FUNCTION: Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family.


FUNCTION: Constitutive trypsin that is expressed 2 days after emergence, coinciding with host seeking behavior of the female. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S1 family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the teretoxin M (TM) superfamily.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TDA11 family.


FUNCTION: Involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I) (PubMed:18179882, PubMed:28853723). May be involved in cell proliferation and survival of hormone-dependent tumor cells. May be a regulator of breast tumor cell invasion. SUBCELLULAR LOCATION: Mitochondrion Membrane; Lipid-anchor. SIMILARITY: Belongs to the NDUFAF4 family.


FUNCTION: Induces relaxation of arterial smooth muscle, by targeting bradykinin receptors (BDKRB). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the bradykinin-related peptide family.


FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. SIMILARITY: Belongs to the ATP-dependent DNA ligase family.


FUNCTION: Trans-acting regulatory protein that activates transcription of the CUP1 gene (metallothionein) in response to copper ions. Binds to the CUP1 UAS sequence 5'-GCTTCTTTTCCGCTGA-3'. Binds DNA only in presence of copper or silver. Copper seems to alter the conformation of the protein. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Required for association of the cohesin complex with chromatin during interphase. Plays a role in sister chromatid cohesion and normal progression through prometaphase (By similarity). SUBCELLULAR LOCATION: Nucleus, nucleoplasm Note=Binds to chromatin from the end of mitosis until prophase. SIMILARITY: Belongs to the SCC4/mau-2 family.


SIMILARITY: Belongs to the arrestin family.


FUNCTION: Catalyzes the addition of alpha-(1->6)-mannose residue. SUBCELLULAR LOCATION: Membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the MptA/B family.


SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family.


FUNCTION: Catalyzes the decarboxylation of carboxynorspermidine and carboxyspermidine. Carboxynorspermidine is decarboxylated 20-fold more efficiently than carboxyspermidine. Exhibits some activity with L- ornithine, but shows no activity with L-arginine, L-lysine or meso- diaminopimelate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family. NspC subfamily.


FUNCTION: A putative methylase, recognizes the double-stranded sequence 5'-GGCC-3', methylates C-?. There is no known cognate restriction enzyme. FUNCTION: A methyltransferase that methylates C-1 within the sequences 5'-GGCC-3' and 5'-GCNGC-3' (PubMed:12654995). Modification confers resistance against restriction enzymes that recognize these sequences (Probable). SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.


FUNCTION: Binds to the SECIS element in the 3'-UTR of some mRNAs encoding selenoproteins. Binding is stimulated by SELB. SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion.


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


FUNCTION: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Localizes to the plus end of microtubules and to the centrosome. SIMILARITY: Belongs to the WD repeat LIS1/nudF family.


SIMILARITY: Belongs to the MCM family.


FUNCTION: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein component 3 family.


FUNCTION: Play a role in cell adhesion by regulating the plasma membrane localization of the palmitoyltransferase ZDHHC5. May be involved in protein transport from Golgi to cell surface. SUBCELLULAR LOCATION: Cell membrane Golgi apparatus membrane; Lipid-anchor. SIMILARITY: Belongs to the ERF4 family.


FUNCTION: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. SIMILARITY: Belongs to the NnrE/AIBP family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the bile acid:sodium symporter (BASS) (TC 2.A.28) family.


SIMILARITY: Belongs to the ubiquitin family.


FUNCTION: Transfers a sulfate group to the hydroxyl group at C3 of non- reducing beta-galactosyl residues. Acts both on type 1 (Gal-beta-1,3- GlcNAc) and type 2 (Gal-beta-1,4-GlcNAc) chains with similar efficiency (By similarity). SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the galactose-3-O-sulfotransferase family.


FUNCTION: Potent inhibitor of cellular proliferation. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side Nucleus, nucleolus Note=May cycle in and out of the nucleolus in a GTP- dependent manner. SIMILARITY: Belongs to the small GTPase superfamily. Ras family.


FUNCTION: Transcriptional repressor which forms a negative regulatory component of the circadian clock and acts independently of the circadian transcriptional repressors: CRY1, CRY2 and BHLHE41. In a histone deacetylase-dependent manner represses the transcriptional activator activity of the CLOCK-BMAL1 heterodimer. Abrogates the interaction of BMAL1 with the transcriptional coactivator CREBBP and can repress the histone acetyl-transferase activity of the CLOCK-BMAL1 heterodimer, reducing histone acetylation of its target genes. Rhythmically binds the E-box elements (5'-CACGTG-3') on circadian gene promoters and its occupancy shows circadian oscillation antiphasic to BMAL1. Interacts with the glucocorticoid receptor (NR3C1) and contributes to the repressive function in the glucocorticoid response (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus, PML body Note=Co-localizes with the CLOCK-BMAL1 heterodimer in the PML body.


SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the GPAT/DAPAT family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the carbamate kinase family.


FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Participates in pre-mRNA splicing. May play a role in the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome. May act as a chaperone. SUBCELLULAR LOCATION: Nucleus speckle Cytoplasm Note=Colocalizes with spliceosomal snRNPs. A small proportion may also be cytoplasmic (By similarity). SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase H subfamily.


FUNCTION: Sphingolipid transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Spinster (TC 2.A.1.49) family.


FUNCTION: A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-CAATTG-3' and cleaves after C-1.


FUNCTION: Receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI- anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections. May also control the segregation of motor and sensory axons during neuromuscular circuit development. In addition to its role in axonal guidance plays a role in synaptic plasticity. Activated by EFNA1 phosphorylates CDK5 at 'Tyr-15' which in turn phosphorylates NGEF regulating RHOA and dendritic spine morphogenesis. In the nervous system, also plays a role in repair after injury preventing axonal regeneration and in angiogenesis playing a role in central nervous system vascular formation. Additionally, its promiscuity makes it available to participate in a variety of cell-cell signaling regulating for instance the development of the thymic epithelium. During development of the cochlear organ of Corti, regulates pillar cell separation by forming a ternary complex with ADAM10 and CADH1 which facilitates the cleavage of CADH1 by ADAM10 and disruption of adherens junctions (By similarity). Phosphorylates CAPRIN1, promoting CAPRIN1-dependent formation of a membraneless compartment (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Cell projection, axon Cell projection, dendrite Postsynaptic density membrane Early endosome Cell junction, adherens junction Note=Clustered upon activation and targeted to early endosome. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the ycf76 family.


FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D- manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase family. HldD subfamily.


SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4 family.


FUNCTION: Removes 5-oxoproline from various penultimate amino acid residues except L-proline. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the peptidase C15 family.


FUNCTION: Binds 5S rRNA, forms part of the central protuberance of the 50S subunit. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uL5 family.


FUNCTION: Anion antiporter that mediates the transport of nicotinate (PubMed:35144162). Possibly involved in nicotinate intestinal reabsorption (By similarity). SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily. Organic cation transporter (TC 2.A.1.19) family.


FUNCTION: Involved in retinal laminar formation. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the FAM3 family.


