FUNCTION: Dehydratase; part of the gene cluster that mediates the biosynthesis of cercosporin, a light-activated, non-host-selective toxin (PubMed:29844193). The perylenequinone chromophore of cercosporin absorbs light energy to attain an electronically-activated triplet state and produces active oxygen species such as the hydroxyl radical, superoxide, hydrogen peroxide or singlet oxygen upon reaction with oxygen molecules (PubMed:11701851). These reactive oxygen species cause damage to various cellular components including lipids, proteins and nucleic acids (PubMed:11701851). The first step of cercosporin biosynthesis is performed by the polyketide synthase CTB1 which catalyzes the formation of nor-toralactone (Probable). The starter unit acyltransferase (SAT) domain of CTB1 initiates polyketide extension by the selective utilization of acetyl-CoA, which is elongated to the heptaketide in the beta-ketoacyl synthase (KS) domain by successive condensations with six malonyl units introduced by the malonyl acyltransferase (MAT) domain. The product template (PT) domain catalyzes C4-C9 and C2-C11 aldol cyclizations and dehydrations to a trihydroxynaphthalene, which is thought to be delivered to the thioesterase (TE) domain for product release (Probable). The bifunctional enzyme CTB3 then methylates nor-toralactone to toralactone before conducting an unusual oxidative aromatic ring opening (Probable). The O-methyltransferase CTB2 further methylates the nascent OH-6 of the CBT3 product, blocking further oxidation at this site before the reductase CTB6 reduces the 2-oxopropyl ketone at position C7, giving naphthalene (Probable). The FAD-dependent monooxygenase CTB5 in concert with the multicopper oxidase CTB12 are responsible for homodimerization of naphthalene with CTB7 installing the dioxepine moiety, finally producing cercosporin (Probable). The fasciclin domain- containing protein CTB11 might act with CTB5 and CTB12 whereas the roles of CTB9 and CTB10 have still to be elucidated (By similarity). SIMILARITY: Belongs to the tpcK family.


FUNCTION: Rho GTPase-activating protein which may be involved in clathrin-mediated endocytosis. GTPase activators for the Rho-type GTPases act by converting them to an inactive GDP-bound state. Has activity toward CDC42 and RAC1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein.


FUNCTION: Cholecystokinin-22: hypotensive neuropeptide that binds cholecystokinin receptor type A receptor (CCKAR). FUNCTION: Cholecystokinin-8: hypotensive neuropeptide that binds cholecystokinin receptor type A receptor (CCKAR). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the gastrin/cholecystokinin family.


FUNCTION: Catalyzes the trimethylation of 'Lys-116' in calmodulin. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. CLNMT methyltransferase family.


FUNCTION: 3'-5' exonuclease that specifically cleaves precursor piRNAs (pre-piRNAs) at their 3' ends (PubMed:26919431). Trims pre-piRNAs to their mature size, a process required for piRNAs maturation and stabilization, and subsequent pre-piRNAs 2'-O-methylation (PubMed:26919431). The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons (PubMed:26919431). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass membrane protein. SIMILARITY: Belongs to the CAF1 family.


FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL30 family.


FUNCTION: May act as a substrate-specific adapter of an E3 ubiquitin- protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.


FUNCTION: Probably plays a role in the assembly of the spore coat proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links. SIMILARITY: Belongs to the bacillus TGase family.


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


FUNCTION: Ubiquitin Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell- cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ubiquitin family.


FUNCTION: Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4). SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the peroxidase family. XPO subfamily.


FUNCTION: Involved in developmental cell fate decision. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 family.


FUNCTION: Effector E3 ubiquitin ligase that interferes with host's ubiquitination pathway and modulates the acute inflammatory responses, thus facilitating bacterial colonization within the host cell (PubMed:18005683, PubMed:20831869, PubMed:24248594, PubMed:29024643, PubMed:29144452, PubMed:31216343, PubMed:33303953). Interacts with IKBKG (NEMO) and TNIP1 (ABIN-1), a ubiquitin-binding adapter protein, which results in TNIP1-dependent 'Lys-27'-linked polyubiquitination of IKBKG (PubMed:18005683). Consequently, polyubiquitinated IKBKG undergoes proteasome-dependent degradation, which perturbs NF-kappa-B activation during bacterial infection (PubMed:18005683, PubMed:20010814). Mediates polyubiquitination of host U2AF1, leading to its proteasomal degradation (PubMed:15950937). Catalyzes 'Lys-48'- linked polyubiquitination and subsequent degradation of a subset of host guanylate-binding proteins (GBP1, GBP2, GBP4 and GBP6), thereby suppressing host cell defense (PubMed:29024643, PubMed:29144452, PubMed:31216343, PubMed:33303953). In contrast, host GBP3 and GBP7 are not ubiquitinated by IpaH9.8 (PubMed:29024643, PubMed:29144452, PubMed:31216343). Uses UBE2D2 (UBCH5B) as an E2 ubiquitin-conjugating enzyme (PubMed:18005683). SUBCELLULAR LOCATION: Secreted Host cytoplasm Host nucleus Note=Secreted via Mxi-Spa type III secretion system (TTSS), and delivered into the host cytoplasm (PubMed:11115111, PubMed:11418613). Transported into the host nucleus (PubMed:11418613). This transport is independent of cytosolic factors, but dependent on temperature and partly on ATP/GTP (PubMed:11418613). SIMILARITY: Belongs to the LRR-containing bacterial E3 ligase family.


FUNCTION: Subunit of the tubulin polyglutamylase complex (TPGC). The complex mediates cilia and flagella polyglutamylation which is essential for their biogenesis and motility. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite Note=Associated with microtubules.


FUNCTION: Spider venom endo-hyaluronidase that is able to degrade purified hyaluronic acid (HA) and chondroitin sulfate (CS). Has no activity on dermatan sulfate (DS) and heparan sulfate (HS). Also increases the dermonecrotic effect of the dermonecrotic toxin (AC P0CE80), when injected in rabbit skin, supporting the hypothesis that venom hyaluronidases are spreading factors. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 56 family.


FUNCTION: Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion or exclusion. It binds specifically to the sequences 5'-YCAY- 3' and regulates splicing in only a subset of regulated exons (PubMed:10811881). Binding to an exonic 5'-YCAY-3' cluster changes the protein complexes assembled on pre-mRNA, blocking U1 snRNP binding and exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster enhances spliceosome assembly and exon inclusion. Binding to 5'-YCAY-3' clusters results in a local and asymmetric action to regulate spliceosome assembly and alternative splicing in neurons. Binding to an exonic 5'-YCAY-3' cluster changed the protein complexes assembled on pre-mRNA, blocking U1 snRNP (small nuclear ribonucleoprotein) binding and exon inclusion, whereas binding to an intronic 5'-YCAY-3' cluster enhanced spliceosome assembly and exon inclusion. With NOVA1, they perform unique biological functions in different brain areas and cell types. Autoregulates its own expression by acting as a splicing repressor. Acts to activate the inclusion of exon E3A in the glycine receptor alpha-2 chain and of exon E9 in gamma-aminobutyric-acid receptor gamma-2 subunit via a distal downstream UCAU-rich intronic splicing enhancer. Acts to regulate a novel glycine receptor alpha-2 chain splice variant (alpha-2N) in developing spinal cord (By similarity). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Dioxygenase that catalyzes the 2-oxoglutarate-dependent selective hydroxylation of free L-proline to cis-3-hydroxy-L-proline (cis-3-Hyp). D-proline, trans-4-hydroxy-L-proline, cis-4-hydroxy-L- proline, cis-4-hydroxy-D-proline, and 3,4-dehydro-DL-proline are not substrates. SIMILARITY: Belongs to the L-proline cis-4-/cis-3-hydroxylase family.


