMed:12050162). Inhibits vascular smooth muscle cells proliferation by increasing expression of cell-cycle regulators such as CDKN2B or CDKN1A independently of TGFB1 signaling (PubMed:20139355). Ligand of integrins ITGAV:ITGB3 and ITGA5:ITGB1, acts directly upon endothelial cells to stimulate pro-angiogenic activities and induces angiogenesis. In endothelial cells, supports cell adhesion, induces directed cell migration (chemotaxis) and promotes cell survival (PubMed:12695522). Also plays a role in cutaneous wound healing acting as integrin receptor ligand. Supports skin fibroblast adhesion through ITGA5:ITGB1 and ITGA6:ITGB1 and induces fibroblast chemotaxis through ITGAV:ITGB5. Seems to enhance bFGF-induced DNA synthesis in fibroblasts (PubMed:15611078). Involved in bone regeneration as a negative regulator (By similarity). Enhances the articular chondrocytic phenotype, whereas it repressed the one representing endochondral ossification (PubMed:21871891). Impairs pancreatic beta-cell function, inhibits beta-cell proliferation and insulin secretion (By similarity). Plays a role as negative regulator of endothelial pro-inflammatory activation reducing monocyte adhesion, its anti-inflammatory effects occur secondary to the inhibition of NF-kappaB signaling pathway (PubMed:21063504). Contributes to the control and coordination of inflammatory processes in atherosclerosis (By similarity). Attenuates inflammatory pain through regulation of IL1B- and TNF-induced MMP9, MMP2 and CCL2 expression. Inhibits MMP9 expression through ITGB1 engagement (PubMed:21871891). SUBCELLULAR LOCATION: Secreted. Cytoplasm Cell junction, gap junction Note=Localizes at the gap junction in presence of GJA1. SIMILARITY: Belongs to the CCN family.


FUNCTION: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B (By similarity). Phosphorylates LPXN on 'Tyr-72' (By similarity). Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation. Phosphorylates SCIMP on 'Tyr-96'; this enhances binding of SCIMP to TLR4, promoting the phosphorylation of TLR4, and a selective cytokine response to lipopolysaccharide in macrophages (By similarity). Phosphorylates CLNK (By similarity). Phosphorylates BCAR1/CAS and NEDD9/HEF1 (By similarity). SUBCELLULAR LOCATION: Cell membrane Nucleus Cytoplasm Cytoplasm, perinuclear region Golgi apparatus Membrane; Lipid-anchor Note=Accumulates in the nucleus by inhibition of Crm1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activity. The trafficking from the Golgi apparatus to the cell membrane occurs in a kinase domain- dependent but kinase activity independent manner and is mediated by exocytic vesicular transport (By similarity). SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.


FUNCTION: Involved in salt stress tolerance. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.


FUNCTION: Inactivates phosphinothricin (PPT) by transfer of an acetyl group from acetyl CoA. This enzyme is an effector of phosphinothricin tripeptide (PTT or bialaphos) resistance. SIMILARITY: Belongs to the acetyltransferase family. PAT/BAR subfamily.


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.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.


FUNCTION: Required for hypophosphite oxidation. SIMILARITY: Belongs to the PhyH family.