FUNCTION: Is a substrate receptor for the CUL4-DDB1 E3 ubiquitin- protein ligase complex (CRL4) (PubMed:29691401, PubMed:30442713). The complex CRL4-DCAF5 is involved in the ubiquitination of a set of methylated non-histone proteins, including SOX2, DNMT1 and E2F1 (PubMed:29691401, PubMed:30442713).


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


FUNCTION: Involved in mitochondrial fission. Has a partially redundant function to CAF4 in acting as an adapter protein required to form mitochondrial fission complexes. Formation of these complexes is required to promote constriction and fission of the mitochondrial compartment at a late step in mitochondrial division (By similarity). SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the WD repeat MDV1/CAF4 family.


FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the SIS family. GmhA subfamily.


FUNCTION: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the ATPase A chain family.


FUNCTION: Hydrolyzes the galactose ester bonds of glycolipids such as galactosylceramide and galactosylsphingosine (PubMed:9192853). Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon (By similarity). SUBCELLULAR LOCATION: Lysosome. SIMILARITY: Belongs to the glycosyl hydrolase 59 family.


FUNCTION: Part of an ATP-driven transport system TP_0034/TP_0035/TP_0036 for a metal. Probably responsible for energy coupling to the transport system. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily.


FUNCTION: Promotes RNA polymerase assembly. Latches the N- and C- terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits. SIMILARITY: Belongs to the RNA polymerase subunit omega family.


FUNCTION: NAD(H)-dependent dehydrogenase/reductase with a preference for cyclic substrates (By similarity). Catalyzes stereoselective conversion of 4-oxo-L-proline to cis-4-hydroxy-L-proline, likely a detoxification mechanism for ketoprolines (By similarity). Mediates the formation of 2,5-dihydroxybenzoate (2,5-DHBA), a siderophore that chelates free cytoplasmic iron and associates with LCN2, thereby regulating iron transport and homeostasis while protecting cells against free radical-induced oxidative stress. The iron-siderophore complex is imported into mitochondria, providing an iron source for mitochondrial metabolic processes in particular heme synthesis (By similarity). May act as a 3-hydroxybutyrate dehydrogenase (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


SIMILARITY: Belongs to the class II ribonucleoside-triphosphate reductase family.


FUNCTION: Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner, facilitating the efficient association of RNA processing factors with their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which is thought to be involved in mRNA degradation by activating the decapping step in the 5'-to-3' mRNA decay pathway. Component of the nuclear LSM2- LSM8 complex, which is involved in splicing of nuclear mRNAs. LSM2-LSM8 associates with multiple snRNP complexes containing the U6 snRNA (U4/U6 di-snRNP, spliceosomal U4/U6.U5 tri-snRNP, and free U6 snRNP). It binds directly to the 3'-terminal U-tract of U6 snRNA and plays a role in the biogenesis and stability of the U6 snRNP and U4/U6 snRNP complexes. LSM2-LSM8 probably also is involved degradation of nuclear pre-mRNA by targeting them for decapping, and in processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6 subfamily.


FUNCTION: Xyloglucan acetyltransferase that catalyzes the acetylation of fucosylated Gal residues on xyloglucan side chains (PubMed:30083810). Predominantly catalyze 6-O-monoacetylation of Gal residues in the Fuc-Gal-Xyl trisaccharide side chains of xyloglucan oligomers (PubMed:30083810). Involved in xyloglucan specific O- acetylation in seeds (PubMed:22086088). SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the PC-esterase family. TBL subfamily.


FUNCTION: Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. SUBCELLULAR LOCATION: Plastid, cyanelle. SIMILARITY: Belongs to the universal ribosomal protein uS13 family.


FUNCTION: Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment. SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the RER1 family.


FUNCTION: Sugar transporter. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family.


FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha- ketoisovalerate to form ketopantoate. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the PanB family.


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: This protein is involved in positive regulation of the metabolism of sugars. SIMILARITY: Belongs to the ner transcriptional regulatory family.


FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit J family.


FUNCTION: Suggested to catalyze the deposition of the aromatic residues of suberin on the cell wall and thus play a role in cell-suberization. FUNCTION: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peroxidase family. Classical plant (class III) peroxidase subfamily.


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: Nucleus Cytoplasm. SIMILARITY: Belongs to the universal ribosomal protein uL5 family.


FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system which inhibits the post-segregational killing (PSK) of plasmid-free cells, also referred to as a plasmid addiction system. Binds to and blocks the activity of CcdB; will also remove bound CcdB protein from the CcdB-GyrA complex by forming a CcdA-CcdB complex, a process termed rejuvenation. Functions as a transcriptional corepressor for the ccdAB operon, repression also requires CcdB (By similarity). SIMILARITY: Belongs to the CcdA antitoxin family.


SIMILARITY: Belongs to the eukaryotic ribosomal protein eL39 family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutamine synthetase family.


FUNCTION: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: In the N-terminal section; belongs to the SecD/SecF family. SecD subfamily. SIMILARITY: In the C-terminal section; belongs to the SecD/SecF family. SecF subfamily.


FUNCTION: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of neosartoricin B, a prenylated anthracenone that probably exhibits T-cell antiproliferative activity, suggestive of a physiological role as an immunosuppressive agent (PubMed:23758576). The non-reducing polyketide synthase nscA probably synthesizes and cyclizes the decaketide backbone (By similarity). The hydrolase nscB then mediates the product release through hydrolysis followed by spontaneous decarboxylation (By similarity). The prenyltransferase nscD catalyzes the addition of the dimethylallyl group to the aromatic C5 (By similarity). The FAD-dependent monooxygenase nscC is then responsible for the stereospecific hydroxylation at C2 (By similarity). Neosartoricin B can be converted into two additional compounds neosartoricins C and D (By similarity). Neosartoricin C is a spirocyclic compound that is cyclized through the attack of C3 hydroxyl on C14, followed by dehydration (By similarity). On the other hand, neosartoricin D is a further cyclized compound in which attack of C2 on C14 in neosartoricin C results in the formation of the acetal- containing dioxabicyclo-octanone ring (By similarity). Both of these compounds are novel and possibly represent related metabolites of the gene cluster (By similarity). SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.


SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the MELT/VEPH family.


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


FUNCTION: Bidirectionally degrades single-stranded DNA into large acid- insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the XseB family.


FUNCTION: Shell component of a type 1 encapsulin nanocompartment in situ; its cargo protects against oxidative stress at low pH. In situ and in E.coli assembles into proteinaceous shells about 22 nm in diameter with 2.5 nm thick walls (PubMed:34751132, PubMed:24855650). Cargo proteins are targeted to the interior via their C-terminal extensions; empty intact shells can be isolated in E.coli in the absence of cargo protein. There are at least 4 possible cargo proteins, DyP (encoded in the same locus), FolB, BfrB and Rv1762c; DyP and Rv1762c have been identified in vivo (PubMed:24855650). Probably involved in protection against oxidative damage from the host immune response (Probable) (PubMed:34751132). A T-cell antigen found in bacterial culture cell filtrates, stimulates mouse immune response. Does not have detectable bacteriocin activity (PubMed:9596740). SUBCELLULAR LOCATION: Encapsulin nanocompartment Secreted Cell membrane; Peripheral membrane protein Note=Encapsulin microcompartments of this protein encapsulating DyP are found in situ (PubMed:34751132). Detected at low levels in short-term culture filtrate, the nanocompartment is very stable and may survive cell lysis, explaining its apparent secretion (PubMed:9596740) (Probable). Detected in infected host (mouse J774 cell line) exosomes (PubMed:20662102). SIMILARITY: Belongs to the encapsulin family. Family 1 subfamily.


