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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A8K2U0 | A2ML1_HUMAN | MWAQLLLGMLALSPAIAEELPNYLVTLPARLNFPSVQKVCLDLSPGYSDVKFTVTLETKDKTQKLLEYSGLKKRHLHCISFLVPPPAGGTEEVATIRVSGVGNNISFEEKKKVLIQRQGNGTFVQTDKPLYTPGQQVYFRIVTMDSNFVPVNDKYSMVELQDPNSNRIAQWLEVVPEQGIVDLSFQLAPEAMLGTYTVAVAEGKTFGTFSVEEYVLPKFKVEVVEPKELSTVQESFLVKICCRYTYGKPMLGAVQVSVCQKANTYWYREVEREQLPDKCRNLSGQTDKTGCFSAPVDMATFDLIGYAYSHQINIVATVVE... | null | null | regulation of endopeptidase activity [GO:0052548] | extracellular exosome [GO:0070062]; extracellular space [GO:0005615] | peptidase inhibitor activity [GO:0030414]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF00207;PF07703;PF07677;PF01835;PF17791;PF17789;PF07678; | 1.50.10.20;2.20.130.20;2.60.120.1540;2.60.40.1930;2.60.40.1940;6.20.50.160;2.60.40.690;2.60.40.10; | Protease inhibitor I39 (alpha-2-macroglobulin) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16298998}. | null | null | null | null | null | FUNCTION: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which... | Homo sapiens (Human) |
A8K4G0 | CLM7_HUMAN | MWLPPALLLLSLSGCFSIQGPESVRAPEQGSLTVQCHYKQGWETYIKWWCRGVRWDTCKILIETRGSEQGEKSDRVSIKDNQKDRTFTVTMEGLRRDDADVYWCGIERRGPDLGTQVKVIVDPEGAASTTASSPTNSNMAVFIGSHKRNHYMLLVFVKVPILLILVTAILWLKGSQRVPEEPGEQPIYMNFSEPLTKDMAT | null | null | immune system process [GO:0002376] | plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; transmembrane signaling receptor activity [GO:0004888] | PF07686; | 2.60.40.10; | CD300 family | PTM: Phosphorylation on Tyr-188 by FYN is required for interaction with GRB2. {ECO:0000269|PubMed:16920917, ECO:0000269|PubMed:17928527}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Acts as an activating immune receptor through its interaction with ITAM-bearing adapter TYROBP, and also independently by recruitment of GRB2. {ECO:0000269|PubMed:16920917, ECO:0000269|PubMed:17928527}. | Homo sapiens (Human) |
A8K7I4 | CLCA1_HUMAN | MGPFKSSVFILILHLLEGALSNSLIQLNNNGYEGIVVAIDPNVPEDETLIQQIKDMVTQASLYLLEATGKRFYFKNVAILIPETWKTKADYVRPKLETYKNADVLVAESTPPGNDEPYTEQMGNCGEKGERIHLTPDFIAGKKLAEYGPQGRAFVHEWAHLRWGVFDEYNNDEKFYLSNGRIQAVRCSAGITGTNVVKKCQGGSCYTKRCTFNKVTGLYEKGCEFVLQSRQTEKASIMFAQHVDSIVEFCTEQNHNKEAPNKQNQKCNLRSTWEVIRDSEDFKKTTPMTTQPPNPTFSLLQIGQRIVCLVLDKSGSMATG... | 3.4.-.- | null | calcium ion transport [GO:0006816]; cellular response to hypoxia [GO:0071456]; monoatomic ion transmembrane transport [GO:0034220]; proteolysis [GO:0006508] | extracellular region [GO:0005576]; microvillus [GO:0005902]; plasma membrane [GO:0005886]; zymogen granule membrane [GO:0042589] | chloride channel activity [GO:0005254]; intracellular calcium activated chloride channel activity [GO:0005229]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF08434;PF13519; | 2.60.40.10;3.40.50.410; | CLCR family | PTM: Glycosylated. {ECO:0000269|PubMed:9828122}.; PTM: The 125-kDa product is autoproteolytically processed by the metalloprotease domain and yields to two cell-surface-associated subunits, a 90-kDa protein and a group of 37- to 41-kDa proteins. The cleavage is necessary for calcium-activated chloride channel (CaCC) ac... | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:15919655}. Cell membrane {ECO:0000269|PubMed:15919655}; Peripheral membrane protein {ECO:0000269|PubMed:15919655}; Extracellular side {ECO:0000269|PubMed:15919655}. Note=Protein that remains attached to the plasma membrane appeared to be predominan... | null | null | null | null | null | FUNCTION: May be involved in mediating calcium-activated chloride conductance. May play critical roles in goblet cell metaplasia, mucus hypersecretion, cystic fibrosis and AHR. May be involved in the regulation of mucus production and/or secretion by goblet cells. Involved in the regulation of tissue inflammation in th... | Homo sapiens (Human) |
A8K830 | OCAT2_HUMAN | MSEKPKVYQGVRVKITVKELLQQRRAHQAASGGTRSGGSSVHLSDPVAPSSAGLYFEPEPISSTPNYLQRGEFSSCVSCEENSSCLDQIFDSYLQTEMHPEPLLNSTQSAPHHFPDSFQATPFCFNQSLIPGSPSNSSILSGSLDYSYSPVQLPSYAPENYNSPASLDTRTCGYPPEDHSYQHLSSHAQYSCFSSATTSICYCASCEAEDLDALQAAEYFYPSTDCVDFAPSAAATSDFYKRETNCDICYS | null | null | null | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA binding [GO:0003677]; POU domain binding [GO:0070974]; transcription coactivator activity [GO:0003713] | null | null | POU2AF family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24154973}. Nucleus {ECO:0000269|PubMed:35576971}. | null | null | null | null | null | FUNCTION: Transcriptional coactivator that specifically associates with POU2F3 (PubMed:35576971). This complex drives the development of tuft cells, a rare a rare chemosensory cells that coordinate immune and neural functions within mucosal epithelial tissues (PubMed:35576971). {ECO:0000269|PubMed:35576971}. | Homo sapiens (Human) |
A8K8P3 | SFI1_HUMAN | MKNLLTEKCISSHNFHQKVIKQRMEKKVDSRYFKDGAVKKPYSAKTLSNKKSSASFGIRRELPSTSHLVQYRGTHTCTRQGRLRELRIRCVARKFLYLWIRMTFGRVFPSKARFYYEQRLLRKVFEEWKEEWWVFQHEWKLCVRADCHYRYYLYNLMFQTWKTYVRQQQEMRNKYIRAEVHDAKQKMRQAWKSWLIYVVVRRTKLQMQTTALEFRQRIILRVWWSTWRQRLGQVRVSRALHASALKHRALSLQVQAWSQWREQLLYVQKEKQKVVSAVKHHQHWQKRRFLKAWLEYLQVRRVKRQQNEMAERFHHVTVLQ... | null | null | null | centriole [GO:0005814]; cytosol [GO:0005829] | phosphatase binding [GO:0019902] | null | null | SFI1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:14504268, ECO:0000269|PubMed:16956364}. Note=Localized close to the centriole. | null | null | null | null | null | FUNCTION: Plays a role in the dynamic structure of centrosome-associated contractile fibers via its interaction with CETN2. {ECO:0000269|PubMed:16956364}. | Homo sapiens (Human) |
A8K8V0 | ZN785_HUMAN | MGPPLAPRPAHVPGEAGPRRTRESRPGAVSFADVAVYFSPEEWECLRPAQRALYRDVMRETFGHLGALGFSVPKPAFISWVEGEVEAWSPEAQDPDGESSAAFSRGQGQEAGSRDGNEEKERLKKCPKQKEVAHEVAVKEWWPSVACPEFCNPRQSPMNPWLKDTLTRRLPHSCPDCGRNFSYPSLLASHQRVHSGERPFSCGQCQARFSQRRYLLQHQFIHTGEKPYPCPDCGRRFRQRGSLAIHRRAHTGEKPYACSDCKSRFTYPYLLAIHQRKHTGEKPYSCPDCSLRFAYTSLLAIHRRIHTGEKPYPCPDCGRR... | null | null | regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF01352;PF00096; | 6.10.140.140;3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}. | Homo sapiens (Human) |
A8KBF3 | PIWL2_XENTR | MDPTRPPFRGSPFHTPLGVRPPVLETKEEGPHGRAVLLPRGRALLGASAPSSDTTQRDPSDSRNVLPALFRGMGIETKPSGIPGRGGPVFGRGFLSTMSSGDGPDQPLSEPSIRPSLSTRVQQASDFSTERVALGRARFPIPPVSMEKPHVPTGRGLLFPSVLPTLTSDPVPKESPIATLQIEKEEKWEPLPKKGSKGSPCQLGLNLIKINFQNEAVYQYHVTFTPIVECRSMRFGMMKDHRSVTGPVTAFDGSILYLPVKLAQTVELESERRTDGQKIKITIQMTKILDPSSDLCLPFYNVVMRRVFKILDLKLVGRNF... | 3.1.26.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9JMB7}; | cell differentiation [GO:0030154]; gamete generation [GO:0007276]; germ-line stem cell population maintenance [GO:0030718]; meiotic cell cycle [GO:0051321]; regulation of translation [GO:0006417]; regulatory ncRNA-mediated gene silencing [GO:0031047]; retrotransposon silencing by heterochromatin formation [GO:0141005];... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; P granule [GO:0043186]; PET complex [GO:1990923]; pi-body [GO:0071546] | metal ion binding [GO:0046872]; piRNA binding [GO:0034584]; RNA endonuclease activity [GO:0004521] | PF08699;PF02170;PF02171; | 3.40.50.2300;2.170.260.10;3.30.420.10; | Argonaute family, Piwi subfamily | PTM: Methylated on arginine residues; required for the interaction with Tudor domain-containing protein and subsequent localization to the meiotic nuage, also named P granule. {ECO:0000269|PubMed:19377467}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2CEI6}. Nucleus {ECO:0000250|UniProtKB:A2CEI6}. Note=Probable component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. {ECO:0000250|UniProtKB:Q8CDG1}. | null | null | null | null | null | FUNCTION: Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Plays an essential role in meiotic differentiation of spermatocytes, germ cell differentiation and in self-renewal of spermato... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A8KBH6 | KPCB_XENTR | MADPAACEPGEDTTTRFARKGALRQKNVHEVKEHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCETCMMNVHKRCVMNVPSLCGTDHTERRGRIHIKAEIREEVLTVTVGDARNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPTWNESFKFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELLKAGVDGWFKLLSQEEGEYFNVPVPPEGEEGNEELRQKFERAKIGPGTKAVEEKVVN... | 2.7.11.13 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P68403, ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000250|UniProtKB:P68403}; | adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; B cell activation [GO:0042113]; B cell receptor signaling pathway [GO:0050853]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; post-translati... | cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleus [GO:0005634] | ATP binding [GO:0005524]; chromatin binding [GO:0003682]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone binding [GO:0042393]; histone H3T6 kinase activity [GO:0035403]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coactivator activity [GO:0030374]; protein serine ki... | PF00130;PF00168;PF00069;PF00433; | 3.30.60.20;2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | PTM: Phosphorylation on Thr-497 within the activation loop renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-638 maintains catalytic competence, and autophosphorylation on Ser-657 appears to release the kinase into the cytosol (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. | 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=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Calcium-activated and phospholipid-dependent serine/threonine-protein kinase involved in various processes such as regulation of the B-cell receptor (BCR) signalosome, apoptosis and transcription regulation. Plays a key role in B-cell activation and function by regulating BCR-induced NF-kappa-B activation and... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A8MPH9 | FOSLD_DROME | MIALKATEMQHNNNALQQQQQLQHQLLQQHQQQHQQQLQQQLNSPDNNYIWATTHNANISRNNAMLQLQQQQLRAPWITDCNKQHHINNNNSMNVNYNQQLTQQPQQQQQQTQYMQHNYNNYTQQQQQQHLVPATTSQSNSHFYQCNQQQQQQQFLAPTTTTAAVVVAAAHQQHQTQQQHQSQQQQQHQRQDYASLQMGRQLGNFETGQSVLTLTTPTLTPTTTRNIEDTLGHLLSDTQTDRVAGCAGFAVPKVLPNAIDVLGMGIPTGVSSLPLQQTFDLSLGQGSESEDSNASYNDTQMNEEQDTTDTSSAHTDSTSY... | null | null | collateral sprouting of injured axon [GO:0048674]; compound eye development [GO:0048749]; dendrite morphogenesis [GO:0048813]; dorsal closure [GO:0007391]; embryo development ending in birth or egg hatching [GO:0009792]; follicle cell of egg chamber migration [GO:0007297]; germ cell development [GO:0007281]; imaginal d... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; transcription factor AP-1 complex [GO:0035976] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; protein heterodimerization activity [GO:0046982]; RNA polymerase II ... | PF00170; | 1.20.5.170; | BZIP family, Fos subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:2116361}. | null | null | null | null | null | FUNCTION: Developmentally regulated transcription factor AP-1 binds and recognizes the enhancer DNA sequence: 5'-TGA[CG]TCA-3'. May play a role in the function or determination of a particular subset of cells in the developing embryo. It is able to carry out its function either independently of or in conjunction with J... | Drosophila melanogaster (Fruit fly) |
A8MPR5 | FTSI2_ARATH | MACRFPLHSSSPSQFLSPENRQRLPRNYPSISCQNNSATNVVHEDGDDNDKAKTNQVNLLAIPITLTIISASLAKPSFAAAKVTERKRTQKKPQEALTLEQLKAWSKDLPVVSNRIPYTDILSLKAEGKLKHVIKPPNLSLRQKAEPVLVVLEDSRVLRTVLPSLEGNKRFWEQWDELGIDVQCVNAYTPPVKRPPVPSPYLGFLWKVPAYMLTWVKPKKESKRAAELKRMREDFKRQRKEEIETMKEERVMMEKTMKAQKKQQERKKRKAVRKKKYEESLREARKNYRDMADMWARLAQDPNVATALGLVFFYIFYRVV... | null | null | protein import into chloroplast stroma [GO:0045037]; proteolysis [GO:0006508] | chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast membrane [GO:0031969]; chloroplast thylakoid [GO:0009534]; Ycf2/FtsHi complex [GO:0062091] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent peptidase activity [GO:0004176]; chloroplast protein-transporting ATPase activity [GO:0016464]; metalloendopeptidase activity [GO:0004222] | PF00004;PF17862;PF01434; | 1.10.8.60;3.40.50.300;1.20.58.760; | AAA ATPase family; Peptidase M41 family | null | SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Required for plastid development during embryogenesis (PubMed:24964212). Might be involved in chaperone functions or play a structural role in the thylakoid FtsH complex (PubMed:12185496). {ECO:0000269|PubMed:24964212, ECO:0000303|PubMed:12185496}. | Arabidopsis thaliana (Mouse-ear cress) |
A8MPY1 | GBRR3_HUMAN | MVLAFQLVSFTYIWIILKPNVCAASNIKMTHQRCSSSMKQTCKQETRMKKDDSTKARPQKYEQLLHIEDNDFAMRPGFGGSPVPVGIDVHVESIDSISETNMDFTMTFYLRHYWKDERLSFPSTANKSMTFDHRLTRKIWVPDIFFVHSKRSFIHDTTMENIMLRVHPDGNVLLSLRITVSAMCFMDFSRFPLDTQNCSLELESYAYNEDDLMLYWKHGNKSLNTEEHMSLSQFFIEDFSASSGLAFYSSTGWYNRLFINFVLRRHVFFFVLQTYFPAILMVMLSWVSFWIDRRAVPARVSLGITTVLTMSTIITAVSAS... | null | null | chemical synaptic transmission [GO:0007268]; chloride transmembrane transport [GO:1902476]; gamma-aminobutyric acid signaling pathway [GO:0007214]; nervous system process [GO:0050877]; regulation of membrane potential [GO:0042391]; signal transduction [GO:0007165] | chloride channel complex [GO:0034707]; GABA-A receptor complex [GO:1902711]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | chloride channel activity [GO:0005254]; extracellular ligand-gated monoatomic ion channel activity [GO:0005230]; GABA-A receptor activity [GO:0004890]; neurotransmitter receptor activity [GO:0030594]; protein domain specific binding [GO:0019904] | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily, GABRR3 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein {ECO:0000255}. Cell membrane; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P50573}; | null | null | null | null | FUNCTION: Rho subunit of the pentameric ligand-gated chloride channels responsible for mediating the effects of gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the brain (By similarity). Rho-containing GABA-gated chloride channels are a subclass of GABA(A) receptors (GABAARs) entirely composed ... | Homo sapiens (Human) |
A8MQ03 | CRTP1_HUMAN | MDPQEMVVKNPYAHISIPRAHLRPDLGQQLEVASTCSSSSEMQPLPVGPCAPEPTHLLQPTEVPGPKGAKGNQGAAPIQNQQAWQQPGNPYSSSQRQAGLTYAGPPPAGRGDDIAHHCCCCPCCHCCHCPPFCRCHSCCCCVIS | null | null | biological process involved in interaction with symbiont [GO:0051702]; establishment of skin barrier [GO:0061436] | cornified envelope [GO:0001533]; extracellular exosome [GO:0070062] | identical protein binding [GO:0042802] | PF10631; | null | CYSRT1 family | null | SUBCELLULAR LOCATION: Cornified envelope {ECO:0000269|PubMed:36804407}. | null | null | null | null | null | FUNCTION: Component of the stratum corneum that may contribute to epidermal antimicrobial host defenses. {ECO:0000269|PubMed:36804407}. | Homo sapiens (Human) |