FUNCTION: [Isoform f]: Functions in the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:24834345). Transcript level in the early adult may play a role in lifespan modulation, but effect is more significant than that played by isoform a (PubMed:24834345). FUNCTION: [Isoform a]: Functions in the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:24834345). May play a role in lifespan modulation, but less significant than that played by isoforms d and f (PubMed:24834345). FUNCTION: Forkhead-type transcription factor (PubMed:9360933). Binds to the promoters of genes that contain the daf-16/FOXO binding element (DBE), TTGTTTAC, in their regulatory region (PubMed:10880363, PubMed:23770237, PubMed:26675724). Functions in the Insulin/IGF-1-like signaling (IIS) mediated pathway which affects lipogenesis, lifespan, starvation survival, heat shock and oxidative stress responses, sleep, associative memory, and dauer formation (PubMed:9360933, PubMed:8247153, PubMed:11747821, PubMed:11747825, PubMed:11381260, PubMed:14622602, PubMed:12750521, PubMed:17900900, PubMed:18358814, PubMed:18762027, PubMed:18832074, PubMed:19103192, PubMed:21531333, PubMed:22081913, PubMed:29523076, PubMed:26675724). Longevity signaling predominantly arises from expression in the intestine (PubMed:14622602). Transcriptional activity of daf-16/FOXO is negatively regulated by interaction with host cell factor homolog hcf- 1; and by cytoplasmic sequestration by association with ftt-2 (PubMed:11381260, PubMed:21531333, PubMed:18828672). Inhibition is required for the carbon dioxide (CO2) avoidance response (PubMed:18524954). Upon loss of inhibition, daf-16 translocates to the nucleus to regulate genes that result in delayed reproduction and growth while increasing stress resistance starvation tolerance and longevity (PubMed:11747825, PubMed:21531333). Association with arginine methyltransferase prmt-1 prevents phosphorylation and allows for translocation to the nucleus and the subsequent transcription of longevity-related genes (PubMed:21531333). Modulation of its activity by cGMP levels in sensory neurons regulates lifespan (PubMed:19489741). Has a protective role against muscle dystrophy (PubMed:18397876). Involved in mediating protection against aberrant protein aggregation proteotoxicity (PubMed:16902091). Influences transcription of genes that code for proteins involved in immunity as part of a general stress response (PubMed:17096597, PubMed:18245330). Targets genes that inhibit and stimulate tumor growth (PubMed:17934462). Targets kinases, phosphatases and transcription factors that are primarily involved in signaling and gene regulation (PubMed:24516399). Thought to regulate ins-7 in FOXO-to-FOXO signaling, which coordinates daf-16 expression (PubMed:18025456). Activity is positively regulated by shc-1-mediated inhibition of daf-2 and activation of JNK pathway (PubMed:18832074, PubMed:22916022). Through the regulation of its activity by shc-1- mediated inhibition of daf-2 and activation of JNK pathway, plays a role in maintaining the integrity of the gonad (PubMed:22916022). Functions by indirect interaction with jnk-1 of the mitogen-activated protein kinase (MAPK) pathway (PubMed:17894411). Involved in increased proteasome activity by activating expression of rpn-6.1 in response to proteotoxic stress, leading to enhanced assembly of the 26S proteasome, followed by higher proteasome activity (PubMed:22922647). Also regulates proteasome activity in the intestine by preventing expression of deubiquitinase ubh-4 (PubMed:23770237). Represses transcription of natc-1 (PubMed:25330323). Involved in regulation of srh-234 expression (PubMed:25357003). Binds to the promoter of the AMPK-gamma regulatory subunit, aakg-4, and activates its transcription (PubMed:24516399). Also activates transcription of AMPK-gamma regulatory subunit, aakg-1 (PubMed:24516399). Maintains endoplasmic reticulum (ER) function by inducing protein degradation and elimination to remove misfolded secretory proteins from the ER independently of the ire-1/xbp-1 unfolded protein response pathway (PubMed:25448701). Regulates epidermal innate immunity to nematophagous fungal infection and physical wounding which trigger bli-3 induced ROS release, leading to daf-16 activation independently of daf-2 signaling (PubMed:24146615). May negatively regulate resistance to stress caused by oxidized cholesterol adducts by preventing the activation of daf-9 and nuclear hormone receptor daf-12, two members of the steroid signaling pathway (PubMed:24957743). Promotes apoptosis during embryonic development (PubMed:25383666). Probably through the regulation of the autophagy genes atg-18 and atg-16.2, plays a role in regulating stem cell number in the germline during larval development (PubMed:28285998). Plays a role in learning and memory; including associative memory, and aversive gustatory associated learning known as salt avoidance learning (PubMed:26675724, PubMed:30779740). Plays a role in regulating gene transcription in response to white light exposure (PubMed:29500338). Binds to the promoter of dex-1 to positively regulate its expression in seam cells during the dauer phase (PubMed:30409788). Plays a role in transgenerational lipid accumulation in response to a high-fat diet (PubMed:35140229). FUNCTION: [Isoform d]: Functions in the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:24834345). Transcript level in the early adult may play a role in lifespan modulation, but effect is more significant than that played by isoform a (PubMed:24834345). SUBCELLULAR LOCATION: [Isoform f]: Nucleus Cytoplasm Note=Ratio of nuclear to cytoplasmic localization is daf-2-dependent. SUBCELLULAR LOCATION: [Isoform a]: Nucleus Cytoplasm Note=Ratio of nuclear to cytoplasmic localization is daf-2-dependent. SUBCELLULAR LOCATION: [Isoform d]: Nucleus Cytoplasm Note=Ratio of nuclear to cytoplasmic localization is daf-2-dependent. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Shuttles between cytoplasm and nucleus (PubMed:11381260, PubMed:17894411). Nuclear translocation is inhibited by phosphorylation by AKT proteins (PubMed:11381260, PubMed:11747825, PubMed:21531333). Association with ftt-2 sequesters daf-16 in the cytoplasm (PubMed:21531333). Association with prmt-1 allows for translocation to the nucleus (PubMed:21531333). Nuclear translocation is promoted by phosphorylation by unc-43 and inhibited by dephosphorylation by tax-6 (PubMed:23805378). Nuclear translocation is promoted by jnk-1 upon heat stress and by sek-1 upon oxidative stress (PubMed:15888317, PubMed:15767565). Nucleocytoplasmic shuttling is induced by starvation, heat treatment, hypergravity, reactive oxygen species (generated by juglone), exposure to tributyltin or 4-hydroxy-E- globularinin (4-HEG) and the flavonoids kaempferol and fisetin (PubMed:11381260, PubMed:17551714, PubMed:18832074, PubMed:19252938, PubMed:21531333, PubMed:23805378). Nuclear localization induced by nematophagous fungal infection (PubMed:24146615).