FUNCTION: Defense against chitin-containing fungal pathogens. Shows activity on chitin, tetra-N-acetylglucosamine and chitosan. SUBCELLULAR LOCATION: Vacuole Note=Vacuolar and protoplast. SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily.


FUNCTION: Catalyzes the radical-mediated synthesis of 5-amino-5-(4- hydroxybenzyl)-6-(D-ribitylimino)-5,6-dihydrouracil from 5-amino-6-(D- ribitylamino)uracil and L-tyrosine. SIMILARITY: Belongs to the radical SAM superfamily. CofH family.


FUNCTION: Functions as an U snRNP-specific nuclear import adapter. Involved in the trimethylguanosine (m3G)-cap-dependent nuclear import of U snRNPs. Binds specifically to the terminal m3G-cap U snRNAs. SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Nucleoplasmic shuttling protein. Its nuclear import involves the nucleocytoplasmic transport receptor importin beta. It is re-exported to the cytoplasm by the XPO1-dependent nuclear export receptor pathway. SIMILARITY: Belongs to the snurportin family.


FUNCTION: May act as a transporter (By similarity). May be involved in establishing and maintaining the luminal fluid microenvironment. SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein Note=Apical membranes of organs. SIMILARITY: Belongs to the major facilitator superfamily. SLC46A family.


FUNCTION: Probable neurotoxin. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Part of the ABC transporter complex FetAB, which is probably involved in iron export and enhances resistance to H(2)O(2)-mediated oxidative stress. Probably responsible for the translocation of the substrate across the membrane. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0014 family.


FUNCTION: Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester (By similarity). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the polysaccharide lyase 3 family.


SIMILARITY: Belongs to the UPF0435 family.


FUNCTION: Part of a binding-protein-dependent transport system for a sugar. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.


FUNCTION: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins (also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase- independent and serine protease activity-dependent mechanism. Can antagonize antiapoptotic activity of th by directly inducing the degradation of th (By similarity). SUBCELLULAR LOCATION: Mitochondrion intermembrane space; Single-pass membrane protein Mitochondrion membrane; Single-pass membrane protein Note=Predominantly present in the intermembrane space. Released into the cytosol following apoptotic stimuli, such as UV treatment. The extramitochondrial protein does not diffuse throughout the cytosol but stays near the mitochondria. SIMILARITY: Belongs to the peptidase S1C family.


FUNCTION: Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover (By similarity). Ccr4 has 3'-5' RNase activity with a strong preference for polyadenylated substrates and also low exonuclease activity towards single-stranded DNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the CCR4/nocturin family.


FUNCTION: Converts Mg-protoporphyrin IX to Mg-protoporphyrin IX methylester using S-adenosyl-L-methionine as a cofactor. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. Magnesium protoporphyrin O-methyltransferase family.


FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation by repressing transcription of myocyte enhancer factors such as MEF2A, MEF2B and MEF2C. During muscle differentiation, it shuttles into the cytoplasm, allowing the expression of myocyte enhancer factors. Positively regulates the transcriptional repressor activity of FOXP3. Serves as a corepressor of RARA, causing its deacetylation and inhibition of RARE DNA element binding (By similarity). In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=In the nucleus, it associates with distinct subnuclear dot-like structures. Shuttles between the nucleus and the cytoplasm. In muscle cells, it shuttles into the cytoplasm during myocyte differentiation. The export to cytoplasm depends on the interaction with the 14-3-3 protein YWHAE and is due to its phosphorylation (By similarity). SIMILARITY: Belongs to the histone deacetylase family. HD type 2 subfamily.


FUNCTION: Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex. SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. SIMILARITY: Belongs to the SEC61-beta family.


FUNCTION: Essential transcriptional regulator necessary for development and differentiation of erythroid and megakaryocytic lineages. Alters histone methylation by recruiting histone methyltransferase to target genes promoters. Plays a role in heterochromatin formation. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1 subfamily.


FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen). SUBCELLULAR LOCATION: Secreted. Secreted, extracellular space. Secreted, extracellular space, extracellular matrix. SIMILARITY: Belongs to the fibrillar collagen family.


FUNCTION: Involved in nucleolar processing of pre-18S ribosomal RNA. SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the UTP14 family.


FUNCTION: Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to a single major terpene scaffold whose chemical structure is still unknown. SIMILARITY: Belongs to the trichodiene synthase family.


FUNCTION: Delta(9)-fatty acid desaturase that acts preferentially on palmitoyl-CoA (hexadecanoyl-CoA) producing the monounsaturated palmitoleoyl-CoA ((9Z)-hexadecenoyl-CoA), which can be elongated to (11Z)-octadecenoyl-CoA (the most abundant monounsaturated fatty acid in Caenorhabditis elegans phospholipids and triacylglycerols). Also acts on pentadecanoyl-CoA, heptadecanoyl-CoA and myristoyl-CoA (tetradecanoyl-CoA), the monounsaturated fatty acids (MUFAs) produced are further used as substrates to synthesize polyunsaturated fatty acids (PUFAs) by several other desaturases and elongases (PubMed:16839188, PubMed:10872837, PubMed:29237573). Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (By similarity). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fatty acid desaturase type 1 family.


FUNCTION: Required for the acetyl modification of the third sugar (glucose) of the octasaccharide subunit of succinoglycan (EPS I). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the acyltransferase 3 family.


FUNCTION: Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death (By similarity). SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the peptidase S10 family.


FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. May play a role in photoperiodic photoreception. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.


FUNCTION: Probable fucosyltransferase. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the glycosyltransferase 10 family.


FUNCTION: Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC), and serves as template for viral transcription and replication (By similarity). SUBCELLULAR LOCATION: Virion. Host cytoplasm. SIMILARITY: Belongs to the tenuiviruses nucleocapsid protein family.


FUNCTION: Transfers a fatty acid residue from the sn-1 position of a phospholipid to the N-linked hydroxyfatty acid chain on the proximal unit of lipid A or its precursors. SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the lipid A palmitoyltransferase family.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the complex I 20 kDa subunit family.


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. Bcr/CmlA family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0754 family.


FUNCTION: Essential cell division protein. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II membrane protein Note=Localizes to the division septum. SIMILARITY: Belongs to the FtsQ/DivIB family. FtsQ subfamily.


FUNCTION: Key oxidase enzyme in the biosynthesis of gibberellin that catalyzes the conversion of GA12 and GA53 to GA9 and GA20 respectively, via a three-step oxidation at C-20 of the GA skeleton, and GA25 is also formed as a minor product. GA53 is less effectively oxidized than GA12. SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase family. GA20OX subfamily.