A8MQ27 | NEU1B_HUMAN | MGNTVHRTLPDPSPPARLLATRPCCGPGPERRPVLGEAPRFHAQAKGKNVRLDGHSRRATRRNSFCNGVTFTQRPIRLYEQVRLRLVAVRPGWSGALRFGFTAHDPSLMSAQDIPKYACPDLVTRPGYWAKALPENLALRDTVLAYWADRHGRVFYSVNDGEPVLFHCGVAVGGPLWALIDVYGITDEVQLLESAFADTLTPARLSQARFSACLPPSSHDAANFDNNELENNQVVAKLGHLALGRAPGPPPADAAAAAIPCGPRERPRPASSPALLEADLRFHATRGPDVSLSADRKVACAPRPDGGRTLVFSERPLRPG... | 2.3.2.27 | null | Notch signaling pathway [GO:0007219]; protein ubiquitination [GO:0016567]; ubiquitin-dependent endocytosis [GO:0070086] | actin cytoskeleton [GO:0015629]; cytosol [GO:0005829]; early endosome [GO:0005769] | metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630] | PF07177;PF13920; | 2.60.120.920;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19723503}. | 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 regulation of the Notch pathway through influencing the stability and activity of several Notch ligands. {ECO:0000269|PubMed:19723503}. | Homo sapiens (Human) |
A8MQA5 | ESF13_ARATH | MKSSHTTLICIIMLSLFALHECEKMEVKEIGRSSKIILPACMHETCSGGFSLKNDCWCCLRLKTKQARCWKEKEFPNAKELCFANCPPLE | null | null | embryonic axis specification [GO:0000578]; suspensor development [GO:0010098] | null | null | PF18209; | null | MEG family | null | null | null | null | null | null | null | FUNCTION: Maternally-contributed central cell peptide regulating suspensor development and correct auxin distribution in early developing embryos. {ECO:0000269|PubMed:24723605}. | Arabidopsis thaliana (Mouse-ear cress) |
A8MQL1 | TRF1B_ARATH | MAEAVDEDSGVGRSLEESSNGQHSQAGEALSEWRSSGQVENGTPSTSPSYWDIDDDDDYGLKPSELYGQYTWKIPKFSEITKREHRSNVFEAGGYKWYILIYPQGCDVCNHLSLFLCVANYDKLLPGSFAILEAGWSQFAQFTISVLSQDLKKSKFSDTLHRFWKKEHDWGWKKFMELPKLKDGFIDESGCLTIEAKVQVIRERVDRPFRCLDCGYRRELVRVYFQNVEQICRRFVEEKRSKLGRLIEDKARWTSFGVFWLGMDQNSRRRMCREKVDVILKGVVKHFFVEKEVSSTLVMDSLYSGLKALEGQTKNMKARS... | null | null | autophagosome organization [GO:1905037]; innate immune response [GO:0045087] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | null | PF00917; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26867179, ECO:0000269|PubMed:28351989}. Cell membrane {ECO:0000269|PubMed:26867179}; Peripheral membrane protein {ECO:0000305|PubMed:26867179}. Note=Predominantly expressed in the cytoplasm (PubMed:26867179, PubMed:28351989). Associates with starvation-induced autopha... | null | null | null | null | null | FUNCTION: Functions redundantly with TRAF1A in the regulation of plant immune response. Contributes to the turnover of the nucleotide-binding domain and leucine-rich repeat-containing (NB-LRR) immune receptors SNC1 and RPS2. May associate with an E3 ubiquitin-protein ligase complex, which modulates ubiquitination and s... | Arabidopsis thaliana (Mouse-ear cress) |
A8MQN2 | LNK1_ARATH | MSDLYIHELGDYLSDEFHGNDDGIVPDSAYEDGGQFPILVSNRKKRRNDDMGSGTNHLKSNTFIKREANMLGKNPWPEKDSGGSSVSRDTGTGKDVQDMTLEDTNTSDHGFNGGHVDVVENFSTGDPMLCDTSAATNDGVYNYSLNSIPDAENDLSFFDNGDKEKNDLFYGWGDIGNFEDVDNMLRSCDSTFGLDSLNNEGDLGWFSSAQPNEETAGAMTDDLKPDKMLENQRTAMLQVEDFLNNSEPNHAVEDEYGYTIEDDSAQGKSSQNVFDTSLQKKDILMLDVEANLEKKQTDHLHHLDGKSDGFSENSFTLQHS... | null | null | circadian regulation of gene expression [GO:0032922]; DNA-templated transcription elongation [GO:0006354]; entrainment of circadian clock [GO:0009649]; regulation of DNA-templated transcription [GO:0006355] | nucleus [GO:0005634] | RNA polymerase binding [GO:0070063]; transcription coregulator activity [GO:0003712] | null | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25012192}. | null | null | null | null | null | FUNCTION: Transcriptional coactivator necessary for expression of the clock genes PRR5 and TOC1 (PubMed:25012192, PubMed:25848708). Antagonizes REV8 function in the regulation of anthocyanin accumulation (PubMed:25848001). Involved in red light input to the clock (PubMed:25012192). Activates clock-controlled genes with... | Arabidopsis thaliana (Mouse-ear cress) |
A8MQY1 | NAC68_ARATH | MMKGLIGYRFSPTGEEVINHYLKNKLLGKYWLVDEAISEINILSHKPSKDLPKLARIQSEDLEWYFFSPIEYTNPNKMKMKRTTGSGFWKPTGVDREIRDKRGNGVVIGIKKTLVYHEGKSPHGVRTPWVMHEYHITCLPHHKRKYVVCQVKYKGEAAEISYEPSPSLVSDSHTVIAITGEPEPELQVEQPGKENLLGMSVDDLIEPMNQQEEPQGPHLAPNDDEFIRGLRHVDRGTVEYLFANEENMDGLSMNDLRIPMIVQQEDLSEWEGFNADTFFSDNNNNYNLNVHHQLTPYGDGYLNAFSGYNEGNPPDHELVM... | null | null | cytokinin-activated signaling pathway [GO:0009736]; leaf morphogenesis [GO:0009965]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of cell division [GO:0051302] | endoplasmic reticulum membrane [GO:0005789]; nuclear membrane [GO:0031965]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700] | PF02365; | 2.170.150.80; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17098812}; Single-pass membrane protein {ECO:0000269|PubMed:17098812}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:17098812}. Note=Localized primarily in plasma membrane or endoplasmic reticulum membrane as dormant form and, upon specific stress o... | null | null | null | null | null | FUNCTION: Transcription activator activated by proteolytic cleavage through regulated intramembrane proteolysis (RIP) mediated by calpain or its functional homolog. Regulates cytokinin signaling during cell division. {ECO:0000269|PubMed:17098812}. | Arabidopsis thaliana (Mouse-ear cress) |
A8MR65 | FHL_ARATH | MDDADKSCSPSLDHSDINDPMIVAVESLDTSKKRKLHAEESDLLPLPKHFCSEHQASLVNSSCPSSVIDYAECSYAMENTKTSDEASSSASFTGPSLYMFKDSIYSTGSSSSGYAATSSIEQCFSKVDHKTQEDTQDFTHMEFIYHDSEFAVEDLQEVLNPVESYILSSARWSVSNQDSKEATTKPTIDQEFEQYFSTLMM | null | null | maintenance of protein location in nucleus [GO:0051457]; positive regulation of DNA-templated transcription [GO:0045893]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]; response to blue light [GO:0009637]; response to far red light [GO:0010218] | cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | nuclear import signal receptor activity [GO:0061608]; protein homodimerization activity [GO:0042803] | null | null | FHY1 protein family | PTM: Inactivated by rapid reversible PHYA-mediated phosphorylation. {ECO:0000305|PubMed:19208901}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21884939}. Cytoplasm {ECO:0000269|PubMed:21884939}. Note=Shuttles from cytoplasm to nuclear bodies in FR but stay in the cytoplasm in other light conditions. {ECO:0000269|PubMed:21884939}. | null | null | null | null | null | FUNCTION: Can activate transcription (By similarity). Essential for light-regulated PHYA nuclear accumulation and subsequent PHYA phototropic signaling processes (PubMed:17566111, PubMed:21969386, PubMed:22374392). PHYA-specific signal transducer in response to continuous FR lights. Mediates the association of PHYA wit... | Arabidopsis thaliana (Mouse-ear cress) |
A8MR93 | ALG12_ARATH | MPTDSKMAKFLQSYGYDLILGSVAAIYVVMAPYTKVEESFNVQSMHDILYHRHHLDSYDHLEFPGVVPRTFIGAFIVSVFASPVVSIISCLGFPKVYSLVAARLVLGCIILSTLRFFRIQIKKKFGNQVETFFVLFTSLQFHFLFYCTRPLPNILALGLVNLAYGNWLKGNFYPALSFLIFATVIFRCDTMLLLGPIGLELLLTKSISFWKALKYCVGTALLAVGLTIFVDSIMWKKFVWPEFEVFWFNSILNRSSDWGTHSIHWYFTSALPRSLLVAYPLSLLGTLVDRRVPFFIVPVLSFVILYSKLPHKELRFIISS... | 2.4.1.260 | null | protein N-linked glycosylation [GO:0006487] | endoplasmic reticulum membrane [GO:0005789] | dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichol alpha-1,6-mannosyltransferase [GO:0052917] | PF03901; | null | Glycosyltransferase 22 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:20023196}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-a... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000305|PubMed:20023196}. | null | null | FUNCTION: Mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lum... | Arabidopsis thaliana (Mouse-ear cress) |
A8MRD9 | PDS5D_ARATH | MTAIVGFDQLSKALIDAGTNLLSPPSSTDDLLTLLDETESLLKNVEQDQPLSMQSALIPSRNALVSVDLLSHPDSDVRVSVVSCLTEIVRITAPETPYSDDLMKEIFRLTIEAFEKLADASSRSYKKAEFVLDNVAKVKSCLVMLDLECYDLILQMFRNFFKFIRSDHPQLVFSSMELIMIAIIDETEQVSTDLLDSLLATVKKENQNVSPMSWSLAEKVLSRCARKLKPYIIEALKSRGTSLDMYSPVVSSICQSVFNTPKVHSPVNTKEHEEKLDLGHSRKENLSKSSSKRPARHETRGINEKEKVRNGNKSSLLKQS... | null | null | cell division [GO:0051301]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; homologous recombination [GO:0035825]; mitotic sister chromatid cohesion [GO:0007064] | chromatin [GO:0000785]; nucleus [GO:0005634] | null | PF20168; | 2.30.30.140; | PDS5 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. | null | null | null | null | null | FUNCTION: Cohesin cofactor dispensable during the meiotic division but playing an important role in DNA repair by homologous recombination (HR) probably by helping SMC5/SMC6 complex (PubMed:26648949). Regulator of sister chromatid cohesion in mitosis which may stabilize cohesin complex association with chromatin (PubMe... | Arabidopsis thaliana (Mouse-ear cress) |
A8MRX0 | GSOX5_ARATH | MAPARTRVNSLNVAVIGAGAAGLVAARELRRENHTVVVFERDSKVGGLWVYTPNSEPDPLSLDPNRTIVHSSVYDSLRTNLPRECMGYRDFPFVPRPEDDESRDSRRYPSHREVLAYLEDFAREFKLVEMVRFKTEVVLVEPEDKKWRVQSKNSDGISKDEIFDAVVVCNGHYTEPRVAHVPGIDSWPGKQIHSHNYRVPDQFKDQVVVVIGNFASGADISRDITGVAKEVHIASRSNPSKTYSKLPGSNNLWLHSMIESVHEDGTIVFQNGKVVQADTIVHCTGYKYHFPFLNTNGYITVEDNCVGPLYEHVFPPALAP... | 1.14.13.237 | null | floral organ morphogenesis [GO:0048444]; glucosinolate biosynthetic process [GO:0019761]; regulation of hormone biosynthetic process [GO:0046885]; regulation of organ growth [GO:0046620] | null | 8-methylthiopropyl glucosinolate S-oxygenase activity [GO:0080107]; flavin adenine dinucleotide binding [GO:0050660]; monooxygenase activity [GO:0004497]; N,N-dimethylaniline monooxygenase activity [GO:0004499]; NADP binding [GO:0050661] | PF00743; | 3.50.50.60; | FMO family | null | null | CATALYTIC ACTIVITY: Reaction=a (Z)-omega-(methylsulfanyl)-N-sulfo-alkylhydroximate S-glucoside + H(+) + NADPH + O2 = a (Z)-omega-(methylsulfinyl)-alkyl-glucosinolate + H2O + NADP(+); Xref=Rhea:RHEA:42208, Rhea:RHEA-COMP:13194, Rhea:RHEA-COMP:13195, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Catalyzes the conversion of methylthioalkyl glucosinolates into methylsulfinylalkyl glucosinolates. Specific for 8-methylthiooctyl (8-MTO) glucosinolates. {ECO:0000269|PubMed:18799661}. | Arabidopsis thaliana (Mouse-ear cress) |
A8MS41 | CCR4D_ARATH | MFSSTTLHHLPRPNLLLPRKVISRRMSTNPAIEPKVRKFESVEGVDIGSRNKSDGFFAIPLYLSKLVALYNCISLSRIGTSNENFVFSGIRFRLVSYNILAQVYVKSALLPHSPPACLKWKARSHAILSVLKNLQADFFCLQEVDEYDSFYRNNMDSLGYSGIYIQRTGQRKRDGCAIFYKPSCAELVTKERIEYNDLVDSIKADSVSCSEQKIETSNEGKDSRKDSRDLNDPLVRLKRDCVGIMAAFRINKPFQHIVIVANTHLYWDPELADVKLAQAKYLLSRLAQFKTLISDEFECTPSLLLAGDFNSIPGDMVYSY... | 3.1.13.4 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:26619288}; | nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; regulation of circadian rhythm [GO:0042752]; rhythmic process [GO:0048511] | chloroplast [GO:0009507]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; poly(A)-specific ribonuclease activity [GO:0004535]; protein self-association [GO:0043621]; RNA binding [GO:0003723]; RNA exonuclease activity [GO:0004532] | PF03372; | 3.60.10.10; | CCR4/nocturin family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P31384}. Cytoplasm {ECO:0000269|PubMed:31093672}. | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; Evidence={ECO:0000269|PubMed:26619288}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:26619288}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25 degrees Celsius. {ECO:0000269|PubMed:26619288}; | FUNCTION: Acts as a catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover (By similarity). Transcriptional regulator of circadian rhythms with poly(A)-degrading activity that affects th... | Arabidopsis thaliana (Mouse-ear cress) |
A8MS68 | PLPD1_ARATH | MQSAMALSFSQTSFTRPNHVLGSSGSVFSTPRSLRFCGLRREAFGFSTSNQLAIRSNRIQFLSRKSFQVSASASSNGNGAPPKSFDYDLIIIGAGVGGHGAALHAVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSGRMRELQNEHHMKSFGLQVSAAGYDRQGVADHANNLATKIRNNLTNSMKAIGVDILTGFGSVLGPQKVKYGKDNIITAKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVPEWIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINPRKIDYHTGVFAS... | 1.8.1.4 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per subunit. {ECO:0000250}; | acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; response to arsenic-containing substance [GO:0046685] | chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; nucleolus [GO:0005730] | dihydrolipoyl dehydrogenase activity [GO:0004148]; flavin adenine dinucleotide binding [GO:0050660] | PF07992;PF02852; | 3.30.390.30;3.50.50.60; | Class-I pyridine nucleotide-disulfide oxidoreductase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:11056213}. | CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4; | null | null | null | null | FUNCTION: Lipoamide dehydrogenase is a component of the plastidial pyruvate dehydrogenase complex (PDC). {ECO:0000269|PubMed:11056213}. | Arabidopsis thaliana (Mouse-ear cress) |
A8MS85 | SPT61_ARATH | MARNAISDDEEDHELEDDDGEPVHGDPAEHDENDDEEDDDDVGNEYENDGFIVNDEDEEEEEEEDEERKDSDEERQKKKKKRKKKDEGLDEDDYLLLQDNNVKFKKRQYKRLKKAQREQGNGQGESSDDEFDSRGGTRRSAEDKIKDRLFDDVDVDDPPDDVGDEEDLVVEEDVVGSEDEMADFIVDEDDEHGPPKRGNSKKKKYRQGSDITAMRDANEIFGDVDELLTIRKKGLASNQRMERRLEDEFEPTVLSEKYMTGNDDEIRQLDIPERMQISEESTGSPPVDEISIEEESNWIYAQLASQLRESDGTFDGRGFS... | null | null | embryo development ending in seed dormancy [GO:0009793]; nucleosome organization [GO:0034728]; transcription elongation-coupled chromatin remodeling [GO:0140673] | plasmodesma [GO:0009506]; transcription elongation factor complex [GO:0008023] | histone binding [GO:0042393]; nucleosome binding [GO:0031491]; translation elongation factor activity [GO:0003746] | PF14635;PF17674;PF14633;PF14632;PF21710;PF14639; | 2.40.50.140;1.10.10.650;3.30.505.10;1.10.10.2740;1.10.150.850;1.10.3500.10;3.30.420.140; | SPT6 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Transcription elongation factor that enhances the transcription elongation by RNA polymerase II (RNAPII) (By similarity). Plays an important role in regulating embryo apical and basal patterning during early embryogenesis, partly through negative regulation of the transcription factors PHABULOSA and PHAVOLUTA... | Arabidopsis thaliana (Mouse-ear cress) |
A8MT69 | CENPX_HUMAN | MEGAGAGSGFRKELVSRLLHLHFKDDKTKVSGDALQLMVELLKVFVVEAAVRGVRQAQAEDALRVDVDQLEKVLPQLLLDF | null | null | cell division [GO:0051301]; chromosome segregation [GO:0007059]; interstrand cross-link repair [GO:0036297]; kinetochore assembly [GO:0051382]; positive regulation of protein ubiquitination [GO:0031398]; replication fork processing [GO:0031297]; resolution of meiotic recombination intermediates [GO:0000712] | chromatin [GO:0000785]; cytosol [GO:0005829]; FANCM-MHF complex [GO:0071821]; Fanconi anaemia nuclear complex [GO:0043240]; inner kinetochore [GO:0000939]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677] | PF09415; | 1.20.5.4980;6.10.130.30; | CENP-X/MHF2 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:24522885}. Chromosome, centromere {ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:24522885}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:24522885}. Note=Assembly of CENPS and CENPX and its partner su... | null | null | null | null | null | FUNCTION: DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage (PubMed:20347428, Pub... | Homo sapiens (Human) |
