FUNCTION: Required for the proteolytic cleavage of the transcription factor RIM101 in response to alkaline ambient pH. May act as a scaffold protein that recruits the calpain-like protease RIM13 via SNF7 to its substrate RIM101 (By similarity). Required for filamentation. SIMILARITY: Belongs to the palA/RIM20 family.


FUNCTION: May contribute to neddylation of cullin components of SCF- type E3 ubiquitin ligase complexes. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity (By similarity).


FUNCTION: Catalyzes the oxidative sulfurization of hercynine (N- alpha,N-alpha,N-alpha-trimethyl-L-histidine) into hercynyl-gamma-L- glutamyl-L-cysteine sulfoxide, a step in the biosynthesis pathway of ergothioneine. SIMILARITY: Belongs to the EgtB family.


FUNCTION: A minor component of the bacterial microcompartment (BMC) shell. Expression of 5 proteins in E.coli (BMC-H (Hoch_5815), BMC-P (Hoch_5814), and 3 BMC-T (Hoch_5812, Hoch_5816, Hoch_3341)) forms 40 nm artificial BMCs with a molecular mass of 6.5 MDa. This protein does not form stacked pseudohexamers in the BMC. There are 20 BMC-T pseudohexamers per BMC, composed of mixed BMC-T1, BMC-T2 and BMC-T3. The shell facets are 20-30 Angstroms thick, with 1 of BMC-T trimers protruding to the exterior. SUBCELLULAR LOCATION: Bacterial microcompartment. SIMILARITY: Belongs to the bacterial microcompartments protein family.


SIMILARITY: Belongs to the UPF0253 family.


FUNCTION: Myohemerythrin is an oxygen-binding protein found in the retractor muscles of certain worms. The oxygen-binding site contains two iron atoms (By similarity). SIMILARITY: Belongs to the hemerythrin family.


FUNCTION: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the AB hydrolase superfamily. Carboxylesterase BioH family.


FUNCTION: Catalyzes the transformation of p-hydroxyphenylpyruvate into HGA. Has hemolytic and brown pigment production activity. SIMILARITY: Belongs to the 4HPPD family.


FUNCTION: Catalyzes the trans-addition of the 3 molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. Required for the membrane attachment of ypt7 and rhb1. May be involved in vesicle trafficking and protein sorting. Required for forespore membrane formation. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the FPP/GGPP synthase family.


FUNCTION: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). SUBCELLULAR LOCATION: Nucleus Nucleus speckle.


FUNCTION: ATP-dependent RNA helicase involved nonsense-mediated mRNA decay and ribosome biogenesis through rRNA processing. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the DEAD box helicase family. DDX5/DBP2 subfamily.


FUNCTION: E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys- 48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote the formation of 'Lys-63'- linked polyubiquitin chains and functions with the specific ubiquitin- conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress (By similarity). SUBCELLULAR LOCATION: Nucleus, PML body. SIMILARITY: Belongs to the CHFR family.


FUNCTION: May play a role in mitochondrial dynamics by controlling mitochondrial membrane fission. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.


FUNCTION: Ion channel gated by extracellular ATP involved in a variety of cellular responses, such as excitatory postsynaptic responses in sensory neurons, neuromuscular junctions (NMJ) formation, hearing, perception of taste and peristalsis. In the inner ear, regulates sound transduction and auditory neurotransmission, outer hair cell electromotility, inner ear gap junctions, and K(+) recycling. Mediates synaptic transmission between neurons and from neurons to smooth muscle. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Note=Localizes to the apical membranes of hair cells in the organ of Corti. SIMILARITY: Belongs to the P2X receptor family.


FUNCTION: Sodium-independent, high-affinity transport of small and large neutral amino acids such as alanine, serine, threonine, cysteine, phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Acts as an amino acid exchanger. Has higher affinity for L-phenylalanine than LAT1 but lower affinity for glutamine and serine. L-alanine is transported at physiological concentrations. Plays a role in basolateral (re)absorption of neutral amino acids. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Plays an essential role in the reabsorption of neutral amino acids from the epithelial cells to the bloodstream in the kidney. SUBCELLULAR LOCATION: Cytoplasm Basolateral cell membrane; Multi-pass membrane protein Note=Localized to the cytoplasm when expressed alone (By similarity). When coexpressed with SLC3A2/4F2hc, is localized to the plasma membrane. Colocalized with SLC3A2/4F2hc at the basolateral membrane of kidney cortex proximal tubules and small intestine epithelia of the villi (By similarity). SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family.


FUNCTION: Troponin I is the actomyosin ATPase inhibitory subunit present in the thin filament regulatory complex. SIMILARITY: Belongs to the troponin I family.


FUNCTION: A P subtype restriction enzyme that recognizes the double- stranded sequence 5'-GGCC-3' and cleaves after G-2.


FUNCTION: May play an important role in lymphopoiesis.


SUBCELLULAR LOCATION: Fimbrium. SIMILARITY: Belongs to the fimbrial protein family.


FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex. This protamine condenses spermiogenic chromatin in a pattern which comprises fibers with a progressively larger diameter and lamellae that finally undergo definitive coalescence. SUBCELLULAR LOCATION: Nucleus Chromosome.


FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. SIMILARITY: Belongs to the NqrA family.


FUNCTION: Catalyzes the conversion of methylthioalkyl glucosinolates of any chain length into methylsulfinylalkyl glucosinolates. SIMILARITY: Belongs to the FMO family.


FUNCTION: Involved in the ornithine fermentation pathway. Catalyzes the thiolytic cleavage of 2-amino-4-ketopentanoate (AKP) with coenzyme A (CoA) to form acetyl-CoA and alanine. It is strictly specific for AKP. SIMILARITY: Belongs to the threonine synthase family.


FUNCTION: Converts zeaxanthin into antheraxanthin and subsequently violaxanthin. Involved in the epoxidation of zeaxanthin. Plays an important role in resistance to stresses, seed development and dormancy. SUBCELLULAR LOCATION: Plastid, chloroplast.


FUNCTION: Putative oxidoreductase. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: Required for the biosynthesis of the tetrasaccharide linkage region of proteoglycans, especially for small proteoglycans in skin fibroblasts. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single- pass type II membrane protein. Note=Cis cisternae of Golgi stack. SIMILARITY: Belongs to the glycosyltransferase 7 family.


SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the BI1 family.


FUNCTION: Secreted alkaline protease that allows assimilation of proteinaceous substrates. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the peptidase S8 family.


FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase VIII family.


FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. However, because of the low catalytic rate, the question remains whether L-cysteine is the actual biological substrate. SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family. YbdK subfamily.


FUNCTION: Transcriptional repressor, which probably repress transcription by binding directly the 5'-CTGTCAA-3' DNA sequence or by interacting with TGF-beta activated SMAD proteins. Probably represses transcription via the recruitment of histone deacetylase proteins (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Excluded from nucleoli. SIMILARITY: Belongs to the TALE/TGIF homeobox family.


FUNCTION: Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met-MCA, Arg-LCA and Lys- LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C. SUBCELLULAR LOCATION: Membrane; Single- pass type II membrane protein. SIMILARITY: Belongs to the peptidase M1 family.


FUNCTION: Inhibits several voltage-gated sodium channels and only one voltage-gated calcium channel (Cav2.2/CACNA1B (IC(50)=1.1 uM) and Nav1.2/SCN2A (IC(50)=3.7-80 nM), Nav1.3/SCN3A (IC(50)=88-5570 nM), Nav1.1/SCN1A (IC(50)=170-407 nM), Nav1.7/SCN9A (IC(50)=95.5-230 nM), Nav1.6/SCN6A (IC(50)=49.9-3990 nM), Nav1.4/SCN4A (IC(50)=113-400 nM or >10 uM), Nav1.5/SCN5A (IC(50)=1524-1634 nM or >10 uM)) (PubMed:16267209, PubMed:28880874, PubMed:29703751). The toxin acts by shifting the voltage dependence of channel activation to more depolarized potentials and by blocking the inward component of the sodium current (PubMed:16267209). It shows moderate affinity for lipid bilayers without cholesterol and high affinity for lipid bilayers containing cholesterol (PubMed:29703751). In vivo, this toxin causes general ataxia, lack of response to stimuli, and semiparalysis (PubMed:16267209). After a few minutes, the mice are unable to stand, and breathing is reduced in rhythm and intensity (PubMed:16267209). Symptoms gradually increase with progressive slowing of breathing and flaccid paralysis; death occurred within 10 to 20 minutes post injection (PubMed:16267209). Animals remain totally flaccid, and no symptoms of excitatory neurotoxicity are observed (PubMed:16267209). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 04 (CcoTx1) subfamily.