FUNCTION: Dominant regulator of apoptotic cell death. The long form displays cell death repressor activity, whereas the short isoform promotes apoptosis. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis (By similarity). SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane protein Nucleus membrane; Single- pass membrane protein; Cytoplasmic side Mitochondrion matrix Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Cytoplasm, cytosol Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane Note=After neuronal stimulation, translocates from cytosol to synaptic vesicle and mitochondrion membrane in a calmodulin-dependent manner. SIMILARITY: Belongs to the Bcl-2 family.


FUNCTION: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates (PubMed:19073142, PubMed:19766732, PubMed:23416111, PubMed:24767988). Efficiently phosphorylates AMP and dAMP using ATP as phosphate donor, but phosphorylates only AMP when using GTP as phosphate donor (PubMed:19073142, PubMed:19766732, PubMed:23416111). Also displays broad nucleoside diphosphate kinase activity (PubMed:19073142, PubMed:19766732, PubMed:23416111). Plays a role in controlling cellular ATP levels by regulating phosphorylation and activation of the energy sensor protein kinase AMPK (PubMed:24767988, PubMed:26980435). Plays a protective role in the cellular response to oxidative stress (PubMed:19130895, PubMed:23474458, PubMed:26980435). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the adenylate kinase family. AK3 subfamily.


FUNCTION: Probably involved in intron recognition and spliceosome assembly. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the splicing factor SR family. RS2Z subfamily.


FUNCTION: The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Necessary for proper vacuole morphology. Plays an important role in osmotically-induced vacuole fragmentation. Required for cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy and starvation- induced autophagy. Involved in correct ATG9 trafficking to the pre- autophagosomal structure. Might also be involved in premeiotic DNA replication (By similarity). SUBCELLULAR LOCATION: Preautophagosomal structure membrane; Peripheral membrane protein Vacuole membrane; Peripheral membrane protein Endosome membrane; Peripheral membrane protein. SIMILARITY: Belongs to the WD repeat PROPPIN family.


SIMILARITY: Belongs to the PPR family. PCMP-E subfamily.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the bacterial ribosomal protein bL19 family.


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


FUNCTION: Global transcriptional repressor of the maltodextrin transport gene cluster (mdxE operon) and most likely of all genes encoding glycolytic enzymes. Acts by binding to the conserved TGM (Thermococcales-Glycolytic-Motif) sequences in their promoter region. Can also interact with non-TGM sequences. SIMILARITY: Belongs to the transcriptional regulator TrmB family.


FUNCTION: NTP-dependent helicase that catalyzes unidirectional unwinding of 3'tailed duplex RNAs and plays an important role during transcription of early mRNAs, presumably by preventing R-loop formation behind the elongating RNA polymerase. Might also play a role in the export of newly synthesized mRNA chains out of the core into the cytoplasm. Required for replication and propagation of viral particles (By similarity). SUBCELLULAR LOCATION: Virion. Note=Localizes to the virion core. SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.


SIMILARITY: Belongs to the UPF0147 family.


FUNCTION: Part of the yfcOPQRSUV fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes. Probably involved in the export and assembly of fimbrial subunits across the outer membrane. SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the fimbrial export usher family.


FUNCTION: Involved in spermatogenesis and sperm function. Plays a role in regulation of cell growth. Binds to double-stranded DNA and RNA. Binds most efficiently to poly(I:C) RNA than to poly(dI:dC) DNA. Binds also to single-stranded poly(G) RNA. Binds non-specifically to the mRNA PRM1 3'-UTR and adenovirus VA RNA (By similarity). SUBCELLULAR LOCATION: Cytoplasm Note=Microtubule- associated that localizes to the manchette in developing spermatids.


SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family.


FUNCTION: NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metabolism, apoptosis and autophagy. Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression. Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively. Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction. Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT). Component of the eNoSC (energy- dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Deacetylates 'Lys-266' of SUV39H1, leading to its activation. Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1. Deacetylates H2A and 'Lys-26' of H1-4. Deacetylates 'Lys-16' of histone H4 (in vitro). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression. Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting. Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1. Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2. This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response. Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence. Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I. Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability. Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation. Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis. Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing. Deacetylates RELA/NF-kappa- B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha. Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1. Deacetylates FOXO1 resulting in its nuclear retention and enhancement of its transcriptional activity leading to increased gluconeogenesis in liver. Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation. Involved in HES1- and HEY2-mediated transcriptional repression. In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62'. Deacetylates MEF2D. Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3. Represses HNF1A-mediated transcription. Required for the repression of ESRRG by CREBZF. Deacetylates NR1H3 AND NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteasomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed. Involved in lipid metabolism: deacetylates LPIN1, thereby inhibiting diacylglycerol synthesis. Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2. Deacetylates p300/EP300 and PRMT1. Deacetylates ACSS2 leading to its activation, and HMGCS1 deacetylation. Involved in liver and muscle metabolism. Through deacetylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletal muscle under low-glucose conditions and is involved in glucose homeostasis. Involved in regulation of PPARA and fatty acid beta-oxidation in liver. Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2. Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation. Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression. Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and facilitating recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2. Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN. Promotes DNA double-strand breaks by mediating deacetylation of SIRT6. Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling. Transcriptional suppression of TP73 probably involves E2F4 and PCAF. Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage. Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1. Catalyzes deacetylation of ERCC4/XPF, thereby impairing interaction with ERCC1 and nucleotide excision repair (NER). Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria. Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis. Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8. Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation. Proposed to play role in regulation of STK11/LBK1-dependent AMPK signaling pathways implicated in cellular senescence which seems to involve the regulation of the acetylation status of STK11/LBK1. Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear. In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation. Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation. Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability. Deacetylates MECOM/EVI1. Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization. During the neurogenic transition, represses selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation. Regulates the circadian expression of several core clock genes, including BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling. Deacetylates BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator. Deacetylates PER2, facilitating its ubiquitination and degradation by the proteasome. Protects cardiomyocytes against palmitate-induced apoptosis. Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity. Deacetylates PCK1 and directs its activity toward phosphoenolpyruvate production promoting gluconeogenesis. Involved in the CCAR2-mediated regulation of PCK1 and NR1D1. Deacetylates CTNB1 at 'Lys-49'. In POMC (pro-opiomelanocortin) neurons, required for leptin-induced activation of PI3K signaling. In addition to protein deacetylase activity, also acts as protein-lysine deacylase by mediating protein depropionylation and decrotonylation. Mediates depropionylation of Osterix (SP7). Catalyzes decrotonylation of histones; it however does not represent a major histone decrotonylase. Deacetylates SOX9; promoting SOX9 nuclear localization and transactivation activity. Involved in the regulation of centrosome duplication. Deacetylates CENATAC in G1 phase, allowing for SASS6 accumulation on the centrosome and subsequent procentriole assembly (By similarity). Deacetylates NDC80/HEC1 (By similarity). SUBCELLULAR LOCATION: Nucleus, PML body Cytoplasm Nucleus Note=Recruited to the nuclear bodies via its interaction with PML. Colocalized with APEX1 in the nucleus. May be found in nucleolus, nuclear euchromatin, heterochromatin and inner membrane (By similarity). Shuttles between nucleus and cytoplasm (By similarity). Colocalizes in the nucleus with XBP1 isoform 2 (By similarity). SIMILARITY: Belongs to the sirtuin family. Class I subfamily.


