Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
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A0A644F7M7 | GCP2_GIAIC | MSSVFADPRVKELLNLHRSPKLATEGKTPPSQVQDLVNKYSRLGSNVVSHPTRSSPEKTTDKPADSKPSIPPLKSESVMTRLTALSSNNTTQNVASLVTAIASHPATAALPKQEASQQPVIPTSVEKRAVTQPLSQQNMNKLMNAIDPQAAPLIEDQVAGKHTGTKPLLTLQQQQAISSLPTKSERESALNEIALNTAIQSAQHANMELSKAGITFPMWFFGVQNQSDLVSRSFISLAHIQQPMVMNDSLLQEHLLVSDCIAVLQGCMQTTYLQVSEQNKEYVVTIRKEVATELPATLVAMTQRVLVHAHARFQIVNTIY... | null | null | cytoplasmic microtubule organization [GO:0031122]; meiotic cell cycle [GO:0051321]; microtubule nucleation [GO:0007020]; mitotic cell cycle [GO:0000278]; spindle assembly [GO:0051225] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; equatorial microtubule organizing center [GO:0000923]; gamma-tubulin complex [GO:0000930]; microtubule [GO:0005874]; motile cilium [GO:0031514]; spindle pole [GO:0000922] | gamma-tubulin binding [GO:0043015]; microtubule minus-end binding [GO:0051011] | PF04130;PF17681; | 1.20.120.1900; | TUBGCP family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000269|PubMed:30318753}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:30318753}. Note=Localizes to basal bodies, axonemes and median bodies of the trophozoites during interf... | null | null | null | null | null | FUNCTION: Component of the gamma-tubulin small complex (gamma-TuSC) involved in microtubule (MT) nucleation for the formation of median bodies and in the biogenesis of flagella. Gamma-TuSC may be required for the correct positioning of EB1 within the trophozoites. {ECO:0000269|PubMed:30318753}. | Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia) |
A0A649V088 | BLC14_ECOLX | MVTKRVQRMMFAAAACIPLLLGSAPLYAQTSAVQQKLAALEKSSGGRLGVALIDTADNTQVLYRGDERFPMCSTSKVMAAAAVLKQSETQKQLLNQPVEIKPADLVNYNPIAEKHVNGTMTLAELSAAALQYSDNTAMNKLIAQLGGPGGVTAFARAIGDETFRLDRTEPTLNTAIPGDPRDTTTPRAMAQTLRQLTLGHALGETQRAQLVTWLKGNTTGAASIRAGLPTSWTVGDKTGSGDYGTTNDIAVIWPQGRAPLVLVTYFTQPQQNAESRRDVLASAARIIAEGL | 3.5.2.6 | null | beta-lactam antibiotic catabolic process [GO:0030655]; response to antibiotic [GO:0046677] | null | beta-lactamase activity [GO:0008800] | PF13354; | 3.40.710.10; | Class-A beta-lactamase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A5R8T042}. | CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000269|PubMed:26169409, ECO:0000269|PubMed:26282414}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=72 uM for ampicillin (at pH 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:26169409}; KM=12 uM for ampicillin (at pH 7.0 and 30 degrees Celsius) {ECO:0000269|PubMed:26282414}; KM=64 uM for cefalotin (at pH 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:26169409};... | null | null | null | FUNCTION: Extended-spectrum beta-lactamase (ESBL) which confers resistance to penicillins, as well as first, second, and third-generation cephalosporins (PubMed:26169409, PubMed:26282414). Has cefotaxime-hydrolyzing activity (PubMed:26282414). {ECO:0000269|PubMed:26169409, ECO:0000269|PubMed:26282414}. | Escherichia coli |
A0A6B7FMR5 | VMMP3_VIPAA | MIQVLLVIICLAVFPYQVSSIILESGNINNYEVVYPQKVTALPKGAIQQLEQKYEDAMQYQFKVKGEPVVLHLEKNKDFFPEDYSETHYSPDDREITTNPPVEDHCYYYGHIQNDADSTASISACNGLKGYFTLRGVTYLIEPLKIPESEAHAIYKYENVEKEDEDPKKCEFRRAGTECRPARSECDVAEYCTGQSAECPTDVFHSNGKPCLNNFGYCYNGNCPIMYHQCYALFGPNATVGQDGCFEWNKKGESYFYCRKENDVPIPCAPEDIKCGRLFCELIKNTCKYDYSEDPDYGMVDHGTKCGDGKVCINRHCVDV... | null | null | null | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; toxin activity [GO:0090729] | PF08516;PF00200;PF01562; | 4.10.70.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIe sub-subfamily | PTM: N-glycosylated. Exists in at least six differently N-glycosylated forms. The glycans likely have a stabilizing purpose. {ECO:0000269|PubMed:35448841}.; PTM: Cys-199 forms a disulfide bond with Cys-192 in 90% and with Cys-179 in 10% of the protein molecules; alternative disulfide bonds may have a major effect on th... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31017792, ECO:0000269|PubMed:35448841}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Structurally relatively unstable in pure water, but more stable in various buffers between pH 5-9. Most stable in 20 mM HEPES buffer at pH 7 with the addition of 2 mM Ca(2+). {ECO:0000269|PubMed:35448841}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Unfolds at 47 degrees Celsius in pure water, but structurally more stable in various buffers up to 60 degrees Celsius. {ECO:0000269|PubMed:35448841}; | FUNCTION: Abolishes platelet aggregation induced by collagen, ADP (IC(50)=292 nM) and arachidonic-acid. The inhibition of collagen-induced platelet aggregation may be due to its ability to bind collagen and block the binding site on collagen for platelets and/or to its ability to bind to the platelet alpha-2/beta-1 col... | Vipera ammodytes ammodytes (Western sand viper) |
A0A6B9HER0 | PIPCL_PIPNI | MEKSGYGNDGIYRSLRPPVLFPNDPNLSVTSYLFQRSDAYPDRLALADANSGETLNFAQFKAMVQRVSHGLSRLGIKKGDVVLIFSPNSIYFPVCFLAIVALGAVVTTGNPQYTSAEITKQANDSKPKLVITVPQLWDKVNHLGLPAVFLGSKISGDGTIAPSNRNINGTVTYFSNLVELGGHVSEFPPVSIKRSDIAALLYSSGTSGTSKGVILTHRNLISTACMTTSDQEFDGEDPNVFLCFLPMSHVFGLVIICYSQLMRGNSVVSVEKFDLEMVLRSVGKYRVTYLCVVPPVMIALAKQNWGKIYDLSSLKRIICG... | 6.2.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O24146}; | aromatic compound biosynthetic process [GO:0019438] | peroxisome [GO:0005777] | ATP binding [GO:0005524]; butyrate-CoA ligase activity [GO:0047760]; CoA-ligase activity [GO:0016405]; long-chain fatty acid-CoA ligase activity [GO:0004467] | PF00501;PF13193; | 3.30.300.30;3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q9M0X9}. | CATALYTIC ACTIVITY: Reaction=a carboxylate + ATP + CoA = AMP + an acyl-CoA + diphosphate; Xref=Rhea:RHEA:24336, ChEBI:CHEBI:29067, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:31837062}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=43.3 uM for piperic acid {ECO:0000269|PubMed:31837062}; KM=24.3 uM for 5-phenylpentanoic acid {ECO:0000269|PubMed:31837062}; Vmax=19.6 nmol/sec/mg enzyme with piperic acid as substrate {ECO:0000269|PubMed:31837062}; Vmax=27.9 nmol/sec/mg enzyme with 5-phenylpentano... | PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:31837062}. | null | null | FUNCTION: Involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl-piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative,... | Piper nigrum (Black pepper) |
A0A6J2ATK2 | AMPQ_ACIJB | MGPPSSSGFYVSRAVALLLAALAAALLLALAVLAALYGRCARVQPSDLHHGGVPDAASSPRGTQEEQLPTWPPRPTREPAGTATPGHWRPPGPWDQLRLPPWLVPLHYELELWPRLRPNEFQSPTLSFTGRVNITVRCTAATARLLLHSLFLDCESAEVRGPLSSGPRDGAVGRVPVDDVWFAFDMQYMVLELGATLQPGSRYELQLSFSGLVYRDLREGLFFSIYTDQGERRALLASQMEPTFARSVFPCFDEPALKATFNITIIHHPSYGALSNMPKLGQSEKRDVNGSVWTITTFSTTPHMPTYLVALAICDYDHVS... | 3.4.11.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:M3XFH7}; | peptide catabolic process [GO:0043171]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; membrane [GO:0016020] | metalloaminopeptidase activity [GO:0070006]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270] | PF11838;PF01433;PF17900; | 1.25.50.20;2.60.40.1910;1.10.390.10;2.60.40.1730; | Peptidase M1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q6Q4G3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6Q4G3}. | null | null | null | null | null | FUNCTION: Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface (By similarity). Involved in coat pigmentation patterns. During skin development, may be required to establish the periodicity of tabby markings, initiating a pre-pattern ... | Acinonyx jubatus (Cheetah) |
A0A6J4B487 | LUC5_FUSSX | MGAPNSTREPIAIVGTACRFPGGANTPSKLWDLLCEKRDVQTRIPPERFNPDAFYHRNGEKSGCTDVKKAYLLTEDIRAFDASFFKINPREAEAMDPQQRLLLETVYEATEAAGLPYEDLKGSNTAVYVGSMTGDYHEMLLRDPQDMPKYMATGTARSILSNRVSYFFDWKGPSMTIDTACSSSLVAVHEAVTALRLGVSNIACAAGTNLILGPEMMISESKLHMLSPTGRSKMWDASANGYARGEGTAAIMMKTLSQALSDGDHVYGIIRETGVNSDGHTNGITLPSSESQKTLIRQTYANAGLDLIKERCQFFEAHGT... | 2.3.1.-; 6.3.2.- | null | amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; toxin biosynthetic process [GO:0009403] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; isomerase activity [GO:0016853]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | null | null | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:32043422, ECO:0000269|PubMed:35484225}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of the mycotoxin lucilactaene and the lucilactaene-related compound NG-391 that act as cell cycle inhibitors with potent growth inhibitory activity against malarial parasites, moderate growth inhibitory activity against cancer... | Fusarium sp |
A0A6M7H989 | DLMIS_ECO57 | MKRSAINDILGHTRQFFSQHDVHLPPFASFSPAQWQQLDTAAWEEVFDLKLGWDVTAFGRNNFAAHGLTLFTLRNGSAKGMPYVKCYAEKIMHVRDAQVTPMHFHWRKREDIINRGGGNLIVELWNADSNEQTADSDITVVIDGCRQKHTAGSQLRLSPGESICLPPGLYHSFWAEAGFGDVLVGEVSSVNDDDHDNHFLQPLDRYNLIDEDEPAQLVLCNEYRQFR | 5.3.1.15; 5.3.1.7 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:20615418}; | null | null | isomerase activity [GO:0016853]; metal ion binding [GO:0046872] | PF07385; | 2.60.120.10; | D-lyxose ketol-isomerase family | null | null | CATALYTIC ACTIVITY: Reaction=D-lyxose = D-xylulose; Xref=Rhea:RHEA:14201, ChEBI:CHEBI:16789, ChEBI:CHEBI:17140; EC=5.3.1.15; Evidence={ECO:0000269|PubMed:20615418}; CATALYTIC ACTIVITY: Reaction=D-mannose = D-fructose; Xref=Rhea:RHEA:22604, ChEBI:CHEBI:4208, ChEBI:CHEBI:37721; EC=5.3.1.7; Evidence={ECO:0000269|PubMed:20... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=16.1 mM for D-lyxose {ECO:0000269|PubMed:20615418}; KM=19.8 mM for D-mannose {ECO:0000269|PubMed:20615418}; KM=55.2 mM for L-gulose {ECO:0000269|PubMed:20615418}; Vmax=14.1 umol/min/mg enzyme with D-lyxose as substrate {ECO:0000269|PubMed:20615418}; Vmax=13.1 umol/... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:20615418}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:20615418}; | FUNCTION: Sugar isomerase that catalyzes the reversible isomerization of D-lyxose to D-xylulose, and D-mannose to D-fructose (PubMed:20615418). Shows similar activity toward D-lyxose and D-mannose with a turnover and catalytic efficiency for D-lyxose as a substrate only 1.1- and 1.3-fold higher than those for D-mannose... | Escherichia coli O157:H7 |
A0A6P3CW73 | CYCTI_TITOB | MKFIIVLLLLTALTLTSIPVIEGILKRCKTYDDCKDVCKARKGKCEFGICKCMIKSGK | null | null | null | extracellular region [GO:0005576] | serine-type endopeptidase inhibitor activity [GO:0004867] | null | null | null | PTM: This is a cyclic peptide. {ECO:0000269|PubMed:32787139}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32787139}. | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Is very stable at high temperature. {ECO:0000269|PubMed:32787139}; | FUNCTION: First cyclic scorpion trypsin inhibitor (Kd~0.5 nM). Does not inhibit chymotrypsin. {ECO:0000269|PubMed:32787139}. | Tityus obscurus (Amazonian scorpion) (Tityus cambridgei) |
A0A6P3HVI0 | SL9B2_BISBB | MRNQDKRAAHKDSEPSTEVNHTASSYQGRQQETGMNLRGIDGNEPTEGSNLLNNNEKMQGTPAEPNHLQRRRQIHACPPRGLLARVITNVTMVILLWAVVWSVTGSECLPGGNLFGIIMLFYCAIIGGKLFGLIKLPTLPPLPPLLGMLLAGFLIRNVPVISDNIQIKHKWSSALRSIALSVILVRAGLGLDSNALKKLKGVCVRLSLGPCLIEACTSAVLAYFLMGLPWQWGFMLGFVLGAVSPAVVVPSMLLLQEGGYGVEKGIPTLLMAAGSFDDILAITGFNTCLGMAFSTGSTVFNVLKGVLEVIIGVVTGLVLG... | null | null | lithium ion transport [GO:0010351]; sodium ion homeostasis [GO:0055078]; sodium ion transport [GO:0006814] | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; endosome membrane [GO:0010008]; lysosomal membrane [GO:0005765]; mitochondrial membrane [GO:0031966]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; sperm principal piece [GO:0097228]... | identical protein binding [GO:0042802]; lithium:proton antiporter activity [GO:0010348]; metal ion binding [GO:0046872]; sodium:proton antiporter activity [GO:0015385] | PF00999; | 1.20.1530.20; | Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:35173351}; Multi-pass membrane protein {ECO:0000269|PubMed:35173351}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000269|PubMed:35173351}. Endosome membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {E... | CATALYTIC ACTIVITY: Reaction=H(+)(in) + Li(+)(out) = H(+)(out) + Li(+)(in); Xref=Rhea:RHEA:72407, ChEBI:CHEBI:15378, ChEBI:CHEBI:49713; Evidence={ECO:0000269|PubMed:35173351}; CATALYTIC ACTIVITY: Reaction=Li(+)(in) + Na(+)(out) = Li(+)(out) + Na(+)(in); Xref=Rhea:RHEA:72415, ChEBI:CHEBI:29101, ChEBI:CHEBI:49713; Eviden... | null | null | null | null | FUNCTION: Electroneutral Na(+) Li(+)/H(+) antiporter that extrudes Na(+) or Li(+) in exchange for external protons across the membrane (PubMed:35173351). Uses the proton gradient/membrane potential to extrude sodium (By similarity). Contributes to the regulation of intracellular pH and sodium homeostasis (By similarity... | Bison bison bison (North American plains bison) |
A0A6P6DKR7 | APOE_OCTDE | MKVLCTVLVVTLLAGCRADVEPEPEVLEPAVWKSGQPWELALGRFWDYVRWVQTLSDQVQEELLSSQVTQELTVLMEDTMKAVKAYKSELEQELVPMAEDTKARLSKELQAAQARLGADMEEVRNRLAQYRNEMQAMLGQSADELRARLASHLRKLRKRMLRDAEDLQKRLAVYKDGASEGAERGVSAIRERLGSLVEQSRVRAALTGQPLQERAQAWGKQLRGRLEEVRGQAQDRLEEMREQMEEVRVKIEEQAEAFQTRLKGWFEPMVEDMRRQWADLIEKVQAAVGASTPVPSQKP | null | null | cholesterol catabolic process [GO:0006707]; lipid transport [GO:0006869]; lipoprotein catabolic process [GO:0042159]; melanosome organization [GO:0032438]; negative regulation of neuron apoptotic process [GO:0043524]; regulation of amyloid-beta clearance [GO:1900221] | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lipoprotein particle [GO:0034361] | amyloid-beta binding [GO:0001540]; heparin binding [GO:0008201]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | 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. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Octodon degus (Degu) (Sciurus degus) |
A0A6P6W6H5 | TPS1_COFAR | MAIINLPVPTNSSSEVNKHNHLRSCLPSGRATFTTLSAAAMRSATMAAANVREQSGQKQQLINRRSGNYEAPLWEFDYIQSLKNEYAGDIYVSRANELKEQVKMMLDEEDMKLLDCMELVDGLERLGLAYHFEGRINRLLSSDYKAIHEGNHQRNKEDLYAAALEFRIFRQNGFNVPQDIFNDFITEDGEFDESLSEDTMGLLSLYEASFLSLEGEATLDLAREFTTKHLNNYLGKENTDQNLRILVYHALELPLRWRAPRIEARWYIDAYERSPNVNPTLLELAKIDFNIVQAIHQQDLKHVSWWWKNIRIAEKLTFIR... | 4.2.3.-; 4.2.3.113; 4.2.3.15; 4.2.3.47 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7}; | alpha-pinene biosynthetic process [GO:0046248]; diterpenoid biosynthetic process [GO:0016102]; limonene biosynthetic process [GO:0046250]; monoterpenoid metabolic process [GO:0016098] | chloroplast [GO:0009507] | magnesium ion binding [GO:0000287]; myrcene synthase activity [GO:0050551]; pinene synthase activity [GO:0050550]; sabinene synthase activity [GO:0080015] | PF01397;PF03936; | 1.10.600.10;1.50.10.130; | Terpene synthase family, Tpsb subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate = (E)-beta-farnesene + diphosphate; Xref=Rhea:RHEA:27425, ChEBI:CHEBI:10418, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.47; Evidence={ECO:0000269|PubMed:23398891}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27426; Evidence={ECO:0000269|PubMed:2339... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:23398891}. | null | null | FUNCTION: Monoterpene synthase (mono-TPS) involved in the biosynthesis of monoterpenes natural products, constituent of coffee beverage aroma (PubMed:23398891). Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into limonene, beta-pinene, sabinene and beta-myrcene, and, as minor products, alpha-pinene and alph... | Coffea arabica (Arabian coffee) |
A0A6S6QJ62 | PLE4_RHOPP | MRIPNIFLSYLRQVAVDGTLSSCSGVKSRKPVIAFGFDDSQDSLVDENDEKILEPFGYYRHLLKGKSARTVLMHCFNAFLGLPEDWVLGVTKAIEDLHNASLLIDDIEDESALRRGSPAAHMKYGIALTMNAGNLVYFTVLQDIYDLGMRTGGTQVANAMAHIYTEEMIELHRGQGIEIWWRDQRSPPSVDQYIHMLEQKTGGLLRLGVRLLQCHPGGNNRADLSAIALRIGVYYQLRDDYINLMSTSYHDERGFAEDITEGKYTFPMLHSLKRSPDSGLREILDLKPADIALKKKAIAIMQETGSLIATRNLLGAVKND... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | antibiotic biosynthetic process [GO:0017000]; plastoquinone biosynthetic process [GO:0010236]; terpenoid biosynthetic process [GO:0016114]; ubiquinone biosynthetic process [GO:0006744] | mitochondrion [GO:0005739]; transferase complex [GO:1990234] | metal ion binding [GO:0046872]; prenyltransferase activity [GO:0004659] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000250|UniProtKB:Q12051}; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl dip... | null | PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:28924980}. | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase; part of the gene cluster that mediates the biosynthesis of pleuromutilin, a tricyclic diterpene showing antibacterial properties (PubMed:28924980). The geranylgeranyl diphosphate (GGPP) synthase ple4 catalyzes the first step in pleuromutilin biosynthesis (PubMed:28924980... | Rhodocybe pseudopiperita (Clitopilus pseudopiperitus) |
A0A7E6FSU6 | OXDD_OCTVU | MVKIAVIGAGVVGLSTALQVKQNFPFCSVTVVAEKFNTETTSDGAGGLFRPNFLTLSANPLESIKQWSQDTFSHFNNLFNSPEASDCGIALMSGFLLSNKEKLDMIEDISLGQSKMTAEQIAKMGFDCKHVTKVLTYTMECRRYMPWLTSKFLSLGGSMHHHRLKSLEELVGVYDVVVNCSGLGAKDLVPDPLVYPVKGQLIQVEAPWVKHFYFFEDDTYVIPNINRTSLGGIRIKNDYSTEVDPEISKSIWQRCTSRIPSLQKAKVLWEWAGLRPHRDPIRIEQDVMNFPKGTLKVVHNYGHGANGVSLSWGTAKHATR... | 1.4.3.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:7915543}; | D-amino acid catabolic process [GO:0019478] | peroxisomal matrix [GO:0005782] | D-aspartate oxidase activity [GO:0008445]; FAD binding [GO:0071949] | PF01266; | 3.30.9.10;3.40.50.720; | DAMOX/DASOX family | null | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:Q99489}. | CATALYTIC ACTIVITY: Reaction=D-aspartate + H2O + O2 = H2O2 + NH4(+) + oxaloacetate; Xref=Rhea:RHEA:12512, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938, ChEBI:CHEBI:29990; EC=1.4.3.1; Evidence={ECO:0000269|PubMed:7915543}; PhysiologicalDirection=left-to-right; Xref=Rhea:R... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.3 mM for D-aspartate (at 25 degrees Celsius and at pH 7) {ECO:0000269|PubMed:7915543}; KM=9.7 mM for D-glutamate (at 25 degrees Celsius and at pH 7) {ECO:0000269|PubMed:7915543}; KM=47.7 mM for N-methyl D-aspartate(at 25 degrees Celsius and at pH 7) {ECO:0000269|... | null | null | null | FUNCTION: Selectively catalyzes the oxidative deamination of acidic amino acids (PubMed:7915543). Suppresses the level of D-aspartate in the brain, an amino acid that can act as an agonist for glutamate receptors (By similarity). Protects the organism from the toxicity of D-amino acids (By similarity). May also functio... | Octopus vulgaris (Common octopus) |