FUNCTION: Part of a bifunctional enzyme complex that functions as an NADPH-dependent hydrogen-evolving hydrogenase with sulfur reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity not exhibited with NAD. The beta and gamma subunits form the sulfur reducing component that catalyzes the cytoplasmic production of hydrogen sulfide in the presence of elemental sulfur. Not active in the presence of sodium sulfate, sodium sulfite, sodium thiosulfate or cysteine. SUBCELLULAR LOCATION: Cytoplasm.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family.


FUNCTION: Alcohol dehydrogenase active against primary long-chain alcohols. Pentan-1-ol is the optimum substrate in vitro, but also shows efficient dehydrogenase activity on propanol, hexanol, and ethanol. SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase family.


FUNCTION: Component of the spliceosome A complex. Regulates alternative splicing of a number of mRNAs. May modulate splice site pairing after recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of the intron. May both positively and negatively regulate apoptosis by regulating the alternative splicing of several genes involved in this process, including FAS and CASP2/caspase-2. In the case of FAS, promotes production of a soluble form of FAS that inhibits apoptosis. In the case of CASP2/caspase-2, promotes production of a catalytically active form of CASP2/Caspase-2 that induces apoptosis (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the RBM5/RBM10 family.


FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.


FUNCTION: Toxic component of a type I toxin-antitoxin (TA) system (Probable). When overexpressed kills cells within 2 minutes; causes collapse of the transmembrane potential and arrest of respiration (PubMed:3019679). FUNCTION: Toxic component of a type I toxin-antitoxin (TA) system (By similarity). When overexpressed kills cells within minutes; causes collapse of the transmembrane potential and arrest of respiration (By similarity). Its toxic effect is probably neutralized by an antisense antitoxin Sok RNA (By similarity). SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the Hok/Gef family.


FUNCTION: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity). SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the adenylosuccinate synthetase family.


FUNCTION: 3'-to-5' exoribonuclease specific for small oligoribonucleotides. SIMILARITY: Belongs to the oligoribonuclease family.


FUNCTION: DNA-binding protein that induces severe bending of DNA. Required for DNA-binding by the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair (By similarity). SUBCELLULAR LOCATION: Nucleus Chromosome. SIMILARITY: Belongs to the NHP6 family.


FUNCTION: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum. FUNCTION: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the VMA21 family.


FUNCTION: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box- dependent processing (PubMed:21078872, PubMed:23097424). Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1, U2, U4 and U5 (PubMed:21078872). May mediate recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (By similarity). SUBCELLULAR LOCATION: Nucleus membrane; Multi-pass membrane protein Nucleus Cytoplasm. SIMILARITY: Belongs to the Integrator subunit 5 family.


FUNCTION: Translational regulator that ensures constant high levels of translation under amino acid starvation. Plays a role as a negative regulator of the gcn2 kinase activity; impairs gcn1-mediated gcn2 activation, and hence gcn2-mediated eIF-2-alpha phosphorylation in amino acid-starved cells and subsequent down-regulation of protein synthesis. In normal conditions, it resides in a actin complex and has no activity. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the IMPACT family.


FUNCTION: Adapter protein that plays a role in endocytosis via clathrin-coated pits. Contributes to the internalization of cell surface receptors, such as integrin ITGB1 and transferrin receptor (PubMed:29887380). Promotes endocytosis of EGFR in cancer cells, and thereby contributes to the down-regulation of EGFR signaling (PubMed:30249660). Recruited to clathrin-coated pits during a mid-to- late stage of assembly, where it is required for normal progress from U-shaped intermediate stage pits to terminal, omega-shaped pits (PubMed:29887380). Binds to membranes enriched in phosphatidylinositol 3,4-bisphosphate or phosphatidylinositol 3,4,5-trisphosphate (PubMed:29887380). When bound to membranes, promotes actin polymerization via its interaction with WAS and/or WASL which leads to the activation of the Arp2/3 complex. Does not promote actin polymerisation in the absence of membranes (PubMed:29887380). SUBCELLULAR LOCATION: Cytoplasm Cell junction Membrane, clathrin-coated pit Cell membrane; Peripheral membrane protein; Cytoplasmic side Cell projection, stereocilium Note=Partially localized at clathrin-coated pits at the cell membrane (PubMed:30249660). Detected at the cell membrane at sites around clathrin-coated pits, very close to the clathrin-coated pits but not an intrinsic part of the clathrin-coated pits (PubMed:29887380). Colocalizes at cell-cell contacts with CDH1, but is not detected at tight junctions (PubMed:14627983).


FUNCTION: Couples the hydrolysis of ATP with the transport of cadmium, zinc and cobalt out of the cell. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily.


FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (PubMed:23892723). Involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6 (By similarity). Mediates 'Lys-63'- linked polyubiquitination of IRAK1. Can activate AP1/JUN and ELK1 (By similarity). Acts as a regulator of innate immunity by mediating 'Lys- 63'-linked polyubiquitination of RIPK2 downstream of NOD1 and NOD2, thereby transforming RIPK2 into a scaffolding protein for downstream effectors, ultimately leading to activation of the NF-kappa-B and MAP kinases signaling (PubMed:23892723). Catalyzes 'Lys-63'-linked polyubiquitination of RIPK2 in parallel of XIAP (PubMed:23892723). SIMILARITY: Belongs to the pellino family.


FUNCTION: Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. FUNCTION: Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the universal ribosomal protein uS19 family. SIMILARITY: Belongs to the universal ribosomal protein uS19 family.


FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Cell projection, lamellipodium Cell projection, filopodium Synapse Cell junction, focal adhesion Note=Targeted to the leading edge of lamellipodia and filopodia by MRL family members. Colocalizes at filopodial tips with a number of other proteins including vinculin and zyxlin. Colocalizes with N-WASP at the leading edge. Colocalizes with GPHN and PFN at synapses (By similarity). SIMILARITY: Belongs to the Ena/VASP family.


FUNCTION: Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine. SUBCELLULAR LOCATION: Cytoplasm, cytosol Microsome Mitochondrion. SIMILARITY: Belongs to the glutamine synthetase family.


FUNCTION: S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 1370 (Gm1370) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a conserved modification in the peptidyl transferase domain of the mtLSU rRNA. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.


FUNCTION: Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to substrate proteins as a monomer or a lysine- linked polymer (By similarity). The so-called ufmylation requires the ufm-1-activating E1 enzyme uba-5, the ufm-1-conjugating E2 enzyme ufc- 1, and probably the ufm-1-ligase E3 enzyme ufl-1 (PubMed:23449979). SIMILARITY: Belongs to the UFM1 family.


FUNCTION: Receptor for the cytotoxic ligand TNFSF10/TRAIL (PubMed:26457518). The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis (PubMed:19090789). Promotes the activation of NF- kappa-B (PubMed:9430227). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein Membrane raft Cytoplasm, cytosol Note=Palmitoylation is required for association with membranes.


FUNCTION: Confers resistance to lithium. FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur- activation pathway by converting PAPS to APS. SIMILARITY: Belongs to the inositol monophosphatase superfamily.


FUNCTION: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). SUBCELLULAR LOCATION: Plastid. SIMILARITY: Belongs to the peptidase S14 family.


FUNCTION: Possibly involved in pGI2 replication mechanism.


FUNCTION: Acts in the modification of cell walls via demethylesterification of cell wall pectin. SUBCELLULAR LOCATION: Secreted, cell wall. SIMILARITY: Belongs to the pectinesterase family.


FUNCTION: May play a role in signal transduction of hyperosmotic response. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.


FUNCTION: Key assembly factor specifically required for the stability of axonemal dynein heavy chains in cytoplasm. SUBCELLULAR LOCATION: Dynein axonemal particle.


FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7- methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the Maf family. YceF subfamily.


FUNCTION: N-alpha-acetyltransferase that specifically mediates the acetylation of N-terminal residues of the transmembrane proteins, with a strong preference for N-termini facing the cytosol. Displays N- terminal acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal segregation during anaphase. May also show histone acetyltransferase activity; such results are however unclear in vivo and would require additional experimental evidences. SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side Note=Probably forms a intramembrane hairpin-like structure in the membrane. SIMILARITY: Belongs to the acetyltransferase family. NAA60 subfamily.


FUNCTION: Symporter that cotransports neutral amino acids and sodium ions from the extraccellular to the intracellular side of the cell membrane (PubMed:11118514). The transport is electrogenic, pH dependent and partially tolerates substitution of Na(+) by Li(+) (PubMed:11118514). Preferentially transports smaller amino acids, such as glycine, L-alanine, L-serine, L-asparagine and L-threonine, followed by L-cysteine, L-histidine, L-proline and L-glutamine and L-methionine (PubMed:11118514). SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein Cell projection, microvillus membrane; Multi- pass membrane protein Note=Microvillus membrane localization in placenta. SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.


FUNCTION: Microbicidal activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cathelicidin family.


FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and also probably that of HMP to HMP-P. SIMILARITY: In the C-terminal section; belongs to the thiaminase-2 family. SIMILARITY: In the N-terminal section; belongs to the ThiD family.


FUNCTION: Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. PrfC subfamily.


FUNCTION: Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex. SUBCELLULAR LOCATION: Plastid, chloroplast. SIMILARITY: Belongs to the BchN/ChlN family.


SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Pg turripeptide superfamily.


FUNCTION: Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine at position 1191 (Psi1191) in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Required for processing 35S pre-rRNA at site D. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the TDD superfamily. TSR3 family.


FUNCTION: Blocks human voltage-gated potassium channel Kv11.1/KCNH2/ERG1 (IC(50)=16.9 nM). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the ergtoxin family. Gamma-KTx 1 subfamily.


FUNCTION: Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the SLX4 family.


FUNCTION: Involved in poly(A) tail length control in neuronal cells. Binds the polyadenosine RNA oligonucleotides. SUBCELLULAR LOCATION: Nucleus speckle Note=Colocalizes with poly(A) RNA in nuclear speckles. SIMILARITY: Belongs to the ZC3H14 family.


FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers (PubMed:6504138, PubMed:2207090, PubMed:7704569). 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 (PubMed:6504138, PubMed:2207090, PubMed:7704569). 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. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. SIMILARITY: Belongs to the tubulin family.


FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. SUBCELLULAR LOCATION: Nucleus. Chromosome. SIMILARITY: Belongs to the histone H1/H5 family.


FUNCTION: Component of the nuclear pore complex (PubMed:24011592). Plays a direct role in nuclear protein import (By similarity). Required for anoxia-induced prophase arrest; may function in concert with cdk-1 to arrest prophase blastomeres in response to anoxia (PubMed:20053678). SUBCELLULAR LOCATION: Nucleus, nuclear pore complex Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side.


FUNCTION: Catalyzes the last step in the trans-sulfuration pathway from L-methionine to L-cysteine in a pyridoxal-5'-phosphate (PLP)-dependent manner, which consists on cleaving the L,L-cystathionine molecule into L-cysteine, ammonia and 2-oxobutanoate. Part of the L-cysteine derived from the trans-sulfuration pathway is utilized for biosynthesis of the ubiquitous antioxidant glutathione. Besides its role in the conversion of L-cystathionine into L-cysteine, it utilizes L-cysteine and L- homocysteine as substrates (at much lower rates than L,L-cystathionine) to produce hydrogen sulfide (H2S). In vitro, it converts two L-cysteine molecules into lanthionine and H2S, and two L-homocysteine molecules to homolanthionine and H2S, which can be particularly relevant under conditions of severe hyperhomocysteinemia. Lanthionine and homolanthionine are structural homologs of L,L-cystathionine that differ by the absence or presence of an extra methylene group, respectively (By similarity). Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target proteins: sulfhydration consists of converting -SH groups into -SSH on specific cysteine residues of target proteins such as GAPDH, PTPN1 and NF-kappa-B subunit RELA, thereby regulating their function (PubMed:19903941, PubMed:22244329). By generating the gasotransmitter H2S, it participates in a number of physiological processes such as vasodilation, bone protection, and inflammation (PubMed:18948540) (By similarity). Plays an essential role in myogenesis by contributing to the biogenesis of H2S in skeletal muscle tissue (PubMed:33826201). Can also accept homoserine as substrate (By similarity). Catalyzes the elimination of selenocystathionine (which can be derived from the diet) to yield selenocysteine, ammonia and 2-oxobutanoate (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the trans-sulfuration enzymes family.


FUNCTION: Proline isomerase that belongs to an abundant class of enzymes that catalyze the cis-trans isomerization of X-Pro peptide bonds and can accelerate the refolding of proline-containing polypeptides (PubMed:7925954, PubMed:8051210, PubMed:7525596). Specifically binds nuclear localization sequences (PubMed:7925954). May be involved in the assembly or folding of ribosomal proteins (PubMed:8051210). SUBCELLULAR LOCATION: Nucleus, nucleolus. SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.


FUNCTION: Putative microtubule-associated force-producing protein, able to bind and hydrolyze GTP. SUBCELLULAR LOCATION: Cytoplasm Cytoplasm, cytoskeleton Note=Microtubule-associated. SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.


FUNCTION: Probable DEAD-box RNA helicase. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the DEAD box helicase family. CshB subfamily.


FUNCTION: Cecropins have lytic and antibacterial activity against several Gram-positive and Gram-negative bacteria. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the cecropin family.


FUNCTION: Recognizes and binds the palindromic sequence 5'- TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the CTF/NF-I family.


FUNCTION: Hydrolyzes o-nitrophenyl-beta-D-galactopyranoside (ONPG) and p-nitrophenyl-beta-D-fucopyranoside (PNPF), but not p-nitrophenyl-beta- D-glucopyranoside (PNPG), p-nitrophenyl-beta-D-xylopyranoside (PNPX) or p-nitrophenyl-beta-D-arabinopyranoside (PNPA). Also hydrolyzes lactose, including lactose in milk. SIMILARITY: Belongs to the glycosyl hydrolase 42 family.


FUNCTION: Probable serine/threonine kinase.


FUNCTION: Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity).


FUNCTION: Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the pescadillo family.


FUNCTION: Plays a role in mitochondrial biogenesis and protein folding. SUBCELLULAR LOCATION: Mitochondrion.


FUNCTION: May be signaling molecules that resemble neuropeptides and that act by binding to alpha-neurexins and possibly other receptors. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the neurexophilin family.


FUNCTION: Required for normal Golgi function. SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. SIMILARITY: Belongs to the COG4 family.


FUNCTION: Probable neurotoxin with unknown target. Possibly targets ion channels. SUBCELLULAR LOCATION: Secreted.


FUNCTION: Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome. SUBCELLULAR LOCATION: Nucleus, nucleolus Nucleus, nucleoplasm. SIMILARITY: Belongs to the WD repeat WDR12/YTM1 family.


FUNCTION: Cytokine produced by activated CD4-positive helper T-cells and to a lesser extend activated CD8-positive T-cells and natural killer (NK) cells that plays pivotal roles in the immune response and tolerance. Binds to a receptor complex composed of either the high- affinity trimeric IL-2R (IL2RA/CD25, IL2RB/CD122 and IL2RG/CD132) or the low-affinity dimeric IL-2R (IL2RB and IL2RG). Interaction with the receptor leads to oligomerization and conformation changes in the IL-2R subunits resulting in downstream signaling starting with phosphorylation of JAK1 and JAK3. In turn, JAK1 and JAK3 phosphorylate the receptor to form a docking site leading to the phosphorylation of several substrates including STAT5. This process leads to activation of several pathways including STAT, phosphoinositide-3-kinase/PI3K and mitogen-activated protein kinase/MAPK pathways. Functions as a T-cell growth factor and can increase NK-cell cytolytic activity as well. Promotes strong proliferation of activated B-cells and subsequently immunoglobulin production. Plays a pivotal role in regulating the adaptive immune system by controlling the survival and proliferation of regulatory T-cells, which are required for the maintenance of immune tolerance. Moreover, participates in the differentiation and homeostasis of effector T-cell subsets, including Th1, Th2, Th17 as well as memory CD8-positive T-cells. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the IL-2 family.