FUNCTION: Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type I membrane protein.


FUNCTION: Mu-conotoxins block voltage-gated sodium channels. This toxin reversibly blocks voltage-gated sodium channel in cephalopods, with no alteration in the voltage dependence of sodium conductance or on the kinetics of inactivation (By similarity). SUBCELLULAR LOCATION: Secreted.


FUNCTION: Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels.


FUNCTION: Helicopsin exhibits robust neurotoxic activity as shown by immediate death (about 8 minutes) of mice due to respiratory paralysis. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the CRISP family.


FUNCTION: Encapsidates the genome protecting it from nucleases (Probable). The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication (Probable). The nucleocapsid has a left-handed helical structure (By similarity). As a trimer, specifically binds and acts as a chaperone to unwind the panhandle structure formed by the viral RNA (vRNA) termini (By similarity). Involved in the transcription and replication initiation of vRNA by mediating primer annealing (By similarity). Plays a role in cap snatching by sequestering capped RNAs in P bodies for use by the viral RdRp during transcription initiation (By similarity). Substitutes for the cellular cap-binding complex (eIF4F) to preferentially facilitate the translation of capped mRNAs (By similarity). Initiates the translation by specifically binding to the cap and 40S ribosomal subunit (By similarity). Prevents the viral glycoprotein N (Gn) from autophagy-dependent breakdown maybe by blocking autophagosome formation (By similarity). Inhibits host EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown in cells and thus the activation of the antiviral state (By similarity). Also displays sequence-unspecific DNA endonuclease activity (By similarity). SUBCELLULAR LOCATION: Virion Host cytoplasm, host perinuclear region Host Golgi apparatus, host cis-Golgi network Note=Internal protein of virus particle. SIMILARITY: Belongs to the hantavirus nucleocapsid protein family.


FUNCTION: May affect the rate of fibrils formation. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix Secreted. SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class I subfamily.


FUNCTION: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. SUBCELLULAR LOCATION: Endosome, multivesicular body membrane; Peripheral membrane protein. SIMILARITY: Belongs to the SNF7 family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 68 family.


SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peroxisomal membrane protein PXMP2/4 family.


FUNCTION: Transcription activator (PubMed:14581622). Binds to the DNA consensus sequence 5'-[ACG]CGCG[GTC]-3' (By similarity). Regulates transcriptional activity in response to calcium signals (Probable). Binds calmodulin in a calcium-dependent manner (By similarity). Involved in response to cold. Contributes together with CAMTA3 to the positive regulation of the cold-induced expression of DREB1A/CBF3, DREB1B/CBF1 and DREB1C/CBF2 (PubMed:28351986). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CAMTA family.


FUNCTION: Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity (PubMed:25358400). In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z- line structures (PubMed:24200904, PubMed:25394388, PubMed:26724190). May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction. Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin (By similarity). SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line Cytoplasm Cell membrane, sarcolemma Nucleus Note=Localizes in the intercalated disks which occur at the Z line of cardiomyocytes (PubMed:24200904, PubMed:26724190). Localizes in the nucleus exclusively in differentiating cardiac progenitor cells and premature cardiomyocytes (By similarity). SIMILARITY: Belongs to the intermediate filament family.


FUNCTION: Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:8675619). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (By similarity). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386). Recruited to its site of action on vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:20620994, PubMed:24726386, PubMed:27811232). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Extracellular side Secreted Secreted, extracellular space, extracellular matrix Note=Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells (PubMed:27811232). Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non- coated endocytic vesicles (By similarity). SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.


FUNCTION: SNARE that may be involved in targeting and fusion of Golgi- derived retrograde transport vesicles with the ER. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type IV membrane protein. SIMILARITY: Belongs to the USE1 family.


FUNCTION: Together with ArcA, is essential for positively regulating the expression of transfer genes that are involved in the conjugal transfer of DNA between bacterial cells. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: May serve as docking site to facilitate the association of other proteins to the plasma membrane. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.


FUNCTION: Putative GTPase-activating protein. SUBCELLULAR LOCATION: Cytoplasm.


SIMILARITY: Belongs to the peptidase S1 family.


FUNCTION: Removes the formyl group from the N-terminal Met of newly synthesized proteins. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the polypeptide deformylase family.


FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the GST superfamily. Alpha family.


FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.


FUNCTION: Ligand for the frizzled7 transmembrane receptor. Primarily acts via non-canonical Wnt pathways mediated by either Ca(2+) and PKC, or by JNK and dvl2/dsh. Depending on the cellular context, can also signal via the canonical Wnt pathway mediated by beta-catenin and dvl2/dsh. May also inhibit canonical Wnt signaling. Maternally initiates dorsal/ventral axis formation by a canonical route, which signals via lrp6. In a complex with wnt5a, activates the canonical and non-canonical processes involved in axis formation. In the non- canonical pathway, acts through fzd7/fz7 to induce phosphorylation of dvl2/dsh. Signals through a non-canonical Wnt pathway to regulate convergent extension movements during gastrulation. Interactions with the secreted Wnt antagonist sfrp5 to coordinate foregut development, acting via a non-canonical Wnt pathway whereby sfrp5 restricts wnt11b activity to prevent inappropriate foregut formation. Mediates cardiogenesis via non-canonical Wnt signaling involving JNK-activation and PKC. Acts redundantly with wnt11/wnt11r during pronephros induction. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the Wnt family.


FUNCTION: Probable transcription factor. Together with STOP2, plays a critical role in tolerance to major stress factors in acid soils such as proton H(+) and aluminum ion Al(3+). Required for the expression of genes in response to acidic stress (e.g. ALMT1 and MATE), and Al- activated citrate exudation. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions (By similarity). SIMILARITY: Belongs to the parvalbumin family.


FUNCTION: Involved in control of the biosynthesis of leucine. FUNCTION: Involved in control of the biosynthesis of leucine.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eL30 family.


FUNCTION: Pattern recognition receptor (PRR) which binds Gram-positive and Gram-negative bacteria (PubMed:9468508). Also plays a role in binding of unopsonized particles by alveolar macrophages (By similarity). Binds to the secretoglobin SCGB3A2 (PubMed:12847263). SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein.


FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. As part of the 5S RNP/5S ribonucleoprotein particle it is an essential component of the LSU, required for its formation and the maturation of rRNAs. It also couples ribosome biogenesis to p53/TP53 activation. As part of the 5S RNP it accumulates in the nucleoplasm and inhibits MDM2, when ribosome biogenesis is perturbed, mediating the stabilization and the activation of TP53. SUBCELLULAR LOCATION: Cytoplasm Nucleus, nucleolus. SIMILARITY: Belongs to the universal ribosomal protein uL18 family.


FUNCTION: Vacuolar cation/proton exchanger (CAX). Translocates Ca(2+) and other metal ions into vacuoles using the proton gradient formed by H(+)-ATPase and H(+)-pyrophosphatase. Cation selectivity transport in tobacco root tonoplast vesicles is Cd(2+)>Zn(2+)>>Ca(2+)>>>Mn(2+). SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein Note=Tonoplast. SIMILARITY: Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. Cation/proton exchanger (CAX) subfamily.


FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of fusarielins F, G and H, decaketide compounds with 5 methylations and a decaline core that act as mycoestrogens as they stimulate growth of MCF-7 breast cancer cells (PubMed:22252016, PubMed:27983606). The initial compound in the pathway is produced by the reducing polyketide synthase FSL1. FSL1 lacks an active enoyl reductase (ER) domain and biosynthesis of fusarielins relies on the trans-acting enoyl reductase FSL5, before it is released through hydrolysis catalyzed by the thioesterase FSL2 (PubMed:22252016, PubMed:27983606). Fusarielins F, G, and H have a C11=C12 cis double bond and is fully reduced between C10 and C11 and between C12 and C13. FSL3 can be involved in the formation of the C11=C12 cis double bond by moving a hypothetical C10=C11 or C12=C13 trans double bond to form prefusarielin (PubMed:27983606). Prefusarielin is oxygenated at C15 and C16 by FSL4, resulting in fusarielin F, which subsequently is epoxidized into fusarielin G by the same enzyme (PubMed:27983606). The final step in the pathway is a reduction of the carboxylic acid moiety to yield fusarielin H via a still undetermined mechanism (PubMed:27983606). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Catalytic subunit of a heterodimeric structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SLX1 family.