FUNCTION: May regulate the stability of some mitochondrial mRNA species. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the FAST kinase family.


FUNCTION: Involved in methylamine metabolism. Essential for the maturation of the beta subunit of MADH, presumably via a step in the biosynthesis of tryptophan tryptophylquinone (TTQ), the cofactor of MADH. SUBCELLULAR LOCATION: Periplasm.


FUNCTION: Converts palmitoyl-ACP to (4Z)-hexadec-4-enoyl-ACP by introduction of a cis double bond between carbons 4 and 5 of the acyl chain. SUBCELLULAR LOCATION: Plastid, chloroplast. Plastid. Note=In green tissue, found in chloroplasts. In non-photosynthetic tissue, found in plastids. SIMILARITY: Belongs to the fatty acid desaturase type 2 family.


SUBCELLULAR LOCATION: Cytoplasm Membrane Secreted Note=Predominantly found in association with the membrane fraction, but also located in the cytoplasm and in the supernatant. SIMILARITY: Belongs to the receptors of complement activation (RCA) family.


FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wyosine derivatives biosynthesis pathway. Probably methylates N-4 position of wybutosine-86 to produce wybutosine-72. SIMILARITY: Belongs to the TYW3 family.


FUNCTION: Required for cilia biogenesis and maintenance in the kidney, the lateral line organ and eye. Appears to function within the multiple intraflagellar transport complex B (IFT-B). SUBCELLULAR LOCATION: Nucleus Cell projection, cilium. SIMILARITY: Belongs to the CLUAP1 family.


FUNCTION: Adapter that links the PapG adhesin to the distal end of the tip fibrillum. PapF is required for the correct presentation of the adhesin at the distal end of the tip fibrillum. Pili are polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, and enable bacteria to colonize the epithelium of specific host organs. SUBCELLULAR LOCATION: Secreted. Fimbrium. Note=At the tip of the pili.


FUNCTION: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone (PubMed:23706169). The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non- reducing polyketide synthase pkfA (PubMed:22510154). Hydroxylation, methylation of one of the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E (PubMed:23706169). The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: May play a role during the beginning of fruiting.


SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. SIMILARITY: Belongs to the p35 lipoprotein family.


FUNCTION: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the SFT2 family.


FUNCTION: Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine > N- myristoylethanolamine > N-stearoylethanolamine > N-oleoylethanolamine > N-linoleoylethanolamine > N-arachidonoylethanolamine. SUBCELLULAR LOCATION: Lysosome Membrane; Peripheral membrane protein. SIMILARITY: Belongs to the acid ceramidase family.


FUNCTION: Activates expression of the rhaBAD and rhaT operons. SUBCELLULAR LOCATION: Cytoplasm.


SIMILARITY: Belongs to the ROK (NagC/XylR) family.


FUNCTION: Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L- methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5- carboxymethoxyuridine (cmo5U) at position 34 in tRNAs. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. CmoB family.


FUNCTION: Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released. SIMILARITY: In the C-terminal section; belongs to the MoeA family. SIMILARITY: In the N-terminal section; belongs to the MoaB/Mog family.


FUNCTION: [Delta-peptide]: Viroporin that permeabilizes mammalian cell plasma membranes. It acts by altering permeation of ionic compounds and small molecules. This activity may lead to viral enterotoxic activity. FUNCTION: [Small/secreted glycoprotein]: Seems to possess an anti- inflammatory activity as it can reverse the barrier-decreasing effects of TNF alpha. Might therefore contribute to the lack of inflammatory reaction seen during infection in spite the of extensive necrosis and massive virus production. Does not seem to be involved in activation of primary macrophages. Does not seem to interact specifically with neutrophils. SUBCELLULAR LOCATION: [Delta-peptide]: Secreted. SUBCELLULAR LOCATION: [Small/secreted glycoprotein]: Secreted. SIMILARITY: Belongs to the filoviruses glycoprotein family.


FUNCTION: May catalyze the ATP-dependent phosphorylation of lipids other than diacylglycerol (DAG). SIMILARITY: Belongs to the diacylglycerol/lipid kinase family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the glycoprotein hormones subunit beta family.


FUNCTION: Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU. SIMILARITY: Belongs to the heat shock protein 70 family.


FUNCTION: Synthesizes alpha-1,4-glucan chains using ADP-glucose. SIMILARITY: Belongs to the glycosyltransferase 1 family. Bacterial/plant glycogen synthase subfamily.


SIMILARITY: Belongs to the UPF0284 family.


SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.


FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.


FUNCTION: Small calcium binding protein that plays important roles in several biological processes such as Ca(2+) homeostasis, chondrocyte biology and cardiomyocyte regulation (PubMed:11909974, PubMed:16952982). In response to an increase in intracellular Ca(2+) levels, binds calcium which triggers conformational changes. These changes allow interactions with specific target proteins and modulate their activity. Regulates a network in cardiomyocytes controlling sarcoplasmic reticulum Ca(2+) cycling and mitochondrial function through interaction with the ryanodine receptors RYR1 and RYR2, sarcoplasmic reticulum Ca(2+)-ATPase/ATP2A2 and mitochondrial F1-ATPase (PubMed:17438143). Facilitates diastolic Ca(2+) dissociation and myofilament mechanics in order to improve relaxation during diastole (By similarity). SUBCELLULAR LOCATION: Cytoplasm Sarcoplasmic reticulum Mitochondrion. SIMILARITY: Belongs to the S-100 family.


FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the tubulin family.


FUNCTION: Involved in cobalamin metabolism and trafficking. Plays a role in regulating the biosynthesis and the proportion of two coenzymes, methylcob(III)alamin (MeCbl) and 5'-deoxyadenosylcobalamin (AdoCbl). Promotes oxidation of cob(II)alamin bound to MMACHC. The processing of cobalamin in the cytosol occurs in a multiprotein complex composed of at least MMACHC, MMADHC, MTRR (methionine synthase reductase) and MTR (methionine synthase) which may contribute to shuttle safely and efficiently cobalamin towards MTR in order to produce methionine. SUBCELLULAR LOCATION: Cytoplasm Mitochondrion.


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. Implicated in the regulation of centrosome duplication. Negatively regulates cilium formation and structure. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cell projection Cytoplasm, cytoskeleton, cilium axoneme Cytoplasm, cytoskeleton, cilium basal body Cytoplasm, cytoskeleton, microtubule organizing center Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole Note=Enriched in centrioles of microtubule asters during prophase, prometaphase and telophase stages of mitosis. Localized at centrioles and in the nucleus at interphase. Colocalizes with nubp-2 at prometaphase. Specifically localizes to the axenome of motile cilia as opposed to primary non- motile cilia. Localization is independent of NUBP2 and KIFC1. SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. NUBP1/NBP35 subfamily.


SIMILARITY: Belongs to the TrbE/VirB4 family.


FUNCTION: Structural protein of the sulfur globules, which are intracellular globules that serve for sulfur storage in purple sulfur bacteria. SIMILARITY: To C.vinosum CV2 and T.roseopersicina TR0.