A8MTA8 | CMI2B_HUMAN | MAVASTFIPGLNPQNPHYIPGYTGHCPLLRFSVGQTYGQVTGQLLRGPPGLAWPPVHRTLLPPIRPPRSPEVPRESLPVRRGQERLSSSMIPGYTGFVPRAQFIFAKNCSQVWAEALSDFTHLHEKQGSEELPKEAKGRKDTEKDQVPEPEGQLEEPTLEVVEQASPYSMDDRDPRKFFMSGFTGYVPCARFLFGSSFPVLTNQALQEFGQKHSPGSAQDPKHLPPLPRTYPQNLGLLPNYGGYVPGYKFQFGHTFGHLTHDALGLSTFQKQLLA | null | null | null | axonemal microtubule [GO:0005879] | null | PF10629; | null | CIMIP2 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:36191189}. | null | null | null | null | null | FUNCTION: Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating. {ECO:0000269|PubMed:36191189}. | Homo sapiens (Human) |
A8MTJ3 | GNAT3_HUMAN | MGSGISSESKESAKRSKELEKKLQEDAERDARTVKLLLLGAGESGKSTIVKQMKIIHKNGYSEQECMEFKAVIYSNTLQSILAIVKAMTTLGIDYVNPRSAEDQRQLYAMANTLEDGGMTPQLAEVIKRLWRDPGIQACFERASEYQLNDSAAYYLNDLDRITASGYVPNEQDVLHSRVKTTGIIETQFSFKDLHFRMFDVGGQRSERKKWIHCFEGVTCIIFCAALSAYDMVLVEDEEVNRMHESLHLFNSICNHKYFSTTSIVLFLNKKDIFQEKVTKVHLSICFPEYTGPNTFEDAGNYIKNQFLDLNLKKEDKEIY... | null | null | adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; detection of chemical stimulus involved in sensory perception of bitter taste [GO:0001580]; response to nicotine [GO:0035094]; sensory perception of sweet taste [GO:0050916]; sensory perception of umami taste [GO:0050917] | acrosomal vesicle [GO:0001669]; apical plasma membrane [GO:0016324]; axoneme [GO:0005930]; cytoplasm [GO:0005737]; heterotrimeric G-protein complex [GO:0005834]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | G protein-coupled receptor binding [GO:0001664]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872] | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family, G(i/o/t/z) subfamily | PTM: Potential N-myristoylation may anchor alpha-subunit to the inner surface of plasma membrane. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8015379}. Note=Dual distribution pattern; plasmalemmal pattern with apical region localization and cytosolic pattern with localization throughout the cytoplasm. | null | null | null | null | null | FUNCTION: Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction. Transduction by this alpha subunit involves coupling of specific cell-... | Homo sapiens (Human) |
A8MTJ6 | FOXI3_HUMAN | MALYCGDNFGVYSQPGLPPPAATAAAPGAPPAARAPYGLADYAAPPAAAANPYLWLNGPGVGGPPSAAAAAAAAYLGAPPPPPPPGAAAGPFLQPPPAAGTFGCSQRPFAQPAPAAPASPAAPAGPGELGWLSMASREDLMKMVRPPYSYSALIAMAIQSAPERKLTLSHIYQFVADSFPFYQRSKAGWQNSIRHNLSLNDCFKKVPRDEDDPGKGNYWTLDPNCEKMFDNGNFRRKRKRRSEASNGSTVAAGTSKSEEGLSSGLGSGVGGKPEEESPSTLLRPSHSPEPPEGTKSTASSPGGPMLTSTPCLNTFFSSLS... | null | null | anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; epidermal cell fate specification [GO:0009957]; hair follicle development [GO:0001942]; odontogenesis of dentin-containing tooth [GO:0042475]; otic placode development [GO:1905040]; parathyroid gland development [GO:0060017]; pharyngeal... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00250; | 1.10.10.10; | null | PTM: Phosphorylation promotes the transcription factor activity. Dephosphorylation by protein phosphatase 2A (PP2A) reduces its activity. {ECO:0000250|UniProtKB:D3Z120}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:37041148}. | null | null | null | null | null | FUNCTION: Transcription factor required for pharyngeal arch development, which is involved in hair, ear, jaw and dental development (PubMed:37041148). May act as a pioneer transcription factor during pharyngeal arch development (By similarity). Required for epithelial cell differentiation within the epidermis (By simil... | Homo sapiens (Human) |
A8MTQ0 | NOTO_HUMAN | MPSPRPRGSPPPAPSGSRVRPPRSGRSPAPRSPTGPNTPRAPGRFESPFSVEAILARPDPCAPAASQPSGSACVHPAFWTAASLCATGGLPWACPTSWLPAYLSVGFYPVPGPRVAPVCGLLGFGVTGLELAHCSGLWAFPDWAPTEDLQDTERQQKRVRTMFNLEQLEELEKVFAKQHNLVGKKRAQLAARLKLTENQVRVWFQNRRVKYQKQQKLRAAVTSAEAASLDEPSSSSIASIQSDDAESGVDG | null | null | brain development [GO:0007420]; central nervous system development [GO:0007417]; dorsal/ventral pattern formation [GO:0009953]; embryonic pattern specification [GO:0009880]; heart looping [GO:0001947]; motile cilium assembly [GO:0044458]; neuron differentiation [GO:0030182]; notochord development [GO:0030903]; regulati... | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00046; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. | null | null | null | null | null | FUNCTION: Transcription regulator acting downstream of both FOXA2 and Brachyury (T) during notochord development. Required for node morphogenesis. Is essential for cilia formation in the posterior notochord (PNC) and for left-right patterning; acts upstream of FOXJ1 and RFX3 in this process and is required for the expr... | Homo sapiens (Human) |
A8MTZ0 | BBIP1_HUMAN | MLKAAAKRPELSGKNTISNNSDMAEVKSMFREVLPKQGPLFVEDIMTMVLCKPKLLPLKSLTLEKLEKMHQAAQNTIRQQEMAEKDQRQITH | null | null | cilium assembly [GO:0060271]; eating behavior [GO:0042755]; protein transport [GO:0015031]; receptor localization to non-motile cilium [GO:0097500] | BBSome [GO:0034464]; ciliary membrane [GO:0060170]; cytoplasm [GO:0005737]; cytosol [GO:0005829] | null | PF14777; | null | BBIP10 family | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|Ref.4}. Cytoplasm {ECO:0000269|Ref.4}. Note=Localizes inside the primary cilium but not at centriolar satellites. | null | null | null | null | null | FUNCTION: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange f... | Homo sapiens (Human) |
A8MU46 | SMTL1_HUMAN | MEQKEGKLSEDGTTVSPAADNPEMSGGGAPAEETKGTAGKAINEGPPTESGKQEKAPAEDGMSAELQGEANGLDEVKVESQREAGGKEDAEAELKKEDGEKEETTVGSQEMTGRKEETKSEPKEAEEKESTLASEKQKAEEKEAKPESGQKADANDRDKPEPKATVEEEDAKTASQEETGQRKECSTEPKEKATDEEAKAESQKAVVEDEAKAEPKEPDGKEEAKHGAKEEADAKEEAEDAEEAEPGSPSEEQEQDVEKEPEGGAGVIPSSPEEWPESPTGEGHNLSTDGLGPDCVASGQTSPSASESSPSDVPQSPPES... | null | null | actin cytoskeleton organization [GO:0030036]; muscle organ morphogenesis [GO:0048644]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of vasoconstriction [GO:0045907]; response to activity [GO:0014823]; response to xenobiotic stimulus [GO:0009410]; vasoconstriction [GO:0042310] | contractile fiber [GO:0043292]; cytoplasm [GO:0005737]; filamentous actin [GO:0031941]; I band [GO:0031674]; M band [GO:0031430]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634] | calmodulin binding [GO:0005516]; CH domain binding [GO:0051401]; disordered domain specific binding [GO:0097718]; protein phosphatase 1 binding [GO:0008157]; protein self-association [GO:0043621]; tropomyosin binding [GO:0005523] | PF00307; | 1.10.418.10; | Smoothelin family | PTM: Maximal phosphorylation of Ser-336 correlates with maximal relaxation of aorta in response to acetylcholine. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, myofibril {ECO:0000269|PubMed:18310078}. Cytoplasm, myofibril, sarcomere, I band {ECO:0000250}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250}. Nucleus {ECO:0000250}. Note=Colocalizes with MYH2. In its unphosphorylated state, localizes to the cytoplasm (By similarity). Phosphoryl... | null | null | null | null | null | FUNCTION: Plays a role in the regulation of contractile properties of both striated and smooth muscles. When unphosphorylated, may inhibit myosin dephosphorylation. Phosphorylation at Ser-299 reduces this inhibitory activity (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
A8MUP2 | CSKMT_HUMAN | MAALRRMLHLPSLMMGTCRPFAGSLADSCLADRCLWDRLHAQPRLGTVPTFDWFFGYDEVQGLLLPLLQEAQAASPLRVLDVGCGTSSLCTGLYTKSPHPVDVLGVDFSPVAVAHMNSLLEGGPGQTPLCPGHPASSLHFMHADAQNLGAVASSGSFQLLLDKGTWDAVARGGLPRAYQLLSECLRVLNPQGTLIQFSDEDPDVRLPCLEQGSYGWTVTVQELGPFRGITYFAYLIQGSH | 2.1.1.- | null | peptidyl-lysine dimethylation [GO:0018027]; peptidyl-lysine monomethylation [GO:0018026]; peptidyl-lysine trimethylation [GO:0018023]; protein methylation [GO:0006479] | mitochondrion [GO:0005739] | lysine N-methyltransferase activity [GO:0016278]; protein-lysine N-methyltransferase activity [GO:0016279] | PF13847; | 3.40.50.150; | Methyltransferase superfamily | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25023281, ECO:0000269|PubMed:28887308}. | CATALYTIC ACTIVITY: Reaction=L-lysyl-[citrate synthase] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[citrate synthase] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:55544, Rhea:RHEA-COMP:14212, Rhea:RHEA-COMP:14213, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; ... | null | null | null | null | FUNCTION: Protein-lysine methyltransferase that selectively trimethylates citrate synthase (CS) in mitochondria (PubMed:28391595, PubMed:28887308). Seems to conduct trimethylation in a highly distributive manner rather than in a processive manner, and thus introduces a single methyl group per binding event (PubMed:2888... | Homo sapiens (Human) |
A8MV65 | VGLL3_HUMAN | MSCAEVMYHPQPYGASQYLPNPMAATTCPTAYYQPAPQPGQQKKLAVFSKMQDSLEVTLPSKQEEEDEEEEEEEKDQPAEMEYLNSRCVLFTYFQGDIGSVVDEHFSRALGQAITLHPESAISKSKMGLTPLWRDSSALSSQRNSFPTSFWTSSYQPPPAPCLGGVHPDFQVTGPPGTFSAADPSPWPGHNLHQTGPAPPPAVSESWPYPLTSQVSPSYSHMHDVYMRHHHPHAHMHHRHRHHHHHHHPPAGSALDPSYGPLLMPSVHAARIPAPQCDITKTEPTTVTSATSAWAGAFHGTVDIVPSVGFDTGLQHQDKS... | null | null | regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | null | PF07545; | null | Vestigial family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N8G2}. | null | null | null | null | null | FUNCTION: May act as a specific coactivator for the mammalian TEFs. {ECO:0000250|UniProtKB:Q8N8G2}. | Homo sapiens (Human) |
A8MVW5 | HECA2_HUMAN | MGQDAFMEPFGDTLGVFQCKIYLLLFGACSGLKVTVPSHTVHGVRGQALYLPVHYGFHTPASDIQIIWLFERPHTMPKYLLGSVNKSVVPDLEYQHKFTMMPPNASLLINPLQFPDEGNYIVKVNIQGNGTLSASQKIQVTVDDPVTKPVVQIHPPSGAVEYVGNMTLTCHVEGGTRLAYQWLKNGRPVHTSSTYSFSPQNNTLHIAPVTKEDIGNYSCLVRNPVSEMESDIIMPIIYYGPYGLQVNSDKGLKVGEVFTVDLGEAILFDCSADSHPPNTYSWIRRTDNTTYIIKHGPRLEVASEKVAQKTMDYVCCAYNN... | null | null | cell division [GO:0051301]; centrosome cycle [GO:0007098] | centrosome [GO:0005813]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; spindle [GO:0005819] | null | PF13927; | 2.60.40.10; | null | PTM: Poly-ADP-ribosylated (PARsylated) by tankyrase TNKS during late G2 and prophase, leading to translocation to mitotic centrosomes.; PTM: N-glycosylated. {ECO:0000269|PubMed:19358830, ECO:0000269|PubMed:22864114}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:19358830, ECO:0000269|PubMed:22864114}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19358830, ECO:0000269|PubMed:22864114}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {E... | null | null | null | null | null | FUNCTION: Required during prometaphase for centrosome maturation. Following poly-ADP-ribosylation (PARsylation) by TNKS, translocates from the Golgi apparatus to mitotic centrosomes and plays a key role in the formation of robust microtubules for prompt movement of chromosomes: anchors AKAP9/CG-NAP, a scaffold protein ... | Homo sapiens (Human) |
A8MW92 | P20L1_HUMAN | MSKKPPNRPGITFEIGARLEALDYLQKWYPSRIEKIDYEEGKMLVHFERWSHRYDEWIYWDSNRLRPLERPALRKEGLKDEEDFFDFKAGEEVLARWTDCRYYPAKIEAINKEGTFTVQFYDGVIRCLKRMHIKAMPEDAKGQVKSQHPLSWCCPIDPAGSCNQSMGSEDWIALVKAAAAAAAKNKTGSKPRTSANSNKDKDKDERKWFKVPSKKEETSTCIATPDVEKKEDLPTSSETFGLHVENVPKMVFPQPESTLSNKRKNNQGNSFQAKRARLNKITGLLASKAVGVDGAEKKEDYNETAPMLEQAISPKPQSQK... | null | null | negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of protein catabolic process [GO:0042177]; regulation of transcription by RNA polymerase II [GO:0006357] | NSL complex [GO:0044545]; nucleoplasm [GO:0005654] | metal ion binding [GO:0046872]; methylation-dependent protein binding [GO:0140034] | PF16660;PF20826;PF18104; | 2.30.30.140;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24492612}. Note=Localized to the perinucleolar region. {ECO:0000269|PubMed:24492612}. | null | null | null | null | null | FUNCTION: Is a negative regulator of proteasomal degradation of a set of methylated proteins, including DNMT1 and SOX2 (PubMed:24492612, PubMed:29358331). Involved in the maintainance of embryonic stem cells pluripotency, through the regulation of SOX2 levels (By similarity). {ECO:0000250|UniProtKB:Q8CCJ9, ECO:0000269|... | Homo sapiens (Human) |
A8MW95 | BECN2_HUMAN | MSSIRFLCQRCHQALKLSGSSESRSLPAAPAPTSGQAEPGDTREPGVTTREVTDAEEQQDGASSRSPPGDGSVSKGHANIFTLLGELGAMHMLSSIQKAAGDIFDIVSGQAVVDHPLCEECTDSLLEQLDIQLALTEADSQNYQRCLETGELATSEDEAAALRAELRDLELEEARLVQELEDVDRNNARAAADLQAAQAEAAELDQQERQHYRDYSALKRQQLELLDQLGNVENQLQYARVQRDRLKEINCFTATFEIWVEGPLGVINNFRLGRLPTVRVGWNEINTAWGQAALLLLTLANTIGLQFQRYRLIPCGNHSY... | null | null | autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cellular response to nitrogen starvation [GO:0006995]; endosome to lysosome transport [GO:0008333]; G protein-coupled receptor catabolic process [GO:1990172]; late endosome to vacuole transport [GO:0045324]; mitophagy [GO:0000423] | phagophore assembly site [GO:0000407]; phosphatidylinositol 3-kinase complex, class III, type I [GO:0034271]; phosphatidylinositol 3-kinase complex, class III, type II [GO:0034272] | phosphatidylinositol 3-kinase binding [GO:0043548]; protein-macromolecule adaptor activity [GO:0030674] | PF04111;PF17675; | 6.10.250.3110;1.10.418.40; | Beclin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Involved in 2 distinct lysosomal degradation pathways: acts as a regulator of autophagy and as a regulator of G-protein coupled receptors turnover. Regulates degradation in lysosomes of a variety of G-protein coupled receptors via its interaction with GPRASP1/GASP1. {ECO:0000269|PubMed:23954414}. | Homo sapiens (Human) |
A8MW99 | MEI4_HUMAN | MDVQKWYLRTSKLALALAIIRSKPADKSSREYTEHLAMLLSEEQSKWRSKVEILEAEVMQLRQKLLVSRLCSGSFKSGYVSSQLEAQEPKSSESTLTSMEDSGCDLSNEQRTESSDLSQHFVESCTPTHFPPLPLVKRPCAILQNPLSSHMQFLQYLLELKNLTESGNLKRDLTHFEKDSSTVSDSVFQLLDGLITFYRNPKLPFSRFWTEAVGTLASLISDYNLSSHILKKCSKKLEEFEKTLLHAILGNNHINQFQVQHYVSQSLVTLGNCSLLRKSIISLLLSEVNGFADDLGAINQEQASYDVSRYENIFYLFWVL... | null | null | DNA recombination [GO:0006310]; homologous chromosome pairing at meiosis [GO:0007129]; meiotic DNA double-strand break formation [GO:0042138]; oogenesis [GO:0048477]; spermatogenesis [GO:0007283] | chromosome [GO:0005694]; lateral element [GO:0000800] | null | PF13971; | null | MEI4L family | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q8BRM6}. Note=Specifically localizes to unsynapsed chromosomal regions during meiosis. Located in discrete foci on the axes of meiotic chromosomes. The number of foci is highest at leptonema, decreases at zygonema and is strongly reduced in pachynema and subsequen... | null | null | null | null | null | FUNCTION: Required for DNA double-strand breaks (DSBs) formation in unsynapsed regions during meiotic recombination. Probably acts by forming a complex with IHO1 and REC114, which activates DSBs formation in unsynapsed regions, an essential step to ensure completion of synapsis. {ECO:0000250|UniProtKB:Q8BRM6}. | Homo sapiens (Human) |