FUNCTION: Glucuronoyl esterase which may play a significant role in biomass degradation, as it is considered to disconnect hemicellulose from lignin through the hydrolysis of the ester bond between 4-O- methyl-D-glucuronic acid residues of glucuronoxylans and aromatic alcohols of lignin. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the carbohydrate esterase 15 (CE15) family.


FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL29 family.


FUNCTION: Required for the expression of the CS1 and CS2 adhesins of enterotoxygenic E.coli. SUBCELLULAR LOCATION: Cytoplasm.


FUNCTION: Contributes to the L-alanine germination response. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the GerABKA family.


FUNCTION: Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis. SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.


SIMILARITY: Belongs to the adhesin P1 family.


FUNCTION: The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion. SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor. SIMILARITY: Belongs to the variable large protein (Vlp) family. Delta subfamily.


FUNCTION: Together with HAPSTR1 plays a central regulatory role in the cellular response to molecular stressors, such as DNA damage, nutrient scarcity, and protein misfolding. Regulates these multiple stress response signaling pathways by stabilizing HAPSTR1, but also independently of HAPSTR1. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the HAPSTR1 family.


FUNCTION: Inhibitor of cathepsin D (aspartic protease) and trypsin (serine protease). May protect the plant by inhibiting proteases of invading organisms. SUBCELLULAR LOCATION: Vacuole. SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz- type inhibitor) family.


FUNCTION: Golgi matrix protein playing a role in tethering of vesicles to Golgi membranes and in maintaining the overall structure of the Golgi apparatus. Functions in the anterograde transport of storage protein precursors from the endoplasmic reticulum (ER) to the Golgi complex. SUBCELLULAR LOCATION: Golgi apparatus Golgi apparatus, Golgi stack Note=Concentrates only on one side of the Golgi bodies.


FUNCTION: Orphan receptor; could be a chemoattractant receptor. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family.


FUNCTION: Has vitronectin and fibronectin-binding activity. FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.


FUNCTION: Catalyzes the reversible cleavage of pseudouridine 5'- phosphate (PsiMP) to ribose 5-phosphate and uracil. Functions biologically in the cleavage direction, as part of a pseudouridine degradation pathway. SIMILARITY: Belongs to the pseudouridine-5'-phosphate glycosidase family.


FUNCTION: Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Restricts the CLOCK and BMAL1 localization to the cytoplasm. Plays a role in both the input and output pathways of the circadian clock: in the input component, is involved in modulating the magnitude of photic entrainment and in the output component, contributes to the regulation of a variety of liver clock-controlled genes involved in lipid metabolism. SUBCELLULAR LOCATION: Cytoplasm Nucleus.


FUNCTION: Likely catalyzes the NAD(P)-dependent oxidative deamination of (3R)-3-methyl-D-ornithyl-N6-L-lysine, resulting in the formation of pyrrolysine after spontaneous dehydration and cyclization of the intermediate. Is required for the biosynthesis of pyrrolysine. SIMILARITY: Belongs to the PylD family.


FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins. Also able to mediate N-terminal lysine myristoylation of proteins: catalyzes myristoylation of ARF6 on both 'Gly-2' and 'Lys-3'. Lysine myristoylation is required to maintain ARF6 on membranes during the GTPase cycle. SUBCELLULAR LOCATION: Cytoplasm Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the NMT family.


FUNCTION: This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. FUNCTION: This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. SIMILARITY: Belongs to the annexin family.


FUNCTION: Downstream effector for rab11. May be involved in vesicle recycling (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, perinuclear region. Endosome membrane. Golgi apparatus, trans-Golgi network.


FUNCTION: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme (By similarity). FUNCTION: Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, Cajal body Note=Also localized to Cajal bodies (coiled bodies). SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, Cajal body Note=Also localized to Cajal bodies (coiled bodies). SIMILARITY: Belongs to the NOP10 family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the teretoxin A (TA) superfamily.


FUNCTION: Component of the transition zone in primary cilia. Required for ciliogenesis. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein Cell projection, cilium Note=Localizes at the proximal region of primary cilia were observed, consistent with localization to the transition zone. SIMILARITY: Belongs to the TMEM237 family.


FUNCTION: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of neosartoricin, a prenylated anthracenone that exhibits T-cell antiproliferative activity, suggestive of a physiological role as an immunosuppressive agent (PubMed:23758576, PubMed:23368997). The non-reducing polyketide synthase nscA probably synthesizes and cyclizes the decaketide backbone (PubMed:23368997). The hydrolase nscB then mediates the product release through hydrolysis followed by spontaneous decarboxylation (PubMed:23368997). The prenyltransferase nscD catalyzes the addition of the dimethylallyl group to the aromatic C5 (PubMed:23368997). The FAD-dependent monooxygenase nscC is then responsible for the stereospecific hydroxylation at C2 (PubMed:23368997). There is no gene encoding O-acetyltransferase in the nsc gene cluster; thus, the last step of 2-O-acetylation leading to neosartoricin may be catalyzed by an unidentified O-acetyltransferase (PubMed:23368997). SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.


FUNCTION: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid- beta precursor protein) (PubMed:10993067, PubMed:12679784, PubMed:25043039, PubMed:26280335, PubMed:30598546, PubMed:30630874). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels. SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein Cytoplasmic vesicle membrane; Single-pass type I membrane protein Melanosome Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. SIMILARITY: Belongs to the nicastrin family.


FUNCTION: Catalyzes the oxidative deamination and cyclization of 2- amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3- dehydroquinate (DHQ), which is fed into the canonical shikimic pathway of aromatic amino acid biosynthesis. SIMILARITY: Belongs to the archaeal-type DHQ synthase family.


FUNCTION: Component of the chloroplast ribosome (chloro-ribosome), a dedicated translation machinery responsible for the synthesis of chloroplast genome-encoded proteins, including proteins of the transcription and translation machinery and components of the photosynthetic apparatus. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL11 family.


FUNCTION: Beta-glucosidase acting poorly on artificial aryl beta- glucosides. Has no activity toward the chromogenic substrate 6-bromo-2- naphthyl-beta-D-glucoside (6BNGlc). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the glycosyl hydrolase 1 family.


FUNCTION: General factor that plays a major role in the activation of eukaryotic genes transcribed by RNA polymerase II. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFIIB family.


FUNCTION: Negative regulator of the mitotic exit network (MEN), required for multiple cell cycle checkpoints. Required for daughter cell separation and chromosome stability. Involved in copper sensitivity. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the AMN1 family.


FUNCTION: Responsible for the transport of dicarboxylates such as succinate, fumarate, and malate from the periplasm across the inner membrane. FUNCTION: Responsible for the transport of dicarboxylates such as succinate, fumarate, and malate from the periplasm across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family.


FUNCTION: Palmitoyl acyltransferase. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family.


FUNCTION: May participate in chromosomal partitioning during cell division. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ScpB family.


FUNCTION: Snake venom serine protease that has fibrinogenolytic activities. Preferentially cleaves the Bbeta-chain (FGB) and more slowly the Aa-chain (FGA) of fibrinogen, but does not affect the gamma- chain. Has also fibrinolytic activity. May play a role in antithrombotic reaction as well as thrombolytic reaction. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family. Snake venom subfamily.