A0A7G6KN55 | DFB13_CROPO | MRLLYLLFAAVMLLFLQAVPANGSYYSTLQCRNNHGHCRRLCFHGEQWIGNCNGRHQHCCK | null | null | cell chemotaxis [GO:0060326]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; killing of cells of another organism [GO:0031640] | extracellular space [GO:0005615] | CCR6 chemokine receptor binding [GO:0031731]; chemoattractant activity [GO:0042056]; identical protein binding [GO:0042802]; phosphatidic acid binding [GO:0070300] | PF00711; | null | Beta-defensin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:33309943, ECO:0000305|PubMed:36859344}. | null | null | null | null | null | FUNCTION: Exhibits antimicrobial activity against fungi (PubMed:36859344). Antimicrobial activity in a pH-dependent manner against the yeast C.albicans; activity is salt tolerant and retains antifungal activity in NaCl concentrations of 100mM (PubMed:36859344). Permeabilizes C.albicans cell membranes via targeting plas... | Crocodylus porosus (Saltwater crocodile) (Estuarine crocodile) |
A0A7J6K7I9 | WNG2_TOXGO | MMFPAVAAPPRRLPGERLQRSQNPVETSWLSFRILATRGPCVTSTFLFLTVAFLGLSWVSVAVAAHAEHPEDSATNFLFSFAENSLANREPPEDSAARPSSRSGGAERRRLDSLIPGFLKRRRIFKQLRPVDEFQLREFQEASSKVKAQFFSAGHSKVTFVDRPSAALLSFLHLEEEDVPYGVVIKAIPYDAFDFYESVAEPYIHRMFDDPRKFPYVVPVLAALRSTSKRVLYLVLPLYRELPETVDEEARSLDFVLLLAEMAMAVCQLHERNLAHRDLKEDNFLVSPEGHIVVSDLATLDITDNKSFLIGTSGYMPPET... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A7J6K7Y0}; | phosphorylation [GO:0016310] | extracellular region [GO:0005576] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, WNG subfamily | null | SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:30850550}. Secreted {ECO:0000269|PubMed:30850550}. Parasitophorous vacuole lumen {ECO:0000269|PubMed:30850550}. Note=In tachyzoites, localizes to dense granules. {ECO:0000269|PubMed:30850550}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:A0A7J6K7Y0}; CATA... | null | null | null | null | FUNCTION: Probable serine/threonine-protein kinase. {ECO:0000305}. | Toxoplasma gondii |
A0A7J6K7Y0 | WNG1_TOXGO | MPEQDLASGFLLRFQNARPVCLSVGSFVSFRTVQPRKMRDRGWRCVWHRMAGVGALFGIFGVLCTVEAGATVAAPQVETGPLLSVRAPRSPLHLRDVDAPEVTHASSEGSPQFESSLSQQRLRRPADRGEAHNGEEPRKDAATQTVRGYGGQSTEPPPASIVPVSSEAPQDGAEQRQASSAAESLAGLDPDAGDTGLRSQEMDEEGSGAAQDMERAHAAQPTVSTWDDAHLVQVSTSHPDMFPVDGSFSKKQEGRRERRLAVRGDDSFARGHNRDRDASNGRSILRRAPGWAKIAALATGLLVSAFGYSSYKHGGPRVAL... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:30850550}; | chromosome segregation [GO:0007059]; microtubule-based process [GO:0007017]; phosphorylation [GO:0016310] | centrosome [GO:0005813]; cortical microtubule [GO:0055028]; extracellular region [GO:0005576]; nucleus [GO:0005634] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, WNG subfamily | null | SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:30850550}. Secreted {ECO:0000269|PubMed:30850550}. Parasitophorous vacuole lumen {ECO:0000269|PubMed:30850550}. Note=In tachyzoites, localizes to dense granules. {ECO:0000269|PubMed:30850550}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:30850550}; CATALYTIC... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=520 uM for ATP (at pH 7.5 and 30 degrees Celsius) {ECO:0000269|PubMed:30850550}; | null | null | null | FUNCTION: Serine/threonine-protein kinase which, at the tachyzoite stage, phosphorylates several parasitophorous vacuole (PV)-resident proteins such as GRA2, GRA6 and GRA7 (PubMed:30850550). By phosphorylating GRA2 and GRA6, regulates the formation of a functional intravacuolar network (IVN); IVN is composed of membran... | Toxoplasma gondii |
A0A7L8UVC9 | FFSA_ASPFV | MATTTAPTTQGHNQPSREPIAIVGSACRFPGGASSPSKLWKLLEHPRDVLKEIPPDRFSVDGFYHPDNMHHGTSNVRHSYILDDDIRVFDAQFFGIKPVEANSIDPQQRLLMETVYEGIESAGLQLNKMKGSQTGVYVGLMSNDYADMLGNDQESFPTYFATGTARSIVSNRVSYFFDWHGPSMTIDTACSSSLVAMHQAVQYLRSGDGSDVAIAAGTNILLNPDQYIAESKLKMLSPDGRSQMWDEKANGYARGDGIAVVVLKTLSQALRDGDHIECIVRETHINQDGKTKGITMPSATAQTALIRSTYKNAGLDITKP... | 2.3.1.-; 6.3.2.- | null | amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; toxin biosynthetic process [GO:0009403] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; isomerase activity [GO:0016853]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | null | null | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000305|PubMed:32913332}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of the cytotoxic leucine-containing cytochalasans, including aspochalasin C, aspochalasin E, TMC-169, flavichalasine F, aspergillin PZ, aspochalasin M and flavichalasine G (PubMed:32913332). The first step in the pathway is ca... | Aspergillus flavipes |
A0A7L9EYL1 | XENE_XENSI | MSGQDPVKESGQREPIAVVGSGFRFPGSSNNPSKLWDLLVKPRDLLTKIPENRFNSDAFYHPKPFHHGTSDVRESYFLEEDHRQFDAAFFNIKPVEVHAIDPQQRILMEAVYESLEAAGLSMESLAGSRTGVYVGLMCADYVDLLNNDVNSLPTYTPTGTARSIMSNRISYFFDWHGPSMTIDTACSSSLVAVHQAVQLLRSGDSDVAVAAGANLMLGPLPYIAESKLQMLSSNSRSRMWDIDASGYARGEGVAAVVLKRLSSAIADGDQIECIIRESGINQDGRTKGITMPSSVAQADLISRTYAKAGLNPRDPTERCQ... | 2.3.1.-; 6.3.2.- | null | amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; toxin biosynthetic process [GO:0009403] | null | 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | null | null | null | PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:34900544}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of xenoacremones such as xenoacremone A, a compound that shows inhibitory activity toward the PI3K/AKT signaling pathway and which has the ability to induce apoptosis of A549 lung cancer cells (PubMed:34900544). Within the pat... | Xenoacremonium sinensis (Endophyte fungus) |
A0A7U9P668 | CDAS_GEOTM | MRKEAIHHRSTDNFAYAYDSETLHLRLQTKKNDVDHVELLFGDPYEWHDGAWQFQTMPMRKTGSDGLFDYWLAEVKPPYRRLRYGFVLRAGGEKLVYTEKGFYHEAPSDDTAYYFCFPFLHRVDLFQAPDWVKDTVWYQIFPERFANGNPAISPKGARPWGSEDPTPTSFFGGDLQGIIDHLDYLADLGITGIYLTPIFRAPSNHKYDTADYFEIDPHFGDKETLKTLVKRCHEKGIRVMLDAVFNHCGYEFGPFQDVLKNGAASRYKDWFHIREFPLQTEPRPNYDTFAFVPQMPKLNTAHPEVKRYLLDVATYWIREF... | 3.2.1.54 | null | pullulan catabolic process [GO:0051678] | null | cyclomaltodextrinase activity [GO:0047798]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803] | PF00128;PF02903;PF16657; | 3.20.20.80;2.60.40.1180;2.60.40.10; | Glycosyl hydrolase 13 family | null | null | CATALYTIC ACTIVITY: Reaction=cyclomaltodextrin + H2O = linear maltodextrin; Xref=Rhea:RHEA:23980, Rhea:RHEA-COMP:14584, Rhea:RHEA-COMP:14707, ChEBI:CHEBI:15377, ChEBI:CHEBI:17623, ChEBI:CHEBI:18398; EC=3.2.1.54; Evidence={ECO:0000269|PubMed:31212108}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23981; Evidence... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 mM for alpha-cyclodextrin {ECO:0000269|PubMed:31212108}; KM=0.6 mM for beta-cyclodextrin {ECO:0000269|PubMed:31212108}; KM=0.4 mM for gamma-cyclodextrin {ECO:0000269|PubMed:31212108}; Vmax=1200 umol/min/mg enzyme with alpha-cyclodextrin as substrate {ECO:000026... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0 for hydrolysis of alpha-cyclodextrin. {ECO:0000269|PubMed:31212108}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius for hydrolysis of alpha-cyclodextrin. Thermostable. No significant loss of catalytic activity even after overnight incubation at 65 degrees. EDTA enhances the thermostability, the half-life being 90 minutes at 70 degrees C... | FUNCTION: Hydrolyzes alpha-, beta- and gamma-cyclodextrins with the highest activity with alpha-cyclodextrin (cyclomaltohexaose). Pullulan is the preferred substrate from linear substrates. Maltose is a major product of these reactions. Is also able to hydrolyze maltotriose and acarbose, and transglycosylate their hydr... | Geobacillus thermopakistaniensis (strain MAS1) |
A0A858E6N7 | GGDPS_MELLI | MKPLPSTNGKVNGNGKHHDSSLSSTSSTSSSSSSDTQFNISDRYGDFLHRLDTLDTWPKSNEQILLEPYTYLNNIPGKEIRSMMIDAFNHWLQIPRPALEIIKKIVGQLHTASLLMDDVEDDSDLRRGVPVTHKIYGIPQTINTANYVYFLAYQELSKLKPCLSSNASTDLWSLVNDELLQLHRGQGMDLYWRDSLTCPTEEEYLQMVNNKTGGLFRIAIKLMIALSPLTETPDYLPLVNLVGIIFQIRDDLLNLSSVYTKNKGFCEDLTEGKFSFPIVHSIRADSSNHQLMNILRQKPTDIGTKTFAVSYMKDQTKSLQ... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | isoprenoid biosynthetic process [GO:0008299]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744] | mitochondrion [GO:0005739]; transferase complex [GO:1990234] | lyase activity [GO:0016829]; metal ion binding [GO:0046872]; prenyltransferase activity [GO:0004659] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000269|PubMed:32913319}; PhysiologicalDirection=left-to-right; Xref=Rhe... | null | null | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase that catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate (PubMed:32913319). Does not show any monoterpene nor sesquiterpene synthase activity (PubMed:32913319). {ECO:0000269|PubMed:32913319}. | Melampsora lini (Rust fungus) |
A0A858E7G0 | GGDPS_MELLP | MKPVPSTNGKVDDKVEHHNLSSSSSSSSSSSSSDTKFNISNRYGNFLQRLEALDIWPESNEQILLEPYTYLTNIPGKEIRSMMIDAFNHWLQVPRPALEIIKKIVGQLHTASLLMDDVEDDSDLRRGVPVTHKIYGIPQTINTANYVYFLAYQELTKLKPCLRSDATTDLWSLVNDELLQLHRGQGMDLYWRDSLTCPTEEEYLQMVNNKTGGLFRIAIKLMIALSPIPETPDYLPLVNLVGIIFQIRDDLLNLSSVYTKNKGFCEDLTEGKFSFPIVHSIRSDSTNHQLMNILRQKPTDIGTKAFAVSYMKDRTKSLEY... | 2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q12051}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051}; | isoprenoid biosynthetic process [GO:0008299]; plastoquinone biosynthetic process [GO:0010236]; ubiquinone biosynthetic process [GO:0006744] | mitochondrion [GO:0005739]; transferase complex [GO:1990234] | lyase activity [GO:0016829]; metal ion binding [GO:0046872]; prenyltransferase activity [GO:0004659] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; Evidence={ECO:0000269|PubMed:32913319}; PhysiologicalDirection=left-to-right; Xref=Rhe... | null | null | null | null | FUNCTION: Geranylgeranyl pyrophosphate synthase that catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate (PubMed:32913319). Does not show any monoterpene nor sesquiterpene synthase activity (PubMed:32913319). {ECO:0000269|PubMed:32913319}. | Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf rust fungus) |
A0A8B7DWS6 | ACTL1_HYDVU | MLLYICLVNLLLPLSVGAASGAALGVIAKVGVDAALQQIDDVWKGKTVRYWKCAVENRSSKTLYALGTTQESGSMTTVFADIPPKSTGVFVWEKSRGAAKGAVGVVHYKYGNKVLNIMASIPYDWNLYKAWANVHLSDHKESFSDLYKGKNGAKYPTRAGNWGEVDGTKFFLTEKSHAEFKVIFSG | null | null | cytolysis in another organism [GO:0051715]; monoatomic cation transport [GO:0006812]; pore complex assembly [GO:0046931] | extracellular region [GO:0005576]; nematocyst [GO:0042151]; other organism cell membrane [GO:0044218]; pore complex [GO:0046930] | channel activity [GO:0015267]; toxin activity [GO:0090729] | PF06369; | 2.60.270.20; | Actinoporin family, HALT subfamily | null | SUBCELLULAR LOCATION: Nematocyst {ECO:0000269|PubMed:31513812}. Secreted {ECO:0000250|UniProtKB:B9W5G6}. Target cell membrane {ECO:0000250|UniProtKB:B9W5G6}. Note=Is found in differentiating stenoteles (one type of nematocyst) (PubMed:31513812). Forms an alpha-helical membrane channel in the prey (By similarity). {ECO:... | null | null | null | null | null | FUNCTION: Pore-forming protein that forms hydrophilic pores and causes cytolysis (PubMed:24768765, PubMed:31513812). Compared to equinatoxin-2 (AC P61914), it reveals lower cytolysis activity (5-12-fold difference, tested on erythrocytes), a larger pore size (probably 2-3 nm) and different affinity to membrane lipids (... | Hydra vulgaris (Hydra) (Hydra attenuata) |
A0A8H8CMW1 | CUBA_PSICU | MSTEQFVLPDLLESCPLKDATNPYYKEAAAESRAWINGYDIFTDRKRAEFIQGQNELLCSHVYWYAGREQLRTTCDFVNLLFVVDEVSDEQNGKGARETGQVFFKAMKYPDWDDGSILAKVTKEFMARFTRLAGPRNTKRFIDLCESYTACVGEEAELRERSELLDLASYIPLRRQNSAVLLCFALVEYILGIDLADEVYEDEMFMKAYWAACDQVCWANDIYSYDMEQSKGLAGNNIVSILMNENGTNLQETADYIGERCGEFVSDYISAKSQISPSLGPEALQFIDFVGYWMIGNIEWCFETPRYFGSRHLEIKETRV... | 4.2.3.-; 4.2.3.127; 4.2.3.128; 4.2.3.129; 4.2.3.91; 4.2.3.98 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UR08}; | null | null | metal ion binding [GO:0046872]; terpene synthase activity [GO:0010333] | PF19086; | 1.10.600.10; | Terpene synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + H2O = cubebol + diphosphate; Xref=Rhea:RHEA:31823, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019, ChEBI:CHEBI:63446, ChEBI:CHEBI:175763; EC=4.2.3.91; Evidence={ECO:0000269|PubMed:37614035}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31824; Evidence={ECO:00002... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:37614035}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 29 degrees Celsius. {ECO:0000269|PubMed:37614035}; | FUNCTION: Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to various sesquiterpenes, including cubebol as the major product and beta-copaene, delta-cadinene, germacrene D, germacrene D-4-ol, sativene, tau-muurolol, beta-cubebene and beta-elemene as minor compounds, along with minute amounts... | Psilocybe cubensis (Psychedelic mushroom) (Stropharia cubensis) |
A0A8I3NFE2 | SHIP2_CANLF | MASACGAPGPGGAGPGGALGSPAPAWYHRDLSRAAAEELLARAGRDGSFLVRDSESVAGAFALCVLYQKHVHTYRILPDGEDFLAVQTSQGVPVRRFQTLGELIGLYAQPNQGLVCALLLPVEREREPDPPDDRDVSDGEDEKPPLPPRSGSTSISAPVGPGSPPAAPETPTTPAAESAPNGLSTVSHEYLKGSYGLDLEAVRGGASNLPHLTRTLATSCRRLHSEVDKVLAGLEILSKVFDQQSSPMVTRLLQQQNPAQTGEQELESLVLKLSVLKDFLSGIQKKALKVLQDMSSTAPPAPPQPAIRKAKTVPVQAFEV... | 3.1.3.86 | null | immune system process [GO:0002376]; negative regulation of insulin-like growth factor receptor signaling pathway [GO:0043569]; phosphatidylinositol dephosphorylation [GO:0046856]; regulation of immune response [GO:0050776] | basal plasma membrane [GO:0009925]; cytosol [GO:0005829]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; nuclear speck [GO:0016607]; spindle pole [GO:0000922] | actin binding [GO:0003779]; inositol-polyphosphate 5-phosphatase activity [GO:0004445]; SH3 domain binding [GO:0017124] | PF00536;PF00017; | 3.60.10.10;3.30.505.10;1.10.150.50; | Inositol 1,4,5-trisphosphate 5-phosphatase family | PTM: Tyrosine phosphorylated by the members of the SRC family after exposure to a diverse array of extracellular stimuli such as insulin, growth factors such as EGF or PDGF, chemokines, integrin ligands and hypertonic and oxidative stress. May be phosphorylated upon IgG receptor FCGR2B-binding. Phosphorylated at Tyr-99... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15357}. Membrane {ECO:0000250|UniProtKB:O15357}; Peripheral membrane protein. Cell projection, filopodium {ECO:0000250|UniProtKB:O15357}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O15357}. Basal cell membrane {ECO:0000269|PubMed:27926875}. Nuc... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + phosphate; Xref=Rhea:RHEA:25528, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57658, ChEBI:CHEBI:57836; EC=3.1.3.86; Evidence={ECO:0000... | null | null | null | null | FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways (By similarity). Required for correct mitotic spindle orien... | Canis lupus familiaris (Dog) (Canis familiaris) |
A0A8I3P7X4 | CCD47_CANLF | MKASLAFCVVLLVFGSVSEAKFDDFEDEEDIVEYDDNDFAEFEDVTEDSVTESPQRVITTEDDEDETTVELEGQDENQEGDFEDADTQEGDTESEPYDDEEFEGYEDKPDTSSSKNKDPITIVDVPAHLQNSWESYYLEILMVTGLLAYIMNYIIGKNKNSRLAQAWFNTHRELLESNFTLVGDDGTNKEATSTGKLNQENEHIYNLWCSGRVCCEGMLIQLRFLKRQDLLNVLARMMRPVSDQVQIKVTMNDEDMDTYVFAVGTRKALVRLQKEMQDLSEFCSDKPKSGAKYGLPDSLAILSEMGEVTEGMMDTKMVHF... | null | null | endoplasmic reticulum calcium ion homeostasis [GO:0032469]; multi-pass transmembrane protein insertion into ER membrane [GO:0160063] | endoplasmic reticulum membrane [GO:0005789]; multi-pass translocon complex [GO:0160064]; rough endoplasmic reticulum membrane [GO:0030867] | calcium ion binding [GO:0005509] | PF07946; | null | CCDC47 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:36261528}; Single-pass type I membrane protein {ECO:0000269|PubMed:36261528}. Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9D024}; Single-pass type I membrane protein {ECO:0000269|PubMed:36261528}. | null | null | null | null | null | FUNCTION: Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes (PubMed:36261528). The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 ... | Canis lupus familiaris (Dog) (Canis familiaris) |
A0A8I3PDQ1 | CASL_CANLF | MWARNLMARALYDNVPECAEELAFRKGDILTVIEQNTGGLEGWWLCSLHGRQGIVPGNRVKLLIGPIQETPSGQDQPTSGLMHQTFGQQKLYQVPNPHSAPRDTIYQVPPSYQHQGIYQVPTSHGIQEQDVYQVPPSVQRSIGAANGPHLSKKVVTPVRTGQGYVYEYPSRHQKDIYDIPPSHTTQGVYDIPPSSVKVPVFSLPVGEIKPQGVYDIPPTKGLYAIPPSACRDEAGLREKEYDFPPPMRQAGRLDVRPEGVYDIPPTSTKPTGKDLHIKYNCDAPGAAELATRRHQSVLLNHAPSQLGQSPGAQNDAYDVP... | null | null | cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell division [GO:0051301]; cell migration [GO:0016477]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | basolateral plasma membrane [GO:0016323]; cell cortex [GO:0005938]; cilium [GO:0005929]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; spindle pole [GO:0000922] | null | PF12026;PF08824;PF14604; | 1.20.120.230;1.20.120.830;2.30.30.40; | CAS family | PTM: Polyubiquitinated by ITCH/AIP4, leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q14511}.; PTM: PTK2/FAK1 phosphorylates the protein at the YDYVHL motif (conserved among all cas proteins) following integrin stimulation (By similarity). The SRC family kinases (FYN, SRC, LCK and CRK) are recruited to the p... | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q14511}. Nucleus {ECO:0000250|UniProtKB:Q14511}. Golgi apparatus {ECO:0000250|UniProtKB:Q14511}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q14511}. Cytoplasm {ECO:0000250|UniProtKB:Q14511}. Cell junction, focal adhesion {ECO:0000250|UniProt... | null | null | null | null | null | FUNCTION: Negatively regulates embryonic fibroblast migration (By similarity). May play an important role in integrin beta-1 or B cell antigen receptor (BCR) mediated signaling in B- and T-cells. Integrin beta-1 stimulation leads to recruitment of various proteins including CRKl and SHPTP2 to the tyrosine phosphorylate... | Canis lupus familiaris (Dog) (Canis familiaris) |