A8MXD5 | GRCR1_HUMAN | MLKREMKPESDRPRKVRFRIASSHSGRVLKEVYEDGQPSGSLDSECASICGIDGLGDSDGQQNGHIESEGDENENDQDSLLVLARAASEKGFGTRRVNILSKNGTVRGVKYKVSAGQALFNNLTKVLQQPSTDLEFDRVVIYTTCLRVVRTTFERCELVRKIFQNHRVKFEEKNIALNGEYGKELDERCRRVSEAPSLPVVFIDGHYLGGAEKILSMNESGELQDILTKIERVQHPHECPSCGGFGFLPCSVCHGSKMSMFRNCFTDSFKALKCTACNENGLQRCKNCAG | null | null | cochlea development [GO:0090102]; inner ear auditory receptor cell differentiation [GO:0042491]; inner ear receptor cell development [GO:0060119]; inner ear receptor cell stereocilium organization [GO:0060122]; sensory perception of sound [GO:0007605]; vestibular receptor cell development [GO:0060118] | kinocilium [GO:0060091]; microvillus [GO:0005902]; stereocilium [GO:0032420] | null | PF00462; | 3.40.30.10; | GRXCR1 family | null | SUBCELLULAR LOCATION: Cell projection, stereocilium {ECO:0000250}. Cell projection, microvillus {ECO:0000250}. Cell projection, kinocilium {ECO:0000250}. Note=In the inner ear, localized to stereocilia, apical microvilli of sensory cells and kinocilia. {ECO:0000250}. | null | null | null | null | null | FUNCTION: May play a role in actin filament architecture in developing stereocilia of sensory cells. {ECO:0000250}. | Homo sapiens (Human) |
A8MXV4 | NUD19_HUMAN | MSSSLRPGPSRWRRAASIVLAAGWSRPETATPPSRPPPAEGFRLLLLQRSPHQGFMPGAHVFSGGVLDAADRSADWLGLFAPHHGPPRFGLGPAPFSRTAFPSLPDTDDHKTDNTGTLPEDVAFRICAVREAFEEAGVLLLRPRTSPPGPAPGPGLALEPPPGLASWRDRVRQDPRHFLRLCAHLDCTPDIWALHNWSAWLTPFLRGTTRRFDTAFFLCCLREPPPVYPDLAEVVGYQWSSPSEATESFLSKEIWLPPPQFYEVRRLANFASLSDLHKFCLGRALEGLERWLPIILLTADGMVHLLPGDELYLEDSDFLE... | 3.6.1.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P11930}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P11930}; | butyryl-CoA catabolic process [GO:0044580]; coenzyme A catabolic process [GO:0015938]; fatty acid catabolic process [GO:0009062]; malonyl-CoA catabolic process [GO:2001294]; medium-chain fatty-acyl-CoA catabolic process [GO:0036114]; propionyl-CoA metabolic process [GO:1902858]; succinyl-CoA catabolic process [GO:19012... | cytosol [GO:0005829]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782] | coenzyme A diphosphatase activity [GO:0010945]; magnesium ion binding [GO:0000287] | null | 3.90.79.10; | Nudix hydrolase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:P11930}. | CATALYTIC ACTIVITY: Reaction=an acyl-CoA + H2O = adenosine 3',5'-bisphosphate + an acyl-4'-phosphopantetheine + 2 H(+); Xref=Rhea:RHEA:50044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58342, ChEBI:CHEBI:58343, ChEBI:CHEBI:132023; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xre... | null | null | null | null | FUNCTION: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (By similarity). Mediates the hydrolysis of a wide range of CoA esters, including choloyl-CoA and branched-chain fatty-acyl-CoA esters and at low substrate concentratio... | Homo sapiens (Human) |
A8MYU2 | KCNU1_HUMAN | MFQTKLRNETWEDLPKMSCTTEIQAAFILSSFVTFFSGLIILLIFRLIWRSVKKWQIIKGTGIILELFTSGTIARSHVRSLHFQGQFRDHIEMLLSAQTFVGQVLVILVFVLSIGSLIIYFINSADPVGSCSSYEDKTIPIDLVFNAFFSFYFGLRFMAADDKIKFWLEMNSIVDIFTIPPTFISYYLKSNWLGLRFLRALRLLELPQILQILRAIKTSNSVKFSKLLSIILSTWFTAAGFIHLVENSGDPWLKGRNSQNISYFESIYLVMATTSTVGFGDVVAKTSLGRTFIMFFTLGSLILFANYIPEMVELFANKRK... | null | null | potassium ion transmembrane transport [GO:0071805]; reproductive process [GO:0022414] | membrane [GO:0016020]; monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211] | potassium channel activity [GO:0005267] | PF03493;PF00520;PF21014; | 1.10.287.70;3.40.50.720; | Potassium channel family, Calcium-activated (TC 1.A.1.3) subfamily, KCa5.1/KCNU1 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O54982}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O54982}. | null | null | null | null | null | FUNCTION: Testis-specific potassium channel activated by both intracellular pH and membrane voltage that mediates export of K(+). May represent the primary spermatozoan K(+) current. In contrast to KCNMA1/SLO1, it is not activated by Ca(2+) or Mg(2+). Critical for fertility. May play an important role in sperm osmoregu... | Homo sapiens (Human) |
A8MZ59 | LEUTX_HUMAN | MFEGPRRYRRPRTRFLSKQLTALRELLEKTMHPSLATMGKLASKLQLDLSVVKIWFKNQRAKWKRQQRQQMQTRPSLGPANQTTSVKKEETPSAITTANIRPVSPGISDANDHDLREPSGIKNPGGASASARVSSWDSQSYDIEQICLGASNPPWASTLFEIDEFVKIYDLPGEDDTSSLNQYLFPVCLEYDQLQSSV | null | null | regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046; | 1.10.10.60; | Paired homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27578796}. | null | null | null | null | null | FUNCTION: [Isoform 1]: Paired-like homeobox transcription factor involved in embryogenesis (PubMed:27578796, PubMed:30479355). May act as a regulator of embryo genome activation (PubMed:27578796). Binds to a 36 bp DNA elements containing a 5'-TAATCC-3' sequence motif, referred to as EEA motif (EGA-enriched Alu-motif), ... | Homo sapiens (Human) |
A8NCG7 | LP9_COPC7 | MKSFASLLFLAATAAAHATWQQIWVNGVDGGTSCLRRAANNNPIDVGAKELACNAHTLSPNVCTIKPGDKVTVEMHAQHGDRSCAQEAIGGNHYGPVMVYMAKVDDARTADANAADWFKVSEMGMASNNPVYWAVQVLNDNCGHWTFTVPDLAPGNYLIRSEVIALHVAGSIGGAQFYPGCFQVNVVGNGSGRPTETVKFPGAYKATDPGVLFDMYRPQSTYIIPGPRPYGTSPATVANTPYPTTATWNTALQPTTVPTVTPPVGGGTNPPPVTTVAPPVVTSQPPVPPTTQQPPVVTPTAPPSGPLQTQYGQCGGQGWN... | 3.2.1.4 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q4WP32}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q4WP32}; | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulase activity [GO:0008810]; cellulose binding [GO:0030248]; metal ion binding [GO:0046872] | PF03443;PF00734; | 2.70.50.70; | Polysaccharide monooxygenase AA9 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:37463979}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; Evidence={ECO:0000269|PubMed:37463979}; | null | null | null | null | FUNCTION: Lytic polysaccharide monooxygenase (LMPO) that depolymerizes crystalline and amorphous polysaccharides via the oxidation of scissile alpha- or beta-(1-4)-glycosidic bonds, yielding C1 oxidation products (PubMed:37463979). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I)... | Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003) (Inky cap fungus) (Hormographiella aspergillata) |
A8NMB4 | ARO1_COPC7 | MAVADDTKADLLKVSILGKESIHCGFHLTPYIVQTVLTTLPSSTYVLITDDNIAKLHLNKFEEAFAKGIEKSAANPKPRFLSHVIPPGETSKSREGKARIEDFLLFHKCTRDSVILALGGGVIGDLVGFVAATFMRGVRFCQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPEYIFIDAAYLETLPTREFSNGMAEVVKTAAIWDEKEFTSLESRSAELFAAIQTPSTNYAGRTLETRSEAQKLLLSTIAASIGVKAHIVTIDERETGLRNLVNFGHSIGHAIEAVLTPTILHGECVSIGMILEAELSRQLGILTQ... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF18317;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003) (Inky cap fungus) (Hormographiella aspergillata) |
A8NS89 | GOB1_BRUMA | MTETVTDQGKQRSSKLQKNEAAKDEQVEGKGKETLESGTDKSAEQNSSLLVGQPDVIDNDNVQTVDDFKNLMYKMQETRRAIVFALLNEKDLTKDDVEILKRAYEKLTDNQTHSFQREMCTLTTKLSVNIGDETRGLEKDLKYLDALMNIRREEPNLLWPIIMSRVDLFSILANYHPKGKETFLKEYEDTVKFLKTFISSEAITGKKPIFITDWDGTMKDYCSQYATNLQPVYSAVGMTRFAASFTRISAVLTAGPLRGPGILDLTAMPIDGPVMFSGSWGREWWLSGKRVVHQDGITDEGFNALQRLDDEMKDLLHTSD... | 3.1.3.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24992307}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:24992307}; | carbohydrate derivative catabolic process [GO:1901136]; dephosphorylation [GO:0016311]; trehalose biosynthetic process [GO:0005992] | null | magnesium ion binding [GO:0000287]; trehalose-phosphatase activity [GO:0004805] | PF21141;PF18572; | 1.20.58.1800;3.30.70.3080;3.40.50.1000; | Gob-1 trehalose phosphatase family | null | null | CATALYTIC ACTIVITY: Reaction=alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate; Xref=Rhea:RHEA:23420, ChEBI:CHEBI:15377, ChEBI:CHEBI:16551, ChEBI:CHEBI:43474, ChEBI:CHEBI:58429; EC=3.1.3.12; Evidence={ECO:0000269|PubMed:24992307}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=360 uM for trehalose 6-phosphate {ECO:0000269|PubMed:24992307}; Note=kcat is 24 sec(-1) for trehalose 6-phosphate. {ECO:0000269|PubMed:24992307}; | null | null | null | FUNCTION: Catalyzes the hydrolysis of trehalose 6-phosphate to trehalose and phosphate; prevents the accumulation of toxic levels of trehalose 6-phosphate. {ECO:0000269|PubMed:24992307}. | Brugia malayi (Filarial nematode worm) |
A8PUY1 | LIP1_MALGO | MLFSRFVLLAFGSVAAVSASSIYARGRGGSSTDQPVANPYNTKEISLAAGLVQQTYCDSTENGLKIGDSELLYTMGEGYARQRVNIYHSPSLGIAVAIEGTNLFSLNSDLHDAKFWQEDPNERYIQYYPKGTKLMHGFQQAYNDLMDDIFTAVKKYKKEKNEKRVTVIGHSLGAAMGLLCAMDIELRMDGGLYKTYLFGLPRLGNPTFASFVDQKIGDKFHSIINGRDWVPTVPPRALGYQHPSDYVWIYPGNSTSAKLYPGQENVHGILTVAREFNFDDHQGIYFHTQIGAVMGECPAQVGAH | 3.1.1.- | null | lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | hydrolase activity [GO:0016787]; metal ion binding [GO:0046872] | PF01764; | 3.40.50.1820; | AB hydrolase superfamily, Lipase family, Class 3 subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18000048}. Secreted, cell wall {ECO:0000269|PubMed:18000048}. | CATALYTIC ACTIVITY: Reaction=a monoacylglycerol + H2O = a fatty acid + glycerol + H(+); Xref=Rhea:RHEA:15245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17408, ChEBI:CHEBI:17754, ChEBI:CHEBI:28868; Evidence={ECO:0000269|PubMed:17460728, ECO:0000269|PubMed:24556587, ECO:0000269|PubMed:25837472, ECO:0000269|PubMed... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0. {ECO:0000269|PubMed:24556587}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25 degrees Celsius. {ECO:0000269|PubMed:24556587}; | FUNCTION: Secreted lipase involved in Dandruff and seborrheic dermatitis (D/SD) probably via lipase-mediated breakdown of sebaceous lipids and release of irritating free fatty acids (PubMed:17460728, PubMed:18000048). Shows activity against monoglyceride and diglyceride substrates, but not triglyceride substrates and d... | Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated fungus) |
A8QCB2 | ARO1_MALGO | MSQVSGGKVPSYHAPPFDSPLSGATIHELRCLDTKVQLGFHLVPHIAKTLITELPSSAYVLVTDTNLAKLGAIDKFRKAFEAIPGARLLVYELAPGEESKSRETKAAIEDWMLEHRLTRDTVVLACGGGVIGDLVGFVAATFMRGLKYVQIPTTLLAMVDSSVGGKTAIDHPHGKNLIGAFHQPRYVFIDAAWLLTLPEREFSNGMAEVIKTAAIWDAADFEKLESESASIRAAVMGDEARQQSAAQGHTLATRTSSQSLLLDVIRGSVGVKAHIVTIDEKETGLRNLVNFGHSVGHAIEAVLTPDILHGECVAVGMVLE... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}. | Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated fungus) |
A8QL52 | OXLA_BUNFA | MNVFSIFSLVFLAAFGSCADDRRSALEECFREADYEEFLEIARNGLKKTSNPKHVVVVGAGMAGLSAAYVLAGAGHRVTLLEASDRVGGRVNTYRDEKEGWYVNMGPMRLPERHRIVRTYIAKFGLKLNEFFQENENAWYFIRNIRKRVWEVKKDPGVFKYPVKPSEEGKSASQLYRESLKKVIEELKRTNCSYILDKYDTYSTKEYLIKEGNLSRGAVDMIGDLLNEDSSYYLSFIESLKNDDLFSYEKRFDEISDGFDQLPKSMHQAIAEMVHLNAQVIKIQRDAEKVRVAYQTPAKTLSYVTADYVIVCATSRAVRR... | 1.4.3.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P81382}; | amino acid catabolic process [GO:0009063]; apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | L-glutamate oxidase activity [GO:0050025]; L-lysine oxidase activity [GO:0050029]; L-phenylalaine oxidase activity [GO:0106329]; toxin activity [GO:0090729] | PF01593; | 3.90.660.10;3.50.50.60;1.10.405.10; | Flavin monoamine oxidase family, FIG1 subfamily | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19393676}. | CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|PubMed:19393676}; CATALYTIC ACTIVITY: Reaction=H2O... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=28.28 mM for L-Ala {ECO:0000269|PubMed:19393676}; KM=18.75 mM for L-Arg {ECO:0000269|PubMed:19393676}; KM=0.04 mM for L-Asp {ECO:0000269|PubMed:19393676}; KM=19.07 mM for L-Asn {ECO:0000269|PubMed:19393676}; KM=5.88 mM for L-Gln {ECO:0000269|PubMed:19393676}; KM=1.... | null | null | null | FUNCTION: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:19393676). Is highly active against L-Tyr, L-Asp, L-Phe, L-Glu, L-Trp, L-His, L-Gln, L-Ile, L-Met, L-Leu and mode... | Bungarus fasciatus (Banded krait) (Pseudoboa fasciata) |
A8QL56 | VSP1_OPHHA | MALIRVLASLLILQLSYAVTPFDRIIGGFECNEYEHRSLVHLYNSSGFFCSGTLLNHEWVLTAAHCNRDDIQIKLGVHNVSVNYEDEQIRVPKEKLCCHSTNNCTQLGQDIMLIRLNSSVNYSEHIAPLSLPSNRPSMGSVCRVMGWGLLTSPEVTFPKVPHCVDINILHIQVCQAAYPSMSENYLLCAGVLEGGKDSCKGDSGGPLICNREIQGIVSWGGFPCAQLLEPGVYTKVFDYIDWIEGIIAGNTSVTCPSDNF | 3.4.21.- | null | proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom serine protease that possesses potent fibrinogenolytic (on both alpha- (FGA) and beta-chains (FGB)) and amidolytic activities. Selectively cleaves Arg-|-Xaa or Lys-|-Xaa bonds. {ECO:0000269|PubMed:8079373}. | Ophiophagus hannah (King cobra) (Naja hannah) |
A8QW53 | OMT3_SORBI | MVLISEDSRELLQAHVELWNQTYSFMKSVALAVALDLHIADAIHRRGGAATLSQILGEIGVRPCKLPGLHRIMRVLTVSGTFTIVQPSAETMSSESDGREPVYKLTTASSLLVSSESSATASLSPMLNHVLSPFRDSPLSMGLTAWFRHDEDEQAPGMCPFTLMYGTTLWEVCRRDDAINALFNNAMAADSNFLMQILLKEFSEVFLGIDSLVDVAGGVGGATMAIAAAFPCLKCTVLDLPHVVAKAPSSSIGNVQFVGGDMFESIPPANVVLLKWILHDWSNDECIKILKNCKQAIPSRDAGGKIIIIDVVVGSDSSDT... | 2.1.1.n7 | null | aromatic compound biosynthetic process [GO:0019438]; methylation [GO:0032259] | null | 5-n-alk(en)ylresorcinol O-methyltransferase activity [GO:0102990]; O-methyltransferase activity [GO:0008171]; protein dimerization activity [GO:0046983]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | PF08100;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family, COMT subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(8Z,11Z)-5-(pentadeca-8,11,14-trien-1-yl)resorcinol + S-adenosyl-L-methionine = (8Z,11Z)-5-(pentadeca- 8,11,14-trien-1-yl)resorcinol-3-methyl ether + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:26325, ChEBI:CHEBI:15378, ChEBI:CHEBI:52680, ChEBI:CHEBI:52681, ChEBI:CHEBI:57856, ChEBI:CHE... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1436 uM for 5-n-propyl-resorcinol {ECO:0000269|PubMed:17998204}; KM=481 uM for 5-n-butyl-resorcinol {ECO:0000269|PubMed:17998204}; KM=152 uM for 5-n-pentyl-resorcinol {ECO:0000269|PubMed:17998204}; KM=72 uM for 5-n-hexyl-resorcinol {ECO:0000269|PubMed:17998204}; KM... | null | null | null | FUNCTION: O-methyltransferase involved in the biosynthetic pathway of the phytotoxin sorgoleone, a potent broad-spectrum inhibitor active against many agronomically important monocot and dicot weed species. Substrate specificity for alkylresorcinols. Strong preference for a five carbons alkyl side chain. {ECO:0000269|P... | Sorghum bicolor (Sorghum) (Sorghum vulgare) |