FUNCTION: Involved in the degradation of L-fucose and D-arabinose (PubMed:13898172). Catalyzes the reversible cleavage of L-fuculose 1- phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L- lactaldehyde (PubMed:13898172, Ref.8, Ref.9, PubMed:10821675, PubMed:11054289). Also able to catalyze the reversible cleavage of D- ribulose 1-phosphate, but FucA has a higher affinity for L-fuculose 1- phosphate and L-lactaldehyde than for D-ribulose 1-phosphate and glycolaldehyde, respectively (PubMed:4928018). FucA possesses a high specificity for the dihydroxyacetone phosphate (DHAP), but accepts a great variety of different aldehydes and has a strong preference for L- configurated alpha-hydroxy aldehydes (PubMed:13898172, Ref.8, PubMed:10821675). FucA generates a vicinal diol unit having the absolute (3R,4R)-cis configuration (D-erythro) (Ref.8, PubMed:10821675). FUNCTION: Involved in the degradation of L-fucose and D-arabinose. Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and L-lactaldehyde. SIMILARITY: Belongs to the aldolase class II family. AraD/FucA subfamily. SIMILARITY: Belongs to the aldolase class II family. AraD/FucA subfamily.


FUNCTION: Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DsbB family.


FUNCTION: May initiate with G9P the virion concomitant assembly-budding process, by interacting with the packaging signal of the viral genome. The assembly-budding takes place at the host inner membrane. In turn, G7P and G9P are present at the end of the filamentous virion that emerges first from the bacterial host (By similarity). SUBCELLULAR LOCATION: Virion Host membrane; Single-pass membrane protein Note=Prior to assembly, is found associated with the bacterial host inner membrane. There are about five copies of this protein per mature phage that are located on the tail side of the filamentous virion with G9P (By similarity). SIMILARITY: Belongs to the inovirus G7P protein family.


FUNCTION: Involved in the differentiation of haploid spermatids.


FUNCTION: Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant cellulose synthase-like E subfamily.


FUNCTION: Required for early embryogenesis and tissue differentiation. Required for pre-mRNA splicing and for exon-junction complex (EJC) assembly. Hinders EIF4A3 from non-specifically binding RNA and escorts it to the splicing machinery to promote EJC assembly on mature mRNAs. Through its role in EJC assembly, required for nonsense-mediated mRNA decay (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus speckle. SIMILARITY: Belongs to the CWC22 family.


FUNCTION: Is responsible for Site-2 cleavage of the RsiW anti-sigma factor. This results, after a third proteolytic step catalyzed by the ClpXP protease, in the release of SigW and the transcription activation of the genes under the control of the sigma-W factor (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the peptidase M50B family.


FUNCTION: Contributes to the release of free fatty acids from fatty acid synthase (FASN). Has broad substrate specificity, giving rise to a range of free fatty acids with chain lengths between 10 and 16 carbon atoms (C10 - C16). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the thioesterase family.


FUNCTION: UDP-D-glucuronate 4-epimerase involved in the synthesis of the negatively charged monosaccharide that forms the backbone of pectic cell wall components. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family.


SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SNURF family.


FUNCTION: Catalyzes the reversible dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA. SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.


FUNCTION: Disease resistance (R) protein that induces localized, salicylic acid-dependent defenses (PubMed:11141561). Confers resistance to powdery mildew (e.g. Erysiphe cichoracearum UCSC1) (PubMed:11141561, PubMed:15155802, PubMed:17565954). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the plant RPW8 protein family.


FUNCTION: Has 5'-3' exonuclease activity and no 3'-5' exonuclease activity. SIMILARITY: Belongs to the DNA polymerase type-A family.


FUNCTION: Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon- carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). FUNCTION: Involved in the final reduction of the elongation cycle of fatty acid synthesis (FAS II). Catalyzes the reduction of a carbon- carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). SIMILARITY: Belongs to the TER reductase family.


FUNCTION: Lipase that primarily hydrolyzes triglycerides and galactosylglycerides (PubMed:8656075, PubMed:9822688). In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides (By similarity). Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity (PubMed:8656075). Can completely deacylate triacylglycerols (By similarity). When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase (By similarity). Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids (By similarity). Hydrolyzes medium- and long-chain fatty acyls in galactolipids (PubMed:9822688). May act together with LIPF to hydrolyze partially digested triglycerides (By similarity). Hydrolyzes long-chain monoglycerides with high efficiency. In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity). Also has low phospholipase activity (PubMed:8656075, PubMed:9822688). In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (PubMed:32963038). The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (PubMed:32963038). SUBCELLULAR LOCATION: Secreted Zymogen granule membrane; Peripheral membrane protein Cell projection, neuron projection Note=Localizes to neurite tips in neuronal cells. SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.


FUNCTION: Interconversion of serine and glycine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SHMT family.


SIMILARITY: Belongs to the triosephosphate isomerase family.


FUNCTION: Mediates positive regulation of the ptsG/glcA and glcB genes by functioning as an antiterminator factor of transcription via its interaction with the RNA-antiterminator (RAT) sequence located upstream of the ptsG/glcA gene. SIMILARITY: Belongs to the transcriptional antiterminator BglG family. GlcT subfamily.


FUNCTION: Plays a role in normal growth and development. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Mainly localizes to the nucleus.


FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Mediates the polyubiquitination and proteasomal degradation of CAMK1 leading to disruption of cyclin D1/CDK4 complex assembly which results in G1 cell cycle arrest in lung epithelia (By similarity).


FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reduction of methionine sulfoxide in proteins to methionine (PubMed:12145281, PubMed:30529269). Does not catalyze the reverse reaction involving the oxidation of methionine residues (PubMed:30529269). SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.


FUNCTION: May play a role in cell protection during the inflammatory response. In epithelial cells, negatively regulates IL6 production and apoptosis through the regulation of MT2A expression. SIMILARITY: Belongs to the EOLA family.


FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Involved in the maintenance of mitochondrial (mtDNA). Required for both repair of mitochondrial DNA and recognition of a recombinogenic signal characterized by a 26-bp palindromic at sequence in the ery region of mitochondrial DNA. May have a general role in chromosomal replication by affecting Okazaki fragment maturation. Required for the completion of S-phase. SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion. SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus, nucleolus Note=Mainly concentrated in the nucleolus, and occasionally redistributes to single nuclear foci outside the nucleolus, probably sites of DNA repair. SIMILARITY: Belongs to the helicase family. PIF1 subfamily.


FUNCTION: Has antibacterial activity against Gram-positive bacteria B.subtilis ATCC 6633, L.garvieae ATCC 49156 and S.iniae F-8502, and Gram-negative bacteria E.coli WT-2, V.anguillarum ATCC 19264, V.penaeicida KHA, V.harveyi ATCC 14126, V.vulnificus ATCC 33148 and A.salmonicida NCMB 1102. Has hemolytic activity against human red blood cells. Seems to disrupt the membranes by adopting an alpha helical conformation. May play a significant role in innate host defense. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the pleurocidin family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA5 subfamily.


FUNCTION: Substrate-specific adapter for an E3 ubiquitin-protein ligase complex. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Required for genome encapsidation. Forms ribonucleoprotein complexes along with TGB1 helicase and viral RNA. SUBCELLULAR LOCATION: Virion. SIMILARITY: Belongs to the potexvirus capsid protein family.


FUNCTION: Adapter protein, which negatively regulates T-cell receptor (TCR) signaling. Inhibits T-cell antigen-receptor induced activation of nuclear factor of activated T-cells. May act by linking signaling proteins such as ZAP70 with CBL, leading to a CBL dependent degradation of signaling proteins. SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane. Cytoplasmic vesicle. Note=Localized to the plasma membrane and intracellular vesicles, including late endosomal vesicles. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm Note=May be cytoplasmic and is not localized to membranes.