A0A8I3PI99 | TMCO1_CANLF | MSTMFADTLLIVFISVCTALLAEGITWVLVYRTDKYKRLKAEVEKQSKKLEKKKETITESAGRQQKKKIERQEEKLKNNNRDLSMVRMKSMFAIGFCFTALMGMFNSIFDGRVVAKLPFTPLSYIQGLSHRNLLGDDTTDCSFIFLYILCTMSIRQNIQKILGLAPSRAATKQAGGFLGPPPPSGKFS | null | null | endoplasmic reticulum calcium ion homeostasis [GO:0032469]; multi-pass transmembrane protein insertion into ER membrane [GO:0160063] | endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; multi-pass translocon complex [GO:0160064] | calcium channel activity [GO:0005262] | PF01956; | null | TMCO1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:36261528}; Multi-pass membrane protein {ECO:0000269|PubMed:36261528}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UM00}; Multi-pass membrane protein {ECO:0000269|PubMed:36261528}. Note=The first transmembrane region is required for localizat... | null | null | null | null | null | FUNCTION: Calcium-selective channel required to prevent calcium stores from overfilling, thereby playing a key role in calcium homeostasis (By similarity). In response to endoplasmic reticulum (ER) overloading, assembles into a homotetramer, forming a functional calcium-selective channel, regulating the calcium content... | Canis lupus familiaris (Dog) (Canis familiaris) |
A0A8I3S724 | AURKA_CANLF | MDKSKENCIAGPVKTAIALGDGPKRVLVTQQVPSQNPLSANSGQAQRVLCPSNSSQRVPPQTQKLVSSHKPAQNLKQKQLQATGVPRPASRSLNNTQKSEQPSSSAPGNNSEKELATKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILAIKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGAVYRELQKLSKFDEQRTATYITELADALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLC... | 2.7.11.1 | null | cell division [GO:0051301]; meiotic spindle organization [GO:0000212]; mitotic centrosome separation [GO:0007100]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of mitotic cell cycle [GO:0045931]; regulation of cytokinesis [GO:0032465] | basolateral plasma membrane [GO:0016323]; centriole [GO:0005814]; chromosome passenger complex [GO:0032133]; cilium [GO:0005929]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; neuron projection [GO:0043005]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]; spindle pole [GO:0000922]; spindle pole cent... | ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily | PTM: Activated by phosphorylation at Thr-289; this brings about a change in the conformation of the activation segment (By similarity). Phosphorylation at Thr-289 varies during the cell cycle and is highest during M phase (By similarity). Autophosphorylated at Thr-289 upon TPX2 binding (By similarity). Thr-289 can be p... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O14965}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:27926875}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P97477}. Cell projection, neu... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:O14965}; CATALYTI... | null | null | null | null | FUNCTION: Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression (By similarity). Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, c... | Canis lupus familiaris (Dog) (Canis familiaris) |
A0A8I3S9V6 | RCAF1_CANLF | MSGGRRKEEPPQPQLANGALKVSVWSKVLRSDAAWEDKDEFLDVIYWFRQIIAVVLGVIWGVLPLRGFLGIAGFCVINAGVLYLYFSNYLQIDEEEYGGTWELTKEGFMTSFALFMVIWIIFYTAIHYD | null | null | mitochondrial respirasome assembly [GO:0097250]; multi-pass transmembrane protein insertion into ER membrane [GO:0160063] | endoplasmic reticulum membrane [GO:0005789]; mitochondrial inner membrane [GO:0005743]; multi-pass translocon complex [GO:0160064] | null | PF07019; | null | EMC6 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:36261528}; Multi-pass membrane protein {ECO:0000269|PubMed:36261528}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9BUV8}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes (PubMed:36261528). The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 ... | Canis lupus familiaris (Dog) (Canis familiaris) |
A0A8I5ZN27 | CNGB1_RAT | MLGWVQRVLPQPPGTPQKTEEGAGPQPETESKPEANPQPEPEVQPEPEPEPEPAPEEAAPEVQTLPPEEPVEGEDVAEAGPSLQETQEADPPQPTSQAQVAVVKVNRPSSWMLSWFWKGMEKVVPQPVYSSSGGQNLAAGEGGPDQDGAQTLEPCGTGDPGSEDGSDKTSKTQDTEPSLWLLRWLELNLEKVLPQPPTPSQAWKVEPEGAVLEPDPPGTPMEVEPTENPSQPNPGPVEPEEEPAAEPQPGFQASSLPPPGDPVRLIEWLLHRLEMALPQPVLHGKAAEQEPSCPGTCDVQTISILPVEQAEHDLVLEDVD... | null | null | detection of chemical stimulus involved in sensory perception of smell [GO:0050911]; detection of light stimulus involved in visual perception [GO:0050908]; ion channel modulating, G protein-coupled receptor signaling pathway [GO:0099105]; membrane depolarization [GO:0051899]; monoatomic cation transmembrane transport ... | intracellular cyclic nucleotide activated cation channel complex [GO:0017071]; membrane [GO:0016020]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]; terminal bouton [GO:0043195]; transmembrane transporter complex [GO:1902495] | cAMP binding [GO:0030552]; cGMP binding [GO:0030553]; cyclic nucleotide-activated monoatomic ion channel activity [GO:0043855]; intracellularly cAMP-activated cation channel activity [GO:0005222]; intracellularly cGMP-activated cation channel activity [GO:0005223]; intracellularly cyclic nucleotide-activated monoatomic... | PF00027; | 1.10.287.70;1.10.287.630;2.60.120.10; | Cyclic nucleotide-gated cation channel (TC 1.A.1.5) family, CNGB1 subfamily | null | SUBCELLULAR LOCATION: [Isoform 2]: Cell projection, cilium membrane {ECO:0000269|PubMed:10377344}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:9878057}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10377344}; CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); ... | null | null | null | null | FUNCTION: Pore-forming subunit of the rod cyclic nucleotide-gated channel. Mediates rod photoresponses at dim light converting transient changes in intracellular cGMP levels into electrical signals. In the dark, cGMP levels are high and keep the channel open enabling a steady inward current carried by Na(+) and Ca(2+) ... | Rattus norvegicus (Rat) |
A0A8I5ZNK2 | OXSR1_RAT | MSEDSSALPWSINRDDYELQEVIGSGATAVVQAAYCAPKKERVAIKRINLEKCQTSMDELLKEIQAMSQCHHPNIVSYYTSFVVKDELWLVMKLLSGGSVLDIIKHIVAKGEHKGGVLDESTIATILREVLEGLEYLHKNGQIHRDVKAGNILLGEDGSVQIADFGVSAFLATGGDITRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPSLDTGVQDKEMLKKYGKSFRKMISLCLQKDPEKRPTAAELLRHKFFQKAKNKEFLQEKILQRAPTISERSKKVRR... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O95747}; | cell volume homeostasis [GO:0006884]; cellular hyperosmotic response [GO:0071474]; cellular hypotonic response [GO:0071476]; cellular response to chemokine [GO:1990869]; chemokine (C-C motif) ligand 21 signaling pathway [GO:0038116]; chemokine (C-X-C motif) ligand 12 signaling pathway [GO:0038146]; intracellular signal... | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; protein kinase binding [GO:0019901]; protein serine/threonine kinase activity [GO:0004674] | PF12202;PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | PTM: Phosphorylation at Thr-185 by WNK kinases (WNK1, WNK2, WNK3 or WNK4) is required for activation (PubMed:16083423). Autophosphorylated; promoting its activity (By similarity). {ECO:0000250|UniProtKB:O95747, ECO:0000269|PubMed:16083423}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95747}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:O95747}; CATALYTI... | null | null | null | null | FUNCTION: Effector serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which is involved in various processes, such as ion transport, response to hypertonic stress and blood pressure (PubMed:22544747). Specifically recognizes and binds proteins with a RFXV motif (By similarity). Acts downstre... | Rattus norvegicus (Rat) |
A0A8I6G705 | RBPMS_RAT | MNGGGKAEKENTPSEANLQEEEVRTLFVSGLPLDIKPRELYLLFRPFKGYEGSLIKLTSKQPVGFVSFDSRSEAEAAKNALNGIRFDPEIPQTLRLEFAKANTKMAKNKLVGTPNPSTPLPNTVPQFIAREPYELTVPALYPSSPEVWAPYPLYPAELAPALPPPAAFTYPASLHAQMRWLPPSEATSQGWKSRQFC | null | null | protein-containing complex assembly [GO:0065003]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; response to oxidative stress [GO:0006979]; SMAD protein signal transduction [GO:0060395] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-body [GO:0000932] | identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; mRNA CDS binding [GO:1990715]; pre-mRNA binding [GO:0036002]; pre-mRNA intronic binding [GO:0097157]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; tr... | PF00076; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q93062}. Cytoplasm {ECO:0000250|UniProtKB:Q93062}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q93062}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q93062}. | null | null | null | null | null | FUNCTION: [Isoform 1]: RNA binding protein that mediates pre-mRNA alternative splicing (AS) regulation (PubMed:31283468, PubMed:37548402). Acts either as activator (FLNB, HSPG2, LIPA1, MYOCD, PTPRF and PPFIBP1) or repressor (TPM1, ACTN1, ITGA7, PIEZO1, LSM14B, MBNL1 and MBML2) of splicing events on specific pre-mRNA ta... | Rattus norvegicus (Rat) |
A0A8M1NHK4 | RBM47_DANRE | MTAEDSASAVAMSNPSPSSSSKSSSGHPQHHCTVPEGVAGAPNEAALVSLMERSGYGMVQENGQRKYGPPPGWQGTSPPRGCEIFVGKIPRDVYEDELVPVFESVGRIYEMRLMMDFDGKNRGYAFVMYTQKHEAKRAVRELNNFEIRPGRLLGVCSSVDNCRLFIGGIPKTKKREEILEEVSKVTEGVLDVIVYASAADKMKNRGFAFVEYESHRAAAMARRKLMPGRIQLWGHQIAVDWAEPEIDVDEDVMETVKILYVRNLMIETSEEILRQTFGQFNPGCVERVKKIRDYAFVHFASRDDAVVAMDNLNGTEIEGS... | null | null | antiviral innate immune response [GO:0140374]; head development [GO:0060322]; lysosomal protein catabolic process [GO:1905146]; mRNA processing [GO:0006397]; regulation of anterior head development [GO:2000742]; RNA splicing [GO:0008380] | lysosome [GO:0005764]; nucleus [GO:0005634] | mRNA binding [GO:0003729] | PF00076; | 3.30.70.330; | RRM RBM47 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0AV96}. Cytoplasm {ECO:0000250|UniProtKB:A0AV96}. | null | null | null | null | null | FUNCTION: Single-stranded RNA-binding protein that functions in a variety of RNA processes, including alternative splicing, RNA stabilization, and RNA editing (By similarity). Independently of its RNA-binding activity, could negatively regulate MAVS by promoting its lysosomal degradation (PubMed:32859727). {ECO:0000250... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A8M2 | L14AA_XENLA | MSGGTPYIGSKISLISKAEIRYEGILYTIDTENSTVALAKVRSFGTEDRPTDRPIPPRDEIFEYIIFRGSDIKDLTVCEPPKPQCSLPQDPAIVQSSLGSSSASSFQSVSSYGPFGRMPAYSQFNTGPLVGPQFGAVGVGSSLTSFGAETTSSTSLPPSSAVGTSFTQEARTLKTQSSQGQSSSPLDSLRKSPNIEQAVQTAAAPHAPSTATVGRRSPVLSRPVPSSIQKTAESPEQRKGELHKMQRPDIDQLKNDKNDPSKRQPVLSALQPRRGRGGNRGGRGRFGVRRDGPMKFEKDFDFESANAQFNKEEIDREFHN... | null | null | negative regulation of translation [GO:0017148]; P-body assembly [GO:0033962]; stress granule assembly [GO:0034063] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; P-body [GO:0000932]; protein-containing complex [GO:0032991]; ribonucleoprotein complex [GO:1990904] | DEAD/H-box RNA helicase binding [GO:0017151]; mRNA binding [GO:0003729]; RNA binding [GO:0003723] | PF09532;PF12701; | 2.30.30.100; | LSM14 family | PTM: Phosphorylated. {ECO:0000269|PubMed:17074753}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17074753}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q8ND56}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q8ND56}. Note=Localizes to cytoplasmic particles in stage VI oocytes and eggs. {ECO:0000269|PubMed:17074753}. | null | null | null | null | null | FUNCTION: RNA-binding component of messenger ribonucleoprotein complexes (mRNPs), storage particles that mask maternal mRNAs from the translational apparatus during oocyte maturation (PubMed:17074753). Acts as a repressor of mRNA translation (PubMed:17074753). Probably involved in the storage of translationally inactiv... | Xenopus laevis (African clawed frog) |
A0A8M3B525 | BRCC3_DANRE | MWKCSTVINKNKLIKAEYHTFYTLLFAMAVNAVHLESDAFLVCMNHALSTEKEEVMGLCIGEVDTNRIVHIHSVIILRRSDKRKDRVEISPEQLSAASTEAERLAEMTGRPMRVVGWYHSHPHITVWPSHVDVRTQAMYQMMDQGFVGLIFSCFIEDKNTKTGRVLYTCFQSVQAQKGSEYERIEIPIHVVPHEAIGKVCLESAVELPRILCQEEQDTYRRIHSLTHLDPITKIHNGSVFTKNLCSQMSAISGPLLQWLEDRLEQNKQSIITLQKEKELLTQELAAL | 3.4.19.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|RuleBase:RU367116, ECO:0000269|PubMed:26344097}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|RuleBase:RU367116, ECO:0000269|PubMed:26344097}; | angiogenesis [GO:0001525]; cell cycle [GO:0007049]; cell division [GO:0051301]; double-strand break repair [GO:0006302]; proteolysis [GO:0006508] | BRCA1-A complex [GO:0070531]; BRISC complex [GO:0070552]; cytoplasm [GO:0005737]; spindle pole [GO:0000922] | cysteine-type deubiquitinase activity [GO:0004843]; metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]; polyubiquitin modification-dependent protein binding [GO:0031593] | PF18110;PF01398; | 3.40.140.10; | Peptidase M67A family, BRCC36 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|RuleBase:RU367116}. Cytoplasm {ECO:0000255|RuleBase:RU367116}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000255|RuleBase:RU367116}. | null | null | null | null | null | FUNCTION: Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains, leaving the last ubiquitin chain attached to its substrates (By similarity). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates; brcc3 does not ... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A8M9PFP2 | CSTN3_DANRE | MARMSFLSFLLFCLTSVAHGNKANKHKPWIETEYQGIVMENDNTVLLNPPLFALDKDAPLHYAGEICGFRVHNGPGGSGSAQFEAVVLDRSTGEGLVRSKEPLDCESQKEHSFTIQAYDCGEGPDGTNSKKSHKATVHVRVNDVNEFSPVFVERRYEASVPEGRLFDRIVRVEAVDADCSPQYSQICFYDIITPNVPFTIDNDGNIKNTEPLDSKRQRVHSFWVTAFDCGKNRAQADAQVIVTVKPSCKPGWIGWTKRIEYTPGSGSIPLFPNLHLETCEETVWNIQATVELQTSHIGKGCDRDSYSDRSVRRLCGAVRG... | null | null | excitatory synapse assembly [GO:1904861]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; inhibitory synapse assembly [GO:1904862]; negative regulation of excitatory synapse assembly [GO:1904890]; positive regulation of inhibitory synapse assembly [GO:1905704]; positive regulation of synap... | cell surface [GO:0009986]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; postsynaptic membrane [GO:0045211] | amyloid-beta binding [GO:0001540]; calcium ion binding [GO:0005509]; cell-cell adhesion mediator activity [GO:0098632]; kinesin binding [GO:0019894]; neurexin family protein binding [GO:0042043]; X11-like protein binding [GO:0042988] | PF00028;PF19699; | 2.60.120.200;2.60.40.60; | Calsyntenin family | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass type ... | null | null | null | null | null | FUNCTION: Synaptic adhesion molecule (PubMed:25463516). Promotes synapse development by acting as a cell adhesion molecule at the postsynaptic membrane, which associates with presynaptic neurexins (By similarity). {ECO:0000250|UniProtKB:Q99JH7, ECO:0000269|PubMed:25463516}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0A8V1ABE9 | DSD1_CHICK | MWLGALLDTLPTPALTIDRTTAHRNAERMRERCRALGVRLRPHVKTHKTLEGGLLATGGTRRGIAVSTLAEARFFADGGFDDILLAYPVPTARLEECAGLARRLDAFHVLLDRPEALASLRQRPLGHGKRWLVWLKLDCGNGRAGVRPTDPAALELAQAIANDAPEEVTLVGVYAHCGNTYGCSGADTIQAIARTTTNAVLSFVAALRQAGVPCPQASIGSTPSCSHPIPEMSQLTELHPGNYIFYDLQQTQLGSCQPQDVAIRVLTRVIGHYAHRGQLLVDCGWAALSLHGAGAGQGPQGCAAIDGHPELRLVGLTQEH... | 4.3.1.18 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:17977854}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:21676877}; | D-serine catabolic process [GO:0036088] | cytoplasm [GO:0005737]; dendrite [GO:0030425] | D-serine ammonia-lyase activity [GO:0008721]; pyridoxal phosphate binding [GO:0030170]; zinc ion binding [GO:0008270] | PF01168;PF14031; | 3.20.20.10;2.40.37.20; | DSD1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24529545}. Cell projection, dendrite {ECO:0000269|PubMed:24529545}. | CATALYTIC ACTIVITY: Reaction=D-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:13977, ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; EC=4.3.1.18; Evidence={ECO:0000269|PubMed:17977854, ECO:0000269|PubMed:21676877, ECO:0000305|PubMed:24529545}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13978; Evidence={E... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=131 uM for D-serine (at pH 7.8 and 37 degrees Celsius) {ECO:0000269|PubMed:17977854}; KM=830 uM for D-serine (at pH 7.5, 37 degrees Celsius and in presence of Zn(2+)) {ECO:0000269|PubMed:21676877}; KM=340 uM for D-serine (at pH 7.5, 37 degrees Celsius and in presen... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 (at 37 degrees Celsius). {ECO:0000269|PubMed:17977854}; | null | FUNCTION: Catalyzes the conversion of D-serine, an allosteric activator of the N-methyl-D-aspartate (NMDA) receptor for L-glutamate, to pyruvate and ammonia. {ECO:0000269|PubMed:17977854, ECO:0000269|PubMed:21676877}. | Gallus gallus (Chicken) |
A0AAR7 | CCAMK_LOTJA | MGYDQTRKLSDEYEISEILGRGGFSVVRKGTKKSGNEKTQVAIKTLRRLGSSPSGTGGGQKSTATVMGFPSLRQVSVSDALLTNEILVMRRIVENVSPHPNVIDLYDVCEDSNGVHLVLELCSGGELFDRIVAQDKYAETEAAAVVRQIAAGLEAVHKADIVHRDLKPENCLFLDSRKDSPLKIMDFGLSSVEEFTDPVVGLFGSIDYVSPEALSQGKITAKSDMWSLGVILYILLSGYPPFIAQNNRQKQQMIINGNFSFYEKTWKGITQSAKQLISSLLTVDPSKRPSAQELLSHPWVRGDKAKDEQMDPEIVSRLQS... | 2.7.11.17 | null | intracellular signal transduction [GO:0035556]; nodulation [GO:0009877]; protein autophosphorylation [GO:0046777]; response to symbiont [GO:0009608] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; protein serine kinase activity [GO:0106310] | PF13202;PF13499;PF00069; | 1.10.238.10;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily | PTM: Autophosphorylation stimulated by calcium. Occurs probably by an intermolecular mechanism. {ECO:0000269|PubMed:16810257}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19074278, ECO:0000269|PubMed:21209278}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.17; Evidence={ECO:0000269|PubMed:25868982}; CATALYTI... | null | null | null | null | FUNCTION: Calcium- and calmodulin-dependent protein kinase necessary and sufficient for dedifferentiation of root cortical cells into nodule initials. Not required for calcium spiking (PubMed:16810257). Acts as central regulator of the nodule organogenesis program. Required for root hair curling and infection thread (I... | Lotus japonicus (Lotus corniculatus var. japonicus) |