A8R3S4 | QEDH_PSEPU | MTIRSLPAALSPLSMAVQAVLLVSSLALAPAANAKPVTWEDIANDHLNTQNVLQYGMGTNAQRWSPLAMVNDKNVFKLTPAWSYSFGDERQRGQESQAIINDGVIYVTGSYSRVFALDAKTGRRLWTYNHRLPDNIRPCCDVVNRGAAIFGDKIYFGTLDARVIALNKDTGKVVWNKKFGDHSAGYTMTGAPTLIKDQKSGKVLLIHGSSGDEFGVVGQLYARDPETGEEVWMRPFVEGHMGRLNGKDSTPTGDVKAPSWPDDPTTETGKVESWSHGGGAPWQSASFDPETNTIIVGAGNPGPWNTWARTSKDGNPHDFD... | 1.1.2.8 | COFACTOR: Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442; Evidence={ECO:0000269|PubMed:7730276}; Note=Binds 1 PQQ group non-covalently per subunit (PubMed:7730276). PQQ is inserted between disulfide Cys-139-Cys-140 and the plane of Trp-282 (By similarity). {ECO:0000250|UniProtKB:Q9Z4J7, ECO:0000269|PubMed:773027... | ethanol catabolic process [GO:0006068] | membrane [GO:0016020]; outer membrane-bounded periplasmic space [GO:0030288] | alcohol dehydrogenase (cytochrome c) activity [GO:0052934]; calcium ion binding [GO:0005509] | PF01011;PF13360; | 2.140.10.10; | Bacterial PQQ dehydrogenase family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:18218017}. | CATALYTIC ACTIVITY: Reaction=a primary alcohol + 2 Fe(III)-[cytochrome c] = an aldehyde + 2 Fe(II)-[cytochrome c] + 2 H(+); Xref=Rhea:RHEA:51020, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.1.2.8; Evidence={ECO:0000305|P... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.163 mM for ethanol {ECO:0000269|PubMed:7730276}; KM=1.62 mM for butan-1-ol {ECO:0000269|PubMed:7730276}; KM=24.9 mM for propane-1,2-diol {ECO:0000269|PubMed:7730276}; Vmax=26.3 umol/min/mg enzyme with ethanol as substrate {ECO:0000269|PubMed:7730276}; Vmax=21.5 u... | PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 1/2. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:7730276}; | null | FUNCTION: Catalyzes the oxidation of ethanol and other primary alcohols to the corresponding aldehydes, except methanol, which is not a substrate (PubMed:7730276). Uses a specific inducible cytochrome c550, encoded by the adjacent gene in the locus, as electron acceptor (By similarity). Is a key enzyme of the carbon an... | Pseudomonas putida (Arthrobacter siderocapsulatus) |
A8R7E6 | CERK1_ARATH | MKLKISLIAPILLLFSFFFAVESKCRTSCPLALASYYLENGTTLSVINQNLNSSIAPYDQINFDPILRYNSNIKDKDRIQMGSRVLVPFPCECQPGDFLGHNFSYSVRQEDTYERVAISNYANLTTMESLQARNPFPATNIPLSATLNVLVNCSCGDESVSKDFGLFVTYPLRPEDSLSSIARSSGVSADILQRYNPGVNFNSGNGIVYVPGRDPNGAFPPFKSSKQDGVGAGVIAGIVIGVIVALLLILFIVYYAYRKNKSKGDSFSSSIPLSTKADHASSTSLQSGGLGGAGVSPGIAAISVDKSVEFSLEELAKATD... | 2.7.11.1 | null | cell surface pattern recognition receptor signaling pathway [GO:0002752]; cellular response to chitin [GO:0071323]; cellular response to molecule of bacterial origin [GO:0071219]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; detection of molecule of fungal origin [GO:0032491]; de... | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; chitin binding [GO:0008061]; chitosan binding [GO:2001080]; identical protein binding [GO:0042802]; kinase activity [GO:0016301]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein self-association [GO:0043621]; protein serine kinase activity [GO:0106... | PF01476;PF07714; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated. Autophosphorylation is induced by chitin and derivatives. {ECO:0000269|PubMed:20610395, ECO:0000269|PubMed:22654057}.; PTM: Ubiquitinated and targeted to the proteasome by hopAB2/avrPtoB of Pseudomonas syringae pv. tomato DC3000. {ECO:0000269|PubMed:19249211}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18042724, ECO:0000269|PubMed:24750441, ECO:0000269|PubMed:27679653}; Single-pass membrane protein {ECO:0000269|PubMed:18042724}. | 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:18042724, ECO:000026... | null | null | null | null | FUNCTION: Lysin motif (LysM) receptor kinase that functions as a cell surface receptor in chitin elicitor (chitooligosaccharides) signaling leading to innate immunity toward both biotic and abiotic stresses (e.g. tolerance to salinity, heavy-metal stresses, and Botrytis cinerea infection). Recognizes microbe-derived N-... | Arabidopsis thaliana (Mouse-ear cress) |
A8R7K9 | VP35C_ARATH | MIADDDEKWLAAAIAAVKQNAFYMQRAIDSNNLKDALKFSAQMLSELRTSKLSPHKYYELYMRVFNELGTLEIFFKEETGRGCSIAELYELVQHAGNILPRLYLLCTIGSVYIKSKDVTATDILKDLVEMCRAVQHPLRGLFLRSYLAQVTRDKLPSIGSDLEGDGDAHMNALEFVLQNFTEMNKLWVRMQHQGPSREKEKREKERNELRDLVGKNLHVLSQLEGVDLGIYRDTVLPRILEQVVNCKDELAQCYLMDCIIQVFPDDFHLQTLDVLLGACPQLQPSVDIKTVLSGLMERLSNYAASSVEALPNFLQVEAFS... | null | null | intracellular protein transport [GO:0006886]; retrograde transport, endosome to Golgi [GO:0042147] | cytosol [GO:0005829]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; multivesicular body [GO:0005771]; retromer complex [GO:0030904]; retromer, cargo-selective complex [GO:0030906] | null | PF03635; | 1.25.40.660; | VPS35 family | null | SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Prevacuolar compartment membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi network membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. | null | null | null | null | null | FUNCTION: Plays a role in vesicular protein sorting. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. Also involved in the efficient sorting of seed storage proteins (By similarity). The VPS29-VPS26-VPS35 subcomplex may be involved in recycling of speci... | Arabidopsis thaliana (Mouse-ear cress) |
A8T644 | PCSK9_PANTR | MGTVSSRRSWWPLPLLLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGTTATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRD... | 3.4.21.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; cholesterol metabolic process [GO:0008203]; low-density lipoprotein particle receptor catabolic process [GO:0032802]; proteolysis [GO:0006508]; regulation of neuron apoptotic process [GO:0043523] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764] | apolipoprotein binding [GO:0034185]; low-density lipoprotein particle binding [GO:0030169]; protein self-association [GO:0043621]; serine-type endopeptidase activity [GO:0004252]; very-low-density lipoprotein particle binding [GO:0034189] | PF05922;PF18459;PF18464;PF18463;PF00082; | 3.30.70.80;3.40.50.200;2.60.120.690; | Peptidase S8 family | PTM: Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation. {ECO:0000250}.; PTM: Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation a... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Cell surface {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi appar... | null | null | null | null | null | FUNCTION: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their... | Pan troglodytes (Chimpanzee) |
A8T650 | PCSK9_GORGO | MGTVSSRRSWWPLPLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGTTATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDA... | 3.4.21.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; cholesterol metabolic process [GO:0008203]; low-density lipoprotein particle receptor catabolic process [GO:0032802]; proteolysis [GO:0006508]; regulation of neuron apoptotic process [GO:0043523] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764] | apolipoprotein binding [GO:0034185]; low-density lipoprotein particle binding [GO:0030169]; protein self-association [GO:0043621]; serine-type endopeptidase activity [GO:0004252]; very-low-density lipoprotein particle binding [GO:0034189] | PF05922;PF18459;PF18464;PF18463;PF00082; | 3.30.70.80;3.40.50.200;2.60.120.690; | Peptidase S8 family | PTM: Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation. {ECO:0000250}.; PTM: Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation a... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Cell surface {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi appar... | null | null | null | null | null | FUNCTION: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their... | Gorilla gorilla gorilla (Western lowland gorilla) |
A8T655 | PCSK9_PANPA | MGTVSSRRSWWPLPLLLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGTTATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAAHRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVRPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRD... | 3.4.21.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; cholesterol metabolic process [GO:0008203]; low-density lipoprotein particle receptor catabolic process [GO:0032802]; proteolysis [GO:0006508]; regulation of neuron apoptotic process [GO:0043523] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764] | apolipoprotein binding [GO:0034185]; low-density lipoprotein particle binding [GO:0030169]; protein self-association [GO:0043621]; serine-type endopeptidase activity [GO:0004252]; very-low-density lipoprotein particle binding [GO:0034189] | PF05922;PF18459;PF18464;PF18463;PF00082; | 3.30.70.80;3.40.50.200;2.60.120.690; | Peptidase S8 family | PTM: Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation. {ECO:0000250}.; PTM: Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation a... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Cell surface {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi appar... | null | null | null | null | null | FUNCTION: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their... | Pan paniscus (Pygmy chimpanzee) (Bonobo) |
A8T658 | PCSK9_PONPY | MGTVSSRRSWWPLPLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGATATFHRCAKDPWRLPGTYVVVLKEETHRSQSERTARRLQAQAARRGYLTKILHVFHDLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLMPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDA... | 3.4.21.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; cholesterol metabolic process [GO:0008203]; low-density lipoprotein particle receptor catabolic process [GO:0032802]; proteolysis [GO:0006508]; regulation of neuron apoptotic process [GO:0043523] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764] | apolipoprotein binding [GO:0034185]; low-density lipoprotein particle binding [GO:0030169]; protein self-association [GO:0043621]; serine-type endopeptidase activity [GO:0004252]; very-low-density lipoprotein particle binding [GO:0034189] | PF05922;PF18459;PF18464;PF18463;PF00082; | 3.30.70.80;3.40.50.200;2.60.120.690; | Peptidase S8 family | PTM: Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation. {ECO:0000250}.; PTM: Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation a... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Cell surface {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi appar... | null | null | null | null | null | FUNCTION: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their... | Pongo pygmaeus (Bornean orangutan) |
A8T662 | PCSK9_MACNE | MGTVSSRRSWWPLPLPLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLADAPEHGATATFHRCAKDPWRLPGTYVVVLKEETHRSQSERTARRLQAQAARRGYLTKILHVFHHLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPKGGSLVEVYLLDTSIQSDHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGAGLRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVFNAACQRLARAGVVLVTAAGNFRD... | 3.4.21.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; cholesterol metabolic process [GO:0008203]; low-density lipoprotein particle receptor catabolic process [GO:0032802]; proteolysis [GO:0006508]; regulation of neuron apoptotic process [GO:0043523] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764] | apolipoprotein binding [GO:0034185]; low-density lipoprotein particle binding [GO:0030169]; protein self-association [GO:0043621]; serine-type endopeptidase activity [GO:0004252]; very-low-density lipoprotein particle binding [GO:0034189] | PF05922;PF18459;PF18464;PF18463;PF00082; | 3.30.70.80;3.40.50.200;2.60.120.690; | Peptidase S8 family | PTM: Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation. {ECO:0000250}.; PTM: Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation a... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Cell surface {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi appar... | null | null | null | null | null | FUNCTION: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their... | Macaca nemestrina (Pig-tailed macaque) |
A8T666 | PCSK9_MACMU | MGTVSSRRSWWPLPLPLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLADAPEHGATATFHRCAKDPWRLPGTYVVVLKEETHRSQSERTARRLQAQAARRGYLTKILHVFHHLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPKGGSLVEVYLLDTSIQSDHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGAGLRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVFNAACQRLARAGVVLVTAAGNFRD... | 3.4.21.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; cholesterol metabolic process [GO:0008203]; low-density lipoprotein particle receptor catabolic process [GO:0032802]; proteolysis [GO:0006508]; regulation of neuron apoptotic process [GO:0043523] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764] | apolipoprotein binding [GO:0034185]; low-density lipoprotein particle binding [GO:0030169]; protein self-association [GO:0043621]; serine-type endopeptidase activity [GO:0004252]; very-low-density lipoprotein particle binding [GO:0034189] | PF05922;PF18459;PF18464;PF18463;PF00082; | 3.30.70.80;3.40.50.200;2.60.120.690; | Peptidase S8 family | PTM: Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation. {ECO:0000250}.; PTM: Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation a... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Cell surface {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi appar... | null | null | null | null | null | FUNCTION: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their... | Macaca mulatta (Rhesus macaque) |
A8T672 | PCSK9_COLGU | MGTVSSRRSWWPLPLPLLLLLLLGLAGARAQEDEDGDYEELVLALRSEEDGLADAPEHGATATFHRCAKDPWRLPGTYVVVLKEETHRSQSERTARRLQAQAARRGYLTKILHVFHHLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPKGGSLVEVYLLDTSIQSDHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGAGLRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVFNAACQRLARAGVVLVTAAGNFRD... | 3.4.21.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; cholesterol metabolic process [GO:0008203]; low-density lipoprotein particle receptor catabolic process [GO:0032802]; proteolysis [GO:0006508]; regulation of neuron apoptotic process [GO:0043523] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764] | apolipoprotein binding [GO:0034185]; low-density lipoprotein particle binding [GO:0030169]; protein self-association [GO:0043621]; serine-type endopeptidase activity [GO:0004252]; very-low-density lipoprotein particle binding [GO:0034189] | PF05922;PF18459;PF18464;PF18463;PF00082; | 3.30.70.80;3.40.50.200;2.60.120.690; | Peptidase S8 family | PTM: Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation. {ECO:0000250}.; PTM: Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation a... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Cell surface {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi appar... | null | null | null | null | null | FUNCTION: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their... | Colobus guereza (Mantled guereza) (Eastern black-and-white colobus monkey) |