FUNCTION: Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N- acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface. SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.


FUNCTION: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). SIMILARITY: Belongs to the HPrK/P family.


FUNCTION: May be required for progression through G1 and entry into S phase of cell growth. May play a regulatory role in pre-mRNA splicing. Autoregulates its own expression. Plays a role in constitutive splicing and can modulate the selection of alternative splice sites (By similarity). FUNCTION: May be required for progression through G1 and entry into S phase of cell growth. May play a regulatory role in pre-mRNA splicing. Autoregulates its own expression. Plays a role in constitutive splicing and can modulate the selection of alternative splice sites (By similarity). Could play an important role in development and differentiation in the spleen and thymus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the splicing factor SR family.


FUNCTION: Hydrolyzes specifically phosphatidic acid (PA) to produce 2- acyl lysophosphatidic acid (LPA; a potent bioactive lipid mediator) and fatty acid (By similarity). Does not hydrolyze other phospholipids, like phosphatidylserine (PS), phosphatidylcholine (PC) and phosphatidylethanolamine (PE) or triacylglycerol (TG) (By similarity). SUBCELLULAR LOCATION: Secreted Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.


FUNCTION: Activates the transcription of the sdsA gene for sodium dodecyl sulfate (SDS) degradation. SIMILARITY: Belongs to the LysR transcriptional regulatory family.


FUNCTION: Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding to feline junctional adhesion molecule A (F11R) and/or to alpha-2,6-linked sialic acid. Once attached, the virion is endocytosed. Acidification of the endosome induces conformational change of capsid protein thereby injecting virus genomic RNA into host cytoplasm (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the caliciviridae capsid protein family.


FUNCTION: Catalyzes the conversion of the 17-keto group of estrone, 4- and 5-androstenes and 5-alpha-androstanes into their 17-beta- hydroxyl metabolites and the conversion of the 3-keto group of 3-, 3,17- and 3,20- diketosteroids into their 3-hydroxyl metabolites. Exhibits reductive 3-beta-hydroxysteroid dehydrogenase activity toward 5-beta-androstanes, 5-beta-pregnanes, 4-pregnenes and bile acids. May also reduce endogenous and exogenous alpha-dicarbonyl compounds and xenobiotic alicyclic ketones. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ycf92 family.


FUNCTION: Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly (By similarity). Prevents also necroptosis and extrinsic apoptosis by sequestering host ZBP1 into large, insoluble supercomplexes and impairing its ability to interact with RIPK3 (PubMed:32649716). SUBCELLULAR LOCATION: Virion Host nucleus. SIMILARITY: Belongs to the herpesviridae TRX1 protein family.


FUNCTION: Taste-modifying protein; sweet-tasting. After curculin, water elicits a sweet taste, and sour substances induce a stronger sense of sweetness.


FUNCTION: Bidirectional proton-coupled monocarboxylate transporter (PubMed:12946269, PubMed:33333023, PubMed:32946811). Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, acetate and the ketone bodies acetoacetate and beta-hydroxybutyrate, and thus contributes to the maintenance of intracellular pH (PubMed:12946269, PubMed:33333023). The transport direction is determined by the proton motive force and the concentration gradient of the substrate monocarboxylate. MCT1 is a major lactate exporter (By similarity). Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis (By similarity). Facilitates the protonated monocarboxylate form of succinate export, that its transient protonation upon muscle cell acidification in exercising muscle and ischemic heart (PubMed:32946811). Functions via alternate outward- and inward-open conformation states. Protonation and deprotonation of 309-Asp is essential for the conformational transition (PubMed:33333023). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein Apical cell membrane; Multi-pass membrane protein Note=Expression at the cell surface requires the ancillary proteins BSG and EMB. Binds preferentially to BSG. SIMILARITY: Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family.