A0AUJ5 | POLG_BVY3 | MPTRYRGADRYGNLGYDKVLQSKADAAKRRGLLFDHGSETYECPRCGEIWRNLDDYMAEGGKMHPKKCLPEECDSDEEQISSCNAALIHEKWGDLDSDTSSKLSEFYKEPSILTYTTRTHCVVEKMRSMTAPQCIEDIVGVRLHGRTAWFFSKDPTLQYGHHPIYYDTHPWNDELDKYLGGAKYNTALVQVYDGTRDLPYHKDDEPCYDITNNPIRTVNVTGTGDLCISKDKRRLYETIPMTSGTVITFPATMQENFYHAVRNPSAGRISITFRNQIRTVERQVAHSANKRWVPIVEARVTTNESRRGDNKQFQEAQSKL... | 2.7.7.48; 3.4.-.-; 3.4.22.44; 3.4.22.45; 3.6.4.- | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805}; | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049] | helical viral capsid [GO:0019029]; host cell cytoplasmic vesicle [GO:0044161] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; dioxygenase activity [GO:0051213]; helicase activity [GO:0004386]; hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides [GO:0016818]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA-dependent RNA pol... | PF00270;PF00271;PF00863;PF00851;PF01577;PF00767;PF08440;PF13608;PF00680; | 3.30.70.270;2.60.120.590;3.90.70.150;3.40.50.300;2.40.10.10; | Potyviridae genome polyprotein family | PTM: [Viral genome-linked protein]: VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.; PTM: [Genome polyprotein]: Genome polyprotein of potyviru... | SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle. Note=Probably colocalizes with 6K2-induced vesicles associated with host chloroplasts. {ECO:0000250|UniProtKB:P13529}.; SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate ... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=Hydrolyz... | null | null | null | null | FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a m... | Blackberry virus Y (isolate Blackberry plant/USA:Arkansas/C3ARK/2005) (BVY) |
A0AV02 | S12A8_HUMAN | MTQMSQVQELFHEAAQQDALAQPQPWWKTQLFMWEPVLFGTWDGVFTSCMINIFGVVLFLRTGWLVGNTGVLLGMFLVSFVILVALVTVLSGIGVGERSSIGSGGVYSMISSVLGGQTGGTIGLLYVFGQCVAGAMYITGFAESISDLLGLGNIWAVRGISVAVLLALLGINLAGVKWIIRLQLLLLFLLAVSTLDFVVGSFTHLDPEHGFIGYSPELLQNNTLPDYSPGESFFTVFGVFFPAATGVMAGFNMGGDLREPAASIPLGSLAAVGISWFLYIIFVFLLGAICTREALRYDFLIAEKVSLMGFLFLLGLYISS... | null | null | cell volume homeostasis [GO:0006884]; chloride ion homeostasis [GO:0055064]; chloride transmembrane transport [GO:1902476]; potassium ion homeostasis [GO:0055075]; potassium ion import across plasma membrane [GO:1990573] | membrane [GO:0016020] | potassium:chloride symporter activity [GO:0015379] | PF00324; | 1.20.1740.10; | SLC12A transporter family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Cation/chloride cotransporter that may play a role in the control of keratinocyte proliferation. {ECO:0000269|PubMed:11863360}. | Homo sapiens (Human) |
A0AV96 | RBM47_HUMAN | MTAEDSTAAMSSDSAAGSSAKVPEGVAGAPNEAALLALMERTGYSMVQENGQRKYGGPPPGWEGPHPQRGCEVFVGKIPRDVYEDELVPVFEAVGRIYELRLMMDFDGKNRGYAFVMYCHKHEAKRAVRELNNYEIRPGRLLGVCCSVDNCRLFIGGIPKMKKREEILEEIAKVTEGVLDVIVYASAADKMKNRGFAFVEYESHRAAAMARRKLMPGRIQLWGHQIAVDWAEPEIDVDEDVMETVKILYVRNLMIETTEDTIKKSFGQFNPGCVERVKKIRDYAFVHFTSREDAVHAMNNLNGTELEGSCLEVTLAKPVD... | null | null | 3'-UTR-mediated mRNA stabilization [GO:0070935]; cytidine to uridine editing [GO:0016554]; hematopoietic progenitor cell differentiation [GO:0002244]; mRNA processing [GO:0006397]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of type I interferon-mediated signaling pathway [GO:0060... | apolipoprotein B mRNA editing enzyme complex [GO:0030895]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | enzyme binding [GO:0019899]; enzyme-substrate adaptor activity [GO:0140767]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; RNA binding [GO:0003723] | PF00076; | 3.30.70.330; | RRM RBM47 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24038582, ECO:0000269|PubMed:24916387}. Cytoplasm {ECO:0000269|PubMed:24916387}. | null | null | null | null | null | FUNCTION: Single-stranded RNA-binding protein that functions in a variety of RNA processes, including alternative splicing, RNA stabilization, and RNA editing (PubMed:24038582, PubMed:24916387, PubMed:27050523, PubMed:30844405, PubMed:31358901, PubMed:34160127). Functions as an enzyme-substrate adapter for the cytidine... | Homo sapiens (Human) |
A0AVF1 | IFT56_HUMAN | MMLSRAKPAVGRGVQHTDKRKKKGRKIPKLEELLSKRDFTGAITLLEFKRHVGEEEEDTNLWIGYCAFHLGDYKRALEEYENATKEENCNSEVWVNLACTYFFLGMYKQAEAAGFKASKSRLQNRLLFHLAHKFNDEKKLMSFHQNLQDVTEDQLSLASIHYMRSHYQEAIDIYKRILLDNREYLALNVYVALCYYKLDYYDVSQEVLAVYLQQIPDSTIALNLKACNHFRLYNGRAAEAELKSLMDNASSSFEFAKELIRHNLVVFRGGEGALQVLPPLVDVIPEARLNLVIYYLRQDDVQEAYNLIKDLEPTTPQEYI... | null | null | axoneme assembly [GO:0035082]; cilium assembly [GO:0060271]; intraciliary anterograde transport [GO:0035720]; intraciliary transport [GO:0042073]; intraciliary transport involved in cilium assembly [GO:0035735]; manchette assembly [GO:1905198]; protein localization to cilium [GO:0061512]; protein transport [GO:0015031]... | centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary base [GO:0097546]; ciliary tip [GO:0097542]; cilium [GO:0005929]; intraciliary transport particle B [GO:0030992]; neuron projection [GO:0043005] | intraciliary transport particle B binding [GO:0120170] | PF12895; | 1.25.40.10; | IFT56 family | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q8BS45}. Note=Localizes at the base to the ciliary transition zone. {ECO:0000250|UniProtKB:Q8BS45}. | null | null | null | null | null | FUNCTION: Component of the intraflagellar transport (IFT) complex B required for transport of proteins in the motile cilium. Required for transport of specific ciliary cargo proteins related to motility, while it is neither required for IFT complex B assembly or motion nor for cilium assembly. Required for efficient co... | Homo sapiens (Human) |
A0AVI4 | TM129_HUMAN | MDSPEVTFTLAYLVFAVCFVFTPNEFHAAGLTVQNLLSGWLGSEDAAFVPFHLRRTAATLLCHSLLPLGYYVGMCLAASEKRLHALSQAPEAWRLFLLLAVTLPSIACILIYYWSRDRWACHPLARTLALYALPQSGWQAVASSVNTEFRRIDKFATGAPGARVIVTDTWVMKVTTYRVHVAQQQDVHLTVTESRQHELSPDSNLPVQLLTIRVASTNPAVQAFDIWLNSTEYGELCEKLRAPIRRAAHVVIHQSLGDLFLETFASLVEVNPAYSVPSSQELEACIGCMQTRASVKLVKTCQEAATGECQQCYCRPMWCL... | 2.3.2.27 | null | ERAD pathway [GO:0036503]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; response to unfolded protein [GO:0006986]; retrograde protein transport, ER to cytosol [GO:0030970]; ubiquitin-dependent protein catabolic process [GO:0006511] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630] | PF10272; | null | TMEM129 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24807418}; Multi-pass membrane protein {ECO:0000269|PubMed:24807418}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase involved in ER-associated protein degradation, preferentially associates with the E2 enzyme UBE2J2. Exploited by viral US11 proteins to mediate HLA class I proteins degradation. {ECO:0000269|PubMed:24807418}. | Homo sapiens (Human) |
A0AVK6 | E2F8_HUMAN | MENEKENLFCEPHKRGLMKTPLKESTTANIVLAEIQPDFGPLTTPTKPKEGSQGEPWTPTANLKMLISAVSPEIRNRDQKRGLFDNRSGLPEAKDCIHEHLSGDEFEKSQPSRKEKSLGLLCHKFLARYPNYPNPAVNNDICLDEVAEELNVERRRIYDIVNVLESLHMVSRLAKNRYTWHGRHNLNKTLGTLKSIGEENKYAEQIMMIKKKEYEQEFDFIKSYSIEDHIIKSNTGPNGHPDMCFVELPGVEFRAASVNSRKDKSLRVMSQKFVMLFLVSTPQIVSLEVAAKILIGEDHVEDLDKSKFKTKIRRLYDIAN... | null | null | cell cycle comprising mitosis without cytokinesis [GO:0033301]; chorionic trophoblast cell differentiation [GO:0060718]; fibroblast proliferation [GO:0048144]; hepatocyte differentiation [GO:0070365]; negative regulation of cytokinesis [GO:0032466]; negative regulation of transcription by RNA polymerase II [GO:0000122]... | chromatin [GO:0000785]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; RNA polymerase II transcription regulator complex [GO:0090575] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity [GO:0001217]; DNA-binding transcription repressor activity, RNA polym... | PF02319; | 1.10.10.10; | E2F/DP family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15897886}. | null | null | null | null | null | FUNCTION: Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represse... | Homo sapiens (Human) |
A0AVT1 | UBA6_HUMAN | MEGSEPVAAHQGEEASCSSWGTGSTNKNLPIMSTASVEIDDALYSRQRYVLGDTAMQKMAKSHVFLSGMGGLGLEIAKNLVLAGIKAVTIHDTEKCQAWDLGTNFFLSEDDVVNKRNRAEAVLKHIAELNPYVHVTSSSVPFNETTDLSFLDKYQCVVLTEMKLPLQKKINDFCRSQCPPIKFISADVHGIWSRLFCDFGDEFEVLDTTGEEPKEIFISNITQANPGIVTCLENHPHKLETGQFLTFREINGMTGLNGSIQQITVISPFSFSIGDTTELEPYLHGGIAVQVKTPKTVFFESLERQLKHPKCLIVDFSNPE... | 6.2.1.45 | null | amygdala development [GO:0021764]; dendritic spine development [GO:0060996]; DNA damage response [GO:0006974]; hippocampus development [GO:0021766]; learning [GO:0007612]; locomotory behavior [GO:0007626]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; FAT10 activating enzyme activity [GO:0019780]; nucleotidyltransferase activity [GO:0016779]; thiosulfate sulfurtransferase activity [GO:0004792]; ubiquitin activating enzyme activity [GO:0004839] | PF16191;PF16190;PF09358;PF00899;PF10585; | 3.40.50.720;2.40.30.180;3.50.50.80;3.40.50.12550;1.10.10.2660;3.10.290.60; | Ubiquitin-activating E1 family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000250|UniProtKB:P22314}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:P22314}. | null | null | FUNCTION: Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Specific for ubiquitin, does not activate ubiquitin-like peptides. Differs from UBE1 in its speci... | Homo sapiens (Human) |
A0AVX7 | CHP3_CHICK | MGSAQSVPPEMRALAERTGFTSEQIEQLHRRFKQLNHNRKTIRKEDFDTIPDLEFNPIRARIVHAFFDKRNLRKAPAGLAEEINFEDFLTIMSYFRPIEMDMDEERLESFRKEKLKFLFHMYDADYDGIITLQEYKNVLDELMSGNPHLEKESLRAIAEGAMLEAASACMARTGPDEVYEGITFEDFLKVWKGIDIETKMHVRFLTMEAIAHCY | null | null | cell differentiation [GO:0030154]; cellular response to retinoic acid [GO:0071300]; positive regulation of granulocyte differentiation [GO:0030854]; positive regulation of sodium:proton antiporter activity [GO:0032417]; protein localization to plasma membrane [GO:0072659]; protein maturation [GO:0051604]; protein stabi... | cytoplasm [GO:0005737]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; ruffle membrane [GO:0032587] | calcium ion binding [GO:0005509]; magnesium ion binding [GO:0000287]; phosphatase inhibitor activity [GO:0019212]; protein homodimerization activity [GO:0042803]; protein kinase inhibitor activity [GO:0004860] | null | 1.10.238.10; | Calcineurin regulatory subunit family, CHP subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19345287}. Cytoplasm {ECO:0000269|PubMed:19345287}. Membrane {ECO:0000250|UniProtKB:Q96BS2}; Lipid-anchor {ECO:0000250|UniProtKB:Q96BS2}. Cell membrane {ECO:0000250|UniProtKB:Q96BS2}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q96BS2}. Cell projection, ruffle... | null | null | null | null | null | FUNCTION: Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Promotes the induction of hematopoietic stem cell differentiation toward megakaryocytic lineage. Essential for the coupling of ERK cascade activation with the expression of ETS family gene... | Gallus gallus (Chicken) |
A0FGR8 | ESYT2_HUMAN | MTANRDAALSSHRHPGCAQRPRTPTFASSSQRRSAFGFDDGNFPGLGERSHAPGSRLGARRRAKTARGLRGHRQRGAGAGLSRPGSARAPSPPRPGGPENPGGVLSVELPGLLAQLARSFALLLPVYALGYLGLSFSWVLLALALLAWCRRSRGLKALRLCRALALLEDEERVVRLGVRACDLPAWVHFPDTERAEWLNKTVKHMWPFICQFIEKLFRETIEPAVRGANTHLSTFSFTKVDVGQQPLRINGVKVYTENVDKRQIILDLQISFVGNCEIDLEIKRYFCRAGVKSIQIHGTMRVILEPLIGDMPLVGALSIF... | null | null | endocytosis [GO:0006897]; endoplasmic reticulum-plasma membrane tethering [GO:0061817]; lipid transport [GO:0006869] | cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-plasma membrane contact site [GO:0140268]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; membrane [GO:0016020]; organelle membrane contact site [GO:004423... | cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; identical protein binding [GO:0042802]; phosphatidylcholine binding [GO:0031210]; phosphatidylethanolamine binding [GO:0008429]; phosphatidylinositol binding [GO:0035091] | PF00168;PF17047; | 2.60.40.150; | Extended synaptotagmin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17360437, ECO:0000269|PubMed:20833364, ECO:0000269|PubMed:23791178, ECO:0000269|PubMed:29469807}; Peripheral membrane protein {ECO:0000269|PubMed:17360437}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23791178, ECO:0000269|PubMed:29469807}; Multi-pass membr... | null | null | null | null | null | FUNCTION: Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport. Plays a role in FGF signaling via its role in the rapid ... | Homo sapiens (Human) |
A0FGR9 | ESYT3_HUMAN | MRAEEPCAPGAPSALGAQRTPGPELRLSSQLLPELCTFVVRVLFYLGPVYLAGYLGLSITWLLLGALLWMWWRRNRRGKLGRLAAAFEFLDNEREFISRELRGQHLPAWIHFPDVERVEWANKIISQTWPYLSMIMESKFREKLEPKIREKSIHLRTFTFTKLYFGQKCPRVNGVKAHTNTCNRRRVTVDLQICYIGDCEISVELQKIQAGVNGIQLQGTLRVILEPLLVDKPFVGAVTVFFLQKPHLQINWTGLTNLLDAPGINDVSDSLLEDLIATHLVLPNRVTVPVKKGLDLTNLRFPLPCGVIRVHLLEAEQLAQ... | null | null | endoplasmic reticulum-plasma membrane tethering [GO:0061817]; lipid transport [GO:0006869] | cytoplasmic side of plasma membrane [GO:0009898]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-plasma membrane contact site [GO:0140268]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; organelle membrane contact site [GO:0044232]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; phosphatidylcholine binding [GO:0031210]; phosphatidylethanolamine binding [GO:0008429]; phosphatidylinositol binding [GO:0035091] | PF00168;PF17047; | 2.60.40.150; | Extended synaptotagmin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17360437, ECO:0000269|PubMed:29469807}; Peripheral membrane protein {ECO:0000269|PubMed:17360437}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:29469807}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum-plasma membrane cont... | null | null | null | null | null | FUNCTION: Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport (By similarity). Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. {ECO:0000250, ECO:0000269|PubMed:2379117... | Homo sapiens (Human) |
A0FI79 | INP5E_PANTR | MPSKAENLRPSEPAPQPPEGRTLQGQLPGAPLAQRAGSPPDVPGSESPALACSTPATPSGEDPPARAAPIAPRPPARPRLERALSLDDKGWRRRRFRGSQEDLEARNGTSPSRGSVQSEGPGAPAHSCSPPCLSTSLQEIPKSRGVLSSERGSPSSGGNPLSGVASSSPNLPHRDAAVAGSSPRLPSLLPPRPPPALSLDIASDSLRTANKVDSDLADYKLRAQPLLVRAHSSLGPGRPRSPLACDDCSLRSAKSSFSLLAPIRSKDVRSRSYLEGSLLASGALLGADELARYFPDRNVALFVATWNMQGQKELPPSLDE... | 3.1.3.36; 3.1.3.86 | null | phosphatidylinositol dephosphorylation [GO:0046856] | axoneme [GO:0005930]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ruffle [GO:0001726] | inositol-polyphosphate 5-phosphatase activity [GO:0004445]; phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity [GO:0034485]; phosphatidylinositol-3,5-bisphosphate 5-phosphatase activity [GO:0043813]; phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439] | null | 3.60.10.10; | Inositol polyphosphate 5-phosphatase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9JII1}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q9JII1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9JII1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9JII1}. Cell membrane {ECO:0000250|UniProtKB:Q9WVR1}; P... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456; EC=3.1.3.36; Evidence={ECO:0000250|UniP... | null | null | null | null | FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3), phosphatidylinositol 4,5-bisphosphate(PtdIns(4,5)P2) and phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Specific for lipid substrates, inactive towards ... | Pan troglodytes (Chimpanzee) |
A0FIN4 | IRF1_PIG | MPITRMRMRPWLEMQINSNQIPGLIWINKEEMIFQIPWKHAAKHGWDINKDACLFRSWAIHTGRYKAGEKEPDPKTWKANFRCAMNSLPDIEEVKDQSRNKGSSAVRVYRMLPPLTKNQRKERKSKSSRDAKCKAKKKSCGESSPDTFSDGLSSSTLPDDHSSYTAQGYIGQDLDIEQALTPALSPCAISSTLPEWRIPVEIVPDSTSDLYNFQVSPMPSTSEAATDEDEEGKLTEDIMKLLEQSGWQQTNVDGKGYLLNEPGAQPTAVYGDFSCKEEPEVESPGGYTGLISSDLKNVDTSWLDNLLTPVRLPSIQAIPC... | null | null | apoptotic process [GO:0006915]; CD8-positive, alpha-beta T cell differentiation [GO:0043374]; cellular response to interferon-beta [GO:0035458]; cellular response to mechanical stimulus [GO:0071260]; defense response to virus [GO:0051607]; immune system process [GO:0002376]; negative regulation of DNA-templated transcr... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976] | PF00605; | 1.10.10.10; | IRF family | PTM: Phosphorylated by CK2 and this positively regulates its activity. {ECO:0000250|UniProtKB:P10914}.; PTM: Sumoylation represses the transcriptional activity and displays enhanced resistance to protein degradation (By similarity). Sumolyated by UBE2I/UBC9 and SUMO1 (By similarity). Inactivates the tumor suppressor ac... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P15314}. Cytoplasm {ECO:0000250|UniProtKB:P15314}. Note=MYD88-associated IRF1 migrates into the nucleus more efficiently than non-MYD88-associated IRF1. {ECO:0000250|UniProtKB:P15314}. | null | null | null | null | null | FUNCTION: Transcriptional regulator which displays a remarkable functional diversity in the regulation of cellular responses (By similarity). Regulates transcription of IFN and IFN-inducible genes, host response to viral and bacterial infections, regulation of many genes expressed during hematopoiesis, inflammation, im... | Sus scrofa (Pig) |