FUNCTION: Key component of innate and adaptive immunity. TLRs (Toll- like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endosome membrane Early endosome. SIMILARITY: Belongs to the Toll-like receptor family.


FUNCTION: This enzyme catalyzes the hydrogen sulfide production from sulfite. It is strictly anaerobic. It is regulated by electron acceptors rather than by cysteine (By similarity). FUNCTION: This enzyme catalyzes the hydrogen sulfide production from sulfite. It is strictly anaerobic. It is regulated by electron acceptors rather than by cysteine. SUBCELLULAR LOCATION: Cytoplasm. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.


FUNCTION: Probable transcription factor which is required for asymmetric division of vulval blast cells (PubMed:1970421, PubMed:15466489). Involved in olfactory plasticity probably by regulating the expression of transcription factor mbr-1 in RIF neurons (PubMed:19561603). Plays a role in the chemorepulsive response toward ascaroside pheromones mediated by the ADL sensory neurons, probably by regulating E-box motif 5'-CANNTG-3' containing target genes in the ADL neurons (PubMed:29672507). Plays a role in the differentiation of the ADL sensory neurons (PubMed:29672507). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein pab1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by xrn1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. pan3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit pan2 to mRNA via its interaction with RNA and with pab1. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. PAN3 family.


SIMILARITY: Belongs to the bymoviruses polyprotein 2 family.


FUNCTION: Possibly involved in structural functions as organizing other membrane components or in targeting the vesicles to the plasma membrane (By similarity). Involved in the regulation of short-term and long-term synaptic plasticity. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Multi-pass membrane protein Synapse, synaptosome. SIMILARITY: Belongs to the synaptophysin/synaptobrevin family.


FUNCTION: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. SUBCELLULAR LOCATION: Golgi apparatus. SIMILARITY: Belongs to the small GTPase superfamily. Arf family.


FUNCTION: Catalyzes the conversion of the important environmental pollutant gamma-hexachlorocyclohexane (gamma-HCH or lindane) to 1,3,4,6-tetrachloro-1,4-cyclohexadiene (1,4-TCDN) via gamma- pentachlorocyclohexene (gamma-PCCH) (PubMed:12450824). Proceeds by two successive 1,2-anti conformationally dependent dehydrochlorinations (By similarity). Also shows activity with alpha- and delta-HCH, giving alpha- and delta-PCCH respectively, but not with the beta isomer (PubMed:12450824). FUNCTION: Catalyzes the conversion of the important environmental pollutant gamma-hexachlorocyclohexane (gamma-HCH or lindane) to 1,3,4,6-tetrachloro-1,4-cyclohexadiene (1,4-TCDN) via gamma- pentachlorocyclohexene (gamma-PCCH), proceeding by two successive 1,2- anti conformationally dependent dehydrochlorinations (PubMed:11099497). Also shows activity with alpha- and delta-HCH, giving alpha- and delta- PCCH respectively, but not with the beta isomer (Ref.6). Is involved in the degradation pathway that allows S.japonicum UT26 to grow on gamma- HCH as the sole source of carbon and energy (PubMed:7686793). SUBCELLULAR LOCATION: Periplasm. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the HCH dehydrochlorinase family.


FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity). Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically. Binds to both single-stranded guanine- and cytosine-rich strands within the nuclease hypersensitive element (NHE) III(1) region of the MYC gene promoter. Does not bind to duplex NHE III(1). Has G-quadruplex (G4) DNA-binding activity, which is independent of its nucleotide-binding and kinase activity. Binds both folded and unfolded G4 with similar low nanomolar affinities. Stabilizes folded G4s regardless of whether they are prefolded or not. Exhibits histidine protein kinase activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell projection, lamellipodium Cell projection, ruffle Nucleus Note=Colocalizes with ITGB1 and ITGB1BP1 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen but not on vitronectin or laminin substrates. SIMILARITY: Belongs to the NDK family.


FUNCTION: Sialidases have been suggested to be pathogenic factors in microbial infections. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycosyl hydrolase 33 family.


FUNCTION: Probable ATP-dependent RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Involved in the secondary piRNAs metabolic process, the production of piRNAs in fetal male germ cells through a ping-pong amplification cycle. SUBCELLULAR LOCATION: Cytoplasm Note=Component of the meiotic nuage, also named P granule, a germ-cell- specific organelle required to repress transposon activity during meiosis. SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA subfamily.


FUNCTION: Functions as transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain (By similarity). Appears to function in modulating the activity of the immune system during the acute-phase reaction. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.


FUNCTION: Glycolytic enzyme the catalyzes the conversion of 2- phosphoglycerate to phosphoenolpyruvate. In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production. SUBCELLULAR LOCATION: Cytoplasm Cell membrane Note=Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is localized to the M-band. SIMILARITY: Belongs to the enolase family.


FUNCTION: Alpha-1,2-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth mannose to trimannosyl-GPIs during GPI precursor assembly. The presence of a fourth mannose in GPI is essential in fungi (By similarity). SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGZ subfamily.


FUNCTION: Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, proton, potassium, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as a uniporter which transports preferentially L-glutamate but also, phosphate from the cytoplasm into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. The L-glutamate or phosphate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane. In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane therefore affects the proton electrochemical gradient and promotes synaptic vesicles acidification. Moreover, functions as a vesicular K(+)/H(+) antiport allowing to maintain the electrical gradient and to decrease chemical gradient and therefore sustain vesicular L-glutamate uptake. The vesicular H(+)/H(+) antiport activity is electroneutral. At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation. The symporter activity is driven by an inside negative membrane potential and is electrogenic (By similarity). Also involved in the regulation of retinal hyaloid vessel regression during postnatal development (By similarity). May also play a role in the endocrine L-glutamatergic system of other tissues such as pineal gland and pancreas (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane Membrane; Multi-pass membrane protein Synapse, synaptosome Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion cotransporter family. VGLUT subfamily.


FUNCTION: Transcription factor involved in unfolded protein response (UPR). In the absence of endoplasmic reticulum (ER) stress, inserted into ER membranes, with N-terminal DNA-binding and transcription activation domains oriented toward the cytosolic face of the membrane. In response to ER stress, transported to the Golgi, where it is cleaved in a site-specific manner by resident proteases S1P/mbtps1 and S2P/mbtps2. The released N-terminal cytosolic domain is translocated to the nucleus to effect transcription of specific target genes. Plays a critical role in chondrogenesis. May protect neuroblastoma cells from ER stress-induced death. In vitro activates transcription of target genes via direct binding to the CRE site. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein Note=ER membrane resident protein. Upon ER stress, translocated to the Golgi apparatus where it is cleaved. The cytosolic N-terminal fragment (processed cyclic AMP-responsive element- binding protein 3-like protein 1) is transported into the nucleus. SUBCELLULAR LOCATION: [Processed cyclic AMP-responsive element-binding protein 3-like protein 2]: Nucleus Note=Upon ER stress, translocated into the nucleus. SIMILARITY: Belongs to the bZIP family. ATF subfamily.


FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Negatively regulates cilium formation and structure. SUBCELLULAR LOCATION: Nucleus Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Cytoplasm, cytoskeleton, microtubule organizing center Note=Enriched at the centrosomes during mitosis. Enriched in centrioles of microtubule asters during prophase, prometaphase and telophase stages of mitosis (By similarity). Localized at centrioles and in the nucleus at interphase (By similarity). Colocalizes with nubp-1 at prometaphase (By similarity). SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP2/CFD1 subfamily.


FUNCTION: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano- cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the chaperonin (HSP60) family.