FUNCTION: Mediator of defense signaling triggered by distinct classes of R proteins. Required during hypersensitive response (HR) that confers disease resistance to turnip crinkle virus (TCV) (PubMed:19704828). Contributes to resistance against Pseudomonas syringae and Hyaloperonospora arabidopsidis, at early stages prior to cytosolic calcium ions Ca(2+) accumulation (PubMed:20332379). Required for pathogen-associated molecular pattern (PAMP)-triggered immunity, basal resistance, non-host resistance and systemic acquired resistance (SAR) (PubMed:23250427). Involved in RNA-directed DNA methylation (RdDM) as a component of the RdDM machinery and required for gene silencing. May also be involved in the regulation of chromatin architecture to maintain gene silencing (PubMed:24799676). Exhibits ATPase activity (By similarity). SUBCELLULAR LOCATION: Nucleus Endosome Note=Present in nuclear bodies near chromocenters. Localized in endosome-like vesicles displaying rapid cytosolic streaming. Accumulates in the nucleus following pathogen- associated molecular pattern (PAMP) treatment or infection with an avirulent pathogen. SIMILARITY: Belongs to the MORC ATPase protein family.


FUNCTION: May catalyze both beta-1,3 and beta-1,4 glycosidic linkage on beta-D-glucan. Essential for (1,3;1,4)-beta-D-glucans synthesis in grasses and cereals (Poaceae). The mixed-linked glucans (which are not present in walls of dicotyledons or most other monocotyledonous plants) are particularly important constituents of the walls of the starchy endosperm and aleurone cells of cereal grains such as oats, wheat, rice and barley. They can account for up to 70% by weight of the wall (By similarity). SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi- pass membrane protein. SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant cellulose synthase-like F subfamily.


FUNCTION: Catalyzes the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O(2) to H(2)O(2). SIMILARITY: Belongs to the GMC oxidoreductase family.


FUNCTION: Component of the U1 snRNP particle, which recognizes and binds the 5'-splice site of pre-mRNA. Together with other non-snRNP factors, U1 snRNP forms the spliceosomal commitment complex, that targets pre-mRNA to the splicing pathway (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the SNU71 family.


FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Can use both ATP and NAD(+), but NAD(+) may be a preferred nucleotide cofactor. SIMILARITY: Belongs to the ATP-dependent DNA ligase family.


FUNCTION: Regulator of mitochondrial fusion: acts by forming homo- and heterodimers at the mitochondrial outer membrane and facilitating the formation of pld6/MitoPLD dimers. May act by regulating phospholipid metabolism via pld6/MitoPLD. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitoguardin family.


FUNCTION: Acts as a transcriptional repressor (PubMed:12741956). Represses the promoter activity of the CDC25C gene stimulated by NFYA (PubMed:12741956). May play a role in retinal development where it regulates the composition of bipolar cell populations, by promoting differentiation of bipolar OFF-type cells (By similarity). In the brain, may promote maintenance and suppress differentiation of neural progenitor cells in the developing cortex (By similarity). SUBCELLULAR LOCATION: Nucleus Note=Colocalizes with EFNB1 intracellular domain in the nucleus. SIMILARITY: Belongs to the ZHX family.


SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.


FUNCTION: Activates E box-dependent transcription in collaboration with TCF3/E47. May be a trans-acting factor involved in the development and maintenance of the mammalian nervous system. Transactivates the promoter of its own gene. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: This protein binds cations of several transition elements. It is thought to be involved in detoxification processes. SIMILARITY: Belongs to the metallothionein superfamily. Type 5 family.


FUNCTION: The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of the neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host. Involved in binding to the small intestine through interactions with glycolipids and glycoproteins containing sialic acid moieties (By similarity). Erythrocyte agglutination only occurs when the entire complex is assembled (PubMed:17581814). Binds eukaryotic host mucins as well as N-acetyl-beta-neuraminic acid, N-acetyl-D-galactosamine and galactose (but not glucose) via 2 sites (By similarity). FUNCTION: Agglutinates human erythrocytes (PubMed:2205574). The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of botulinum neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host (PubMed:9421908). The hemagglutinin (HA) component is involved in binding to the upper small intestine through interactions with glycolipids and glycoproteins containing sialic acid moieties (Probable). Binds galactose or oligosaccharides with galactose at their non-reducing end (PubMed:14663070). Binds eukaryotic host mucins; binding is inhibited by N-acetyl-beta-neuraminic acid, N-acetyl-D- galactosamine, galactose, and methyl N-acetyl-beta-neuraminic acid (PubMed:18178224). Binds N-acetyl-beta-neuraminic acid, N-acetyl-D- galactosamine and galactose (but not glucose) via 2 sites (PubMed:18178224, PubMed:21640703). SUBCELLULAR LOCATION: Secreted. SUBCELLULAR LOCATION: Secreted.


FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the complex I subunit 4L family.


SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the major facilitator superfamily. CAR1 family.


FUNCTION: Highly specific phosphatase involved in the metabolism of ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of tRNA splicing. SIMILARITY: Belongs to the POA1 family.


SIMILARITY: Belongs to the universal ribosomal protein uL6 family.


FUNCTION: Mitochondrial 3-hydroxyacyl-thioester dehydratase, which may be involved in fatty acid biosynthesis. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the HTD2 family.


FUNCTION: Required, but not essential, for D1 (psbA) precursor processing and thus correct photosystem II assembly (PSII). SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid lumen Note=Associated with PSII on the lumenal side of the thylakoid membrane. SIMILARITY: Belongs to the Psb27 family.


FUNCTION: Transcription factor that binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3') and displays two biological functions, as regulator of metabolic and redox processes under normal cellular conditions, and as master transcription factor during integrated stress response (ISR) (By similarity). Binds to asymmetric CRE's as a heterodimer and to palindromic CRE's as a homodimer (By similarity). Core effector of the ISR, which is required for adaptation to various stress such as endoplasmic reticulum (ER) stress, amino acid starvation, mitochondrial stress or oxidative stress. During ISR, ATF4 translation is induced via an alternative ribosome translation re- initiation mechanism in response to EIF2S1/eIF-2-alpha phosphorylation, and stress-induced ATF4 acts as a master transcription factor of stress-responsive genes in order to promote cell recovery (By similarity). Promotes the transcription of genes linked to amino acid sufficiency and resistance to oxidative stress to protect cells against metabolic consequences of ER oxidation (By similarity). Activates the transcription of NLRP1, possibly in concert with other factors in response to ER stress. Activates the transcription of asparagine synthetase (ASNS) in response to amino acid deprivation or ER stress. However, when associated with DDIT3/CHOP, the transcriptional activation of the ASNS gene is inhibited in response to amino acid deprivation (By similarity). Together with DDIT3/CHOP, mediates programmed cell death by promoting the expression of genes involved in cellular amino acid metabolic processes, mRNA translation and the terminal unfolded protein response (terminal UPR), a cellular response that elicits programmed cell death when ER stress is prolonged and unresolved (By similarity). Together with DDIT3/CHOP, activates the transcription of the IRS-regulator TRIB3 and promotes ER stress-induced neuronal cell death by regulating the expression of BBC3/PUMA in response to ER stress. May cooperate with the UPR transcriptional regulator QRICH1 to regulate ER protein homeostasis which is critical for cell viability in response to ER stress (By similarity). In the absence of stress, ATF4 translation is at low levels and it is required for normal metabolic processes such as embryonic lens formation, fetal liver hematopoiesis, bone development and synaptic plasticity (By similarity). Acts as a regulator of osteoblast differentiation in response to phosphorylation by RPS6KA3/RSK2: phosphorylation in osteoblasts enhances transactivation activity and promotes expression of osteoblast-specific genes and post-transcriptionally regulates the synthesis of Type I collagen, the main constituent of the bone matrix (By similarity). Cooperates with FOXO1 in osteoblasts to regulate glucose homeostasis through suppression of beta-cell production and decrease in insulin production. Activates transcription of SIRT4. Regulates the circadian expression of the core clock component PER2 and the serotonin transporter SLC6A4. Binds in a circadian time-dependent manner to the cAMP response elements (CRE) in the SLC6A4 and PER2 promoters and periodically activates the transcription of these genes. Mainly acts as a transcriptional activator in cellular stress adaptation, but it can also act as a transcriptional repressor: acts as a regulator of synaptic plasticity by repressing transcription, thereby inhibiting induction and maintenance of long-term memory (By similarity). Regulates synaptic functions via interaction with DISC1 in neurons, which inhibits ATF4 transcription factor activity by disrupting ATF4 dimerization and DNA-binding (By similarity). SUBCELLULAR LOCATION: Nucleus Nucleus speckle Cytoplasm Cell membrane Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Note=Colocalizes with GABBR1 in hippocampal neuron dendritic membranes (By similarity). Colocalizes with NEK6 at the centrosome. Recruited to nuclear speckles following interaction with EP300/p300 (By similarity). SIMILARITY: Belongs to the bZIP family.