A0FKE6 | TD1_SOLLC | MEVLRFTAVKSLNSCVRPEFTAMSSVIVPISTVKVSGTRKSKKKALICAKATEILSSPATVTEPLKAEPAEAPVPLLRVSPSSLQCEPGYLLPNSPVLGTGGVTGYEYLTNILSSKVYDVAYETPLQKAPKLSERLGVNVWLKREDLQPVFSFKIRGAYNMMAKLPKEQLEKGVICSSAGNHAQGVALSAQRLGCDAVIVMPVTTPDIKWKSVKRLGATVVLVGDSYDEAQAYAKKRAESEGRTFIPPFDHPDVIVGQGTVGMEINRQLKDNIHAIFVPVGGGGLIAGIAAYLKRVAPDIKIIGVEPLDANALALSLHHG... | 4.3.1.19 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|RuleBase:RU362012}; | amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; L-serine catabolic process [GO:0006565]; threonine catabolic process [GO:0006567] | chloroplast [GO:0009507] | L-serine ammonia-lyase activity [GO:0003941]; pyridoxal phosphate binding [GO:0030170]; threonine deaminase activity [GO:0004794] | PF00291;PF00585; | 3.40.50.1100; | Serine/threonine dehydratase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19; Evidence={ECO:0000255|RuleBase:RU362012, ECO:0000269|PubMed:21436043}; | null | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1. {ECO:0000255|RuleBase:RU362012}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Active at alkaline pH. {ECO:0000269|PubMed:21436043}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 16 degrees Celsius. Not active at temperatures above 55 degrees Celsius. Complete loss of activity by incubation at 55 degrees Celsius for 1 minute. {ECO:0000269|PubMed:21436043}; | FUNCTION: Has a housekeeping role in isoleucine biosynthesis (Probable). {ECO:0000305|PubMed:17416643}. | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
A0FKN5 | S26A5_CHICK | MEDAQESGECLVQNQKYCVERPIYNQEILQGQLHKRERTPQSLRQKIEHSCRCSSKKAKSHLYSFLPILKWLPRYPVKEYLLGDIISGISTGVMQLPQGLAYALLAAVPPVFGLYSSFYPVFLYTFFGTSKHISIGTFAVISMMVGGVAVRQVPDEVISVGYNSTNATDASDYYSLRDDKRVQVAVTLAFLSGIIQLCLGFLRFGFVAIYLTEPLVRGFTTAAAVHVFTSQLKYLLGVKTSRYSGPLSVVYSLVAVFSKITTTNIAALIVGLTCIALLLIGKEINLRFKKKLPVPIPMEIIVVIIGTGVSAGMNLTESYG... | null | null | null | plasma membrane [GO:0005886] | bicarbonate transmembrane transporter activity [GO:0015106]; chloride transmembrane transporter activity [GO:0015108]; metal ion binding [GO:0046872]; oxalate transmembrane transporter activity [GO:0019531]; oxalate:chloride antiporter activity [GO:0160046]; sulfate transmembrane transporter activity [GO:0015116]; sulf... | PF01740;PF00916; | 3.30.750.24; | SLC26A/SulP transporter (TC 2.A.53) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17442754}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=chloride(out) + oxalate(in) = chloride(in) + oxalate(out); Xref=Rhea:RHEA:72263, ChEBI:CHEBI:17996, ChEBI:CHEBI:30623; Evidence={ECO:0000269|PubMed:17442754, ECO:0000269|PubMed:24710176}; CATALYTIC ACTIVITY: Reaction=chloride(in) + sulfate(out) = chloride(out) + sulfate(in); Xref=Rhea:RHEA:... | null | null | null | null | FUNCTION: Electrogenic antiporter that exchanges sulfate or oxalate for chloride ion in a strictly coupled manner with a 1:1 stoichiometry (PubMed:17442754, PubMed:22399806, PubMed:24710176). Adopts a dynamic conformation, which alternates between the exposure of the central binding site to the extra- and intracellular... | Gallus gallus (Chicken) |
A0JJU1 | TENS_BEABA | MSPMKQNESESHSVSEPIAIIGSAYRFPGGCNTPSKLWDLLRQPRDILKEIDPERLNLRRYYHPDGETHGSTDVANKAYTLEEDISRFDASFFGISPLEAASMDPQQRTLLEVVYESTETAGIPLDKLRGSLTSVHVGVMTTDWAQMQRRDPETMPQYTATGIASSIISNRISYIFDLKGASETIDTACSSSLVALHNAARALQSGDCEKAIVAGVNLILDPDPFIYESKLHMLSPDARSRMWDAAANGYARGEGAAAVVLKTLGHALRDGDRIEGVIRSTFVNSDGLSSGLTMPSSAAQTALIRQTYRKAGLDPVRDRP... | 2.3.1.-; 6.3.2.- | null | amide biosynthetic process [GO:0043604]; fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; methylation [GO:0032259]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; toxin biosynthetic process [GO:0009403] | null | fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177] | PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765; | 3.30.300.30;3.30.70.3290;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;3.40.50.150; | NRP synthetase family | null | null | null | null | PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:17216664, ECO:0000269|PubMed:18266306, ECO:0000269|PubMed:20575135, ECO:0000269|PubMed:34903054}. | null | null | FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection (PubMed:17216664, PubMed:18266306, PubMe... | Beauveria bassiana (White muscardine disease fungus) (Tritirachium shiotae) |
A0JLT2 | MED19_HUMAN | MENFTALFGAQADPPPPPTALGFGPGKPPPPPPPPAGGGPGTAPPPTAATAPPGADKSGAGCGPFYLMRELPGSTELTGSTNLITHYNLEQAYNKFCGKKVKEKLSNFLPDLPGMIDLPGSHDNSSLRSLIEKPPILSSSFNPITGTMLAGFRLHTGPLPEQCRLMHIQPPKKKNKHKHKQSRTQDPVPPETPSDSDHKKKKKKKEEDPDRKRKKKEKKKKKNRHSPDHPGMGSSQASSSSSLR | null | null | positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; RNA polymerase II preinitiation complex assembly [GO:0051123] | core mediator complex [GO:0070847]; mediator complex [GO:0016592]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | transcription coregulator activity [GO:0003712] | PF10278; | null | Mediator complex subunit 19 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | 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... | Homo sapiens (Human) |
A0JMD4 | TPC2_DANRE | MEEEPLLAGSINQGSGDYGAHSESCLHYPDEHTPRSRRLSYSVTDDSCNVEEDADADLYVQQAVVFIEDAIKYRSINHRVDSGSLRLYRWYYSNLCQWGLGLTIAVVLALAFIERPSSLTYTSDIRVKPKPWEPPCGMTEGIEIVCLCIFILDVTAKGYLIGWEEFRMNKWLLAYLIVITASVIDWMLSISMLCDENLRVRRLIRPFFLLQNSSLMKKTLKCIKRTLPEIASVILLLALHICLFTMIGMLIFAKSDDPKQNGEWQTYFRNLPKALSSLLVLLTTANNPDVMIPAYSLNRGYSIFFILFSVFGTYLLMNLM... | null | null | calcium-mediated signaling [GO:0019722]; endocytosis involved in viral entry into host cell [GO:0075509]; regulation of myotome development [GO:2000290]; skeletal myofibril assembly [GO:0014866]; smooth muscle contraction [GO:0006939]; sodium ion transmembrane transport [GO:0035725] | late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; monoatomic ion channel complex [GO:0034702] | identical protein binding [GO:0042802]; intracellularly phosphatidylinositol-3,5-bisphosphate-gated monatomic cation channel activity [GO:0097682]; ligand-gated sodium channel activity [GO:0015280]; NAADP-sensitive calcium-release channel activity [GO:0072345]; phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]... | PF00520; | 1.10.287.70;1.20.120.350; | Calcium channel alpha-1 subunit (TC 1.A.1.11) family, Two pore calcium channel subfamily | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BWC0}. | SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250|UniProtKB:Q8NHX9}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q8NHX9}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q8NHX9}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:34965; Evidence={ECO:0000250|UniProtKB:Q8NHX9}; CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:C... | null | null | null | null | FUNCTION: Intracellular channel initially characterized as a non-selective Ca(2+)-permeable channel activated by NAADP (nicotinic acid adenine dinucleotide phosphate), it is also a highly-selective Na(+) channel activated directly by PI(3,5)P2 (phosphatidylinositol 3,5-bisphosphate). Localizes to the lysosomal and late... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0JMQ9 | ZRN1B_DANRE | MTDLGLKWSCEYCTYENWPSAIKCTMCRAQRHNAPIITEEPFKSSSSLDPSLCTTQGGSTLLICPDSSARPRVRIADELPETSSKWSCHMCTYLNWPRAIRCTQCLSQRQQGSQQHSPLSPSETPQTSGSRPSPVTSDPCEEYNDRNRLNMHAQRWPCSACTYENWPKSLRCVVCDHPKPSGSPETPQQDSEAESATSPSIVNEQERENVRTAGGGGGGSRGRLRKLSPPMCKGQAEVKIELASGAVGSDNEQEADFKKLKQIRNRMRRSDWLFLNACAGVVEGDLAAVEAYKSSGGDIARQLTADEVRILNRPSAFDAG... | 3.4.19.12 | null | brain development [GO:0007420]; cell migration [GO:0016477]; central nervous system morphogenesis [GO:0021551]; cytoskeleton organization [GO:0007010]; positive regulation of Wnt signaling pathway [GO:0030177]; protein K29-linked deubiquitination [GO:0035523]; protein K33-linked deubiquitination [GO:1990168]; protein K... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; metal ion binding [GO:0046872] | PF18418;PF02338;PF00641; | 1.25.40.560;4.10.1060.10;2.30.30.380; | Peptidase C64 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UGI0}. Nucleus {ECO:0000250|UniProtKB:Q9UGI0}. Note=Enriched in punctate localization in the cytoplasm. {ECO:0000250|UniProtKB:Q9UGI0}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q9UGI0}; | null | null | null | null | FUNCTION: Ubiquitin thioesterase, which specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin (By similarity). Also cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency compared to 'Lys-29'-linked ones (By similarity). Positive regulator of the Wnt signaling pathway that deubiquitinates ap... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0JN54 | DGKA_BOVIN | MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAEYLQGDAIGYEGFQQFLKIYLEVDNVPDHLSQALFQSFQTGYYIEDTVREDVVCLSDVSCYFSLLEGGRPEDKLEFTFKLYDTDRNGILDSSEVDRIIIQMMRMAEYLDWDVSELRPILQEMMKEIDYDGSGSVSLAEWLRAGATTVPLLVLLGLEMTLKDNGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKYIVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLVGLHCVWCHLEIHDDCLPAMGHECDC... | 2.7.1.107; 2.7.1.93 | null | diacylglycerol metabolic process [GO:0046339]; intracellular signal transduction [GO:0035556]; lipid phosphorylation [GO:0046834]; phosphatidic acid biosynthetic process [GO:0006654]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | alkylglycerol kinase activity [GO:0047649]; ATP binding [GO:0005524]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; calcium ion binding [GO:0005509] | PF00130;PF14513;PF00609;PF00781;PF13499; | 2.60.200.40;3.30.60.20;1.10.238.110;1.10.238.10; | Eukaryotic diacylglycerol kinase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P23743}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107; Evidence={ECO:0000250|UniProtKB:P23743}; PhysiologicalDirection=left-to-righ... | null | PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000250|UniProtKB:P23743}. | null | null | FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite e... | Bos taurus (Bovine) |
A0JNB0 | FYN_BOVIN | MGCVQCKDKEATKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHGAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYSERAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTLKPGTMSPESFLEEAQIMKK... | 2.7.10.2 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | adaptive immune response [GO:0002250]; cell differentiation [GO:0030154]; innate immune response [GO:0045087]; peptidyl-tyrosine phosphorylation [GO:0018108]; T cell receptor signaling pathway [GO:0050852]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | cytoplasm [GO:0005737]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; nucleus [GO:0005634]; perikaryon [GO:0043204] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Autophosphorylated at Tyr-420 (By similarity). Phosphorylation on the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an inactive state. PTPRC/CD45 dephosphorylates Tyr-531 leading to activation. Ultraviolet B (UVB) strongly increase phosphorylation at Thr-12 and kinase activity, and promotes translocati... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06241}. Nucleus {ECO:0000250|UniProtKB:P06241}. Cell membrane {ECO:0000250|UniProtKB:P06241}. Perikaryon {ECO:0000250|UniProtKB:Q62844}. Note=Present and active in lipid rafts (By similarity). Palmitoylation is crucial for proper trafficking (By similarity). {ECO:... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail wit... | Bos taurus (Bovine) |
A0JNC1 | CDS2_BOVIN | MTELRQRVAREPEAPPEDKESESEAKADGETASDSESRVEAVTQPPSADDTPEVLNRALSNLSSRWKNWWVRGILTLAMIAFFFIIIYLGPMVLMMIVMCVQIKCFHEIITIGYNVYHSYDLPWFRTLSWYFLLCVNYFFYGETVTDYFFTLVQREEPLRILSKYHRFISFTLYLTGFCMFVLSLVKKHYRLQFYMFGWTHVTLLIVVTQSHLVIHNLFEGMIWFIVPISCVICNDIMAYMFGFFFGRTPLIKLSPKKTWEGFIGGFFATVVFGLLLSYVMSGYRCFVCPVEYNNDTNSFTVDCEPSGLFRLQEYNIPGV... | 2.7.7.41 | null | CDP-diacylglycerol biosynthetic process [GO:0016024]; lipid droplet formation [GO:0140042] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | phosphatidate cytidylyltransferase activity [GO:0004605] | PF01148; | null | CDS family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O95674}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41; Evidence={ECO:0000250|UniProtKB:O95674}; PhysiologicalDirection=le... | null | PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3. | null | null | FUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of phosphatidylglycerol, cardiolipin and phosphatidylinositol (By similarity). Exhibits specificity for the nature of the acyl chains at the sn-1 and sn-2 positions in the substrate, ... | Bos taurus (Bovine) |
A0JNC4 | ELOV7_BOVIN | MAFSDLTSRTVRLYDNWIKDADPRVEDWLLMSSPLPQTIILGFYVYFVTSLGPKLMENRKPFELKKVMITYNFSIVLFSVYMFYEFIMSGWGTGYSFRCDIVDYSQSPTALRMVRTCWLYYFSKFIELLDTIFFILRKKNSQVTFLHVFHHTIMPWTWWFGVKFAAGGLGTFHAFLNTAVHVVMYSYYGLCALGPDYQKYLWWKKYLTSLQLIQFVLITIHISQFFFMEDCKYQFPVFQYIIMSYGCIFLLLFLHFWYRAYTKGQRLPKTVKHGICKNKDH | 2.3.1.199 | null | fatty acid elongation, monounsaturated fatty acid [GO:0034625]; fatty acid elongation, polyunsaturated fatty acid [GO:0034626]; fatty acid elongation, saturated fatty acid [GO:0019367]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; sphingolipid biosynthetic process [GO:0030148]; unsaturated fatty acid bi... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | fatty acid elongase activity [GO:0009922] | PF01151; | null | ELO family, ELOVL7 subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03207}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03207}. | CATALYTIC ACTIVITY: Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199; Evidence={ECO:0000255|HAMAP-Rule:MF_03207}; Ph... | null | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03207}. | null | null | FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme with... | Bos taurus (Bovine) |
A0JNH9 | APLF_BOVIN | MSGGFELQPQDGGPRVALAPGETVIGRGPLLGLHRNPCYYQSSEKSQLLPLKTNIWCWLNPGDHFSLLVDKYIFCVLSTHSEMEMECTLRNSQMLDEDDILNEIPKSSSADLPDKTPSAPRRERSTETAKPQAAANNMSFIGESRDLSKQQPNPSERKRILPAWMLTENSSDQNLSVISGGNNVTWESEKERVCKDKTQVNITQPGKKRLISSGSSESTSAKQDTGKKCKNDDQEESIISSKEMPQSFSAAMLHNTEIDNTKTNPQRSKVPVEALGKVSEHKIITKGSSNEDSTARSCSESYSSTQSKSFCDKPQKSHPE... | 3.1.1.- | null | DNA damage response [GO:0006974]; DNA repair-dependent chromatin remodeling [GO:0140861]; double-strand break repair [GO:0006302]; double-strand break repair via nonhomologous end joining [GO:0006303]; embryo implantation [GO:0007566]; regulation of epithelial to mesenchymal transition [GO:0010717]; single strand break... | cytosol [GO:0005829]; nucleus [GO:0005634]; site of DNA damage [GO:0090734]; site of double-strand break [GO:0035861] | 3'-5' exonuclease activity [GO:0008408]; ADP-D-ribose modification-dependent protein binding [GO:0160002]; DNA endonuclease activity [GO:0004520]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; histone binding [GO:0042393]; histone chaperone activity [GO:0140713]; metal ion binding [GO:0046872]... | PF10283; | 2.60.200.20; | APLF family | PTM: Poly-ADP-ribosylated. In addition to binding non covalently poly-ADP-ribose via its PBZ-type zinc fingers, the protein is also covalently poly-ADP-ribosylated by PARP1. {ECO:0000250|UniProtKB:Q8IW19}.; PTM: Phosphorylated in an ATM-dependent manner upon double-strand DNA break. {ECO:0000250|UniProtKB:Q8IW19}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9D842}. Chromosome {ECO:0000250|UniProtKB:Q8IW19}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9D842}. Note=Localizes to DNA damage sites. Accumulates at single-strand breaks and double-strand breaks via the PBZ-type zinc fingers. {ECO:0000250|UniProtKB:Q8IW19}. | null | null | null | null | null | FUNCTION: Histone chaperone involved in single-strand and double-strand DNA break repair. Recruited to sites of DNA damage through interaction with branched poly-ADP-ribose chains, a polymeric post-translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair re... | Bos taurus (Bovine) |
A0JNI4 | SRR_BOVIN | MCDQYCISFADVEKAHINIRDFIHLTPVLTSSILNQITGRNLFFKCELFQKTGSFKIRGALNAIRGLISAHPEEKPRAVVAHSSGNHGQALSFAARLEGIPAYVIVPETAPNCKKLAIQAYGASIVYSEQSEESRENITKRIAEETEGIMVHPNQEPAVIAGQGTIAMEVLNQVPLVDALVVPVGGGGMLAGIAVTVKALRPSVKVYAAEPLNADDCYQSKLKGELTPNPYPPETIADGIKSSIGLNTWPIIRDLVDDVFTVTEDEIKYATQLVWERMKLLIEPTAGVGVAVVLSQHFRTVPAEVKNICIVLSGGNVDLT... | 4.3.1.17; 4.3.1.18; 5.1.1.18 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9GZT4}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9GZT4}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q9GZT4}; COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={EC... | D-serine biosynthetic process [GO:0070179]; D-serine metabolic process [GO:0070178]; L-serine metabolic process [GO:0006563] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; D-serine ammonia-lyase activity [GO:0008721]; L-serine ammonia-lyase activity [GO:0003941]; magnesium ion binding [GO:0000287]; pyridoxal phosphate binding [GO:0030170]; serine racemase activity [GO:0030378]; threonine racemase activity [GO:0018114] | PF00291; | 3.40.50.1100; | Serine/threonine dehydratase family | PTM: S-nitrosylated, leading to decrease the enzyme activity. {ECO:0000250|UniProtKB:Q9QZX7}. | null | CATALYTIC ACTIVITY: Reaction=L-serine = D-serine; Xref=Rhea:RHEA:10980, ChEBI:CHEBI:33384, ChEBI:CHEBI:35247; EC=5.1.1.18; Evidence={ECO:0000250|UniProtKB:Q9QZX7}; CATALYTIC ACTIVITY: Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169, ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17; Evide... | null | null | null | null | FUNCTION: Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine (By similarity). {ECO:0000250|UniProtKB:Q9QZX7}. | Bos taurus (Bovine) |
A0JNM1 | OSTB_BOVIN | MNYSEKLTGAPPMTEVPLELLEEMLWFFRVEDATPWNCSMFVLAALVAIISFILLGRNIQANRNQKKLPPEKQTPEVLYLAEGGNKDDKNLTSLTETLLSEKPTLAQGEMEAKCSDVPRVHLPDPQEPES | null | null | bile acid and bile salt transport [GO:0015721]; bile acid secretion [GO:0032782]; positive regulation of protein exit from endoplasmic reticulum [GO:0070863]; positive regulation of protein glycosylation [GO:0060050]; positive regulation of protein targeting to membrane [GO:0090314]; regulation of protein stability [GO... | basolateral plasma membrane [GO:0016323]; membrane [GO:0016020]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | bile acid transmembrane transporter activity [GO:0015125]; protein heterodimerization activity [GO:0046982] | PF15048; | null | OST-beta family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Mainly restricted to the lateral and basal membranes of ileal enterocytes. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703, ChEBI:CHEBI:36257; Evidence={ECO:0000250|UniProtKB:Q86UW1}; CATALYTIC ACTIVITY: Reaction=estrone 3-sulfate(out) = estrone 3-sulfate(in); Xref=Rhea:RHEA:71835, ChEBI:CHEBI:60050; Evidence={ECO:0000250|UniProtKB:Q86UW2}; CATALYTIC AC... | null | null | null | null | FUNCTION: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood. The Ost-alpha/Ost-beta complex efficiently transports the major species of bile acids (taurocholate). Taurine conjugates... | Bos taurus (Bovine) |