FUNCTION: Plays an essential role in viral DNA replication by acting as the polymerase accessory subunit. Associates with the viral polymerase to increase its processivity and forms high-affinity direct interactions with DNA. Facilitates the origin-binding protein loading onto DNA thus increasing its ability to assemble into a functional complex capable of unwinding duplex DNA (By similarity). SUBCELLULAR LOCATION: Host nucleus. SIMILARITY: Belongs to the herpesviridae DNA polymerase processivity factor family.


FUNCTION: NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors (By similarity). Participates in the modulation of multiple and diverse biological processes such as cell cycle control, genomic integrity, microtubule dynamics, cell differentiation, metabolic networks, and autophagy. Plays a major role in the control of cell cycle progression and genomic stability. Deacetylates histone H4 at 'Lys-16' (H4K16ac) at the VEGFA promoter (PubMed:24940000). Thereby contributes to regulate expression of vegfa, a key regulator of angiogenesis (PubMed:24940000). In addition to protein deacetylase activity, also has activity toward long-chain fatty acyl groups and mediates protein-lysine demyristoylation and depalmitoylation of target proteins (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the sirtuin family. Class I subfamily.


FUNCTION: Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy (By similarity). Required for both micropexophagy and macropexophagy, but not for the cytoplasm to vacuole transport (Cvt) or autophagy pathways (By similarity). Required for functional micropexophagic apparatus (MIPA) and relocation of ATG11 to the peroxisome-sequestering arms of the vacuole (By similarity). Binds palmytoyl-CoA but not oleyl-CoA (By similarity). SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane protein. SIMILARITY: Belongs to the ATG37 family.


SIMILARITY: Belongs to the UPF0690 family.


FUNCTION: Has an extremely high oxygen affinity. In a vacuum, it takes several minutes to release its oxygen compared to milliseconds for a normal globin. Could be used as an oxygen scavenger for sterol biosynthesis. SUBCELLULAR LOCATION: Secreted, extracellular space. SIMILARITY: Belongs to the globin family.


FUNCTION: Catalyzes the addition of a single glycerol phosphate residue to the prenoldiphosphate-linked disaccharide, as a primer for polymerisation by TagF. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the CDP-glycerol glycerophosphotransferase family.


FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=May not reach the plasma membrane but remain in an intracellular compartment in the absence of KCNB1 or KCNB2. SIMILARITY: Belongs to the potassium channel family. S (TC 1.A.1.2) subfamily. Kv9.2/KCNS2 sub-subfamily.


FUNCTION: Transcription factor that plays a central role in developing and mature glia (By similarity). Specifically activates expression of myelin genes, during oligodendrocyte (OL) maturation, such as DUSP15 and MYRF, thereby playing a central role in oligodendrocyte maturation and CNS myelination (By similarity). Once induced, MYRF cooperates with SOX10 to implement the myelination program (By similarity). Transcriptional activator of MITF, acting synergistically with PAX3 (PubMed:21965087). Transcriptional activator of MBP, via binding to the gene promoter (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the venom protein 11 family. 02 (wap-2) subfamily.


FUNCTION: May be required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus (By similarity). Involved in vesicle fusion with nsfA and probably SNARE proteins. SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein. SIMILARITY: Belongs to the SNAP family.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ycf72 family.


FUNCTION: Catalyzes the hydrolysis of phosphatidylinositol-4,5- bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate (PtdIns-4-P) (By similarity). Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5- monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate (By similarity). Negatively regulates the phagocytosis of large particles by reducing phagosomal phosphatidylinositol 4,5-bisphosphate accumulation during cup formation (By similarity). SUBCELLULAR LOCATION: Late endosome membrane; Multi-pass membrane protein Lysosome membrane; Multi- pass membrane protein Cytoplasmic vesicle, phagosome membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein.


FUNCTION: Secreted effector that completely suppresses elicitor-induced cell death in host and enhances virulence of P.parasitica. SUBCELLULAR LOCATION: Secreted Host cell. SIMILARITY: Belongs to the RxLR effector family.


FUNCTION: Binds both saxitoxin and tetradotoxin. May play a role in toxin accumulation and/or excretion. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Antiporter that transports inorganic anions (sulfate, sulfite, thiosulfate and phosphate) and, to a lesser extent, a variety of dicarboxylates (e.g. malonate, malate and citramalate) and, even more so, aspartate. The sulfate/sulfate exchange is much higher than the phosphate/phosphate and malate/malate exchanges. The transport affinities is higher for sulfate and thiosulfate than for any other substrate. May catalyze the export of sulfite and thiosulfate (the hydrogen sulfide degradation products) from the mitochondria, thereby modulating the level of the hydrogen sulfide. Also may mediate a very low unidirectional transport of sulfate. FUNCTION: Probable transporter. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.


FUNCTION: Dual function macrocyclase-peptidase involved in the biosynthesis of the highly toxic amanitin toxin family of macrocycles (PubMed:22202811, PubMed:28866879, PubMed:29051530). Cleaves peptide bonds on the C-terminal side of prolyl residues (PubMed:29051530). The enzyme first removes 10 residues from the N-terminus of a 35-residue substrate (PubMed:29051530). Conformational trapping of the 25 amino- acid peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (PubMed:29051530). The enzyme rebinds the 25 amino-acid peptide in a different conformation and catalyzes macrocyclization of the N-terminal eight residues (PubMed:28866879, PubMed:29051530). SIMILARITY: Belongs to the peptidase S9A family.


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


FUNCTION: N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN) (PubMed:11106397, PubMed:12496260). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments (PubMed:12496260). Has no direct bacteriolytic activity (PubMed:12496260). FUNCTION: N-acetylmuramyl-L-alanine amidase involved in innate immunity by degrading bacterial peptidoglycans (PGN). Plays a scavenger role by digesting biologically active PGN into biologically inactive fragments. Has no direct bacteriolytic activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.


FUNCTION: Has no ubiquitin ligase activity on its own. The heterodimer with UBC catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. May play a role in the control of progress through the cell cycle and differentiation. Involved in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.


FUNCTION: In the production of energy from fats, this is one of the enzymes that catalyzes the last step of the mitochondrial beta- oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA. Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain unbranched 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms. Also catalyzes the condensation of two acetyl-CoA molecules into acetoacetyl-CoA and could be involved in the production of ketone bodies. Also displays hydrolase activity on various fatty acyl-CoAs (By similarity). Thereby, could be responsible for the production of acetate in a side reaction to beta- oxidation (By similarity). Abolishes BNIP3-mediated apoptosis and mitochondrial damage (By similarity). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.


FUNCTION: Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. SUBCELLULAR LOCATION: Secreted Host cell Note=Secreted via type III secretion system 1 (SPI-1 TTSS), and delivered into the host cell. SIMILARITY: Belongs to the SopA E3 ligase family.


FUNCTION: Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing formation of DNA:RNA hybrids behind the elongating polymerase. It functions in cotranscriptional formation of an export- competent messenger ribonucleoprotein particle (mRNP) by facilitating the loading of ATP-dependent RNA helicase SUB2 and the mRNA export factor YRA1 along the nascent mRNA. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Isoform 1 transcriptionally activates the LYN and BLK promoters and acts synergistically with RUNX1 to transactivate the BLK promoter. FUNCTION: Isoform 2 may function in repression of RUNX1-mediated transactivation. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ETS family.


FUNCTION: Shows excitatory effect on mice by intracranial injection, followed by rigid paralysis of the rear legs and recovering after 30 min. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin M superfamily.


SIMILARITY: Belongs to the orthopoxvirus OPG159 protein family.


FUNCTION: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the insect chemoreceptor superfamily. Heteromeric odorant receptor channel (TC 1.A.69) family. Or67d subfamily.


FUNCTION: Probably contributes to terminal cornification. SIMILARITY: Belongs to the intermediate filament family.