FUNCTION: This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the class-C beta-lactamase family.


FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Promotes ubiquitination of sarcomeric proteins alpha-actinin-2 (ACTN2) and filamin-C (FLNC) (By similarity). SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line.


FUNCTION: A humoral factor that may play a role in stress tolerance. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the Turandot family.


FUNCTION: Identified as a multicopy suppressor of the slow growth phenotype of an rsgA (yjeQ) deletion mutant.


SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite. SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase family.


FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the phytotoxin stemphyloxin II (PubMed:31553484). The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase sthA and the enoyl reductase sthE via condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units and 5 methylations (PubMed:31553484). The C-terminal reductase (R) domain of sthA catalyzes the reductive release of the polyketide chain (PubMed:31553484). Because sthA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase sthE (PubMed:31553484). The short-chain dehydrogenase/reductase sthC then catalyzes reduction of dehydroprobetaenone I to probetaenone I (PubMed:31553484). The cytochrome P450 monooxygenase sthF catalyzes successive epoxidation, oxidation (resulting from epoxide opening) and hydroxylation to install a tertiary alcohol in the decaline ring to yield betaenone C from dehydroprobetaenone I and betaenone B from probetaenone I (PubMed:31553484). The FAD-linked oxidoreductase sthB is responsible for the conversion of betaenone C to betaenone A via an intramolecular aldol reaction between C-1 and C-17 to form the bridged tricyclic system in betaenone A (PubMed:31553484). Finally, the cytochrome P450 monooxygenase sthD catalyzes the hydroxylation of C-15 to afford the final metabolite stemphyloxin II (PubMed:31553484). SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Probably involved in ribonucleotide reductase function. SIMILARITY: Belongs to the NrdI family.


FUNCTION: Necessary for the splicing of pre-mRNA. The SF1-U2AF59-U2AF23 complex has a role in the recognition of the branch site (5'-UACUAAC- 3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the splicing factor SR family.


FUNCTION: Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter (By similarity). SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.


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 8 family.


FUNCTION: Acts as a mediator between the cap-binding complex (CBC) and RNA-mediated gene silencing (RNAi). Involved in innate immunity via the short interfering RNAs (siRNAs) processing machinery by restricting the viral RNA production. Also involved microRNA (miRNA)-mediated silencing by contributing to the stability and delivery of primary miRNA transcripts to the primary miRNA processing complex (By similarity). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the ARS2 family.


FUNCTION: Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices. This capsid constitutes the middle concentric layer of the viral mature particle. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes. VP6 is required for the transcription activity of the DLP. SUBCELLULAR LOCATION: Virion Note=Component of the intermediate capsid. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. SIMILARITY: Belongs to the rotavirus VP6 family.


SIMILARITY: To E.coli YfjT.


FUNCTION: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the adenylosuccinate synthetase family.


FUNCTION: In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. SIMILARITY: Belongs to the DNA polymerase type-A family.


FUNCTION: Minor enzyme contributing to the isomerization of uridine to pseudouridine (pseudouridylation) of specific mitochondrial mRNAs (mt- mRNAs) such as COXI and COXIII mt-mRNAs, modulating the efficiency of mitochondrial protein synthesis without changes in transcript abundance or stability (By similarity). Also catalyzes pseudouridylation of some tRNAs, including synthesis of pseudouridine(55) from uracil-55, in the psi GC loop of a subset of tRNAs (By similarity). SUBCELLULAR LOCATION: Mitochondrion matrix Note=Localizes to mitochondrial RNA granules, platforms for post-transcriptional RNA modification and ribosome assembly. SIMILARITY: Belongs to the pseudouridine synthase TruB family.


FUNCTION: Involved in endoplasmic reticulum-associated protein degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP to the ER during ERAD. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein Nucleus envelope Note=Both the N- and the C-terminus face the cytosol. Also found in the nucleus envelope contiguous to the ER.


SIMILARITY: Belongs to the YkuD family.


FUNCTION: Mitochondrial transporter that mediates citrate export from mitochondria to cytoplasm (PubMed:36177470). Both ctpA, ctpB, and ctpD play important roles in citric acid transport across the mitochondrial membrane and function in a redundant manner (PubMed:36177470). SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.


SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic side. SIMILARITY: Belongs to the synaptobrevin family.


SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.


FUNCTION: Required for 20S pre-rRNA processing. SUBCELLULAR LOCATION: Cytoplasm Nucleus. SIMILARITY: Belongs to the TSR2 family.


SIMILARITY: Belongs to the universal ribosomal protein uS10 family.


FUNCTION: Catalyzes the formation of L-carnitine from gamma- butyrobetaine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the gamma-BBH/TMLD family.


FUNCTION: Chorion membrane (egg shell) protein; plays a role in protecting the egg from the environment. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the chorion protein S16 family.


FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane. SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. SIMILARITY: Belongs to the ATPase F chain family.


FUNCTION: Involved in the biosynthesis of branched-chain polyamines, which support the growth of thermophiles under high-temperature conditions. Catalyzes the sequential condensation of spermidine with the aminopropyl groups of decarboxylated S-adenosylmethionines to produce N(4)-bis(aminopropyl)spermidine via N(4)-aminopropylspermidine. Can also use spermine to produce N(4)-aminopropylspermine. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the branched-chain polyamine synthase family.


FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol- cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 6A family.


FUNCTION: Transcriptional activator that regulates the expression of genes involved in symbiosis. Among other targets it acts on the nolWBTUV operon. SIMILARITY: Belongs to the LysR transcriptional regulatory family.


FUNCTION: Involved in spermatogenesis. Has a probable role in anterograde intraflagellar transport which is essential for the formation of sperm flagella. SUBCELLULAR LOCATION: Cell projection, cilium, flagellum Note=Mainly located in the mid-piece of sperm flagella.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.


FUNCTION: Synthesizes nicotianamine, a polyamine that is the first intermediate in the synthesis of the phytosiderophores of the mugineic acid type found in gramineae which serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron. SIMILARITY: Belongs to the nicotianamine synthase (NAS)-like family.


FUNCTION: Dual-function transcription factor with both repression and activation activities. Binds to 5'-CCATATT-3' motif in target gene promoters (e.g. ABR1) (PubMed:26961720). Binds also to G-rich DNA motif 5'-GGGGGCAGTGG-3' (PubMed:22508367). Regulates the expression of genes involved in diverse cellular pathways, including glucose metabolism, photosynthesis, phototropism and stress response (e.g. salt, drought and osmotic stress) (PubMed:22508367, PubMed:26961720). Regulates plant immunity, especially during necrotrophic fungal infection (e.g. B.cinerea) (PubMed:24451981). Binds to ABR1 promoter and promotes its expression, thus negatively regulating the abscisic acid (ABA) signaling pathway. Represses ABA- and salt-responsive genes expression (PubMed:26961720). SUBCELLULAR LOCATION: Nucleus.


FUNCTION: May have antimicrobial activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the insect defense protein family.


FUNCTION: Catalyzes the oxidation of malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively. SIMILARITY: Belongs to the aldehyde dehydrogenase family. IolA subfamily.


FUNCTION: Repressor of the lactose catabolism operon. Galactose-6- phosphate is the inducer (By similarity).