A0JNT9 | BICL1_MOUSE | MSAFCLGLAGRASAPAEPDSACCMELPAGAGDAVRSPATAAALVSFPGGPGELELALEEELALLAAGERSSEPGEHPQAEPESPVEGHGPPLPPPPTQDPELLSVIRQKEKDLVLAARLGKALLERNQDMSRQYEQMHKELTDKLEHLEQEKHELRRRFENREGEWEGRVSELETDVKQLQDELERQQLHLREADREKTRAVQELSEQNQRLLDQLSRASEVERQLSMQVHALKEDFREKNSSTNQHIIRLESLQAEIKMLSDRKRELEHRLSATLEENDLLQGTVEELQDRVLILERQGHDKDLQLHQSQLELQEVRLS... | null | null | Golgi to secretory granule transport [GO:0055107]; neuron projection development [GO:0031175]; vesicle transport along microtubule [GO:0047496] | centrosome [GO:0005813]; cytoplasm [GO:0005737] | dynactin binding [GO:0034452]; small GTPase binding [GO:0031267] | null | null | BICDR family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305|PubMed:36071160}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20360680}. Note=Localizes around the centrosome. | null | null | null | null | null | FUNCTION: Acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin. Facilitates the interaction between dynein and dynactin and activates dynein processivity (the ability to move along a microtubule f... | Mus musculus (Mouse) |
A0JNU3 | LPP60_MOUSE | MARAMGPERRLLAIYTGGTIGMRSEGGVLVPGRGLAAVLKTLHMFHDEEYAQAHSLPEDTLVLPPASPDQRIIYTVLECQPLFDSSDMTITEWVQIAQTIERHYAQYQGFVVIHGTDTMAFAASVLSFMLENLQKPVVLTGAQVPIHALWSDGRENLLGALLMAGQYVIPEVCLFFQNQLFRGNRTTKVDARRFAAFCSPNLPPLATVGADVTINRELVRKACGKSHLVVHSSMEPDVGLLRLYPGIPASLVRTFLQPPLKGVVMETFGSGNGPTKPDLLQELRVAAEQGLIIVNCTHCLQGAVTSDYASGMAMAGAGIV... | 3.1.1.47; 3.1.1.5; 3.5.1.1 | null | asparagine metabolic process [GO:0006528]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644] | cytosol [GO:0005829] | 1-alkyl-2-acetylglycerophosphocholine esterase activity [GO:0003847]; acyltransferase activity, transferring groups other than amino-acyl groups [GO:0016747]; asparaginase activity [GO:0004067]; lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545] | PF12796;PF00710;PF17763; | 3.40.50.40;1.25.40.20;3.40.50.1170; | Asparaginase 1 family | null | null | CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:O88202}; PhysiologicalDirection=l... | null | null | null | null | FUNCTION: Exhibits lysophospholipase, transacylase, PAF acetylhydrolase and asparaginase activities (By similarity). Can catalyze three types of transacylation reactions: (1) acyl transfer from 1-acyl-sn-glycero-3-phosphocholine (1-acyl-GPC) to the sn-1(3) positions of glycerol and 2-acylglycerol (sn-1 to -1(3) transfe... | Mus musculus (Mouse) |
A0JNW5 | BLT3B_HUMAN | MAGIIKKQILKHLSRFTKNLSPDKINLSTLKGEGELKNLELDEEVLQNMLDLPTWLAINKVFCNKASIRIPWTKLKTHPICLSLDKVIMEMSTCEEPRSPNGPSPIATASGQSEYGFAEKVVEGISVSVNSIVIRIGAKAFNASFELSQLRIYSVNAHWEHGDLRFTRIQDPQRGEVLTFKEINWQMIRIEADATQSSHLEIMCAPVRLITNQSKIRVTLKRRLKDCNVIATKLVLILDDLLWVLTDSQLKAMVQYAKSLSEAIEKSTEQRKSMAPEPTQSSTVVASAQQVKTTQTSNAPDVNDAIVKLFNDFDVKETSH... | null | null | early endosome to Golgi transport [GO:0034498]; intermembrane lipid transfer [GO:0120009] | cytosol [GO:0005829]; early endosome [GO:0005769] | GARP complex binding [GO:0062069]; lipid transfer activity [GO:0120013]; protein homodimerization activity [GO:0042803] | PF12624; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20163565}. Early endosome {ECO:0000269|PubMed:20163565, ECO:0000269|PubMed:35499567}. Note=Localizes on a subpopulation of vesicle clusters in the early endocytic pathway. {ECO:0000269|PubMed:35499567}. | null | null | null | null | null | FUNCTION: Tube-forming lipid transport protein which mediates the transfer of lipids between membranes at organelle contact sites (PubMed:35499567). Required for retrograde traffic of vesicle clusters in the early endocytic pathway to the Golgi complex (PubMed:20163565, PubMed:35499567). {ECO:0000269|PubMed:20163565, E... | Homo sapiens (Human) |
A0JP26 | POTB3_HUMAN | MVAEVCSMPAASAVKKPFDLRSKMGKWCHHRFPCCRGSGKSNMGTSGDHDDSFMKTLRSKMGKCCHHCFPCCRGSGTSNVGTSGDHDNSFMKTLRSKMGKWCCHCFPCCRGSGKSNVGTWGDYDDSAFMEPRYHVRREDLDKLHRAAWWGKVPRKDLIVMLRDTDMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECVLMLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASI... | null | null | null | null | null | PF12796;PF14915; | 1.25.40.20; | POTE family | null | null | null | null | null | null | null | null | Homo sapiens (Human) |
A0JP82 | TET3_XENTR | MDTQPAPVPHVLPQDVYEFPDDQESLGRLRVSEMPAELNGGGGGGSAAAFAMELPEQSNKKRKRCGVCVPCLRKEPCGACYNCVNRSTSHQICKMRKCEQLKKKRVVPMKGVENCSESILVDGPKTDQMEAGPVNHVQEGRLKQECDSTLPSKGCEDLANQLLMEANSWLSNTAAPQDPCNKLNWDKPTIPNHAANNNSNLEDAKNLVAFSAVAEAMSTYGMPASGTPSSVSLQLYEKFNYETNRDNSGHLEGNAPSCPEDLNTLKAALALAKHGVKPPNCNCDGPECPDYLEWLENKIKSTVKGSQESPFPNLGQVSKE... | 1.14.11.80 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q6N021}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6N021}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q6N021}; Note=The zinc ions have a structural role. {ECO:0000250|UniProtKB:Q6N021}; | 5-methylcytosine catabolic process [GO:0006211]; DNA demethylation [GO:0080111]; eye development [GO:0001654]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; positive regulation of transcription by RNA polymerase II [GO:0045944] | chromosome [GO:0005694]; nucleus [GO:0005634] | 5-methylcytosine dioxygenase activity [GO:0070579]; methyl-CpG binding [GO:0008327]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270] | PF12851;PF02008; | null | TET family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23217707}. Chromosome {ECO:0000269|PubMed:23217707}. Note=Detected on chromatin, where it binds to target gene promoters. {ECO:0000269|PubMed:23217707}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-methyl-2'-deoxycytidine in DNA + O2 = a 5-hydroxymethyl-2'-deoxycytidine in DNA + CO2 + succinate; Xref=Rhea:RHEA:52636, Rhea:RHEA-COMP:11370, Rhea:RHEA-COMP:13315, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85454, ChEBI:CHEB... | null | null | null | null | FUNCTION: Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming during embryonic development. Conversion of 5mC into 5hmC probably constitutes the first step in cytosine demethylation. ... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A0JPF9 | ISPD_DANRE | MGTVTIQLSCLRHIRKLCFSCPWEGRRLFKMLLQFHHETQRPLDPGCLLPQDAERSADQPGRAVVDFPVAAVLPAGGSGERMGLTTPKQFCSIFNRPLISYTIQAFERLPWIVMVVVVVAKDNHDLMLNIVRKFNHTKVKVVHGGTTRHRSIYNGLQAFSDSTDSSTPKPKVVIIHDAVRPFVEEDLLLKITLAAKEQGASGAIRPLVSTVIATTSESYLDHSLERAKYRASEMPQGFLYDIIFQAYQRCSEFDLEFGTECLHLALQYCGTNARLIEGPPTLWKVTYKRDLAAAEAIIKETLSVSACIIAEAEEEAVELA... | 2.7.7.40 | null | brain morphogenesis [GO:0048854]; isoprenoid biosynthetic process [GO:0008299]; muscle cell development [GO:0055001]; protein O-linked mannosylation [GO:0035269]; regulation of protein glycosylation [GO:0060049] | cytosol [GO:0005829] | cytidylyltransferase activity [GO:0070567]; D-ribitol-5-phosphate cytidylyltransferase activity [GO:0047349]; protein homodimerization activity [GO:0042803] | PF01128;PF18706; | null | IspD/TarI cytidylyltransferase family, IspD subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:A4D126}. | CATALYTIC ACTIVITY: Reaction=CTP + D-ribitol 5-phosphate + H(+) = CDP-L-ribitol + diphosphate; Xref=Rhea:RHEA:12456, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:57608, ChEBI:CHEBI:57695; EC=2.7.7.40; Evidence={ECO:0000250|UniProtKB:A4D126}; CATALYTIC ACTIVITY: Reaction=CTP + D-ribose 5-phosphat... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:A4D126}. | null | null | FUNCTION: Cytidylyltransferase required for protein O-linked mannosylation (PubMed:22522421). Catalyzes the formation of CDP-ribitol nucleotide sugar from D-ribitol 5-phosphate (By similarity). CDP-ribitol is a substrate of FKTN during the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosami... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0JPL0 | ZN382_RAT | MNCHSVPLQGPVSFKDVTVDFTQEEWQRLDPAQKALYRDVMLENYCHFISVGFHITKPDMIRKLEQGEELWTERMFPSQSYLEDEEVLVKFRDYQDKPPTSIVIINHKKLIKERNNVYEKTLGNNHIISKTLFEYKSDGKVLKNISDFISRDINPVMGTLGDSSEWEESVLTSEQEKTHPVPTLYKQIGRNLSSSLELAQHQKTQIPEQRFECDECDSSFLMTEVAFPHDRAHRGVRDFNCSKDEIAFFEKSDLGIHPHNLMEKKCSTYNKYGKLLCRKSVFVMHPRSQVDERPFQCPYCGNSFRRKSYLIEHQRIHTGE... | null | null | negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of cell growth [GO:0001558]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF01352;PF00096; | 6.10.140.140;3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11154279, ECO:0000269|PubMed:9835615}. | null | null | null | null | null | FUNCTION: Functions as a sequence-specific transcriptional repressor. {ECO:0000269|PubMed:11154279, ECO:0000269|PubMed:9835615}. | Rattus norvegicus (Rat) |
A0JPN2 | S39A4_RAT | MMLPKSLTQGLLLAMLVGTAAMVQPYHLLSLLTSGQGALDRTALDGLLNTLVARVHCTDGPCEKCLSVETALALGKPDKPQLAPESVLESRYITYLSAAAALYLNDPEKTCKDIRAGLLASHVDDYLAKLESPEAMTLGLSQLLQKIEAHDASQPTREETCVDVPQLLEEAEEAGVSRSPGLVLTALLDHVLNGSCFQGLPSPQYFVDFVFRQLSSKPRNITLPELEDLMHHLGVGGEDHSDHGDHVDHSHLDREANHQDSELHATHNSSSSVWDTLCLSAKDVMAVYGLSEEAGVSPQAWAQLTPALVQQQLSEACSSS... | null | null | cellular response to zinc ion starvation [GO:0034224]; intracellular zinc ion homeostasis [GO:0006882]; zinc ion import across plasma membrane [GO:0071578]; zinc ion transmembrane transport [GO:0071577] | apical plasma membrane [GO:0016324]; cytoplasmic vesicle [GO:0031410]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monoatomic cation:bicarbonate symporter activity [GO:0140410]; zinc ion binding [GO:0008270]; zinc ion sensor activity [GO:0106219]; zinc ion sequestering activity [GO:0140486]; zinc ion transmembrane transporter activity [GO:0005385] | PF21116;PF02535;PF18292; | null | ZIP transporter (TC 2.A.5) family | PTM: The extracellular N-terminal ectodomain is cleaved when cells are Zn(2+) deficient, N-terminally cleaved SLC39A4 is internalized at a faster rate. {ECO:0000250|UniProtKB:Q78IQ7}.; PTM: Under excess Zn(2+) conditions, SLC39A4 on the cell surface is rapidly endocytosed, ubiquitinated and degraded. {ECO:0000250|UniPr... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q78IQ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A0H3LM39}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q78IQ7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A0H3LM39}. Apical cell membrane {ECO:0000250|UniProtKB:Q78IQ7}; Multi-pass ... | CATALYTIC ACTIVITY: Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351, ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q6P5W5}; | null | null | null | null | FUNCTION: Selective transporter that mediates the uptake of Zn(2+). Plays an essential role for dietary zinc uptake from small intestine (By similarity). The Zn(2+) uniporter activity is regulated by zinc availability. Exhibits also polyspecific binding and transport of Cu(2+), Cd(2+) and possibly Ni(2+) but at higher ... | Rattus norvegicus (Rat) |
A0JPN4 | ZC12A_RAT | MSDPCGKKLVQEISPTMSLWGLEDRHSCQGQPQPDQDPVAKEASASELQMKVDFFRKLGYSSSEIHSALQKLGVQADTNTVLGELVKHGSATERECQASTDPCPQPPLVPRGGSTPKPSTVEPSLPEEDKESSDLRPVVIDGSNVAMSHGNKEVFSCRGILLAVNWFLERGHTDITVFVPSWRKEQPRPDVPITDQHILRELEKKKILVFTPSRRVGGKRVVCYDDRFIVKLAYESDGVVVSNDTYRDLQGERQEWKRFIEERLLMYSFVNDKFMPPDDPLGRHGPSLDNFLRKKPLPSEHRKQPCPYGRKCTYGIKCRF... | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q5D1E7}; Note=Mg(2+) is required for RNase activity. {ECO:0000250|UniProtKB:Q5D1E7}; | 3'-UTR-mediated mRNA destabilization [GO:0061158]; angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cell differentiation [GO:0030154]; cellular response to chemokine [GO:1990869]; cellular response to glucose starvation [GO:0042149]; cellular response to ionomycin [GO:1904637]; cellular response to lipopolysa... | cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoskeleton [GO:0005856]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; P-body [GO:0000932]; protein-containing complex [GO:0032991]; rough endoplasmic reticulum [GO:0005791]; rough endoplasmic reticulum membrane [GO:0030867] | chromatin binding [GO:0003682]; cysteine-type deubiquitinase activity [GO:0004843]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; miRNA binding [GO:0035198]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; nuclease activity [GO:0004518]; ribosome... | PF18561;PF11977;PF18039; | 3.40.50.11980; | ZC3H12 family | PTM: Phosphorylated by IRAK1; phosphorylation is necessary for subsequent phosphorylation by the I-kappa-B-kinase (IKK) complex. Phosphorylated by I-kappa-B-kinases (IKKs) at Ser-435 and Ser-439 upon lipopolysaccharide (LPS) or IL1B stimulation in macrophages through the MyD88-dependent signaling pathway; these phospho... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5D1E7}. Cytoplasm {ECO:0000250|UniProtKB:Q5D1E7}. Rough endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5D1E7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5D1E7}; Cytoplasmic side {ECO:0000250|UniProtKB:Q5D1E7}. Cytoplasmic granule {ECO:0000250|UniPr... | null | null | null | null | null | FUNCTION: Endoribonuclease involved in various biological functions such as cellular inflammatory response and immune homeostasis, glial differentiation of neuroprogenitor cells, cell death of cardiomyocytes, adipogenesis and angiogenesis. Functions as an endoribonuclease involved in mRNA decay. Modulates the inflammat... | Rattus norvegicus (Rat) |
A0JPQ4 | TRI72_RAT | MSTAPGLLRQELSCPLCLQLFDAPVTAECGHSFCRACLIRVAGEPADDGTVACPCCQASTRPQALSTNLQLARLVEGLAQVPQGHCEEHLDPLSIYCEQDRTLVCGVCASLGSHRGHRLLPAAEAHARLKTQLPQQKAQLQEACMRKEKSVAVLEHQLVEVEETVRQFRGAVGEQLGKMRMFLAALESSLDREAERVRGEAGVALRRELSSLNSYLEQLRQMEKVLEEVADKPQTEFLMKFCLVTSRLQKILSESPPPARLDIQLPVISDDFKFQVWKKMFRALMPELEELTFDPSSAHPSLVVSASGRRVECSEQKAPP... | null | null | exocytosis [GO:0006887]; muscle organ development [GO:0007517]; muscle system process [GO:0003012]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of insulin-like growth factor receptor signaling pathway [GO:0043569]; negative regulation of myotube differentiation [GO:001083... | cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; sarcolemma [GO:0042383] | identical protein binding [GO:0042802]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; phosphatidylserine binding [GO:0001786]; ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF13765;PF00622;PF00643;PF15227; | 2.60.120.920;3.30.160.60;3.30.40.10; | TRIM/RBCC family | PTM: Disulfide bond formation at Cys-242 occurs in case of membrane damage that cause the entry of the oxidized milieu of the extracellular space, resulting in homooligomerization. {ECO:0000250}.; PTM: S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against oxidation-induced protein degradation and cell death... | SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}. Note=Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond forma... | Rattus norvegicus (Rat) |
A0JQ18 | SOP14_ARATH | MAAKTSNLVALLLSLFLLLLSISSQVGLGEAKRNLRNNLRLDCVSHPSPPPPHRSMAPPIFVPPSTSHKGQGP | null | null | defense response [GO:0006952]; defense response to bacterium [GO:0042742]; response to bacterium [GO:0009617]; response to cold [GO:0009409]; response to ethylene [GO:0009723]; response to jasmonic acid [GO:0009753]; response to salicylic acid [GO:0009751]; response to salt stress [GO:0009651]; response to water depriv... | apoplast [GO:0048046]; plasma membrane [GO:0005886] | LRR domain binding [GO:0030275]; receptor serine/threonine kinase binding [GO:0033612] | null | null | Serine rich endogenous peptide (SCOOP) phytocytokine family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31001913}. Secreted, extracellular space, apoplast {ECO:0000269|PubMed:31001913}. Note=The precursor of SCOOP14, PROSCOOP14, accumulates at the plasma membrane and is proteolytically cleaved to release the SCOOP14 in the apoplasm. {ECO:0000269|PubMed:31001913}. | null | null | null | null | null | FUNCTION: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation... | Arabidopsis thaliana (Mouse-ear cress) |
A0KEL1 | FADB_AERHH | MIYQGETLTVSYLEDGIAELRFDAPGSVNKLDRATLLSLSEAIAALQQERELKGLILTSGKDAFIVGADITEFLELFDLPQADLLGWLKKANDIFSAIEDLPVPTLSAIKGHALGGGCETILSTDFRLADTSAKIGLPETKLGIMPGFGGTVRLPRVIGADNALEWITTGKDYRADDALKVGAIDAVVAPDALQSAAVQMIKDAVKGKLDWQGRRAAKKAPLRLSKLEAMMSFTTAAGMVAAVAGKHYPAPMTAVKTVEAAAGMSRDEALAVEAQGFIKLAKTDVAKALVGIFLNDQHIKALAKKAAKQAAKATSHAAVL... | 1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8 | null | fatty acid beta-oxidation [GO:0006635] | fatty acid beta-oxidation multienzyme complex [GO:0036125] | 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403] | PF00725;PF02737;PF00378; | 1.10.1040.50;3.40.50.720; | Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-... | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}. | null | null | FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. | Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049) |
A0KLG5 | BSR_AERHH | MHKKTLLATLILGLLAGQAVAAPYLPLASDHRNGEVQTASNAWLEVDLGAFEHNIQTLKDRLGDKGPKICAIMKADAYGHGIDLLVPSVVKAGIPCIGIASNEEARVAREKGFTGRLMRVRAATPAEVEQALPYKMEELIGSLVSAQGIADIAQRHHTNIPVHIALNSAGMSRNGIDLRLADSKEDALAMLKLKGITPVGIMTHFPVEEKEDVKMGLAQFKLDSQWLLEAGKLDRSKITIHAANSFATLEVPDAYFDMVRPGGLLYGDSIPSYTEYKRVMAFKTQVASVNHYPAGNTVGYDRTFTLKRDSWLANLPLGYS... | 5.1.1.10 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:24419381}; | peptidoglycan biosynthetic process [GO:0009252] | cytosol [GO:0005829]; periplasmic space [GO:0042597] | alanine racemase activity [GO:0008784]; arginine racemase activity [GO:0047679]; lysine racemase activity [GO:0018113]; methionine racemase activity [GO:0018111]; pyridoxal phosphate binding [GO:0030170]; serine racemase activity [GO:0030378] | PF00842;PF01168; | 3.20.20.10; | Alanine racemase family, Bsr subfamily | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q9KSE5, ECO:0000255|HAMAP-Rule:MF_02212}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid = a D-alpha-amino acid; Xref=Rhea:RHEA:18317, ChEBI:CHEBI:59869, ChEBI:CHEBI:59871; EC=5.1.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_02212, ECO:0000269|PubMed:24419381}; CATALYTIC ACTIVITY: Reaction=L-lysine = D-lysine; Xref=Rhea:RHEA:22864, ChEBI:CHEBI:32551, ChEBI:CH... | null | null | null | null | FUNCTION: Amino-acid racemase able to utilize a broad range of substrates. Reversibly racemizes ten of the 19 natural chiral amino acids known, including both non-beta-branched aliphatic amino acids (Ala, Leu, Met, Ser, Cys, Gln and Asn) and positively charged amino acids (His, Lys and Arg). Is not active on negatively... | Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049) |