FUNCTION: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA (PubMed:11118225, PubMed:17932046). Acts as a peptidyl-tRNA hydrolase (PubMed:22857598, PubMed:27934701). In the presence of truncated mRNA in the 70S ribosome, ArfA and RF2 interact such that the GGQ peptide hydrolysis motif of RF2 rises into the peptidyl-transferase center and releases the ribosome (PubMed:27906160, PubMed:27906161, PubMed:27934701, PubMed:28077875). Recruited by ArfA to rescue stalled ribosomes in the absence of a normal stop codon (PubMed:22857598, PubMed:22922063, PubMed:25355516). FUNCTION: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. Note=Recruited to the 70S ribosome by ArfA even in the absence of mRNA (PubMed:22922063, PubMed:25355516, PubMed:27934701). SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family. SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor family.


FUNCTION: Catalyzes juvenile hormone hydrolysis. SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane protein Endoplasmic reticulum membrane; Single-pass membrane protein. SIMILARITY: Belongs to the peptidase S33 family.


FUNCTION: Probably participates in a plant defense mechanism (Probable). Not active against Gram-negative bacteria E.coli ATCC 700926, K.pneumoniae ATTC 13883 and P.aeruginosa ATCC 39018 at concentration up to 100 uM (PubMed:21596752). Has cytotoxic but no hemolytic activity (PubMed:21596752). SIMILARITY: Belongs to the cyclotide family. Moebius subfamily.


FUNCTION: Snake venom phospholipase A2 (PLA2) that has antibacterial activity against S.aureus ATCC 25923 and ATCC 29213, acts by inducing bacterial membrane breakage. Displays a potent inhibitory effect on collagen-induced human platelet aggregation and has indirect hemolytic activity. Does not show cytotoxicity to murine skeletal muscle myoblasts. PLA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.


FUNCTION: Forms part of two intersubunit bridges in the 70S ribosome (By similarity). Binds to 23S rRNA. SIMILARITY: Belongs to the universal ribosomal protein uL14 family.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eL21 family.


FUNCTION: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA domain. FUNCTION: P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite- regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity (By similarity). FUNCTION: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA domain. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the HPr family.


FUNCTION: Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps (By similarity). SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor Note=Anchored to the cell wall by sortase A (By similarity). SIMILARITY: Belongs to the serine-aspartate repeat-containing protein (SDr) family.


FUNCTION: May be involved in photosynthetic membrane biogenesis. SIMILARITY: Belongs to the THF1 family.


FUNCTION: Plays a role in lipoprotein-mediated cholesterol uptake in hepatocytes (PubMed:25732850). Binds cholesterol (PubMed:25732850). Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.


FUNCTION: Dephosphorylates auto-phosphorylated Ca(2+)/calmodulin- dependent protein kinase unc-43/CAMKII in vitro (PubMed:11559703, PubMed:23760267). Involved in the regulation of sex determination (PubMed:8824590). Together with fem-3, required for male sexual development by promoting the proteasomal-mediated degradation of tra-1, a transcription repressor of male-specific genes (PubMed:17609115). Promotes apoptosis (PubMed:11559703). SIMILARITY: Belongs to the PP2C family.


FUNCTION: Urate oxidase is a cofactorless enzyme involved in the metabolism of purines (PubMed:1339455, PubMed:17020862, Ref.3, PubMed:28272834). Catalyzes, in the presence of molecular oxygen, the hydroxylation of uric acid to metastable 5-hydroxyisourate (5-HIU) which is further degraded to allantoin (PubMed:1339455, PubMed:17020862, PubMed:28272834). SUBCELLULAR LOCATION: Peroxisome. SIMILARITY: Belongs to the uricase family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the TVP23 family.


SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the EMC7 family.


FUNCTION: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the RNA methyltransferase RsmE family.


FUNCTION: ATP-binding RNA helicase involved in translation initiation. Remodels RNA in response to ADP and ATP concentrations by facilitating disruption, but also formation of RNA duplexes (By similarity). Redundant to DED1, may be required in conditions in which DED1 expression is decreased. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1 subfamily.


FUNCTION: Involved in DNA replication and cell separation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the SDS23 family.


FUNCTION: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state (PubMed:15897198). Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the poneritoxin-Ae1 family.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the universal ribosomal protein uL14 family.


FUNCTION: Neuroendocrine protein of the granin family that regulates the biogenesis of secretory granules (By similarity). Required for neurovascular modeling of the hindbrain (PubMed:29757409). Acts in a non-cell autonomous manner and is required for migration and proliferation of central artery endothelial cells (PubMed:29757409). Required for normal courting behavior and spawning (PubMed:32467166). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the chromogranin/secretogranin protein family.


FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl- tRNA(Sec) required for selenoprotein biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SepSecS family.


FUNCTION: Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage. SUBCELLULAR LOCATION: Lysosome membrane; Peripheral membrane protein; Lumenal side Lysosome lumen Cell membrane Cytoplasmic vesicle Note=Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but also on the plasma membrane and in intracellular vesicles. SIMILARITY: Belongs to the glycosyl hydrolase 33 family.


FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity). SIMILARITY: Belongs to the prefoldin subunit beta family.


FUNCTION: Potent pro-inflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B- cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T- helper 1 (Th1) cells. Plays a role in angiogenesis by inducing VEGF production synergistically with TNF and IL6. Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. SUBCELLULAR LOCATION: Cytoplasm, cytosol Secreted Lysosome Secreted, extracellular exosome Note=The precursor is cytosolic. In response to inflammasome-activating signals, such as ATP for NLRP3 inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and secreted. Mature form is secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. In contrast, the precursor form is not released, due to the presence of an acidic region that is proteolytically removed by CASP1 during maturation. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10. SIMILARITY: Belongs to the IL-1 family.


FUNCTION: Immunity protein that provides protection for the cell against the toxic effects of SDP, its own SdpC-derived killing factor, and that functions as a receptor/signal transduction protein as well. Once SDP accumulates in the extracellular milieu, SdpI binds to SDP, causing sequestration of SdpR at the bacterial membrane. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.


FUNCTION: Autophagy-specific protein that functions in response to autophagy-inducing signals as a scaffold to recruit other ATG proteins to organize pre-autophagosomal structure (PAS) formation. Modulates the timing and magnitude of the autophagy response, such as the size of the sequestering vesicles. Plays particularly a role in pexophagy and nucleophagy (By similarity). SUBCELLULAR LOCATION: Cytoplasm Preautophagosomal structure membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ATG17 family.


FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 5 family.


FUNCTION: Curlin is the structural subunit of the curli fimbriae. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli can bind to fibronectin. SUBCELLULAR LOCATION: Fimbrium. Note=Part of the curli surface structure. SIMILARITY: Belongs to the CsgA/CsgB family.


FUNCTION: Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the MscS (TC 1.A.23) family.


FUNCTION: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions (Probable). Mediates alternative electron partitioning in conditions of acceptor limitation at photosystem I (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the 2Fe2S plant-type ferredoxin family.


FUNCTION: Regulates the morphogenesis and endocytosis of caveolae (By similarity). Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus. SUBCELLULAR LOCATION: Cell junction, focal adhesion Cytoplasm Cytoplasm, cytoskeleton Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Early endosome Recycling endosome membrane Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side Cell membrane; Peripheral membrane protein; Cytoplasmic side Cell projection Membrane, caveola Note=Detected at the neck of flask-shaped caveolae. SIMILARITY: Belongs to the PACSIN family.


FUNCTION: Regulates centrosome duplication, probably by inhibiting the kinase activity of ROCK2. Proposed to act as co-chaperone for HSP90. May play a role in the regulation of NOD1 via a HSP90 chaperone complex. In vitro, has intrinsic chaperone activity. This function may be achieved by inhibiting association of ROCK2 with NPM1. Plays a role in ensuring the localization of the tyrosine kinase receptor EGFR to the plasma membrane, and thus ensures the subsequent regulation of EGFR activity and EGF-induced actin cytoskeleton remodeling (By similarity). Involved in stress response. Prevents tumorigenesis (By similarity).


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ABC transporter superfamily. ABCI family.


FUNCTION: Bifunctional glycosyltransferase with both alpha-1,3- xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the maturation of alpha-dystroglycan (DAG1) by glycosylation leading to DAG1 binding to laminin G-like domain- containing extracellular proteins with high affinity (PubMed:23125099, PubMed:23135544, PubMed:25138275, PubMed:32975514). Elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure initiated by B4GAT1 by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide (By similarity). Requires the phosphorylation of core M3 (O-mannosyl trisaccharide) by POMK to elongate the glucuronyl-beta-1,4-xylose-beta disaccharide primer (PubMed:32975514). Plays a key role in skeletal muscle function and regeneration (PubMed:15184894, PubMed:24132234). SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II membrane protein. SIMILARITY: In the C-terminal section; belongs to the glycosyltransferase 49 family. SIMILARITY: In the N-terminal section; belongs to the glycosyltransferase 8 family.