A8T677 | PCSK9_PLEMO | MGTVSSRRLWWPLPLLLLLLLGPPGARAQEDDDGDYEELVLALRSEEDGPADALQHGATATFHRCAKDPWRLPGTYVVVLKDSDAHRSQPERTARRLQAQAARRGYLIKLLHVFHHLLPGFLVKMSRDLLELALRLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSSHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLHVLNCQGKGTVSSALIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACRRLAGAGVVLVAAAGNFRDD... | 3.4.21.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; cholesterol metabolic process [GO:0008203]; low-density lipoprotein particle receptor catabolic process [GO:0032802]; proteolysis [GO:0006508]; regulation of neuron apoptotic process [GO:0043523] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764] | apolipoprotein binding [GO:0034185]; low-density lipoprotein particle binding [GO:0030169]; protein self-association [GO:0043621]; serine-type endopeptidase activity [GO:0004252]; very-low-density lipoprotein particle binding [GO:0034189] | PF05922;PF18459;PF18464;PF18463;PF00082; | 3.30.70.80;3.40.50.200;2.60.120.690; | Peptidase S8 family | PTM: Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation. {ECO:0000250}.; PTM: Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation a... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Cell surface {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi appar... | null | null | null | null | null | FUNCTION: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their... | Plecturocebus moloch (Dusky titi monkey) (Callicebus moloch) |
A8T682 | PCSK9_SAGLB | MGTVSSRRLWWPLPLLLLLLLGPAGTRAQEDDDDDYEELVLALRSEEEGLADALQNGATATFHRCAKDPWRLPGTYVVVLKEETHRSQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALRLPHVDYIEEDSSVFAQSIPWNLERITPARYQADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFGSVPKEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLHSLRVLNCQGKGTVSSTLIGLEFICKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARARVVLVAAAGNFRDDA... | 3.4.21.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; cholesterol metabolic process [GO:0008203]; low-density lipoprotein particle receptor catabolic process [GO:0032802]; proteolysis [GO:0006508]; regulation of neuron apoptotic process [GO:0043523] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764] | apolipoprotein binding [GO:0034185]; low-density lipoprotein particle binding [GO:0030169]; protein self-association [GO:0043621]; serine-type endopeptidase activity [GO:0004252]; very-low-density lipoprotein particle binding [GO:0034189] | PF05922;PF18459;PF18464;PF18463;PF00082; | 3.30.70.80;3.40.50.200;2.60.120.690; | Peptidase S8 family | PTM: Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation. {ECO:0000250}.; PTM: Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation a... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Cell surface {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi appar... | null | null | null | null | null | FUNCTION: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their... | Saguinus labiatus (Red-chested mustached tamarin) |
A8T688 | PCSK9_CALJA | MGTVSSRRLWWPLPLLLLLLLGPTGTRAQEEDDDDYEELVLALRSEEDGLVDALQHGATATFHRCAKDSWRLPGTYVVVLKEETHRSQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALRLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFGSVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLRVLNCQGKGTVSSTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVAAAGNFRDDA... | 3.4.21.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; cholesterol metabolic process [GO:0008203]; low-density lipoprotein particle receptor catabolic process [GO:0032802]; proteolysis [GO:0006508]; regulation of neuron apoptotic process [GO:0043523] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764] | apolipoprotein binding [GO:0034185]; low-density lipoprotein particle binding [GO:0030169]; protein self-association [GO:0043621]; serine-type endopeptidase activity [GO:0004252]; very-low-density lipoprotein particle binding [GO:0034189] | PF05922;PF18459;PF18464;PF18463;PF00082; | 3.30.70.80;3.40.50.200;2.60.120.690; | Peptidase S8 family | PTM: Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation. {ECO:0000250}.; PTM: Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation a... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Cell surface {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi appar... | null | null | null | null | null | FUNCTION: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their... | Callithrix jacchus (White-tufted-ear marmoset) |
A8T695 | PCSK9_SAIBB | MGTVSSRRLWWPLPLLLLLLLLGPAGARAQEDDDGDYEELVLALRSEEDGLADALQHGATATFHRCAKEPWRLPGTYVVVLKEETHRSQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFGSVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLRVLNCQGKGTVSSTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVAAAGNFRDD... | 3.4.21.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; cellular response to insulin stimulus [GO:0032869]; cellular response to starvation [GO:0009267]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; kidney development [GO:0001822]; lipoprotein metabolic process [GO:0042157]; liver development [GO:0001889];... | cell surface [GO:0009986]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764]; PCSK9-AnxA2 complex [GO:1990667]... | apolipoprotein binding [GO:0034185]; apolipoprotein receptor binding [GO:0034190]; low-density lipoprotein particle binding [GO:0030169]; low-density lipoprotein particle receptor binding [GO:0050750]; protein self-association [GO:0043621]; serine-type endopeptidase activity [GO:0004252]; signaling receptor inhibitor a... | PF05922;PF18459;PF18464;PF18463;PF00082; | 3.30.70.80;3.40.50.200;2.60.120.690; | Peptidase S8 family | PTM: Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation. {ECO:0000250}.; PTM: Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation a... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Cell surface {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi appar... | null | null | null | null | null | FUNCTION: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their... | Saimiri boliviensis boliviensis (Bolivian squirrel monkey) |
A8T6A1 | PCSK9_ATEGE | MGTVRSRRLWWPLPLLLLLLRGPAGARAQEDDDGDYEELVLALRSEEDGLAEAPQHGATATFHRCAKDPWRLPGTYVVVLKEETQRSQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALRLPHVDYIEEDSYVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLRVLNCQGKGTVSSTLIGLEFIRKNQLVQPVGPLVVLLPLAGGYSRVLNAACQRLAKAGVVLVAAAGNFRDDA... | 3.4.21.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; cholesterol metabolic process [GO:0008203]; low-density lipoprotein particle receptor catabolic process [GO:0032802]; proteolysis [GO:0006508]; regulation of neuron apoptotic process [GO:0043523] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764] | apolipoprotein binding [GO:0034185]; low-density lipoprotein particle binding [GO:0030169]; protein self-association [GO:0043621]; serine-type endopeptidase activity [GO:0004252]; very-low-density lipoprotein particle binding [GO:0034189] | PF05922;PF18459;PF18464;PF18463;PF00082; | 3.30.70.80;3.40.50.200;2.60.120.690; | Peptidase S8 family | PTM: Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation. {ECO:0000250}.; PTM: Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation a... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Cell surface {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi appar... | null | null | null | null | null | FUNCTION: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their... | Ateles geoffroyi (Black-handed spider monkey) (Geoffroy's spider monkey) |
A8T6A6 | PCSK9_LAGLA | MGTVRSRRLWWPLPLLLLLLLGPAGARAQEDDDGDYEELVLALRSEEDGLAEALQHGATATFHRCAKDPWRLPGTYVVVLKEETQRLQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALRLPHVDYIEEDSYVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLRVLNCQGKGTVSSTLIGLEFIRKNQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVAAAGNFRDDA... | 3.4.21.- | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; | apoptotic process [GO:0006915]; cholesterol metabolic process [GO:0008203]; low-density lipoprotein particle receptor catabolic process [GO:0032802]; proteolysis [GO:0006508]; regulation of neuron apoptotic process [GO:0043523] | cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; late endosome [GO:0005770]; lysosome [GO:0005764] | apolipoprotein binding [GO:0034185]; low-density lipoprotein particle binding [GO:0030169]; protein self-association [GO:0043621]; serine-type endopeptidase activity [GO:0004252]; very-low-density lipoprotein particle binding [GO:0034189] | PF05922;PF18459;PF18464;PF18463;PF00082; | 3.30.70.80;3.40.50.200;2.60.120.690; | Peptidase S8 family | PTM: Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation. {ECO:0000250}.; PTM: Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation a... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Secreted {ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Cell surface {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi appar... | null | null | null | null | null | FUNCTION: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their... | Lagothrix lagotricha (Brown woolly monkey) (Humboldt's woolly monkey) |
A8TX70 | CO6A5_HUMAN | MKILLIIFVLIIWTETLADQSPGPGPVYADVVFLVDSSDHLGPKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSPMLNHLKKNFQFIGGSLQIGKALQEAHRTYFSAPINGRDRKQFPPILVVLASAESEDEVEEASKALQKDGVKIISVGVQKASEENLKAMATSHFHFNLRTIRDLSTFSQNMTQIIKDVTKYKEGAVDADMQVHFPISCQKDSLADLVFLVDESLGTGGNLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQQQIKNLSIQVGKSNTGAAIDQ... | null | null | cell adhesion [GO:0007155] | collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576] | extracellular matrix structural constituent conferring tensile strength [GO:0030020] | PF01391;PF00092; | 3.40.50.410; | Type VI collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Deposed in the extracellular matrix of skeletal muscle. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Collagen VI acts as a cell-binding protein. {ECO:0000250}. | Homo sapiens (Human) |
A8VU90 | ANKL1_MOUSE | MADTACLALRLLAALREEEARAVEELLRLGADPNLVLDDGAAAVHLAARASHPRALHCLRMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLLSRGGDPTLRDQDGLRPLDWALQQRHHNCARVLQELDTPTQPDETREPTETFHVAQGSFETETCQGPALAESSGVSQDSELHVHRAELEVEAVEVAVHPQSSEATENSDYSSDASFVTAVEDSLQPGRPGGALELVAGLWVTRGAVSAGKGAPNCQPQVLTLTARDTDKPVLPGDGDLGALHPHSSVPPMSDLQLLQALRALGYSPGPVTPFTRGHYLRRLQEAQ... | 3.1.-.- | null | double-strand break repair via homologous recombination [GO:0000724]; negative regulation of mitotic recombination [GO:0045950]; protein export from nucleus [GO:0006611]; regulation of lymphoid progenitor cell differentiation [GO:1905456]; regulation of myeloid progenitor cell differentiation [GO:1905453]; resolution o... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654] | DNA endonuclease activity [GO:0004520] | PF12796;PF03020; | 1.10.720.40;1.25.40.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8NAG6}. Nucleus {ECO:0000250|UniProtKB:Q8NAG6}. Note=At the steady state, predominantly localizes in the cytoplasm. {ECO:0000250|UniProtKB:Q8NAG6}. | null | null | null | null | null | FUNCTION: Endonuclease that probably plays a role in the DNA damage response and DNA repair. {ECO:0000250|UniProtKB:Q8NAG6}. | Mus musculus (Mouse) |
A8WCF8 | TPRGL_RAT | MLQLRDTVDSAGTSPTAVLAAGEDAGAGRQGAGTPLRQTLWPLNVHDPTRRARVKEYFVFRPGTIEQAVEEIRAVVRPVEDGEIQGVWLLTEVDHWNNEKERLVLVTDQSLLICKYDFISLQCQQVVRVALSAVDTISCGEFQFPPKSLNKREGFGVRIQWDKQSRPSFINRWNPWSTNMPYATFIEHPMAGMDEKTASLCHLESFKALLIQAVKKAQKESPLPGQANNVLVLDRPLLIETYVGLMSFINNEAKLGYSMTRGKIGF | null | null | calmodulin dependent kinase signaling pathway [GO:0099004]; negative regulation of synaptic transmission [GO:0050805]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; regulation of synaptic transmission, glutamatergic [GO:0051966]; regulation of synaptic vesicle exocytosis [GO:2000300]; synaptic ... | calyx of Held [GO:0044305]; cytoplasm [GO:0005737]; extrinsic component of synaptic vesicle membrane [GO:0098850]; glutamatergic synapse [GO:0098978]; presynapse [GO:0098793]; presynaptic active zone [GO:0048786]; synaptic vesicle [GO:0008021] | calmodulin binding [GO:0005516]; identical protein binding [GO:0042802] | PF12456; | null | TPRG1 family | PTM: Phosphorylated. Phosphorylation promotes association with synaptic vesicle membranes. {ECO:0000269|PubMed:23723986}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:17869247, ECO:0000269|PubMed:23723986, ECO:0000269|PubMed:26212709}; Peripheral membrane protein {ECO:0000269|PubMed:23723986, ECO:0000269|PubMed:26212709}. Presynaptic active zone {ECO:0000269|PubMed:17869247, E... | null | null | null | null | null | FUNCTION: Presynaptic protein involved in the synaptic transmission tuning. Regulates synaptic release probability by decreasing the calcium sensitivity of release. {ECO:0000269|PubMed:26212709}. | Rattus norvegicus (Rat) |
A8WFJ9 | ETS4_CAEEL | MNGTGSVGHRWNSLSPEPHSGTESTASTPFVKSEFPFDDDLFGIDQVNNVKPHPMDMPCNLPIQPIEYNRRFSKDADHSTFVKNEIEENILNFNVNPEIAQDNGLDTQQIDIYRDLILRHLIQDISTTCAKLGLPNDFYLWSSEHGARWINEMCMQFNLQPPRNCSITGIDLLGMSQKDFEMILPAGGDTLHAQLQVWKTGTSDYVKAFENYHPPVTVQSSGMTAAENNMQSKTNWLASTNNQTNNMAAAENPNHPFFNGNGGYPNMSMSSFFQQGTVLPSPSNSDTSSNGSSQDMNDDDIDLHMNNSNCGFSNFFHNQG... | null | null | cell differentiation [GO:0030154]; positive regulation of axon extension involved in regeneration [GO:0048691]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00178;PF02198; | 1.10.150.50;1.10.10.10; | ETS family | PTM: Phosphorylation is required for axon regeneration. {ECO:0000269|PubMed:26484536}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20862312}. | null | null | null | null | null | FUNCTION: Transcription factor which binds to 5'-GGAA/T-3' DNA consensus sequences (PubMed:20862312, PubMed:26484536). Both positively and negatively regulates the expression of target genes (PubMed:20862312). Plays a role in the regulation of adult lifespan, which may in part be through modulation of daf-16 activity (... | Caenorhabditis elegans |