A0KR50 | FADB_SHESA | MIYQSPTIQVELLEDNIAKLCFNAPGSVNKFDRETLASLDAALDSIKQQSNIQALVLTSGKDTFIVGADITEFLGLFAQDDAVLLSWIEQANAVFNKLEDLPFPTASAIKGFALGGGCETILATDFRIADTTAKIGLPETKLGIIPGFGGTVRLPRVIGADNALEWITTGKDQRPEDALKVGAVDAVVAPEALEAAAIQMLKDAVAEKLDWQARRQRKMSPLTLPKLEAMMSFTTAKGMVFAVAGKHYPAPMAAVSVVEQAATKGRSDALQIEHQAFIKLAKTDVAKALIGIFLNDQLVKGKAKKAGKLAKDVKSAAVLG... | 1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8 | null | fatty acid beta-oxidation [GO:0006635] | fatty acid beta-oxidation multienzyme complex [GO:0036125] | 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403] | PF00725;PF02737;PF00378; | 1.10.1040.50;3.40.50.720; | Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-... | null | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}. | null | null | FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}. | Shewanella sp. (strain ANA-3) |
A0LFF8 | MDH_SYNFM | MAKKPVRVTVTGAAGQIGYALLFRVASGQMLGPDQPIILQMLELPIDKVQAALKGVMMELEDCAFPLLADMIGTGDPKVAFKDSDYALLVGARPRGPGMERKDLLLENAKIFIEQGKAMNAVASRDIRVIVVGNPANTNAWIAMKSAPDLPKGNFTAMLRLDHNRAKSQLATRTGKPVASVEKMIVWGNHSPTMYPDIRFCTVDGQPAVKLVNDEAWYRNEYIPKVGKRGAAIIEARGLSSAASAANAAIDHMHDWALGTNGKWVTMGLPSDGSYGIPEGTMYGVPVTCTPGKYERVKGLEIDAFSREKMDFTLKELTEE... | 1.1.1.37 | null | malate metabolic process [GO:0006108]; NADH metabolic process [GO:0006734]; oxaloacetate metabolic process [GO:0006107]; tricarboxylic acid cycle [GO:0006099] | null | L-malate dehydrogenase activity [GO:0030060] | PF02866;PF00056; | 3.90.110.10;3.40.50.720; | LDH/MDH superfamily, MDH type 2 family | null | null | CATALYTIC ACTIVITY: Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; Evidence={ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000269|PubMed:8900056}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=50 uM for oxaloacetate (at 37 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:8900056}; KM=30 uM for NADH (at 37 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:8900056}; KM=4 mM for L-malate (at 37 degrees Celsius and pH 9.0) {ECO:0000269|PubMed:8900056}; KM=1.1 m... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 with oxaloacetate as substrate. {ECO:0000269|PubMed:8900056}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius with oxaloacetate as substrate. {ECO:0000269|PubMed:8900056}; | FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. Catalyzes the reduction of oxaloacetate more efficiently than the oxidation of malate. {ECO:0000269|PubMed:8900056}. | Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB) |
A0LNN5 | SFMCT_SYNFM | MADQQTTMPRWVPLLLGLLGSTTCGMLLYAWSVFIKPLNAEFGWSRAEIAMAFAICCLIFGLMTFPAGRLSDKMGPRKVVMTGGVLLAIGFILSGFIQSKYQLYITYGVIAGFGGGMIYLPPIATAPKWWPDRRALATGFAVVGLGLGSFLMGPLATYIIEKPGMGWRYVFWYCGVAMGIMALIAGAFLEPPPAGWKPAGYTPPAPPAGAAAPKVTRDWTYEEAKGDTKFWLLYLAYFCGSFAGLMVIGHLAGFGRDAGLTAMAAAGAVSSLAFSNAATRILSGWFVDKIGIRVYFAALFALQTAAMIAIFQLGGSVVGL... | null | null | null | plasma membrane [GO:0005886] | symporter activity [GO:0015293] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Monocarboxylate porter (TC 2.A.1.13) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:31201333}; Multi-pass membrane protein {ECO:0000255}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=233 uM for L-lactate {ECO:0000269|PubMed:31201333}; | null | null | null | FUNCTION: Proton-coupled L-lactate specific transporter. {ECO:0000269|PubMed:31201333}. | Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB) |
A0LU48 | DOP_ACIC1 | MHRVMGIETEYGISVPHQPNANAMAASSQVVNAYAPIGAPAQRQARWDFEEENPLRDARGFEVAREAADPSQLTDEDLGLANVILTNGARLYVDHAHPEYSTPEVTNPRDAVLWDKAGERIMAEAARRAADLPMGWTIQLYKNNTDNKGASYGCHENYLMNRSTPFADIVRHLIPFFVTRQVFCGAGRVGIGADGRGEGFQLSQRADFFEVEVGLETTLKRPIINTRDEPHADPEKYRRLHVIIGDANMSEIATYLKLGTTALVLAMIEDGFLSQDFSVESPVGALRAVSHDPTLRYQLRLHDGRRLTAVQLQMEYLEQA... | 3.4.-.- | COFACTOR: Name=ATP; Xref=ChEBI:CHEBI:30616; Evidence={ECO:0000250}; Note=ATP is required for the deamidation and depupylation reactions but is not hydrolyzed during the reactions. {ECO:0000250}; | modification-dependent protein catabolic process [GO:0019941]; proteasomal protein catabolic process [GO:0010498]; protein pupylation [GO:0070490] | null | ATP binding [GO:0005524]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides [GO:0016811]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233] | PF03136; | null | Pup ligase/Pup deamidase family, Pup deamidase subfamily | null | null | null | null | PATHWAY: Protein degradation; proteasomal Pup-dependent pathway. | null | null | FUNCTION: Displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; is thus involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins. Is also able to catalyze the deamidation of the C-te... | Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) |
A0M8Q6 | IGLC7_HUMAN | GQPKAAPSVTLFPPSSEELQANKATLVCLVSDFNPGAVTVAWKADGSPVKVGVETTKPSKQSNNKYAASSYLSLTPEQWKSHRSYSCRVTHEGSTVEKTVAPAECS | null | null | adaptive immune response [GO:0002250]; B cell receptor signaling pathway [GO:0050853]; immunoglobulin mediated immune response [GO:0016064] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; IgA immunoglobulin complex [GO:0071745]; IgD immunoglobulin complex [GO:0071738]; IgE immunoglobulin complex [GO:0071742]; IgG immunoglobulin complex [GO:0071735]; IgM immunoglobulin complex [GO:0071753]; plasma membrane [GO:0005886] | antigen binding [GO:0003823] | PF07654; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. | null | null | null | null | null | FUNCTION: Constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trig... | Homo sapiens (Human) |
A0M8R5 | CAV2_PAPAN | MGLETEKADVQLFMDDDSYSHHSGLEYADPEKFADSGQDRDPHRLNSHLKLGFEDVIAEPVTTHSFDKVWICSHALFEISKYVMYKFLTVFLAIPLAFIAGILFATLSCLHIWILMPFVKTCLMVLPSVQTIWKSVTDVFIAPLCTSIGRSFSSVSLQLSQD | null | null | caveola assembly [GO:0070836]; endoplasmic reticulum organization [GO:0007029]; insulin receptor signaling pathway [GO:0008286]; mitochondrion organization [GO:0007005]; negative regulation of endothelial cell proliferation [GO:0001937]; positive regulation of dopamine receptor signaling pathway [GO:0060161]; positive ... | caveola [GO:0005901]; cytoplasmic vesicle [GO:0031410]; focal adhesion [GO:0005925]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane raft [GO:0044853]; sarcolemma [GO:0042383] | D1 dopamine receptor binding [GO:0031748]; molecular adaptor activity [GO:0060090]; protein kinase binding [GO:0019901] | PF01146; | null | Caveolin family | PTM: Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells (By similarity). Phosphorylation on both Tyr-19 and Tyr-27 is required ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphoryla... | null | null | null | null | null | FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role... | Papio anubis (Olive baboon) |
A0M8R6 | CAV1_PAPAN | MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMADELSEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALVWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTVCDPLFEAVGKIFSNVRINLQKEI | null | null | caveola assembly [GO:0070836]; cell differentiation [GO:0030154]; negative regulation of endothelial cell proliferation [GO:0001937]; receptor internalization [GO:0031623]; regulation of cytosolic calcium ion concentration [GO:0051480]; T cell costimulation [GO:0031295] | caveola [GO:0005901]; endosome [GO:0005768]; focal adhesion [GO:0005925]; Golgi membrane [GO:0000139]; membrane raft [GO:0045121]; perinuclear region of cytoplasm [GO:0048471]; sarcolemma [GO:0042383] | molecular adaptor activity [GO:0060090]; oxysterol binding [GO:0008142]; protein kinase binding [GO:0019901]; transmembrane transporter binding [GO:0044325] | PF01146; | null | Caveolin family | PTM: Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress. {ECO:0000250|UniProtKB:Q03135}.; PTM: Ubiquitinated. Undergo monoubiquitination and multi- and/or polyubiquitination. Monoubiquitination of N-terminal lysines promotes integration in a ternary complex with UBXN6 and VCP which promotes oligomeric CAV... | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000250|UniProtKB:P49817}; Peripheral membrane protein {ECO:0000250}. Membrane raft {ECO:0000250|UniProtKB:Q03135}. Note... | null | null | null | null | null | FUNCTION: May act as a scaffolding protein within caveolar membranes. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (By similarity). Interacts directly with G-protein alpha subunits a... | Papio anubis (Olive baboon) |
A0M8R7 | MET_PAPAN | MKAPAVLVPGILVLLFTLVQRSNGECKEALAKSEMNVNMKYQLPNFTAETAIQNVILHEHHIFLGATNYIYVLNEEDLQKVAEYKTGPVLEHPDCFPCQDCSSKANLSGGVWKDNINMALVVDTYYDDQLISCGSVNRGTCQRHVFPHNHTADIQSEVHCIFSPQIEEPSQCPDCVVSALGAKVLSSVKDRFINFFVGNTINSSYFPHHPLHSISVRRLKETKDGFMFLTDQSYIDVLPEFRDSYPIKYIHAFESNNFIYFLTVQRETLNAQTFHTRIIRFCSLNSGLHSYMEMPLECILTEKRKKRSTKKEVFNILQAA... | 2.7.10.1 | null | phosphorylation [GO:0016310]; positive chemotaxis [GO:0050918]; positive regulation of endothelial cell chemotaxis [GO:2001028]; semaphorin-plexin signaling pathway [GO:0071526]; semaphorin-plexin signaling pathway involved in axon guidance [GO:1902287]; transmembrane receptor protein tyrosine kinase signaling pathway ... | membrane [GO:0016020]; semaphorin receptor complex [GO:0002116] | ATP binding [GO:0005524]; semaphorin receptor activity [GO:0017154]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF07714;PF01437;PF01403;PF01833; | 2.60.40.10;1.10.510.10;2.130.10.10; | Protein kinase superfamily, Tyr protein kinase family | PTM: Autophosphorylated in response to ligand binding on Tyr-1234 and Tyr-1235 in the kinase domain leading to further phosphorylation of Tyr-1349 and Tyr-1356 in the C-terminal multifunctional docking site. Dephosphorylated by PTPRJ at Tyr-1349 and Tyr-1365. Dephosphorylated by PTPN1 and PTPN2 (By similarity). {ECO:00... | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphoryl... | Papio anubis (Olive baboon) |
A0M8S6 | CAV2_FELCA | MGLETEKADVQLFMDDDSYSRHSGVDYADPDKFADSGSDRDPHRLNSNLKVGFEDVIAEPVSTHSFDKVWICSHALFEISKYVIYKFLTLFLAIPLAFAAGILFATLSCLHIWIIMPFVKTCLMVLPSVQTIWKSITDVVIAPLCTSVGRSFSSVSLQLSHD | null | null | caveola assembly [GO:0070836]; cell differentiation [GO:0030154]; endoplasmic reticulum organization [GO:0007029]; insulin receptor signaling pathway [GO:0008286]; mitochondrion organization [GO:0007005]; negative regulation of endothelial cell proliferation [GO:0001937]; positive regulation of dopamine receptor signal... | caveola [GO:0005901]; cytoplasmic vesicle [GO:0031410]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane raft [GO:0044853]; sarcolemma [GO:0042383] | D1 dopamine receptor binding [GO:0031748]; molecular adaptor activity [GO:0060090]; protein kinase binding [GO:0019901] | PF01146; | null | Caveolin family | PTM: Phosphorylated on serine and tyrosine residues. CAV1 promotes phosphorylation on Ser-23 which then targets the complex to the plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-36 appears to modulate mitosis in endothelial cells (By similarity). Phosphorylation on both Tyr-19 and Tyr-27 is required ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Golgi apparatus membrane; Peripheral membrane protein. Cell membrane; Peripheral membrane protein. Membrane, caveola; Peripheral membrane protein. Note=Potential hairpin-like structure in the membrane. Membrane protein of caveolae. Tyr-19-phosphoryla... | null | null | null | null | null | FUNCTION: May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role... | Felis catus (Cat) (Felis silvestris catus) |
A0M8S7 | CAV1_FELCA | MSGGKYVDSEGHLYTVPIREQGNIYKPNNKAMAEEINEKQVYDAHTKEIDLVNRDPKHLNDDVVKIDFEDVIAEPEGTHSFDGIWKASFTTFTVTKYWFYRLLSALFGIPMALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYVHTFCDPFFEAVGKIFSNIRINMQKEI | null | null | caveola assembly [GO:0070836]; cell differentiation [GO:0030154]; negative regulation of endothelial cell proliferation [GO:0001937]; receptor internalization [GO:0031623]; regulation of cytosolic calcium ion concentration [GO:0051480]; T cell costimulation [GO:0031295] | caveola [GO:0005901]; cytoplasmic vesicle [GO:0031410]; endosome [GO:0005768]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane raft [GO:0045121]; perinuclear region of cytoplasm [GO:0048471]; sarcolemma [GO:0042383] | molecular adaptor activity [GO:0060090]; oxysterol binding [GO:0008142]; protein kinase binding [GO:0019901]; transmembrane transporter binding [GO:0044325] | PF01146; | null | Caveolin family | PTM: Phosphorylated at Tyr-14 by ABL1 in response to oxidative stress. {ECO:0000250|UniProtKB:Q03135}.; PTM: Ubiquitinated. Undergo monoubiquitination and multi- and/or polyubiquitination. Monoubiquitination of N-terminal lysines promotes integration in a ternary complex with UBXN6 and VCP which promotes oligomeric CAV... | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Membrane, caveola {ECO:0000250|UniProtKB:P49817}; Peripheral membrane protein {ECO:0000250}. Membrane raft {ECO:0000250|UniProtKB:Q03135}. Note... | null | null | null | null | null | FUNCTION: May act as a scaffolding protein within caveolar membranes. Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (By similarity). Interacts directly with G-protein alpha subunits a... | Felis catus (Cat) (Felis silvestris catus) |
A0M8S8 | MET_FELCA | MKAPAVLAPGILVLLFTLVQKSYGECREALVKSEMNVNMKYQLPNFTAETPIQNVVLHKHHIYLGAVNYIYVLNDKDLQKVAEYKTGPVLEHPDCFPCQDCSHKANLSGGVWKDNINMALLIDTYYDDQLISCGSVHRGTCQRHVLPPSNTADILSKVHCMYSPQADEESSHCPDCVVSALGTKVLISEKGRFINFFVGNTINSSYLTDHSLHSISVRRLKETQDGFKFLTDQSYIDVLPEFRDSYPIKYIHAFESNRFIYFLTVQRETLDAQTFHTRIIRFCSVDSGLHSYMEMPLECILTEKRRKRSTREEVFNILQA... | 2.7.10.1 | null | branching morphogenesis of an epithelial tube [GO:0048754]; cell migration [GO:0016477]; endothelial cell morphogenesis [GO:0001886]; establishment of skin barrier [GO:0061436]; liver development [GO:0001889]; negative regulation of hydrogen peroxide-mediated programmed cell death [GO:1901299]; negative regulation of R... | basal plasma membrane [GO:0009925]; receptor complex [GO:0043235]; semaphorin receptor complex [GO:0002116] | ATP binding [GO:0005524]; hepatocyte growth factor receptor activity [GO:0005008]; identical protein binding [GO:0042802]; protein phosphatase binding [GO:0019903]; semaphorin receptor activity [GO:0017154] | PF07714;PF01437;PF01403;PF01833; | 2.60.40.10;1.10.510.10;2.130.10.10; | Protein kinase superfamily, Tyr protein kinase family | PTM: Autophosphorylated in response to ligand binding on Tyr-1235 and Tyr-1236 in the kinase domain leading to further phosphorylation of Tyr-1350 and Tyr-1357 in the C-terminal multifunctional docking site. Dephosphorylated by PTPRJ at Tyr-1350 and Tyr-1366. Dephosphorylated by PTPN1 and PTPN2 (By similarity). {ECO:00... | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphoryl... | Felis catus (Cat) (Felis silvestris catus) |
A0MD28 | RPOA_PRRSS | MSGTFSRCMCTPAARVFWNAGQVFCTRCLSARPLLSPELQDTDLGVVGLFYKPKDKIHWKVPIGIPQVECTPSGCCWLSAVFPLARMTSGNHNFLQRLVKVADVLYRDGCLAPRHLRELQVYERGCSWYPITGPVPGMGLFANSMHVSDQPFPGATHVLTNSPLPQRACRQPFCPFEEAHSDVYRWKKFVIFTDSSPNGRFRMMWTPESDDSAALEVLPPELERQVEILTRSFPAHHPINLADWELTESPENGFSFGTSHSCGHIVQNPNVFDGKCWLTCFLGQSAEVCYHEEHLANALGYQTKWGVHGKYLQRRLQVRG... | 2.7.7.48; 3.4.19.12; 3.4.21.-; 3.4.22.-; 3.6.4.12; 3.6.4.13; 4.6.1.- | null | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; symbiont-mediated suppression of host ISG15-protein conjugation [GO:0039579]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:003956... | host cell endoplasmic reticulum [GO:0044165]; host cell membrane [GO:0033644]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; endonuclease activity [GO:0004519]; lyase activity [GO:0016829]; protein serine/threonine kinase inhibitor activity [GO:0030291]; RNA binding [GO:0003723... | PF16749;PF14757;PF14758;PF05410;PF05411;PF05412;PF05579;PF00680;PF01443; | 3.90.70.160;4.10.80.390;3.30.1330.220;2.30.31.30;3.90.70.70;3.40.50.300;3.90.70.60;2.40.10.10; | Arteriviridae polyprotein family | PTM: [Replicase polyprotein 1ab]: Specific enzymatic cleavages in vivo by its own proteases yield mature proteins. Nsp1 is autocleaved into two subunits, Nsp1-alpha and Nsp1-beta. There are two alternative pathways for processing. Either nsp4-5 is cleaved, which represents the major pathway or the nsp5-6 and nsp6-7 are... | SUBCELLULAR LOCATION: [Nsp1]: Host nucleus {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm {ECO:0000250|UniProtKB:Q04561}.; SUBCELLULAR LOCATION: [Nsp1-alpha papain-like cysteine proteinase]: Host nucleus {ECO:0000250|UniProtKB:Q04561}. Host cytoplasm {ECO:0000250|UniProtKB:Q04561}.; SUBCELLULAR LOCATION: [Nsp1-beta pap... | CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALY... | null | null | null | null | FUNCTION: [Replicase polyprotein 1ab]: Contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.; FUNCTION: [Nsp1-alpha papain-like cysteine protei... | Porcine reproductive and respiratory syndrome virus (isolate Pig/United States/SD 01-08/2001) (PRRSV) |