SIMILARITY: Belongs to the asfivirus B407L family.


FUNCTION: Positively regulates SLC1A1/EAAC1-mediated glutamate transport by increasing its affinity for glutamate in a PKC activity- dependent manner. Promotes the catalytic efficiency of SLC1A1/EAAC1 probably by reducing its interaction with ARL6IP5, a negative regulator of SLC1A1/EAAC1-mediated glutamate transport. Plays a role in the formation and stabilization of endoplasmic reticulum tubules. Negatively regulates apoptosis, possibly by modulating the activity of caspase-9 (CASP9). Inhibits cleavage of CASP9-dependent substrates and downstream markers of apoptosis but not CASP9 itself. May be involved in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation. SUBCELLULAR LOCATION: Endomembrane system; Multi-pass membrane protein Endoplasmic reticulum membrane; Multi-pass membrane protein Endoplasmic reticulum Note=Predominantly localized to intracytoplasmic membranes. Preferentially localizes at the ER tubules and the edge of the ER sheets, both of which are characterized by a high membrane curvature. SIMILARITY: Belongs to the ARL6ip family.


FUNCTION: Plays a role for multiplication of the virus in different cell types. SIMILARITY: Belongs to the poxviridae C7 protein family.


SIMILARITY: Belongs to the ketopantoate reductase family.


FUNCTION: May be involved in transcriptional regulation. SUBCELLULAR LOCATION: Nucleus Chromosome, centromere, kinetochore.


FUNCTION: ATP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit family. ATP-specific subunit beta subfamily.


FUNCTION: Potent antimicrobial peptide with activity against bacteria, fungi and protozoa. Probably acts by disturbing membrane functions with its amphipathic structure. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Dermaseptin subfamily.


FUNCTION: Acts as an adapter protein downstream of several growth factor receptors to promote cell proliferation, migration, and redistribution of actin fibers (By similarity). Specifically involved in INS/insulin signaling pathway by mediating MAPK1/ERK2-MAPK3/ERK1 activation and DNA synthesis (By similarity). Promotes insulin-mediated membrane ruffling (By similarity). In response to vasoconstrictor peptide EDN1, involved in the activation of RAP1 downstream of PTK2B via interaction with phosphorylated BCAR1. Inhibits cell migration and invasion via regulation of TGFB-mediated matrix digestion, actin filament rearrangement, and inhibition of invadopodia activity. May inhibit TGFB-SMAD signaling, via facilitating BCAR1 and SMAD2 and/or SMAD3 interaction (By similarity). Regulates EGF-induced DNA synthesis (By similarity). Required for the maintenance of ocular lens morphology and structural integrity, potentially via regulation of focal adhesion complex signaling. Acts upstream of PTPRA to regulate the localization of BCAR1 and PTPRA to focal adhesions, via regulation of SRC-mediated phosphorylation of PTPRA. Positively regulates integrin-induced tyrosine phosphorylation of BCAR1. Acts as a guanine nucleotide exchange factor (GEF) for small GTPases RALA, RAP1A and RRAS (By similarity). However, in a contrasting study, lacks GEF activity towards RAP1 (By similarity). SUBCELLULAR LOCATION: Cytoplasm Cell junction, focal adhesion Note=Localization to focal adhesions depends on interaction with PTPRA.


SIMILARITY: Belongs to the UPF0337 (CsbD) family.


FUNCTION: Gamma-conotoxins may act on voltage-gated non-specific cation pacemaker channels (HCN). SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the conotoxin O2 superfamily.


FUNCTION: This is one of the subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), the enzyme catalyzing the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl- CoA/(S)-methylmalonyl-CoA. Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase is involved in propionate utilization and in the production of the poly(3-hydroxybutyrate-co-3- hydroxyvalerate)(PHBV), which is a water-insoluble biopolymer used as intracellular energy reserve material when cells grow under conditions of nutrient limitation (PubMed:25398867). Propionyl-CoA carboxylase is also able to catalyze the carboxylation of acetyl-CoA (PubMed:25398867).


FUNCTION: Has no antimicrobial or anticancer activity. SUBCELLULAR LOCATION: Secreted. SIMILARITY: Belongs to the frog skin active peptide (FSAP) family. Aurein subfamily.


FUNCTION: Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates (PubMed:31835031). Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase. FUNCTION: Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of OPG118 and OPG133, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase. SUBCELLULAR LOCATION: Virion Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome. This is necessary because viral early mRNAs are synthesized within minutes after virus entry into the cell and are extruded through pores in the core particle. SUBCELLULAR LOCATION: Virion Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome. This is necessary because viral early mRNAs are synthesized within minutes after virus entry into the cell and are extruded through pores in the core particle. SIMILARITY: Belongs to the poxviridae DNA-directed RNA polymerase 18 kDa subunit family.


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


FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. An RNase. SIMILARITY: Belongs to the PINc/VapC protein family.


SUBCELLULAR LOCATION: Nucleus membrane; Single-pass membrane protein.


FUNCTION: Plays a role in neurogenesis and neuronal migration. Necessary for correct formation of mitotic spindles and chromosome separation during mitosis (By similarity). Necessary for cytokinesis and cell proliferation (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton Nucleus Cytoplasm, cytoskeleton, spindle Midbody Note=A small proportion is nuclear, in a punctate pattern (By similarity). In a filamentous pattern adjacent to the nucleus of migrating cerebellar granule cells. Colocalizes with tubulin and dynein and with the microtubule organizing center. Distributed throughout the cytoplasm of non-migrating cells (By similarity). Localizes to the mitotic spindle in a EML4-dependent manner (By similarity). SIMILARITY: Belongs to the nudC family.


SIMILARITY: Belongs to the serpin family.


FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5- glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 2 subfamily.


FUNCTION: Photoreceptor implicated in non-image-forming responses to light. SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin subfamily.


SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side. SIMILARITY: Belongs to the Psb28 family.


FUNCTION: Involved in DNA repair and in homologous recombination. May regulate the cleavage reactions of the branch-structured DNA. Has a very weak ATPase activity that is not stimulated by DNA. Binds DNA but does not promote DNA strands exchange. SIMILARITY: Belongs to the eukaryotic RecA-like protein family. RadB subfamily.


FUNCTION: May function as histone H3 lysine demethylase and be involved in regulation of gene expression. SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the JARID1 histone demethylase family.


FUNCTION: Specifically dimethylates two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily.


FUNCTION: Cleaves proteins, imported into the mitochondrion, to their mature size. SUBCELLULAR LOCATION: Mitochondrion matrix. SIMILARITY: Belongs to the peptidase M3 family.


FUNCTION: Involved in the secretion of proteases A, B, C and G. SUBCELLULAR LOCATION: Cell outer membrane. SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17) family.


FUNCTION: Might be a catalyst/regulator pair of proteins involved in the temporal controlled sporulation process. The decrease in level of the smaller protein early in sporulation may relieve negative regulation of the activity of the larger protein.


FUNCTION: Responsible for the transport of C4-dicarboxylates. SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the DcuA/DcuB transporter (TC 2.A.13.1) family.


FUNCTION: Component of the KaiBC clock protein complex, which constitutes the main circadian regulator in cyanobacteria; it may modify the ATPase activity of KaiC. FUNCTION: May be a metamorphic protein which reversibly switches between an inactive tetrameric fold and a rare, thioredoxin-like monomeric fold (KaiB(fs)). KaiB(fs) binds phospho-KaiC, and perhaps clock output effectors. SIMILARITY: Belongs to the KaiB family.


FUNCTION: This protein may function to maintain proper structure of myelin. SUBCELLULAR LOCATION: Myelin membrane; Peripheral membrane protein; Cytoplasmic side. Note=Cytoplasmic side of myelin. SIMILARITY: Belongs to the myelin basic protein family.


FUNCTION: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. Mdm12 is required for the interaction of the ER-resident membrane protein mmm1 and the outer mitochondrial membrane-resident beta-barrel protein mdm10. The mdm12-mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all mitochondrial outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the mdm12-mmm1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids. SIMILARITY: Belongs to the MDM12 family.