A8WFU8 | KIF22_DANRE | MAQRVAVNDGAAGSKRTSRVRVAVRLRPYMDKQDEKSEGSCVRGLGPQKLEIINWRNATETLQYQFDVFHGEETTQQEVFLTSVKPILPHILNGQNASVFAYGPTGAGKTHTMLGSQEQPGVIPRAVKEVFNLVGAQKKEQDGWEYSIGMSYLEIYNEKVLDLLSPGSQDLPIREDKDRNILIPGLTHTPLSSFADFDTHFIPASLNRTTASTKLNQRSSRSHAILLIKVVKSQRGPPHRQQTGKLYLVDLAGSEDNRRTGNQGIRLKESGAINLSLFTLSKVVDALNTGAGGRVPYRDSKLTRLLQDSLGGSAHSVMIT... | null | null | axonogenesis [GO:0007409]; brain development [GO:0007420]; central nervous system projection neuron axonogenesis [GO:0021952]; eye morphogenesis [GO:0048592]; microtubule-based movement [GO:0007018]; somitogenesis [GO:0001756]; thigmotaxis [GO:0001966] | cytoplasm [GO:0005737]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; plus-end-directed microtubule motor activity [GO:0008574] | PF12836;PF00225; | 1.10.150.280;3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family | PTM: Ubiquitinated, leading to its subsequent proteasomal degradation. {ECO:0000250|UniProtKB:Q9I869}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9I869}. Cytoplasm, cytoskeleton {ECO:0000305}. | null | null | null | null | null | FUNCTION: Kinesin family member that is involved in spindle formation and the movements of chromosomes during mitosis and meiosis. Binds to microtubules and to DNA. {ECO:0000250|UniProtKB:Q9I869}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8WGA0 | C27C1_DANRE | MALQSTILHMARKNLLQESCRQLLIQTHGLHKSVASGSLEIAAHSQADLKEESAVSPAEEVQKAARVKSLKEMPGPSTVANLLEFFYRDGFSRIHEIQMEHAKKYGKIFKSRFGPQFVVSIADRDMVAQVLRSESATPQRGNMESWKEYRDLRGRSTGLISAEGDEWLKMRSVLRQLIMRPRDVAVFSSDVNDVVADLVKRVKTLRSQQDDSQTVLNINDLFFKYAMEGVATILYETRLGCLENEIPKMSQEYITALHLMFSSFKTTMYAGAIPKWLRPIIPKPWEEFCSSWDGLFKFSQIHVDKRLSEIKKQMEKSEEI... | 1.14.19.53 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | C21-steroid hormone biosynthetic process [GO:0006700]; cellular response to peptide hormone stimulus [GO:0071375]; cholesterol metabolic process [GO:0008203]; cortisol metabolic process [GO:0034650]; glucocorticoid biosynthetic process [GO:0006704] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | all-trans retinal 3,4-desaturase activity [GO:0061897]; all-trans retinoic acid 3,4-desaturase activity [GO:0061898]; all-trans retinol 3,4-desaturase activity [GO:0061896]; all-trans-retinol binding [GO:1904768]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; retinoic ac... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=all-trans-retinol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = all-trans-3,4-didehydroretinol + 2 H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:50292, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17336, ChEBI:CHEBI:33737, ChEBI... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for all-trans retinol {ECO:0000269|PubMed:26549260}; KM=0.48 uM for retinal {ECO:0000269|PubMed:26549260}; KM=0.34 uM for retinoic acid {ECO:0000269|PubMed:26549260}; | null | null | null | FUNCTION: Efficiently catalyzes the conversion of all-trans retinol (also called vitamin A1, the precursor of 11-cis retinal) to 3,4-didehydroretinol (also called vitamin A2, the precursor of 11-cis 3,4-didehydroretinal). Also acts on all-trans retinal and all-trans retinoic acid. The replacement of 11-cis retinal chro... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8WGB1 | CCBE1_DANRE | MIYPGRGASLSVAVALVLFSSGAPWTFREEKEDVDREVCSESKIATTKYPCVKSTGEVTTCYRKKCCEGFKFVLGQCIPEDYDVCAGAPCEQQCTDHFGRVVCTCYDGYRYDRERHRNREKPYCLDIDECANNNETVCSQMCVNTPGSYRCDCHSGFYLEDDGKTCTKGERAPLFEKSDNVMKEGTCSATCEDFHQMKMTVLQLKQKMSLLSSNTEINKQMTNEKMMMTTNSFLPGPPGPPGPAGTPGAKGSSGSPGQMGPPGLPGPRGDMGPIGPSPDLSHIKQGRRGPVGPPGAPGRDGMKGERGFPGPSGPPGPPGS... | null | null | blood vessel morphogenesis [GO:0048514]; lymph vessel development [GO:0001945]; lymphangiogenesis [GO:0001946]; sprouting angiogenesis [GO:0002040]; vascular endothelial growth factor signaling pathway [GO:0038084]; venous blood vessel morphogenesis [GO:0048845]; venous endothelial cell migration involved in lymph vess... | collagen trimer [GO:0005581]; extracellular region [GO:0005576] | calcium ion binding [GO:0005509] | PF01391;PF14670; | 2.10.25.10; | CCBE1 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Required for lymphangioblast budding and angiogenic sprouting from venous endothelium during embryogenesis. Required for the formation of facial lymphatic structures (PubMed:37097004). Necessary for lymphangiogenesis, but is probably not part of either the vegfc-vegfr3 signaling or sox18-prox1 transcriptional... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8WGP3 | PP4CA_DANRE | MCVIMGDFTDLDRQIEQLRRCELIKENEVKALCAKAREILVEESNVQSVDSPVTVCGDIHGQFYDLKELFRVGGEVPETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFFDECHRKYGSATVWRYCTEIFDYLSLSAIVDGKIFCVHGGLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDISMICRAHQLVMEGYKWHFNDTVLTVWSAPNYCYRCGNVAAILELDEHLQKEFIIFEAAPQETRGLPSKKPVADYFL | 3.1.3.16 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; | angiogenesis [GO:0001525]; brain development [GO:0007420]; central nervous system projection neuron axonogenesis [GO:0021952]; determination of ventral identity [GO:0048264]; dorsal/ventral pattern formation [GO:0009953]; double-strand break repair via homologous recombination [GO:0000724] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722] | PF00149; | 3.60.21.10; | PPP phosphatase family, PP-4 (PP-X) subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-... | null | null | null | null | FUNCTION: Protein phosphatase that regulates many processes such as microtubule organization at centrosomes. {ECO:0000250}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8WIP6 | CDK20_DANRE | MDQYSILGRIGEGAHGIVFKAKHIETGETVALKKVALRRLEDGIPNQALREIKALQEIEDNQYVVKLKDVFPHGTGFVLVFEYMLSDLSEVIRNSQRPLTASQVKSYMMMLLKGVAFCHENSIMHRDLKPANLLISSTGHLKIADFGLARLFSNEGDRLYSHQVATRWYRAPELLYGARKYDEGVDLWAVGCIFGELLNNSPLFPGENDIEQLCCVLRVLGTPNQKVWPEITELPDYNKITFKENPPIPLEEIVPDTSPQAVDLLKKFLVYPSKQRISARQALLHPYFFTDPLPAHHSELPIPQRGGKHSRQRMQPPHEF... | 2.7.11.22 | null | cell cycle [GO:0007049]; cell division [GO:0051301]; cilium assembly [GO:0060271]; phosphorylation [GO:0016310] | cilium [GO:0005929]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; cyclin-dependent protein kinase activating kinase activity [GO:0019912]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell projection, cilium {ECO:0000250}. | 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=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Involved in cell growth. Activates cdk2, a kinase involved in the control of the cell cycle, by phosphorylating residue 'Thr-160' (By similarity). Required for high-level Shh responses in the developing neural tube. Together with tbc1d32, controls the structure of the primary cilium by coordinating assembly o... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8WJR8 | MBK2_CAEBR | MAALASFTRNSRSYGQQPIDVTQQGQRDRSVMSLDAQGRSKMSNINYTRPAALSTSDSTIGVFRRAPSSFSGASSSSSNHHHPVYHSHNSLPPTLIGGSPHSASSNSLAQGHRNPALGSGNTLTRSYHQPSSTNSSTSNLHGPLGTYSRDLKQAIRDISPPVINSSANPHLVNYIHTSSFDNGSYEFPSGQAQQQRRLGGSQQHLAPLQQTSSSLYSNPQSSSSQLLGQQAVRSNYAYQQSLPRQQHINSHQTQAFFGTIRAPGNSTNIVTPLRASKTMIDVLAPVRDSVAAQATTGALPSVGTSSSNGSSNSSSGVGSG... | 2.7.12.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9XTF3}; | phosphorylation [GO:0016310]; response to stimulus [GO:0050896]; sensory perception of smell [GO:0007608] | cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 3.30.10.30;1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MNB/DYRK subfamily | PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q9XTF3}. | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q9XTF3}. Note=Maintained at the cortex by the cortical anchor egg-3 before meiotic divisions. During anaphase of meiosis I, egg-3 translocates into the cytoplasm on vesicles and is slowly degraded, releasing mbk-2 (By similarity). {ECO:0000250|UniProtK... | 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=2.7.12.1; Evidence={ECO:0000250|UniProtKB:Q9XTF3}; CATALYTI... | null | null | null | null | FUNCTION: Required for oocyte-to-zygote transition in which it phosphorylates oocyte proteins, including mei-1, oma-1, oma-2, mex-5, and mex-6, modifying their activity and/or stability following meiosis. Through phosphorylation of P granule components including meg-1, promotes the disassembly of zygotic P granules in ... | Caenorhabditis briggsae |
A8WUG4 | KPC3_CAEBR | MSSPTSVEEDGDIKLKTRFHGQVVVLYARPPLILDDFFALLRDACKQHAKQDITVKWIDEDGDPISIDSQMELDEAVRCLNVSQEAELNIHVFVGKPELPGLPCQGEDKTVYRRGARRWKKIYLYNGHRFQGKRLNRRIQCFICHDYIWGIGRQGFRCVDCRLCVHKKCHRHVRTHCGQTPQGPNVPVAPSSGVGSLRGGRLDTSSSTTRSGGGIDNGAFHEHEIESPGSAKDMSRSTNGNGASKWAVSLNDFRLLTVIGRGSYAKVVQAEHIATRQIYAIKIIKKEMFNEDEDIDWVQTEKSVFEAASNYPFLVGLHSC... | 2.7.11.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q19266}; | cell differentiation [GO:0030154]; defense response to fungus [GO:0050832]; embryo development ending in birth or egg hatching [GO:0009792]; establishment or maintenance of cell polarity [GO:0007163]; gastrulation [GO:0007369]; gonad development [GO:0008406]; gonadal mesoderm development [GO:0007506]; intracellular sig... | apical plasma membrane [GO:0016324]; cortical actin cytoskeleton [GO:0030864]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00130;PF00564;PF00069;PF00433; | 3.30.60.20;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q19266}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q19266}. Note=Targeted and anchored at the apical surface (villi) of intestinal and pharyngeal cells, and in proximity with the cortical actin cytoskeleton that lies under the plasma membrane. Tightly bound to... | 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=2.7.11.13; Evidence={ECO:0000250|UniProtKB:Q19266}; CATALYT... | null | null | null | null | FUNCTION: Required for the normal progression of embryogenesis and viability of the organism. Plays an indispensable role in establishing embryonic polarity and in recruiting and maintaining par-6 to the periphery, through interaction with par-3. Required for epithelial cell polarity in the distal spermatheca. Phosphor... | Caenorhabditis briggsae |
A8WVD0 | STX1A_CAEBR | MTKDRLAALKAAQSEDEQDDDMHMETGNAQYMEEFFEQVEEIRGSVDIIANNVEEVKKKHSAILSNPVNDQKTKEELDELMAVIKRAANKVRGKLKLIENAIEHDENQQGAGNADLRIRKTQHSTLSRRFVEVMTDYNKTQTDYRERCKGRIQRQLDIAGKQVGDEDLEEMIESGNPGVFTQGIITDTQQAKQTLADIEARHNDIMKLESSIRELHDMFMDMAMLVESQGEMVDRIEYNVEHAKEFVDRAVADTKKAVQYQSKARRKKIIILIVVTVIIVILSLWLIQYIPGI | null | null | cell differentiation [GO:0030154]; chemical synaptic transmission [GO:0007268]; exocytosis [GO:0006887]; insulin receptor signaling pathway [GO:0008286]; intracellular protein transport [GO:0006886]; locomotion [GO:0040011]; neurotransmitter secretion [GO:0007269]; positive regulation of anterior/posterior axon guidanc... | axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; dendrite [GO:0030425]; endomembrane system [GO:0012505]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; presynaptic active zone membrane [GO:0048787]; SNARE complex [GO:0031201]; synaptic vesicle [GO:0008021] | protein-folding chaperone binding [GO:0051087]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]; structural constituent of cuticle [GO:0042302] | PF05739;PF00804; | 1.20.5.110;1.20.58.70; | Syntaxin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O16000}; Single-pass type IV membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000250|UniProtKB:O16000}. Cell projection, dendrite {ECO:0000250|UniProtKB:O16000}. Perikaryon {ECO:0000250|UniProtKB:O16000}. | null | null | null | null | null | FUNCTION: Plays a critical role in several secretory processes, including cuticle secretion and neurotransmitter release, and probably assists in neuronal membrane maturation or the final stages of neuronal differentiation (By similarity). Plays a role in synaptic vesicle docking and tethering through its association w... | Caenorhabditis briggsae |
A8WVU9 | ROCK_CAEBR | MEQDELLHQLVDPKSPINIESLLDTITALVNDCKIPVLMRMKSVDNFISRYERIVESVAALRMKATDFRQLKVIGRGAFGEVHLVRHTRTNTVYAMKMLNKDDMIKRADSAFFWEERDIMAHANSEWIVRLQYAFQDPRHLYMVMEYMPGGDLVNLMTSYEVSEKWTRFYTAEIVEALAALHNMGYIHRDVKPDNMLISRSGHIKLADFGTCVKMNSNGVVRCSTAVGTPDYISPEVLRNQGKDSEFGKEVDWWSVGVFIYEMLVGETPFYAEALVSTYANIMNHQTSLRFPDEPLISTQAKDIIKKFLSAAPERLGKNN... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13464}; | actomyosin structure organization [GO:0031032]; cortical actin cytoskeleton organization [GO:0030866]; embryonic morphogenesis [GO:0048598]; mitotic cytokinesis [GO:0000281]; oogenesis [GO:0048477]; phosphorylation [GO:0016310]; regulation of cell junction assembly [GO:1901888]; Rho protein signal transduction [GO:0007... | cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; Rho-dependent protein serine/threonine kinase activity [GO:0072518]; small GTPase binding [GO:0031267] | PF00069; | 3.30.60.20;2.30.29.30;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cleavage furrow {ECO:0000250}. Note=Colocalizes with nmy-2 myosin thick filaments at the cleavage furrow. {ECO:0000250|UniProtKB:P92199}. | 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:Q13464}; CATALYTI... | null | null | null | null | FUNCTION: Negatively regulates mel-11 to relieve the inhibition of mlc-4, allowing contraction of the circumferentially oriented microfilaments in epidermal cells and thereby regulating myosin II contractility during spermathecal contraction, cleavage furrow contraction in early embryos, and embryonic elongation and mo... | Caenorhabditis briggsae |
A8WWH5 | POP1_CAEBR | MMADEELGDEVKVFRRDEDADDDPMISGETSEQQLADDKKDAVMEAELDGAGRVPLIGGLKAEIKAEPSPSFPMPSMLPCGPYSPFSGLPIMFPMVVPQYLSPNPNINMMNMMTMRAAMAGAPLSPAFPAMFSPNPLFPFPGVVAKQHLENTMPMHMRAGPLSSLNHMKMPPYMPHQMMPQHNERRGHGGGKVKKEDHIKKPLNAFMWYMKENRPKLLEEVGNDQKQSAELNKELGKRWHDLPKEEQQKYFEMAKKDRESHKEKYPQWSARENYAVNKKKPKRKRDKSVVSGSENNDQKKCRARFGVTNTSMWCKPCQRK... | null | null | asymmetric cell division [GO:0008356]; canonical Wnt signaling pathway [GO:0060070]; chordate pharyngeal muscle development [GO:0043282]; embryonic pattern specification [GO:0009880]; gonad morphogenesis [GO:0035262]; mesodermal cell fate determination [GO:0007500]; mesodermal cell fate specification [GO:0007501]; nega... | beta-catenin-TCF complex [GO:1990907]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | beta-catenin binding [GO:0008013]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; histone acetyltransferase binding [GO:0035035]; histone deacetylase binding [GO:0042826]; protein kinase binding [... | PF00505; | 1.10.30.10; | TCF/LEF family | PTM: Phosphorylated on Ser-125 by lit-1 in the beta-catenin-lit-1 complex (By similarity). Phosphorylation promotes the interaction of pop-1 and par-5 and the subsequent translocation of pop-1 from the nucleus to the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q10666}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q10666, ECO:0000255|PROSITE-ProRule:PRU00267}. Cytoplasm {ECO:0000250|UniProtKB:Q10666}. Note=Predominantly nuclear, but is exported out of the nucleus and into the cytoplasm upon lit-1-mediated phosphorylation (By similarity). Soon after the nuclei reform in telopha... | null | null | null | null | null | FUNCTION: Part of the Wnt signaling pathway essential for the specification of the mesodermal cell fate in early embryos (By similarity). Required for asymmetrical division of somatic gonadal precursor descendants which initiate axis formation required to control organ shape (By similarity). Similarly, involved in asym... | Caenorhabditis briggsae |
A8X181 | FICD_CAEBR | MSVRRRTHSDDFSFRLERTRRPSKLDVLRESPTLPVQQGYSLTTVVLVSLVVTLVCQNVAPPAFSYLNQLIKNSPKRKIPGQSNRLNIGFISTNSPEKFAPAVQKPTFLVDPIYDEKWKGVHTAVPVMTTEPEEKRDNNHAKVKEAILAAKAASRSRRDGNLERAVTIMEHAMALAPNNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRARTNPLVSAIDRKMLKTVHDLRNEFAHLQHSTALRRMMRETYFLYVYHTVAIEGNTLSLGQTRAILESGMVIPGKSIREHNEVIGMDAALRFLNCSLLSK... | 2.7.7.108; 3.1.4.- | null | defense response to Gram-negative bacterium [GO:0050829] | endoplasmic reticulum membrane [GO:0005789]; nuclear membrane [GO:0031965] | AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; hydrolase activity [GO:0016787] | PF02661; | 1.10.3290.10;1.25.40.10; | Fic family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q23544}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q23544}. Nucleus membrane {ECO:0000250|UniProtKB:Q23544}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q23544}. Note=Predominantly localized to the endoplasmic reticulum and to... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q9BVA6}; CATALYTIC ACTIV... | null | null | null | null | FUNCTION: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-273 determines which of the two op... | Caenorhabditis briggsae |