FUNCTION: May function in the transport of nucleosides and/or nucleoside derivatives between the cytosol and the lumen of an intracellular membrane-bound compartment. SUBCELLULAR LOCATION: Endomembrane system; Multi-pass membrane protein Note=May reside in an intracellular membrane-bound compartment. SUBCELLULAR LOCATION: [Isoform Short]: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the LAPTM4/LAPTM5 transporter family.


FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the actin family.


FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are derived from cytosolic proteins while class II derived from extracellular proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class I proteins presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T- lymphocytes (CTLs). This mechanism enables CTLs to recognize and eliminate infected cells and tumor cells. In NK-cells, the presence of CD8A homodimers at the cell surface provides a survival mechanism allowing conjugation and lysis of multiple target cells. CD8A homodimer molecules also promote the survival and differentiation of activated lymphocytes into memory CD8 T-cells. SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Note=CD8A localizes to lipid rafts only when associated with its partner CD8B.


FUNCTION: Transcription regulator that may repress the maturation program during early embryogenesis. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Minor isoform of alcohol oxidase, which catalyzes the oxidation of methanol to formaldehyde and hydrogen peroxide, the first step in the methanol utilization pathway of methylotrophic yeasts. FUNCTION: Minor isoform of alcohol oxidase, which catalyzes the oxidation of methanol to formaldehyde and hydrogen peroxide, the first step in the methanol utilization pathway of methylotrophic yeasts. SUBCELLULAR LOCATION: Peroxisome matrix. SIMILARITY: Belongs to the GMC oxidoreductase family.


FUNCTION: Involved in pre-mRNA splicing. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the ISY1 family.


FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 2 family.


FUNCTION: Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner. SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein. SIMILARITY: Belongs to the ABC transporter superfamily. Lipoprotein translocase (TC 3.A.1.125) family.


FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the eIF-3 subunit M family.


FUNCTION: Cationic amphipathic alpha-helical antimicrobial peptide with potent activity against Gram-negative and Gram-positive bacteria, fungi and protozoa (PubMed:8306981, PubMed:12709067, PubMed:16401077, PubMed:18637027, PubMed:19113844). Acts in a synergistic effect in combination with Plasticin-B1 at doses that are not active alone (PubMed:12709067). Acts by disturbing membrane functions (PubMed:19113844). On model mebranes, induces a strong perturbation of anionic lipid bilayers, resides at the hydrocarbon core-water interface, parallel to the plane of the membrane, and interacts preferentially with the polar head groups and glycerol backbone region of the anionic phospholipids, as well as the region of the lipid acyl chain near the bilayer surface (PubMed:19113844). It induces a positive curvature of the bilayer and clustering of anionic lipids, consistent with a carpet mechanism, that may lead to the formation of mixed peptide-phospholipid toroidal, transient pores and membrane permeation/disruption once a threshold peptide accumulation is reached (PubMed:19113844). Also enhances binding of agonists to adenosine A1 receptors (ADORA1), adenosine A2a receptors (ADORA2A), alpha-2 adrenergic receptors (ADRA2A) and 5-hydroxytryptamine 1A receptors (HTR1A) (PubMed:1438301, PubMed:8565049). In addition, it enhances guanyl nucleotide exchange which may result in the conversion of receptors to a high affinity state complexed with guanyl nucleotide free G-protein (PubMed:7842473). It affects human behavior eliciting profound malaise, followed by listlessness and then euphoria. It does not show cytotoxic activity on CHO cells (PubMed:19113844). It does not act as a chemoattractant (PubMed:18637027). It does not show hemolytic activity (PubMed:8306981, PubMed:19113844). SUBCELLULAR LOCATION: Secreted Target cell membrane Note=Firstly parallelly oriented to the membrane surface, the peptide may mix to phospholipids, forming toroidal and transient pores in the membrane. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily.


FUNCTION: Component of the nuclear pore complex, a complex required for the trafficking across the nuclear membrane. SUBCELLULAR LOCATION: Nucleus, nuclear pore complex Nucleus membrane; Peripheral membrane protein; Cytoplasmic side Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side Note=Biased towards cytoplasmic side. Central region of the nuclear pore complex, within the transporter. SIMILARITY: Belongs to the NUP58 family.


FUNCTION: Component of antiviral defense system Gabija type I, composed of GajA and GajB. Expression of Gabija type I in B.subtilis (strain BEST7003) confers resistance to phages phi105, phi29, rho14, SpBeta and SBSphiC (PubMed:29371424). Expression of Gabija type I in E.coli B (strain ATCC 11303) confers resistance to phage T7 (PubMed:33885789). May be a helicase or contribute to GajA activation (Probable). SIMILARITY: Belongs to the helicase family.


FUNCTION: Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1, isoform 2 and isoform 3 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences. Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 3 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation assembles into the GAIT complex which binds to stem loop- containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation; seems not to be essential for GAIT complex function. SUBCELLULAR LOCATION: Cytoplasm Microsome Endoplasmic reticulum Nucleus Note=The tyrosine phosphorylated form bound to RNA is found in microsomes (By similarity). Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleoplasm Note=Expressed predominantly in the nucleoplasm. SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, nucleoplasm Note=Expressed predominantly in the nucleoplasm. SUBCELLULAR LOCATION: [Isoform 3]: Nucleus, nucleoplasm Note=Expressed predominantly in the nucleoplasm.


FUNCTION: L-rhamnose binding lectin. Has hemagglutinating activity towards rabbit erythrocytes, but not human type B erythrocytes. Hemagglutinating activity is inhibited by smooth-type lipopolysaccharide (LPS) from K.pneumoniae, E.coli K-235, S.flexneri 1A, A.salmonicida and S.minnesota and rough-type LPS from S.flexneri, but not by rough-type LPS from E.coli K12 and E.coli EH100. Agglutinates E.coli K12 and B.subtilis.


FUNCTION: Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo- dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions (By similarity). 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 8-oxo-dGTP. 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. SIMILARITY: Belongs to the FPG family.


SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the class-II DAHP synthase family.


FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of erinacines, cyathane- xylosides that show unique biological activities, including leishmanicidal activity, stimulating activity for nerve growth-factor synthesis, and agonistic activity toward the kappa opioid receptor (PubMed:28371074, PubMed:31535864). The geranylgeranyl diphosphate (GGPP) synthase eriE catalyzes the first step in erinacines biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP) (By similarity). GGPP is then substrate of the diterpene cyclase eriG for the production of cyatha-3,12-diene. The cytochrome P450 monooxygenase eriI then hydroxylates cyatha-3,12-diene at C-14 of the seven-membered ring to produce erinacol, which is further hydroxylated at C-15 by the cytochrome P450 monooxygenase eriC to yield cyathadiol. The cytochrome P450 monooxygenase eriA then catalyzes C-11 hydroxylation in the presence of the short chain dehydrogenase/reductase (SDR) eriH, which leads to the production of cyathatriol. The acetyltransferase eriL converts cyathatriol into 11-O-acetyl-cyathatriol. The SDR eriH catalyzes further oxidation of 11-O-acetyl-cyathatriol into 1-O- acetylcyathin A3. Finally, the glycosyl transferase eriJ tranfers xylose from UDP-xylose onto C-14 of 11-O-acetyl-cyathatriol to form eracine Q. EriJ is also able to convert 11-O-acetyl-cyathatriol to eracine Q2 by using UDP-D-glucose as cosubstrate, but at a lower rate. In the absence of eriL and eriJ, the SDR eriH is able to convert cyathatriol to cyathin A3; this is likely a switching mechanism in the biosynthesis of cyathins (C-14 ketogroup)and erinacines (C-14 glycosylated group). The roles of the SDR eriB, the polyprenyl transferase eriF and the dehydrogenase eriK have still to be identified (Probable). SIMILARITY: Belongs to the FPP/GGPP synthase family.