FUNCTION: TS is a member of the terpene cyclase group of enzymes. It catalyzes the isomerization and cyclization of farnesyl pyro-phosphate to form trichodiene, the first cyclic intermediate in the biosynthetic pathway for trichothecenes. It serves to branch trichothecene biosynthesis from the isoprenoid pathway. SIMILARITY: Belongs to the trichodiene synthase family.


FUNCTION: Binds to the N-acetyl-9-O-acetylneuraminic acid residues on the cell surface, bringing about the attachment of the virus particle to the cell. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induce an irreversible conformational change in HEF2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore. Displays a receptor-destroying activity which is a neuraminidate-O- acetyl esterase. This activity cleaves off any receptor on the cell surface, which would otherwise prevent virions release. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane protein Host cell membrane; Single-pass type I membrane protein. SIMILARITY: Belongs to the influenza viruses hemagglutinin family.


FUNCTION: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily.


FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate. SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein; Matrix side. SIMILARITY: Belongs to the UbiA prenyltransferase family.


FUNCTION: Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1 and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK which is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, cytosol Cytoplasmic vesicle Note=Localizes at the cell membrane upon interaction with frizzled family members. SIMILARITY: Belongs to the DSH family.


FUNCTION: Involved in a peptide intake transport system that plays a role in the resistance to antimicrobial peptides. SUBCELLULAR LOCATION: Periplasm. SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.


SIMILARITY: Belongs to the OXR1 family.


FUNCTION: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr). SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the QueG family.


FUNCTION: May be involved in heavy metals transport. SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cornifelin family.


SIMILARITY: Belongs to the UPF0250 family.


FUNCTION: May be involved in gene regulation within neural lineage cells potentially by direct DNA binding or by binding to other transcription factors. SUBCELLULAR LOCATION: Nucleus.


FUNCTION: Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre- mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is essential since most viral proteins are translated from unspliced or partially spliced pre-mRNAs which cannot exit the nucleus by the pathway used by fully processed cellular mRNAs (By similarity). SUBCELLULAR LOCATION: Host nucleus, host nucleolus. Host cytoplasm. Note=The presence of both nuclear import and nuclear export signals leads to continuous shuttling between the nucleus and cytoplasm.


FUNCTION: Enoyl-ACP reductase of the type II fatty acid syntase (FAS- II) system, which is involved in the biosynthesis of mycolic acids, a major component of mycobacterial cell walls (PubMed:25227413). Catalyzes the NADH-dependent reduction of the double bond of 2-trans- enoyl-[acyl-carrier protein], an essential step in the fatty acid elongation cycle of the FAS-II pathway (PubMed:7599116). Shows preference for long-chain fatty acyl thioester substrates (>C16), and can also use 2-trans-enoyl-CoAs as alternative substrates (PubMed:7599116). The mycobacterial FAS-II system utilizes the products of the FAS-I system as primers to extend fatty acyl chain lengths up to C56, forming the meromycolate chain that serves as the precursor for final mycolic acids (PubMed:25227413). FUNCTION: Enoyl-ACP reductase of the type II fatty acid syntase (FAS- II) system, which is involved in the biosynthesis of mycolic acids, a major component of mycobacterial cell walls. Catalyzes the NADH- dependent reduction of the double bond of 2-trans-enoyl-[acyl-carrier protein], an essential step in the fatty acid elongation cycle of the FAS-II pathway. Shows preference for long-chain fatty acyl thioester substrates (>C16), and can also use 2-trans-enoyl-CoAs as alternative substrates. The mycobacterial FAS-II system utilizes the products of the FAS-I system as primers to extend fatty acyl chain lengths up to C56, forming the meromycolate chain that serves as the precursor for final mycolic acids. FUNCTION: Is the primary target of the first-line antitubercular drug isoniazid (INH) and of the second-line drug ethionamide (ETH) (PubMed:8284673, PubMed:12406221, PubMed:16906155, PubMed:17227913). Overexpressed inhA confers INH and ETH resistance to M.tuberculosis (PubMed:12406221). The mechanism of isoniazid action against InhA is covalent attachment of the activated form of the drug to the nicotinamide ring of NAD and binding of the INH-NAD adduct to the active site of InhA (PubMed:9417034, PubMed:16906155). Similarly, the ETH-NAD adduct binds InhA (PubMed:17227913). FUNCTION: Is the primary target of the first-line antitubercular drug isoniazid (INH) and of the second-line drug ethionamide (ETH) (PubMed:12406221). Overexpressed inhA confers INH and ETH resistance to M.bovis (PubMed:12406221). The mechanism of isoniazid action against InhA is covalent attachment of the activated form of the drug to the nicotinamide ring of NAD and binding of the INH-NAD adduct to the active site of InhA (By similarity). Similarly, the ETH-NAD adduct binds InhA (By similarity). FUNCTION: Enoyl-ACP reductase of the type II fatty acid syntase (FAS- II) system, which is involved in the biosynthesis of mycolic acids, a major component of mycobacterial cell walls. Catalyzes the NADH- dependent reduction of the double bond of 2-trans-enoyl-[acyl-carrier protein], an essential step in the fatty acid elongation cycle of the FAS-II pathway. Shows preference for long-chain fatty acyl thioester substrates, and can also use 2-trans-enoyl-CoAs as alternative substrates. The mycobacterial FAS-II system utilizes the products of the FAS-I system as primers to extend fatty acyl chain lengths up to C56, forming the meromycolate chain that serves as the precursor for final mycolic acids. FUNCTION: Is the primary target of the first-line antitubercular drug isoniazid (INH) and of the second-line drug ethionamide (ETH). Overexpressed inhA confers INH and ETH resistance to M.tuberculosis (PubMed:12406221). The mechanism of isoniazid action against InhA is covalent attachment of the activated form of the drug to the nicotinamide ring of NAD and binding of the INH-NAD adduct to the active site of InhA. Similarly, the ETH-NAD adduct binds InhA (By similarity). SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. FabI subfamily.


FUNCTION: (Microbial infection) Through its interaction with HCV envelope glycoprotein E2, participates in the attachment of HCV to HSPGs and other receptors (LDLr, VLDLr, and SR-B1) on the cell surface and to the assembly, maturation and infectivity of HCV viral particles (PubMed:25122793, PubMed:29695434). This interaction is probably promoted via the up-regulation of cellular autophagy by the virus (PubMed:29695434). FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids (PubMed:6860692, PubMed:1911868, PubMed:14754908). APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance (PubMed:6860692, PubMed:2762297, PubMed:1911868, PubMed:1917954, PubMed:9395455, PubMed:14754908, PubMed:23620513). Apolipoproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma (PubMed:6860692, PubMed:2762297, PubMed:9395455). As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL) (PubMed:6860692, PubMed:1911868). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles (PubMed:2762297, PubMed:1917954, PubMed:7768901, PubMed:8939961, PubMed:12950167, PubMed:20030366, PubMed:2063194, PubMed:8756331, PubMed:20303980, PubMed:1530612, PubMed:7635945). Finally, APOE has also a heparin-binding activity and binds heparan- sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells (PubMed:9395455, PubMed:9488694, PubMed:23676495, PubMed:7635945). A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes (PubMed:1911868, PubMed:1917954, PubMed:9395455, PubMed:23676495, PubMed:29516132). APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues (PubMed:2762297, PubMed:29516132). By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis (PubMed:2762297, PubMed:1917954, PubMed:29516132). APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis (PubMed:9395455, PubMed:14754908, PubMed:23620513). First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues (PubMed:14754908, PubMed:23620513). Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes (PubMed:9395455). APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting (PubMed:8939961, PubMed:25173806). APOE is also involved in innate and adaptive immune responses, controlling for instance the survival of myeloid-derived suppressor cells (By similarity). Binds to the immune cell receptor LILRB4 (PubMed:30333625). APOE may also play a role in transcription regulation through a receptor-dependent and cholesterol-independent mechanism, that activates MAP3K12 and a non-canonical MAPK signal transduction pathway that results in enhanced AP-1-mediated transcription of APP (PubMed:28111074). SUBCELLULAR LOCATION: Secreted Secreted, extracellular space Secreted, extracellular space, extracellular matrix Extracellular vesicle Endosome, multivesicular body Note=In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins (PubMed:1911868, PubMed:8340399). Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner (PubMed:9488694). Lipidation induces the release from the extracellular matrix (PubMed:9488694). Colocalizes with CD63 and PMEL at exosomes and in intraluminal vesicles within multivesicular endosomes. SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.