A0MES8 | ABI4_ARATH | MDPLASQHQHNHLEDNNQTLTHNNPQSDSTTDSSTSSAQRKRKGKGGPDNSKFRYRGVRQRSWGKWVAEIREPRKRTRKWLGTFATAEDAARAYDRAAVYLYGSRAQLNLTPSSPSSVSSSSSSVSAASSPSTSSSSTQTLRPLLPRPAAATVGGGANFGPYGIPFNNNIFLNGGTSMLCPSYGFFPQQQQQQNQMVQMGQFQHQQYQNLHSNTNNNKISDIELTDVPVTNSTSFHHEVALGQEQGGSGCNNNSSMEDLNSLAGSVGSSLSITHPPPLVDPVCSMGLDPGYMVGDGSSTIWPFGGEEEYSHNWGSIWDFI... | null | null | abscisic acid-activated signaling pathway [GO:0009738]; defense response [GO:0006952]; ethylene-activated signaling pathway [GO:0009873]; lateral root development [GO:0048527]; mitochondria-nucleus signaling pathway [GO:0031930]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of L-ascorbic ... | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976] | PF00847; | 3.30.730.10; | AP2/ERF transcription factor family, ERF subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:24451981}. | null | null | null | null | null | FUNCTION: Transcription regulator that probably binds to the GCC-box pathogenesis-related promoter element. Binds also to the S-box (5'-CACTTCCA-3') photosynthesis-associated nuclear genes-related (PhANGs-related) promoter element, and thus acts as a transcription inhibitor. Involved in the regulation of gene expressio... | Arabidopsis thaliana (Mouse-ear cress) |
A0MGZ7 | H6S3B_DANRE | MNDKPNKWIFIPILAILFVMIGYQYVCPAGGQACHFRTGDKLVRIAPLATPDPTTDDLYREQDPEEDNPPKCASKFNFTERDLTRDVDFNIKGDDVIVFLHIQKTGGTTFGRHLVRNIRLEQPCDCKAGQKKCTCHRPGKQESWLFSRFSTGWSCGLHADWTELTNCVPVIMDKRQPPKRKRNFYYITMLRDPVSRYLSEWKHVQRGATWKTSLHMCDGRSPTQDELPTCYNGDDWSGVTLHDFMDCPSNLANNRQVRMLADLSLVGCYNLSTMNESERNPILLASAKSNLKNMAFYGLTEFQRKTQYLFERTFHLRFIS... | 2.8.2.- | null | heparan sulfate proteoglycan biosynthetic process, enzymatic modification [GO:0015015] | membrane [GO:0016020] | 3'-phosphoadenosine 5'-phosphosulfate binding [GO:0050656]; heparan sulfate 6-O-sulfotransferase activity [GO:0017095]; oligosaccharide binding [GO:0070492]; sulfotransferase activity [GO:0008146] | PF03567; | 3.40.50.300; | Sulfotransferase 6 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:56604, Rhea:RHEA-COMP:9830, Rhea:RHEA-COMP:14621, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:C... | null | null | null | null | FUNCTION: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate. {ECO:0000269|PubMed:28103688}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0MLS4 | GHRL_PAPHA | MPSPGTVCSLLLLGMLWLDLAMAGSSFLSPEHQRAQQRKESKKPPAKLQPRALGGWLRPEDGDQAEGAEDELEIQFNAPFDVGIKLSGVQYQQHSQALGKFLQDILWEEAKEAPADK | null | null | actin polymerization or depolymerization [GO:0008154]; decidualization [GO:0046697]; dendrite development [GO:0016358]; gastric acid secretion [GO:0001696]; negative regulation of apoptotic process [GO:0043066]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of inflammatory resp... | axon [GO:0030424]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | ghrelin receptor binding [GO:0031768]; growth hormone-releasing hormone activity [GO:0016608]; hormone activity [GO:0005179]; protein tyrosine kinase activator activity [GO:0030296] | PF04643;PF04644; | null | Motilin family | PTM: O-octanoylated by GOAT/MBOAT4 (By similarity). O-octanoylation is essential for ghrelin activity. {ECO:0000250, ECO:0000250|UniProtKB:Q9EQX0}.; PTM: Amidation of Leu-98 is essential for obestatin activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: [Ghrelin]: Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR). Induces the release of growth hormone from the pituitary. Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation (By similarity). {ECO:0000250}.; FUNCTIO... | Papio hamadryas (Hamadryas baboon) |
A0MLS5 | BMAL1_HORSE | MADQRMDISSTISDFMSPGATDLLSSPLGTSGMDCNRKRKGSSTDYQESMDTDKDDPHGRLEYTEHQGRIKNAREAHSQIEKRRRDKMNSFIDELASLVPTCNAMSRKLDKLTVLRMAVQHMKTLRGATNPYTEANYKPTFLSDDELKHLILRAADGFLFVVGCDRGKILFVSESVFKILNYSQNDLIGQSLFDYLHPKDIAKVKEQLSSSDTAPRERLIDAKTGLPVKTDITPGPSRLCSGARRSFFCRMKCNRPSVKVEDKDFPSTCSKKKADRKSFCTIHSTGYLKSWPPTKMGLDEDNEPDNEGCNLSCLVAIGRL... | null | null | circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of glucocorticoid receptor signaling pathway [GO:2000323]; negative regulation of TOR si... | aryl hydrocarbon receptor complex [GO:0034751]; chromatoid body [GO:0033391]; nucleus [GO:0005634]; PML body [GO:0016605]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region ... | PF00010;PF00989;PF14598; | 4.10.280.10;3.30.450.20; | null | PTM: Ubiquitinated, leading to its proteasomal degradation. Deubiquitinated by USP9X. {ECO:0000250|UniProtKB:Q9WTL8}.; PTM: O-glycosylated; contains O-GlcNAc. O-glycosylation by OGT prevents protein degradation by inhibiting ubiquitination. It also stabilizes the CLOCK-BMAL1 heterodimer thereby increasing CLOCK-BMAL1-m... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. Cytoplasm {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Note=Shuttles between the nucleus and the cytoplasm and this nucleocytoplasmic shuttling is essential for the nuclear accumulation of CLOCK, target gene transcription and the degradation of th... | null | null | null | null | null | FUNCTION: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism a... | Equus caballus (Horse) |
A0MQA3 | ASP5_TOXGO | MEAGAMGGSSFLSFSSGPSAETSPSSLSPPTSSSPSPSPQLVSDSVESLHAKRPLAQSSRSSSRTAASTCFCWQGEGQENEAAPTISQEERRGGSMTAASAGHLETAREEAARCLGCSYTGEERRGASSATSVLSLGGERGRPPSRSSSLWTFSGLLSPLAFRSRRCCPQFSSSSSPLSPLPHPRGAPASACGSAVITDRAGRPASPLSFSRLASPVSDPSGVCPPRVVAARVWRLLSSVLFSLVNCARLFPRRLSRRPDPLRKPRAQVWSASSRSLQALLLATVALFAACSSLHGSSLLGAQAASPTPPFLSLSSSPRS... | 3.4.23.- | null | proteolysis [GO:0006508] | Golgi membrane [GO:0000139] | aspartic-type endopeptidase activity [GO:0004190] | PF14541;PF14543; | 2.40.70.10; | Peptidase A1 family | PTM: May be auto-cleaved to produce a 55 kDa form. {ECO:0000269|PubMed:26576949}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:26473595, ECO:0000269|PubMed:26576949}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:26576949}; | null | FUNCTION: In tachyzoites, plays an essential role in the export of several dense granule proteins into the host cell by cleaving the localization motif RRLxx (termed Toxoplasma export element (TEXEL)) located downstream of the N-terminal secretory signal sequence (PubMed:26270241, PubMed:26473595, PubMed:26576949, PubM... | Toxoplasma gondii |
A0MQH0 | DICER_CRIGR | MKSPALQPLSMAGLQLMTPASSPMGPFFGLPWQQEAIHDNIYTPRKYQVELLEAALDHNTIVCLNTGSGKTFIAVLLTKELAHQIRGDLNPRAKRTVFLVNSANQVAQQVSAVRTHSDLKVGEYSNLEVNASWTKERWSQEFTKHQVLIMTCYVALNVLKNGYLSLSDINLLVFDECHLAILDHPYREIMKLCESCPSCPRILGLTASILNGKCDPEELEEKIQKLEKILKSNAETATDLVVLDRYASQPCEIVVDCGPFTDRSGLYERLLMELEEAINFINDCNVSVHSKERDSTLISKQILSDCRAVLVVLGPWCADK... | 3.1.26.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; | apoptotic DNA fragmentation [GO:0006309]; global gene silencing by mRNA cleavage [GO:0098795]; negative regulation of tumor necrosis factor production [GO:0032720]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; pre-miRNA processing [GO:0031054]; RISC complex assembly [GO:0070922]... | extracellular exosome [GO:0070062]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; RISC complex [GO:0016442]; RISC-loading complex [GO:0070578] | ATP binding [GO:0005524]; deoxyribonuclease I activity [GO:0004530]; DNA binding [GO:0003677]; double-stranded RNA binding [GO:0003725]; helicase activity [GO:0004386]; metal ion binding [GO:0046872]; pre-miRNA binding [GO:0070883]; protein domain specific binding [GO:0019904]; ribonuclease III activity [GO:0004525]; s... | PF03368;PF20932;PF20930;PF20931;PF00271;PF02170;PF04851;PF00636; | 3.30.160.20;3.30.160.380;3.40.50.300;2.170.260.10;1.10.1520.10; | Helicase family, Dicer subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPY3}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3; | null | null | null | null | FUNCTION: Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3' overhang of two nucleotides, produci... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
A0MSJ1 | CRA1B_DANRE | MEPDNTPSSRLRAAGVGGRAVFFCMVLYCTCCLRLAQAQSADVDVLQRLGLVGKRPPQGFIPIKSGVILTTRARIDVPVSSVIPVSLGSTFSIILSVCSHRINNAFLFTIVTKRKRLHLGVQFIPGQILVYLGQNSSVNFDYNVHNGQWHNLALEIQGQKVTLYTSCGNTSIQANLDFQNEETLDSEGSFRLGKMSQNSVQFEGAICQFDIHPSAQAAHNYCKYIKKQCREADTYRPNLPPLLPLLPLDPNRSTIQTPKVVTDINERHLSLTRDKMNINHEGQTTVPPMITQPTLQLPLQTTAQTTASIRNRTSQISPKP... | null | null | bone mineralization [GO:0030282]; extracellular matrix organization [GO:0030198]; notochord morphogenesis [GO:0048570]; skeletal system development [GO:0001501] | collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615] | extracellular matrix structural constituent conferring tensile strength [GO:0030020]; metal ion binding [GO:0046872] | PF01410;PF01391; | 2.60.120.1000;2.60.120.200; | Fibrillar collagen family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. | null | null | null | null | null | FUNCTION: May play a role during the calcification of cartilage and the transition of cartilage to bone (By similarity). Together with col27a1a, plays a role in development of the notochord and axial skeleton. {ECO:0000250, ECO:0000269|PubMed:20041163}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0MTA1 | APEX1_DANRE | MPKRAKKNEEGVDGEADNGTAAAKKEKKGKEPEAPILYEDPPEKLTSKDGRAANMKITSWNVDGLRAWVKKNGLDWVRKEDPDILCLQETKCAEKALPADITGMPEYPHKYWAGSEDKEGYSGVAMLCKTEPLNVTYGIGKEEHDKEGRVITAEFPDFFLVTAYVPNASRGLVRLDYRKTWDVDFRAYLCGLDARKPLVLCGDLNVAHQEIDLKNPKGNRKNAGFTPEEREGFTQLLEAGFTDSFRELYPDQAYAYTFWTYMMNARSKNVGWRLDYFVLSSALLPGLCDSKIRNTAMGSDHCPITLFLAV | 3.1.11.2; 3.1.21.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P27695}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P27695}; Note=Probably binds two magnesium or manganese ions per subunit. {ECO:0000250|UniProtKB:P27695}; | base-excision repair [GO:0006284]; heart contraction [GO:0060047]; heart looping [GO:0001947]; negative regulation of apoptotic process [GO:0043066]; positive regulation of gene expression [GO:0010628]; positive regulation of gene expression via CpG island demethylation [GO:0044029] | endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634] | class II DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0052720]; DNA-(abasic site) binding [GO:0140431]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; double-stranded DNA 3'-5' DNA exonuclease activity [GO:0008311]; metal ion binding [GO:0046872]; phosphoric diester hydrolase a... | PF03372; | 3.60.10.10; | DNA repair enzymes AP/ExoA family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00764}. Nucleus, nucleolus {ECO:0000250}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00764}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00764}. Mitochondrion {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence={ECO:0000250|UniProtKB:P27695}; | null | null | null | null | FUNCTION: Functions as an apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents (PubMed:16966376). Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent ... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A0MTQ2 | BAPA_SPHMI | MHYLKFPAIIAGMLLAGAASAEGPRARDLGVPFAGKPGANNAITDVAGVEVGYVSLISGEGKLERGKGPVRTGVTAVLPRGKESRTPVYAGWETSNAAGEMTGTVWLEERGYFDGPMMITNTHSVGVVRDAVVGWLADVKWPGAWFTPVVAETYDGMLNDINGFHVKPEHALRAIQTAASGPVAEGNVGGGVGMQCFGFKGGTGTASRVVEMDGKSYTVGVLVQCNFGMRPWLRVAGAPVGEELAGKYLPETRGTQTAAATNNGVAPGDGSIIVVMATDAPMLPHQLKRLAKRAAAGMGRMGDAGSNGSGDIFVAFSTAN... | 3.4.11.25 | null | proteolysis [GO:0006508] | periplasmic space [GO:0042597] | aminopeptidase activity [GO:0004177] | PF03576; | 3.60.70.12; | Peptidase S58 family | PTM: Autoproteolytic processing to generate the alpha and beta subunit is required for self-activation and is proposed to use a similar mechanism as substrate cleavage. {ECO:0000250|UniProtKB:Q52VH2}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q52VH2}. | CATALYTIC ACTIVITY: Reaction=Cleaves N-terminal beta-homoamino acids from peptides composed of 2 to 6 amino acids.; EC=3.4.11.25; Evidence={ECO:0000269|PubMed:17064315}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=39 mM for beta-homoVal-beta-homoAla-beta-homoLeu; KM=41 mM for beta-homoAla-beta-homoLeu; KM=4.4 mM for beta-3homoAla-pNA; Vmax=0.84 umol/min/mg enzyme with beta-homoVal-beta-homoAla-beta-homoLeu as substrate; Vmax=3.1 umol/min/mg enzyme with beta-homoAla-beta-homo... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10. {ECO:0000269|PubMed:17064315}; | null | FUNCTION: Beta-aminopeptidase that can cleave synthetic beta-peptides which consist of backbone-elongated beta-amino acid residues that are not processed by common proteolytic enzymes. Can cleave the beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu. Requires a beta-amino acid at the N-... | Sphingosinicella microcystinivorans |
A0MZ66 | SHOT1_HUMAN | MNSSDEEKQLQLITSLKEQAIGEYEDLRAENQKTKEKCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQNHLEIEKTCRESAEALATKLNKENKTLKRISMLYMAKLGPDVITEEINIDDEDSTTDTDGAAETCVSVQCQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETLHKEIHNLKQQLELLEEDKKEL... | null | null | actin filament bundle retrograde transport [GO:0061573]; axonogenesis [GO:0007409]; Cdc42 protein signal transduction [GO:0032488]; cytoplasmic actin-based contraction involved in cell motility [GO:0060327]; endoplasmic reticulum polarization [GO:0061163]; netrin-activated signaling pathway [GO:0038007]; neuron project... | axon [GO:0030424]; axonal growth cone [GO:0044295]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; filopodium [GO:0030175]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; microtubule cytoskeleton [GO:0015630]; perikaryon [GO:0043204]... | actin filament binding [GO:0051015]; cadherin binding [GO:0045296]; identical protein binding [GO:0042802]; kinesin binding [GO:0019894] | null | 1.20.5.1160; | Shootin family | PTM: Phosphorylated on Ser-101 and Ser-249 by PAK1 through a CDC42- and RAC1-dependent signaling pathway, which enhances its association with F-actin retrograde flow in filopodia and lamellipodia of axonal growth cones. Phosphorylation on Ser-101 and Ser-249 is increased by netrin-1. {ECO:0000250|UniProtKB:A0MZ67}. | SUBCELLULAR LOCATION: Perikaryon {ECO:0000250|UniProtKB:Q8K2Q9}. Cell projection, axon {ECO:0000250|UniProtKB:Q8K2Q9}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q8K2Q9}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8K2Q9}. Cell projection, filopodium {ECO:0000250|UniProtKB:A0MZ67}. Cell projection, lamelli... | null | null | null | null | null | FUNCTION: Involved in the generation of internal asymmetric signals required for neuronal polarization and neurite outgrowth. Mediates netrin-1-induced F-actin-substrate coupling or 'clutch engagement' within the axon growth cone through activation of CDC42, RAC1 and PAK1-dependent signaling pathway, thereby converting... | Homo sapiens (Human) |
A0MZ67 | SHOT1_RAT | MNSSDEEKQLQLITSLKEQAIGEYEDLRAENQKTKETCDKIRQERDEAVKKLEEFQKISHMVIEEVNFMQNHLEIEKTCRESAEALATKLNKENKTLKRISMLYMAKLGPDVITEEINIDDDDPGTDTDAAAETCVSVQCQKQIKELRDQIVSVQEEKKVLAIELESLKSKLGEVMEEVNKVKQEKAVLNSEVLEQRKVLEKCNRVSVLAVEEYEELQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSLPDQQLLKALDENAKLIQQLEEERIQHQQKVKELEERLENEALHKEIHNLRQQLELLEDDKREL... | null | null | actin filament bundle retrograde transport [GO:0061573]; axonogenesis [GO:0007409]; Cdc42 protein signal transduction [GO:0032488]; cytoplasmic actin-based contraction involved in cell motility [GO:0060327]; endoplasmic reticulum polarization [GO:0061163]; netrin-activated signaling pathway [GO:0038007]; neuron project... | axon [GO:0030424]; axonal growth cone [GO:0044295]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; filopodium [GO:0030175]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; microtubule associated complex [GO:0005875]; microtubule cytoskeleton [GO:0015630]; perikaryon [GO:0043204]; pe... | actin filament binding [GO:0051015]; cell adhesion molecule binding [GO:0050839]; kinesin binding [GO:0019894] | null | null | Shootin family | PTM: Phosphorylated on Ser-101 and Ser-249 by PAK1 through a CDC42- and RAC1-dependent signaling pathway, which enhances its association with F-actin retrograde flow in filopodia and lamellipodia of axonal growth cones (PubMed:23453953). Phosphorylation on Ser-101 and Ser-249 is increased by netrin-1 (PubMed:23453953).... | SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:17030985, ECO:0000269|PubMed:20664640}. Cell projection, axon {ECO:0000269|PubMed:17030985, ECO:0000269|PubMed:20664640}. Cell projection, growth cone {ECO:0000269|PubMed:17030985, ECO:0000269|PubMed:18519736, ECO:0000269|PubMed:20664640, ECO:0000269|PubMed:23453953}... | null | null | null | null | null | FUNCTION: Involved in the generation of internal asymmetric signals required for neuronal polarization and neurite outgrowth (PubMed:17030985, PubMed:17439943, PubMed:18519736, PubMed:20664640). Mediates netrin-1-induced F-actin-substrate coupling or 'clutch engagement' within the axon growth cone through activation of... | Rattus norvegicus (Rat) |
A0NLY7 | ISAHY_ROSAI | MSAQSALSGLGAKLLSGEVEVVDCTGVLGPNTPILQLPPDFAKNTPKVEIHKISEYDSDGPFFAWNWMVLGEHSGTHFDAPHHWITGKDYSDGFTDTLDVQRLIAPVNVIDCSKESAADPDFLLTADLIKAWEAEHGEIGAGEWVVMRTDWDKRAGDEAAFLNADETGPHSPGPTPDAIEYLLSKKIVGWGSQCIGTDAGQAGGMEPPFPAHNLLHRDNCFGLASLANLDKLPAKGAILIAAPLKIERGTGSPIRALALVPKA | 3.5.2.20 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:24917679}; Note=Binds 1 manganese ion per subunit. {ECO:0000269|PubMed:24917679}; | tryptophan catabolic process to kynurenine [GO:0019441] | null | arylformamidase activity [GO:0004061]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides [GO:0016812]; manganese ion binding [GO:0030145] | PF04199; | 3.50.30.50; | Cyclase 1 superfamily | null | null | CATALYTIC ACTIVITY: Reaction=H2O + isatin = H(+) + isatinate; Xref=Rhea:RHEA:43232, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27539, ChEBI:CHEBI:82904; EC=3.5.2.20; Evidence={ECO:0000269|PubMed:24917679}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.8 uM for isatin {ECO:0000269|PubMed:24917679}; Vmax=0.24 umol/sec/mg enzyme {ECO:0000269|PubMed:24917679}; Note=kcat is 24 sec(-1) for isatin as substrate. {ECO:0000269|PubMed:24917679}; | null | null | null | FUNCTION: Involved in the degradation of the plant hormone indole-3-acetic acid (IAA). Catalyzes the hydrolysis of the cyclic amide bond (lactam) of isatin (1H-indole-2,3-dione) to yield isatinate (2-(2-aminophenyl)-2-oxoacetate). {ECO:0000269|PubMed:24917679}. | Roseibium aggregatum (strain ATCC 25650 / DSM 13394 / JCM 20685 / NBRC 16684 / NCIMB 2208 / IAM 12614 / B1) (Stappia aggregata) |
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