SIMILARITY: Belongs to the UPF0304 family.


SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.


FUNCTION: Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DnaA family.


SIMILARITY: Belongs to the FBPase class 1 family.


FUNCTION: Auxin receptor that mediates Aux/IAA proteins proteasomal degradation and auxin-regulated transcription. The SCF(TIR1) E3 ubiquitin ligase complex is involved in auxin-mediated signaling pathway that regulate root and hypocotyl growth, lateral root formation, cell elongation, and gravitropism. Appears to allow pericycle cells to overcome G2 arrest prior to lateral root development. Plays a role in ethylene signaling in roots. Confers sensitivity to the virulent bacterial pathogen P.syringae. SUBCELLULAR LOCATION: Nucleus.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the bacterial glucokinase family.


FUNCTION: Associates with KCNQ3 to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons. Therefore, it is important in the regulation of neuronal excitability. May contribute, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the potassium channel family. KQT (TC 1.A.1.15) subfamily. Kv7.5/KCNQ5 sub-subfamily.


FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the peptidase T1A family.


FUNCTION: H(+)-stimulated, divalent metal cation uptake system. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the NRAMP family.


FUNCTION: Hydrolyzes a wide range of dipeptides. SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family.


FUNCTION: Plays a role in fertilization through the acrosome reaction. SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome Cytoplasmic vesicle, secretory vesicle, acrosome outer membrane. SIMILARITY: Belongs to the FAM170 family.


FUNCTION: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3- dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo- domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3- dihydroxybenzoate (DHB) and L-serine, respectively. SUBCELLULAR LOCATION: Membrane. SIMILARITY: Belongs to the P-Pant transferase superfamily. EntD family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.


FUNCTION: Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation. Important for G1/S transition and S phase progression. Phosphorylates nek6 and nek7 and stimulates their activity. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily.


SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0060 family.


FUNCTION: Probable lipid hydrolase. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the PLPL family.


FUNCTION: With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric- sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily.


FUNCTION: Putative cyclic nucleotide-gated ion channel. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC 1.A.1.5) family.


FUNCTION: Putative COX assembly factor. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the COA4 family.


FUNCTION: Catalyzes a salvage reaction resulting in the formation of IMP that is energically less costly than de novo synthesis. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. Archaeal HPRT subfamily.


SIMILARITY: Belongs to the OsmC/Ohr family.


FUNCTION: Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol. SIMILARITY: Belongs to the NPC2 family.


SIMILARITY: Belongs to the globin family.


FUNCTION: Recruits the ubiquitination machinery to RNA polymerase II for polyubiquitination, removal and degradation, when the transcription-coupled repair (TCR) factor RAD26 fails to efficiently displace stalled RNA polymerase II. Also involved in telomere length regulation. Binds DNA. SUBCELLULAR LOCATION: Cytoplasm Nucleus Chromosome, telomere Note=During transcription stress, localizes to the nucleus following proteolytic cleavage by the proteasome. SIMILARITY: Belongs to the DEF1 family.


FUNCTION: RAB2B effector protein required for accurate acrosome formation and normal male fertility (PubMed:34714330). In complex with RAB2A/RAB2B, seems to suppress excessive vesicle trafficking during acrosome formation (PubMed:34714330). SUBCELLULAR LOCATION: Golgi apparatus. SIMILARITY: Belongs to the GARIN family.


FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene- specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the Mediator complex subunit 31 family.


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


FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast.


SIMILARITY: Belongs to the malic enzymes family.


FUNCTION: Probable DNA-binding transcriptional activator. It is a key determinant of the keratinocyte proliferation-differentiation switch involved in appropriate epidermal development. Plays a role in regulating mammary epithelial cell proliferation (By similarity). May regulate WDR65 transcription (By similarity). SUBCELLULAR LOCATION: Nucleus Cytoplasm Note=Translocates to nucleus in response to an activating signal. SIMILARITY: Belongs to the IRF family.


FUNCTION: May only reduce GSH-thiol disulfides, but not protein disulfides. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the glutaredoxin family. CC-type subfamily.


FUNCTION: Involved in transcription antitermination. Required for transcription of ribosomal RNA (rRNA) genes. Binds specifically to the boxA antiterminator sequence of the ribosomal RNA (rrn) operons. SIMILARITY: Belongs to the NusB family.


SIMILARITY: To E.coli YbeR.


FUNCTION: Component of LSM protein complexes, which are involved in RNA processing. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by promoting decapping and leading to accurate 5'-3' mRNA decay. The cytoplasmic LSM1-LSM7 complex regulates developmental gene expression by the decapping of specific development- related transcripts. Component of the nuclear LSM2-LSM8 complex which is involved splicing nuclear mRNAs. LSM2-LSM8 binds directly to the U6 small nuclear RNAs (snRNAs) and is essential for accurate splicing of selected development-related mRNAs through the stabilization of the spliceosomal U6 snRNA. Plays a critical role in the regulation of development-related gene expression (PubMed:23221597, PubMed:23620288). Involved in the control of plant sensitivity to abscisic acid (ABA) and drought (PubMed:11740939). Functions with ABH1 as negative regulator of ABA signaling in guard cells (PubMed:12427994). Required for regulation of splicing efficiency of many stress-responsive genes under stress conditions (PubMed:24393432). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the snRNP Sm proteins family.


SIMILARITY: Belongs to the universal ribosomal protein uL29 family. SIMILARITY: Belongs to the universal ribosomal protein uL29 family.


FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. SIMILARITY: Belongs to the GcvT family.


FUNCTION: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the PlsY family.


FUNCTION: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the radical SAM superfamily. Lipoyl synthase family.


SIMILARITY: Belongs to the BshC family.


FUNCTION: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the MetA family.


FUNCTION: Phosphatidylserine receptor that plays an important functional role in regulatory B-cells homeostasis including generation, expansion and suppressor functions (PubMed:21821911, PubMed:25645598, PubMed:32668241). As P-selectin/SELPLG ligand, plays a specialized role in activated but not naive T-cell trafficking during inflammatory responses (PubMed:24703780). Controls thereby T-cell accumulation in the inflamed central nervous system (CNS) and the induction of autoimmune disease (PubMed:24703780). Regulates also expression of various anti-inflammatory cytokines and co-inhibitory ligands including IL10 (PubMed:25582854, PubMed:25645598). Acts as regulator of T-cell proliferation (PubMed:15793576). May play a role in kidney injury and repair (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the immunoglobulin superfamily. TIM family.