FUNCTION: Catalyzes the oxidation of naphthalene dihydrodiol into 1,2- dihydroxynaphthalene. SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.


FUNCTION: Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Also plays a role in the assembly of the exocyst (By similarity). SUBCELLULAR LOCATION: Bud Bud neck. SIMILARITY: Belongs to the EXO70 family.


SIMILARITY: Belongs to the BtpA family.


FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6- phosphogluconate. SUBCELLULAR LOCATION: Cytoplasm, cytosol. SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. 6-phosphogluconolactonase subfamily.


FUNCTION: Binds to the 23S rRNA. Binds deacetylated tRNA in the E site; when the tRNA binds a stretch of 7 amino acids are displaced to allow binding. SIMILARITY: Belongs to the eukaryotic ribosomal protein eL42 family.


FUNCTION: Transcription factor that binds to the immunoglobulin enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcription (By similarity). SUBCELLULAR LOCATION: Nucleus.


SUBCELLULAR LOCATION: Mitochondrion. SIMILARITY: Belongs to the AIM24 family.


FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins. SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass membrane protein; Stromal side. SIMILARITY: In the C-terminal section; belongs to the peptidase M41 family. SIMILARITY: In the central section; belongs to the AAA ATPase family.


FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcriptional activator of several progesteron-dependent promoters in a variety of cell types. Involved in activation of SRC-dependent MAPK signaling on hormone stimulation. SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling is both hormone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases (By similarity). SIMILARITY: Belongs to the nuclear hormone receptor family.


SIMILARITY: Belongs to the pseudouridine synthase RluA family.


FUNCTION: Flavodoxins are low-potential electron donors to a number of redox enzymes. NifF is the electron donor to nitrogenase, and is thus implicated in nitrogen fixation. Does not function as an electron donor to nitrite reductase. SIMILARITY: Belongs to the flavodoxin family.


SIMILARITY: Belongs to the LacAB/RpiB family.


FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Macronuclei.


FUNCTION: Contacts the emerging nascent chain on the ribosome. SIMILARITY: Belongs to the NAC-alpha family.


FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit (By similarity). Upon interaction with GNA12 promotes dephosphorylation of microtubule associated protein TAU/MAPT (By similarity). Required for proper chromosome segregation and for centromeric localization of SGO1 in mitosis (By similarity). Together with RACK1 adapter, mediates dephosphorylation of AKT1 at 'Ser-473', preventing AKT1 activation and AKT-mTOR signaling pathway. Dephosphorylation of AKT1 is essential for regulatory T-cells (Treg) homeostasis and stability (By similarity). SUBCELLULAR LOCATION: Chromosome, centromere Nucleus Cytoplasm Lateral cell membrane Cell projection, dendrite Note=Centromeric localization requires the presence of BUB1. SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family.


FUNCTION: Acts as an adapter for myotubularin-related phosphatases (PubMed:19038970, PubMed:22647598). Increases lipid phosphatase MTMR6 catalytic activity, specifically towards phosphatidylinositol 3,5- bisphosphate and MTMR6 binding affinity for phosphorylated phosphatidylinositols (PubMed:19038970, PubMed:22647598). Positively regulates lipid phosphatase MTMR7 catalytic activity (By similarity). Increases MTMR8 catalytic activity towards phosphatidylinositol 3- phosphate (PubMed:22647598). The formation of the MTMR6-MTMR9 complex, stabilizes both MTMR6 and MTMR9 protein levels (PubMed:19038970). Stabilizes MTMR8 protein levels (PubMed:22647598). Plays a role in the late stages of macropinocytosis possibly by regulating MTMR6-mediated dephosphorylation of phosphatidylinositol 3-phosphate in membrane ruffles (PubMed:24591580). Negatively regulates autophagy, in part via its association with MTMR8 (PubMed:22647598). Negatively regulates DNA damage-induced apoptosis, in part via its association with MTMR6 (PubMed:19038970, PubMed:22647598). Does not bind mono-, di- and tri- phosphorylated phosphatidylinositols, phosphatidic acid and phosphatidylserine (PubMed:19038970). SUBCELLULAR LOCATION: Cytoplasm Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side Cytoplasm, perinuclear region Endoplasmic reticulum Note=Localizes to ruffles during EGF-induced macropinocytosis (By similarity). Colocalizes with MTMR6 to the perinuclear region (PubMed:19038970). Partially localizes to the endoplasmic reticulum (PubMed:19038970). SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- receptor class myotubularin subfamily.


FUNCTION: Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair. Mre11 binds to DSB ends and has both double-stranded 3'-5' exonuclease activity and single-stranded endonuclease activity (By similarity). In polyploid organisms, the Rad50/Mre11 complex appears to restrain the repair of double-strand breaks by homologous recombination, allowing another pathway to act as the primary mode of repair (PubMed:19593371). SIMILARITY: Belongs to the MRE11/RAD32 family.


SIMILARITY: Belongs to the homoserine dehydrogenase family.


FUNCTION: Component of the transcription regulatory CCAAT-binding complex. Required for the reprogramming of the cell for iron use. Down- regulates pcl1, sdh4, and isa1 underlow-iron conditions. SUBCELLULAR LOCATION: Cytoplasm Nucleus Cytoplasm, cytoskeleton, spindle pole. Note=Iron starvation induces nuclear accumulation and iron induces relocalization to the cytoplasm, in association with exportin crm1.


FUNCTION: Required for high-affinity tryptophan transport. Also transports cysteine, phenyalanine and tyrosine. SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) superfamily. YAT (TC 2.A.3.10) family.


SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. SIMILARITY: Belongs to the UPF0114 family.


SUBCELLULAR LOCATION: Cytoplasm. SIMILARITY: Belongs to the disproportionating enzyme family.


FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Ligand for integrins alpha-E/beta-7, ITGAE:ITGAB7, alpha-4/beta-7, ITGA4:ITGAB7 and alpha-4/beta-1, ITGA4:ITGAB1 through which modulates CD4(+) T cells activation (PubMed:28051089). SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.


FUNCTION: Catalyzes the C6-oxidation step in brassinosteroids biosynthesis (PubMed:15710611). Converts 6-deoxocastasterone (6- deoxoCS) to castasterone (CS) (PubMed:15710611, PubMed:9990098). May also convert 6-deoxoteasterone (6-deoxoTE) to teasterone (TE), 3- dehydro-6-deoxoteasterone (6-deoxo3DT, 6-deoxo3DHT) to 3- dehydroteasterone (3DT, 3-DHT), and 6-deoxotyphasterol (6-deoxoTY) to typhasterol (TY), but not castasterone (CS) to brassinolide (BL) (PubMed:15710611). SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. SIMILARITY: Belongs to the cytochrome P450 family.


FUNCTION: Potential calcium-dependent cell-adhesion protein. May be required for the structural integrity of the outer segment (OS) of photoreceptor cells (By similarity). SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein Note=Localized at the junction between the inner and outer segments of rod and cone photoreceptors cells. Confined to the base of the OS. Localized on the edges of nascent evaginating disks on the side of the OS opposite the connecting cilium. Expressed at postnatal day 2 at the apical tip of the rod photoreceptor cells, the site of the developing OS. Colocalized with rhodopsin between postnatal days 2 and 9 at the base of the growing OS region (By similarity).


FUNCTION: Involved in cell wall 1,6-beta-glucan assembly possibly by the addition of linear side chains of 1,6-linked Glc units to a highly branched 1,6- and 1,3-linked glucan backbone. FUNCTION: Involved in cell wall 1,6-beta-glucan assembly possibly by the addition of linear side chains of 1,6-linked Glc units to a highly branched 1,6- and 1,3-linked glucan backbone. SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI- anchor Secreted, cell wall. SIMILARITY: Belongs to the KRE1 family.


FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for synaptic transmission (By similarity). The BCR(KCTD13) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and promoting synaptic transmission (PubMed:29088697). SUBCELLULAR LOCATION: Nucleus. SIMILARITY: Belongs to the BACURD family.