FUNCTION: Trichothecene C-15 hydroxylase; part of the core gene cluster that mediates the biosynthesis of trichothecenes, a very large family of chemically related bicyclic sesquiterpene compounds acting as mycotoxins, including T2-toxin (PubMed:11352533, PubMed:9435078). The biosynthesis of trichothecenes begins with the cyclization of farnesyl diphosphate to trichodiene and is catalyzed by the trichodiene synthase TRI5 (PubMed:3800398). Trichodiene undergoes a series of oxygenations catalyzed by the cytochrome P450 monooxygenase TRI4 (PubMed:7651333). TRI4 controls the addition of four oxygens at C-2, C-3, C-11, and the C-12, C-13-epoxide to form the intermediate isotrichotriol (PubMed:16917519). Isotrichotriol then undergoes a non-enzymatic isomerization and cyclization to form isotrichodermol (PubMed:2317042). During this process, the oxygen at the C-2 position becomes the pyran ring oxygen and the hydroxyl group at C-11 is lost (PubMed:2317042). More complex type A trichothecenes are built by modifying isotrichodermol through a series of paired hydroxylation and acetylation or acylation steps (PubMed:11352533). Isotrichodermol is converted to isotrichodermin by the acetyltransferase TRI101 (PubMed:10583973). TRI101 encodes a C-3 transacetylase that acts as a self-protection or resistance factor during biosynthesis and that the presence of a free C-3 hydroxyl group is a key component of Fusarium trichothecene phytotoxicity (PubMed:10583973). A second hydroxyl group is added to C-15 by the trichothecene C-15 hydroxylase TRI11, producing 15-decalonectrin, which is then acetylated by TRI3, producing calonectrin (PubMed:9435078, PubMed:8593041). A third hydroxyl group is added at C-4 by the cytochrome P450 monooxygenase TRI13, converting calonectrin to 3,15-diacetoxyspirpenol, which is subsequently acetylated by the acetyltransferase TRI7 (PubMed:12135578, PubMed:11352533). A fourth hydroxyl group is added to C-8 by the cytochrome P450 monooxygenase TRI1, followed by the addition of an isovaleryl moiety by TRI16 (PubMed:12620849, PubMed:14532047). Finally, the acetyl group is removed from the C-3 position by the trichothecene C-3 esterase TRI8 to produce T-2 toxin (PubMed:12039755). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: May be a substrate targeting component of a cullin-RING-based E3 ubiquitin-protein ligase complex RTT101(MMS1-ESC2). Involved in HMR and telomere silencing via the recruitment or stabilizing of the SIR (silent information regulators) complex (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus.


FUNCTION: Controls the rotational direction of flagella during chemotaxis. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the FliL family.


FUNCTION: Catalyzes the methylation of the lipid moiety of the intermediate compounds phthiotriol and glycosylated phenolphthiotriol dimycoserosates to form phthiocerol dimycocerosates (DIM A) and glycosylated phenolphthiocerol dimycocerosates (PGL). SIMILARITY: Belongs to the methyltransferase superfamily. Phthiotriol/phenolphthiotriol dimycocerosates methyltransferase family.


FUNCTION: ATP-driven pump that supplies the Golgi apparatus with Ca(2+) and Mn(2+) ions, both essential cofactors for processing and trafficking of newly synthesized proteins in the secretory pathway. Within a catalytic cycle, acquires Ca(2+) or Mn(2+) ions on the cytoplasmic side of the membrane and delivers them to the lumenal side. The transfer of ions across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state. Induces Ca(2+) influx independently of its ATP-driven pump function. At the basolateral membrane of mammary epithelial cells, interacts with Ca(2+) channel ORAI1 and mediates Ca(2+) entry independently of the Ca(2+) content of endoplasmic reticulum or Golgi stores. May facilitate transepithelial transport of large quantities of Ca(2+) for milk secretion via activation of Ca(2+) influx channels at the plasma membrane and active Ca(2+) transport at the Golgi apparatus. SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Basolateral cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIA subfamily.


FUNCTION: Actin-bundling protein. When linked to F-actin the actin filaments form preferentially anti-parallel bundles that associate into meshworks. Plays a major role in cytokinesis (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the cortexillin family.


FUNCTION: ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates including 5-formyltetrahydrofolate and thiamine. Expression of the complex plus FolT or ThiT in Lactococcus lactis subsp. cremoris (strain NZ9000) allows 5-formyltetrahydrofolate or thiamine uptake respectively; 5-formyltetrahydrofolate or thiamine are not taken up in the absence of FolT/ThiT or the EcfA1A2T complex. Deenergized L.lactis subsp. cremoris (treated with 2-deoxyglucose) does not take up substrate. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Energy-coupling factor EcfA family.


SIMILARITY: Belongs to the glutamine synthetase family. Type 3 subfamily.


FUNCTION: Ion channel inhibitor. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 13 (insecticidal toxin ABC) family. ICK-21 subfamily.


FUNCTION: Monomer: The beta chain has no enzymatic activity and is not toxic by itself. FUNCTION: Heterotrimer: Snake venom phospholipase A2 (PLA2) that has presynaptic neurotoxicity. Inhibits nerve-evoked twitch contractions but not responses to cholinergic agonists acetylcholine and carbachol and to depolarizing agonist KCl. Causes a fade in tetanic contractions. Displays a triphasic mode of action with depression, enhancement and blockade of neurotransmission. Does not display myotoxic activity such as changes in baseline muscle tension or inhibition of directly stimulated muscle twitches. All subunits are necessary for maximum toxicity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the phospholipase A2 family. Group I subfamily.


FUNCTION: Transcription factor which plays a key role in defining the composition of the RNA polymerase II (RNAPII) elongation complex and in modulating the production of mature mRNA transcripts. Acts as an assembly factor to recruit various factors to the RNAPII elongation complex and is recruited to the complex via binding to the transcription elongation factor SUPT6H bound to the C-terminal domain (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone modifying enzymes (such as SETD2) to ensure proper mRNA splicing, efficient mRNA export and elongation-coupled H3K36 methylation, a signature chromatin mark of active transcription. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the IWS1 family.


FUNCTION: Efflux pump that might be required for efficient secretion of hypothemycin or other secondary metabolies produced by the hypothemycin gene cluster (PubMed:18567690). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet family.


FUNCTION: Inhibits protein synthesis in vitro. SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily.


FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase superfamily. OTCase family.


FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II LacEF PTS system is involved in lactose transport, but can also use galactose, isopropyl beta-thio-galactopyranoside and thiomethyl beta-D-galactopyranoside (TMG) as substrates. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.


SIMILARITY: Belongs to the FAM91 family.


SIMILARITY: Belongs to the WD repeat WDR55 family.


FUNCTION: Possible component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit D may have a function related to the maturation of the monooxygenase complex, rather than direct involvement in catalysis. PaaD could assist either in maturation of PaaE or PaaA.


FUNCTION: Major facilitator superfamily transporter that may be involved in A.fumigatus adaptation to azoles such as vorizonazole. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family.


FUNCTION: Cytoplasmic polyadenylation element binding protein that binds to and regulates the translation of specific mRNAs (By similarity). May not be required for oogenesis.


FUNCTION: Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Plays a role in the regulation of alternative splicing events. Binds G-rich sequences in pre-mRNAs and keeps target RNA in an unfolded state (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm. SUBCELLULAR LOCATION: Nucleus, nucleoplasm.


FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of ilicicolin H, a 4-hydroxy-2- pyridonealkaloid that has potent and broad antifungal activities by inhibiting the mitochondrial respiration chain (PubMed:34947016). IliC catalyzes the ring expansion of the tetramate intermediate to the acyclic 2-pyridone intermediate that contains the trans bis-diene chain (PubMed:34947016). The biosynthesis of ilicicolin H starts with formation of the tetramic acid by the hybrid PKS-NRPS synthetase iliA with the partnering trans-enoyl reductase iliB since iliA lacks a designated enoylreductase (ER) domain. The cytochrome P450 monooxygenase iliC then catalyzes the ring expansion of the tetramate to the acyclic 2-pyridone. The pericyclase iliD further converts the acyclic 2-pyridone into 8-epi-ilicicolin H. 8-epi-ilicicolin H might then spontaneously convert to ilicicolin H since ilicicolin H is produced in the absence of the epimerase iliE, in contrast to what was observed for the Talaromyces variabilis ilicolin H biosynthetic pathway (PubMed:34947016) (Probable). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Acts as a MYO6/Myosin VI adapter protein that targets myosin VI to endocytic structures (PubMed:23023224). May also play a role in recruiting clathrin to endosomes (PubMed:16412388). May regulate growth factor-induced mitogenic signaling (PubMed:16479011). SIMILARITY: Belongs to the TOM1 family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RER1 family.


FUNCTION: Involved in the export of PMA1, possibly through the monitoring or assisting of PMA1 folding and acquisition of competence to enter vesicles. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the SOP4 family.


FUNCTION: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. SIMILARITY: Belongs to the MICOS complex subunit Mic19 family.


FUNCTION: D-mannose-binding lectin which binds alpha-D-linked mannose (PubMed:10388566, PubMed:1874921, PubMed:14505313, PubMed:2350177, PubMed:1645507). Displays a high affinity for alpha-(1-6)-mannose oligomers (PubMed:2350177, PubMed:1645507). Able to interact with both terminal and internal alpha-D-mannosyl residues (PubMed:2350177). Displays antiviral activity and therefore may contribute to defense against infections (PubMed:1645507, PubMed:7481093). SUBCELLULAR LOCATION: Secreted.


FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) and its derivatives such as guanidinohydantoin:C and spiroiminodihydantoin:C, however it also acts on thymine glycol:G, 5,6-dihydrouracil:G and 5-hydroxyuracil:G. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Cleaves ssDNA containing an AP site. FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. SIMILARITY: Belongs to the FPG family. SIMILARITY: Belongs to the FPG family.


FUNCTION: Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation (By similarity). Methylates caffeoyl-CoA to feruloyl-CoA, also able to methylate 5-hydroxyferuloyl-CoA (PubMed:26620524). SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family. CCoAMT subfamily.


FUNCTION: ESCRT-III-like protein involved in cytokinesis, nuclear envelope reassembly and endosomal tubulation (By similarity). Is required for efficient abscission during cytokinesis (By similarity). Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells (By similarity). During late anaphase, involved in nuclear envelope reassembly and mitotic spindle disassembly together with the ESCRT-III complex: IST1 acts by mediating the recruitment of SPAST to the nuclear membrane, leading to microtubule severing (By similarity). Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2 (By similarity). Regulates early endosomal tubulation together with the ESCRT-III complex by mediating the recruitment of SPAST (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Midbody Nucleus envelope Note=Localizes to centrosome and midbody of dividing cells. Colocalized with SPART to the ends of Flemming bodies during cytokinesis. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase. SIMILARITY: Belongs to the IST1 family.


FUNCTION: Acts as a major beta-cyanoalanine synthase. The cyanoalanine synthesis reaction is more efficient than the cysteine synthase activity. Probably unable to interact with SAT and to form the decameric Cys synthase complex (CSC) and is therefore not an enzymatically true OASTL protein. Probably involved in the detoxification of cyanide that arises from ethylene biosynthesis. Maintains a low level of cyanide for proper root hair development. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the cysteine synthase/cystathionine beta- synthase family.


FUNCTION: One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light- induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PsbB/PsbC family. PsbB subfamily.


FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA. FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex) (PubMed:28781166). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA (PubMed:10523320). SUBCELLULAR LOCATION: Nucleus. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the snRNP Sm proteins family.


FUNCTION: Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, proton, potassium, sodium and phosphate. At the synaptic vesicle membrane, mainly functions as an uniporter which transports preferentially L-glutamate but also phosphate from the cytoplasm into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. The L-glutamate or phosphate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H(+)-ATPase across the synaptic vesicle membrane. In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane that affects the proton electrochemical gradient and promotes synaptic vesicles acidification. Moreover, may function as a K(+)/H(+) antiport allowing to maintain the electrical gradient and to decrease chemical gradient and therefore sustain vesicular glutamate uptake. The vesicular K(+)/H(+) antiport activity is electroneutral. At the plasma membrane, following exocytosis, functions as a symporter of Na(+) and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation. The symporter activity is driven by an inside negative membrane potential and is electrogenic (By similarity). Is necessary for synaptic signaling of visual-evoked responses from photoreceptors (By similarity). SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane Cell membrane; Multi-pass membrane protein Synapse, synaptosome. SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion cotransporter family. VGLUT subfamily.


FUNCTION: Functions as a calcium- and DAG-regulated nucleotide exchange factor specifically activating Rap through the exchange of bound GDP for GTP. May also activate other GTPases such as RRAS, RRAS2, NRAS, KRAS but not HRAS. Functions in aggregation of platelets and adhesion of T-lymphocytes and neutrophils probably through inside-out integrin activation. May function in the muscarinic acetylcholine receptor M1/CHRM1 signaling pathway. SUBCELLULAR LOCATION: Cytoplasm, cytosol Cell membrane; Peripheral membrane protein Synapse, synaptosome Cell projection, ruffle membrane; Peripheral membrane protein Note=Found both in the cytosol and associated with membranes. Enriched at juxtamembrane areas and membrane ruffles. Localizes to the cell bodies and axons of striatal neurons. SIMILARITY: Belongs to the RASGRP family.


FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 2 complex (dynein-2 complex), a motor protein complex that drives the movement of cargos along microtubules within cilia and flagella in concert with the intraflagellar transport (IFT) system. Required for proper retrograde ciliary transport. SUBCELLULAR LOCATION: Dynein axonemal particle. SIMILARITY: Belongs to the dynein light chain Tctex-type family.


FUNCTION: Required for the transport of GPI-anchored proteins to the plasma membrane. Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI- anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and is usually removed soon after the attachment of GPIs to proteins. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PIGW family.


FUNCTION: Inhibits coagulant activity in human plasma, possibly by interfering with one step of hemostasis (modulation of platelet aggregation, or coagulation cascade, for example) (Ref.1). Does not show fibrinogen-clotting activity and does not inhibit ADP-induced platelet aggregation (Ref.1). Also does not show hemorrhagic activity in mice (Ref.1). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the snaclec family.


FUNCTION: May increase cell susceptibility to TNF-induced apoptosis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein phosphatase inhibitor 1 family.


FUNCTION: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Allophycocyanin has a maximum absorption at approximately 650 nanometers. SUBCELLULAR LOCATION: Plastid, cyanelle thylakoid membrane; Peripheral membrane protein; Stromal side Note=Forms the core of the phycobilisome. SIMILARITY: Belongs to the phycobiliprotein family.


FUNCTION: Binds specifically to voltage-gated sodium channels (Nav), thereby delaying their inactivation during signal transduction. Causes death to crabs. SUBCELLULAR LOCATION: Secreted Nematocyst. SIMILARITY: Belongs to the sea anemone sodium channel inhibitory toxin family. Type I subfamily.


FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Dephosphorylates and activates transcription factor NFATC1. Dephosphorylates and inactivates transcription factor ELK1. Dephosphorylates DARPP32. SUBCELLULAR LOCATION: Mitochondrion Note=Localizes in the mitochondria in a SPATA33-dependent manner. SIMILARITY: Belongs to the PPP phosphatase family. PP-2B subfamily.


FUNCTION: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Also processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. May modulate key aspects of gene expression as its absence has extensive effects on the abundance of about 200 different transcripts. Probably processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the ribonuclease III family.