FUNCTION: Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant. FUNCTION: Regulates transcriptional attenuation of the pyrimidine nucleotide (pyr) operon by binding in a uridine-dependent manner to specific sites on pyr mRNA. This disrupts an antiterminator hairpin in the RNA and favors formation of a downstream transcription terminator, leading to a reduced expression of downstream genes. SIMILARITY: Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrR subfamily.


FUNCTION: Pyruvate kinase that catalyzes the conversion of phosphoenolpyruvate to pyruvate with the synthesis of ATP, and which plays a key role in glycolysis. SIMILARITY: Belongs to the pyruvate kinase family.


SIMILARITY: Belongs to the TrpC family.


FUNCTION: Detoxification of puromycin.


FUNCTION: Hydrolyzes abscisic acid glucose ester (ABA-GE) which represents the predominant form of conjugated ABA (biologically inactive). No activity with beta-D-glucopyranosyl zeatin. The hydrolysis of ABA-GE in the endoplasmic reticulum (ER) forms free ABA and contributes to increase its cellular levels under dehydration conditions. ABA-GE hydrolyzing activity is enhanced by dehydration stress-induced polymerization into higher molecular weight forms. The ABA produced by BGLU18 contributes to the initiation of intracellular signaling as well as the increase in the extracellular ABA level. SUBCELLULAR LOCATION: Endoplasmic reticulum lumen Note=Located in ER bodies. SIMILARITY: Belongs to the glycosyl hydrolase 1 family.


FUNCTION: Involved in development during embryogenesis. SUBCELLULAR LOCATION: Nucleus.


SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the filoviruses glycoprotein family.


FUNCTION: Binds promoter DNA and regulates initiation of transcription (By similarity). Regulator of mitochondrial ribosome biogenesis and translation that is essential for development (PubMed:16787637, PubMed:23300484). Required for normal mitochondrial transcription and translation (PubMed:16787637, PubMed:23300484). Required for assembly of mitochondrial respiratory complexes and normal mitochondrial function (PubMed:23300484). Maintains 16S rRNA levels and functions in mitochondrial ribosome assembly by regulating the biogenesis of the 39S ribosomal subunit (PubMed:23300484). SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the mTERF family.


FUNCTION: Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively. Has a clear preference for cytidine over uridine. Strictly specific for ribonucleosides. SIMILARITY: Belongs to the IUNH family. RihB subfamily.


FUNCTION: Involved in the biosynthesis of one of the two 2,6- deoxysugars, dTDP-L-oleandrose, attached to the macrolactone ring oleandolide to produce the aglycone antibiotic oleandomycin (PubMed:10770761). Probably catalyzes the conversion of dTDP-4-keto- 2,6-dideoxy-alpha-D-glucose to dTDP-4-keto-2,6-dideoxy-beta-L- galactose. SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose 3,5-epimerase family.


SIMILARITY: Belongs to the threonine aldolase family.


FUNCTION: Its primary function is the prevention of hypercalcemia. Upon release into the circulation, it lowers calcium transport by the gills, thereby reducing its rate of influx from the environment into the extracellular compartment. STC also stimulates phosphate reabsorption by renal proximal tubules. The consequence of this action is increased levels of plasma phosphate, which combines with excess calcium and promotes its disposal into bone and scales. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the stanniocalcin family.


FUNCTION: Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFB2 family.


FUNCTION: Thioredoxin reductase (TR) that exhibits both TR and thioredoxin (Trx) activities. Contains a C-terminal functional Trx domain. Functions as an electron donor for plastidial 2-Cys peroxiredoxins and participates in a NADPH-dependent hydrogen peroxide scavenging system in chloroplasts in the dark. Required for chlorophyll biosynthesis and biogenesis of the photosynthetic apparatus. Activates aerobic cyclase which converts Mg-protoporhyrin monomethyl ester into protochlorophyllide. Involved in a light-dependent regulation of starch biosynthesis by redox activation of the ADP-glucose pyrophosphorylase (AGPase), a central enzyme of starch synthesis. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.


FUNCTION: Binds to the 23S rRNA. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL24 family.


FUNCTION: VirB proteins are suggested to act at the bacterial surface and there play an important role in directing T-DNA transfer to plant cells. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the TrbI/VirB10 family.


FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family. YbdK subfamily.


FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 3 family.


FUNCTION: Involved in pre-mRNA splicing, specifically in spliceosome disassembly during late-stage splicing events. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the TFP11/STIP family.


FUNCTION: Catalyzes the addition and repair of the essential 3'- terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded. SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family. Bacterial CCA-adding enzyme type 3 subfamily.


FUNCTION: A segment polarity gene required for wingless (wg)-dependent patterning processes, acting in both wg-sending cells and wg-target cells. In non-neuronal cells wls directs wg secretion. The wls traffic loop encompasses the Golgi, the cell surface, an endocytic compartment and a retrograde route leading back to the Golgi, and involves clathrin-mediated endocytosis and the retromer complex (a conserved protein complex consisting of Vps35 and Vps26). In neuronal cells (the larval motorneuron NMJ), the wg signal moves across the synapse via the release of wls-containing exosome-like vesicles. Postsynaptic wls is required for the trafficking of fz2 through the fz2-interacting protein Grip (By similarity). SUBCELLULAR LOCATION: Presynaptic cell membrane; Multi-pass membrane protein Postsynaptic cell membrane; Multi-pass membrane protein Cell membrane; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Endosome membrane; Multi-pass membrane protein Golgi apparatus membrane; Multi-pass membrane protein Note=In non-neuronal cells, wls binds to wg in the Golgi and accompanies it to the plasma membrane where the two proteins dissociate. Wg is secreted and wls is then internalized and returns to the Golgi apparatus in a retromer-dependent manner. Wls and wg colocalize in the Golgi apparatus in wg-producing cells, and reduced expression is seen in non-producing cells. Endoplasmic reticulum expression is unchanged in wg-producing versus non-producing cells. In neuronal cells, wls is localized both pre- and postsynaptically and is transferred trans-synaptically from the pre- to the postsynaptic compartment (By similarity). SIMILARITY: Belongs to the wntless family.


FUNCTION: May play a role in viral pathogenesis or transmission by insects vectors. SIMILARITY: Belongs to the rhabdoviruses C protein family.


FUNCTION: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane. SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm Note=Distribution is 50-50. SIMILARITY: Belongs to the SecA family.


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


FUNCTION: DNA-binding transcription factor that can both act as an activator and a repressor. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein family.


FUNCTION: Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis. SUBCELLULAR LOCATION: Host Golgi apparatus membrane; Single-pass type III membrane protein Note=The cytoplasmic tail functions as a Golgi complex-targeting signal. SIMILARITY: Belongs to the gammacoronaviruses E protein family.


FUNCTION: Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. The specific recruitment at scission sites is mediated by membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial membranes. While the recruitment by the membrane receptors is GTP- dependent, the following hydrolysis of GTP induces the dissociation from the receptors and allows DNM1L filaments to curl into closed rings that are probably sufficient to sever a double membrane (By similarity). May play a role in the circadian control of mitochondrial ATP production (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytosol Golgi apparatus Endomembrane system; Peripheral membrane protein Mitochondrion outer membrane; Peripheral membrane protein Peroxisome Membrane, clathrin-coated pit Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.