A8X3A7 | PAT2_CAEBR | MREGSFPRRTRLLCLLAAVVLISTVTSFNIDTKNVVLHHMANNYFGYSLDFYNEQKGMPVLVVGAPEAETTNPNLSGIRRPGAVYACSVNRPTCREVHVDKMKGNLKKLNGSHLVPIEDKAYQFFGATVKSNDKHDKLLMCAPKYKYFYSKFEVIEPVGTCFYAENGFEKTEEFSSCKQEPARHGRHRLGYGQCGFSGAIPGKKNQDRVFLGAPGVWYWQGAIFSQNTKNQTDRPNTEYGSKEYDHDMMGYATATGDFDGDGIDDIVAGVPRGNDLHGKLVLYTSKLKMMINLTDEVSTQHGQYCGGALAVADVNKDGRD... | null | null | cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; integrin-mediated signaling pathway [GO:0007229]; mitochondrion organization [GO:0007005]; muscle cell cellular homeostasis [GO:0046716]; negative regulation of epidermal growth factor receptor signaling... | external side of plasma membrane [GO:0009897]; integrin complex [GO:0008305]; M band [GO:0031430]; striated muscle dense body [GO:0055120] | integrin binding [GO:0005178]; transmembrane signaling receptor activity [GO:0004888] | PF01839;PF08441;PF20805;PF20806;PF00357; | 1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530; | Integrin alpha chain family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q3UV74}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q3UV74}. | null | null | null | null | null | FUNCTION: Required for muscle development probably through the regulation of the actin-myosin cytoskeleton. During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles, probably through lamins such as epi-1, lam-2 and unc-52. Required for distal t... | Caenorhabditis briggsae |
A8X5H5 | GSK3_CAEBR | MNKQLLSCSLKSGKQVTMVVASVATDGVDQQVEISYYDQKVIGNGSFGVVFLAKLSTTNEMVAIKKVLQDKRFKNRELQIMRKLNHPNIVKLKYFFYSSGDKKDELYLNLILEYVPETVYRVARHYSKQRQSIPMIYVKLYMYQLLRSLAYIHSIGICHRDIKPQNLLIDPETGILKLCDFGSAKYLVRNEPNVSYICSRYYRAPELIFGATNYTNSIDVWSAGTVIAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIQSMNPNYKEFKFPQIKAHPWNKVFRVHTPAEAIDLISKIIEYTPTSRPTPQAACQHAFF... | 2.7.11.26 | null | cell differentiation [GO:0030154]; engulfment of apoptotic cell [GO:0043652]; establishment of mitotic spindle orientation [GO:0000132]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; germ cell development [GO:0007281]; insulin receptor signaling pathway [GO:0008286]; left/right axis specifica... | axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; tau-protein kinase activity [GO:0050321] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, GSK-3 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26; Evidence={ECO:0000250|UniProtKB:P49841}... | null | null | null | null | FUNCTION: Phosphorylates oma-1, a regulator of the oocyte-to-embryo transition, enabling its degradation. Phosphorylates skn-1, preventing it from accumulating in nuclei and thus inhibiting phase II gene expression in the oxidative stress defense. Involved in mesendoderm specification and mitotic spindle orientation in... | Caenorhabditis briggsae |
A8X633 | APR1_CAEBR | MSSSSSDENETTIHSSSNPGSSGIYSQLKAGSSKRPSVRHDVSDAEDDEEPYEGFRKDMNMEVDERITTLLSSLHFEHKRDVVTADEDDNKLRELHENIFSLITTEPDFHRRRRLKKALPASNCIREQVYYLRRKPITPPDSYYHRLNAALHTIVKESFGEEYRKVATVLGLVEALAEVLILEVHAFGIPETNAVEHRNIRKLIANALTNLTYGQILSKRRLCSYDGFIRCVVRIIIESPNITQVYAGLIRNLSWNADSGMSEALQPTVHALSLAAVYAHTHRFDVTAILSALWNLAGHSVENKRTICETPNCLKVLANI... | null | null | asymmetric cell division [GO:0008356]; cell cycle [GO:0007049]; cell fate specification [GO:0001708]; cell migration [GO:0016477]; cellular component organization [GO:0016043]; embryonic morphogenesis [GO:0048598]; endoderm development [GO:0007492]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; n... | adherens junction [GO:0005912]; beta-catenin destruction complex [GO:0030877]; catenin complex [GO:0016342]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; nucleus [GO:0005634] | beta-catenin binding [GO:0008013]; gamma-catenin binding [GO:0045295]; microtubule binding [GO:0008017] | null | 1.25.10.10; | Adenomatous polyposis coli (APC) family | null | SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250|UniProtKB:Q21227}. Cytoplasm {ECO:0000250|UniProtKB:Q21227}. Nucleus {ECO:0000250|UniProtKB:Q21227}. Note=Found in clusters near the ends of microtubules that extend into regions of actively migrating plasma membranes. Shuttles between the cytoplasm an... | null | null | null | null | null | FUNCTION: Has a role in endoderm cell specification and pharyngeal development. Required for the migration of epithelial cells, organization of the anterior seam cells and ceh-13 expression during embryo morphogenesis. Prevents hyperactivation of the Wnt signaling pathway during endoderm development, probably by preven... | Caenorhabditis briggsae |
A8X811 | WRM1_CAEBR | MEERGPDIEKYGSQPCTPLSFDPMLPSTSRVATPVRPSSTLSARQAPASPFRAQPQNMEPSISRVHELREGAAVKRSYTNDWMQGNYIPPNPQQQQYQRPPSMIGSTISNMSNLSHMTKFSALSVNTQCGQFDNWIYQSQPALSKVSHSSVENQDPMKRRERMSIPEIVQSLASYEMSDQVAAIRELEPLAKAEALESTYCQADLGKIINALFEVLVPRPQENENVIRKVFEILHRAAVPKHVRMTEKIFHSLNLELMNTNSSKHSFQVPRPYSIYELVIERASRLDTAYDQAAMLLLAQICCKPFFMKYVFSEKEQSAG... | null | null | asymmetric protein localization involved in cell fate determination [GO:0045167]; canonical Wnt signaling pathway [GO:0060070]; cell-cell adhesion [GO:0098609]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic body morphogenesis [GO:0010172]; endoderm development [GO:0007492]; endodermal cell ... | adherens junction [GO:0005912]; catenin complex [GO:0016342]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; serine/threonine protein kinase complex [GO:1902554] | alpha-catenin binding [GO:0045294]; cadherin binding [GO:0045296]; DNA-binding transcription factor binding [GO:0140297]; nuclear receptor binding [GO:0016922]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein phosphatase binding [GO:0019903]; protein serine/threonine kinase activator ... | null | 1.25.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q10953}. Nucleus {ECO:0000250|UniProtKB:Q10953}. Note=Located in the anterior cell cortex before and during asymmetric cell division. After division, located preferentially in the nucleus of the posterior daughter cell (By similarity). {ECO:0000250|Uni... | null | null | null | null | null | FUNCTION: Antagonistic role in the Wnt signaling pathway that operates in embryogenesis (By similarity). When located at the cortex it has been shown to inhibit Wnt signaling during asymmetric cell division but when relocated to the nucleus it shows positive regulation (By similarity). Has a role in blastomere signalin... | Caenorhabditis briggsae |
A8Y987 | VP2_POVSM | MGALLAVLAEVVELASVTGLSVESFISGEAFATAELLEAHIANLVTVGGLTEAEALAATEVPAEAYAALTSLSSTFPQAFTAVAATELATTGTLTVGATVAAALYPYYYDYSTPVANLNRGLNPEMALQLWFPEIDYEFPGLMPFVRFINYIDPTQWATNLFETIGRYSWESAQRYGQNLIAHEVRSASRELATRTAQGFSEAVARYFENARWAVSTLPRSLYSGLQSYYEQLPSLNPMQVRDLHRRLGQPIPNRIALEEQAIKSAEYVQKVDPPGGANQRIAPDWLLPLILGLYGDISPSWESTLEDIEEEEDAPQKKK... | null | null | symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732] | host cell [GO:0043657]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; viral capsid [GO:0019028] | DNA binding [GO:0003677]; structural molecule activity [GO:0005198] | PF00761; | null | Polyomaviruses capsid protein VP2 family | null | SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}. | null | null | null | null | null | FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic ret... | Squirrel monkey polyomavirus |
A8YPR6 | SVMI_ECHOC | MFVSRLAASGLLLLSLLALSLDGKPLPQRQPHHIQPMEQKWLAPDAPPLEQKWLAPDAPPLEQKWLAPAAPPLEQKWLAPDAPPMEQKWLAPDAPPMEQKWLAPDAPPMEQKWLAPDAPPMEQKWLAPDAAPLEQKWLAPDAPPMEQKWLAPDAPPMEQKWQPQIPSLMEQRQLSSGGTTALRQELSPRAEAASGPAVVGGGGGGGGGSKAALALPKPPKAKGAAAATSRLMRDLRPDGKQASQKWGRLVDHDHDHHHHHHPGSSVGGGGGGGGGGARRLKGLAKKGVAKGCFGLKLDRIGSMSGLGC | null | null | cGMP biosynthetic process [GO:0006182]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of blood pressure [GO:0008217]; vasodilation [GO:0042311] | extracellular region [GO:0005576] | hormone activity [GO:0005179]; peptidase inhibitor activity [GO:0030414]; toxin activity [GO:0090729] | PF00212; | null | Natriuretic peptide family; PHpG family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18029259}. | null | null | null | null | null | FUNCTION: pEKW and poly-His-poly-Gly peptides may serve as metalloproteinase inhibitors during glandular storage. Their inhibition may be instantly disengaged, by dilution or physiochemical change, when venom is injected into tissue of the prey. {ECO:0000303|PubMed:18029259}.; FUNCTION: [C-type natriuretic peptide]: ha... | Echis ocellatus (Ocellated saw-scaled viper) |
A8YPR9 | SVMI1_CERCE | MSVSRLAASGLLLVSLLALALDGKPVEKWSPWLWPPRPRPPIPPLQQQKWLDPPIPQQQKWLDPPIPQQQKWLDPPIPQQQKWLNPPIPQQQKWLDPPIPQQQKWLNPPIPQQQKWLNPPIPQQQKWLNPPIPQQQKWLNPPIPQQQKWLDPPIPQQQKWLDPPIPQQQKWLDPPIPQQQKWLNPPIPQQQKWLDPPIPQQQKWLDPPIPQQQKWLNPPIPQQQKWQRPLQPEVPSLMELHQERQKQGRMMHHDEDPGDAAEGPRRQKKEPGKPEGNGCFGKKIDRINAGFGCPKLPPSGGH | null | null | regulation of blood pressure [GO:0008217]; vasodilation [GO:0042311] | extracellular region [GO:0005576] | peptidase inhibitor activity [GO:0030414]; toxin activity [GO:0090729] | null | null | Natriuretic peptide family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18029259}. | null | null | null | null | null | FUNCTION: pEKW peptides may serve as metalloproteinase inhibitors during glandular storage. Their inhibition may be instantly disengaged, by dilution or physiochemical change, when venom is injected into tissue of the victim. {ECO:0000269|PubMed:18029259}.; FUNCTION: [C-type natriuretic peptide]: Exhibits hypotensive a... | Cerastes cerastes (Horned desert viper) |
A8YZP8 | HCHA_STAAT | MSQDVNELSKQPTPDKAEDNAFFPSPYSLSQYTAPKTDFDGVEHKGAYKDGKWKVLMIAAEERYVLLENGKMFSTGNHPVEMLLPLHHLMEAGFDVDVATLSGYPVKLELWAMPTEDEAVISTYNKLKEKLKQPKKLADVIKNELGPDSDYLSVFIPGGHAAVVGISESEDVQQTLDWALDNDRFIVTLCHGPAALLSAGLNREKSPLEGYSVCVFPDSLDEGANIEIGYLPGRLKWLVADLLTKQGLKVVNDDMTGRTLKDRKLLTGDSPLASNELGKLAVNEMLNAIQNK | 3.1.2.-; 3.5.1.-; 3.5.1.124 | null | DNA repair [GO:0006281]; methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243]; protein repair [GO:0030091] | cytoplasm [GO:0005737] | glyoxalase III activity [GO:0019172]; protein deglycase activity [GO:0036524]; thiolester hydrolase activity [GO:0016790] | PF01965; | 3.40.50.880; | Peptidase C56 family, HchA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01046}. | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Staphylococcus aureus (strain USA300 / TCH1516) |
A9BHI9 | GPGS_PETMO | MKDNILKRSFHHSKFENIKELVKLKEKQDVKISLAFPSLNEEKTIGKEIIIMKSELMEKYPLLDEIAVIDSGSEDETVSIAKEYGAKVFYSSDILPEYGFYKGKGENLWKSLYALDGDIIVWVDSDIENIHPKFVYGLVGALLNYPEIGYVKAFYDRPIVGKSAMQPTGGGRVTELVARPLFSLFYPELSTIIQPLSGEYAGRREILEKLPFFVGYGVEIAHLIDIAEKFGSEIIAQVDLELRIHDNQPLHSLSKMAFELTKVVLKRLEKYGKLDLNTELTDKHIMIQKKENEKVLVPTEILSVERPPMITIPEYKEKFS... | 2.4.1.266 | COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:20061481}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20061481}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:20061481}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:20061481}; Na... | null | null | glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872] | PF00535; | null | Glycosyltransferase 2 family | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + an NDP-alpha-D-glucose = (2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + a ribonucleoside 5'-diphosphate + H(+); Xref=Rhea:RHEA:47244, ChEBI:CHEBI:15378, ChEBI:CHEBI:57930, ChEBI:CHEBI:58272, ChEBI:CHEBI:62600, ChEBI:CHEBI:76533; EC=2.4.1.266; Evidence={ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 mM for 3-PGA (at 60 degrees Celsius) {ECO:0000269|PubMed:20061481}; KM=0.5 mM for 3-PGA (at 70 degrees Celsius) {ECO:0000269|PubMed:20061481}; KM=1 mM for UDP-glucose (at 60 degrees Celsius) {ECO:0000269|PubMed:20061481}; KM=0.9 mM for UDP-glucose (at 70 degree... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0 (at 60 degrees Celsius). {ECO:0000269|PubMed:20061481}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70 degrees Celsius. {ECO:0000269|PubMed:20061481}; | FUNCTION: Involved in the biosynthesis of the compatible solute mannosylglucosylglycerate through a phosphorylating pathway. Catalyzes the transfer of the glucose moiety from a nuleotide sugar such as UDP-alpha-D-glucose to the position 2 of 3-phospho-D-glycerate (3-PGA) to form glucosyl-3-phosphoglycerate (GPG). UDP-g... | Petrotoga mobilis (strain DSM 10674 / SJ95) |
A9C3R8 | RP65C_DANRE | MVSRLEHPAGGYKKVFESCEELAEPIPAHVSGEIPAWLSGSLLRMGPGLFEVGDEPFYHLFDGQALLHKFDLKDGRVTYHRRFIRTDAYVRAMTEKRVVITEFGTTAYPDPCKNIFSRFFTYFQGIEVTDNCLVNIYPIGEDFYACTETNFITKVDPDTLETVKKVDLCNYLSVNGLTAHPHIEADGTVYNIGNCFGKNMSLAYNIVKIPPLQEDKSDQFEKSKILVQFPSSERFKPSYVHSFGITENHFVFVETPVKINLLKFLTSWSIRGSNYMDCFESNDKMGTWFHLAAKNPGKYIDHKFRTSAFNIFHHINCFED... | 3.1.1.64; 3.1.1.90; 5.3.3.22 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000305|PubMed:21676174}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000305|PubMed:21676174}; | retinal metabolic process [GO:0042574]; retinoid metabolic process [GO:0001523]; zeaxanthin biosynthetic process [GO:1901827] | cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; plasma membrane [GO:0005886] | all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity [GO:0052885]; all-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity [GO:0052884]; beta-carotene 15,15'-dioxygenase activity [GO:0003834]; metal ion binding [GO:0046872]; retinol isomerase activity [GO:0050251] | PF03055; | null | Carotenoid oxygenase family | PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q28175}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21676174}. Cell membrane {ECO:0000269|PubMed:21676174}; Lipid-anchor {ECO:0000269|PubMed:21676174}. Note=Attached to the membrane by a lipid anchor when palmitoylated (membrane form), soluble when unpalmitoylated. {ECO:0000250|UniProtKB:Q28175}. | CATALYTIC ACTIVITY: Reaction=an all-trans-retinyl ester + H2O = 13-cis-retinol + a fatty acid + H(+); Xref=Rhea:RHEA:31779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:45479, ChEBI:CHEBI:63410; EC=3.1.1.90; Evidence={ECO:0000269|PubMed:21676174}; CATALYTIC ACTIVITY: Reaction=lutein = (3R,3'S)-z... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.91 uM for 11-cis retinol {ECO:0000269|PubMed:21676174}; KM=2.95 uM for 13-cis retinol {ECO:0000269|PubMed:21676174}; Vmax=1.82 nmol/h/mg enzyme for 11-cis retinol {ECO:0000269|PubMed:21676174}; Vmax=0.91 nmol/h/mg enzyme for 13-cis retinol {ECO:0000269|PubMed:216... | null | null | null | FUNCTION: Catalyzes both 11-cis retinol and 13-cis retinol, 2 stereoisomeric forms of retinoic acid from all-trans-retinyl ester. Acts as an alternative isomerohydrolase in retinal Mueller cells by catalyzing formation of 11-cis retinol, to meet the high demand for the chromophore by cones (PubMed:21676174). Capable of... | Danio rerio (Zebrafish) (Brachydanio rerio) |
A9C3R9 | RP65B_DANRE | MVSRLEHPAGGYKKVFESCEELAEPIPAHVSGKIPAWLSGSLLRMGPGLFEIGDEPFNHLFDGQALIHKFDLKDGRVTYHRKFIRTDAYVRAMTEKRVVITELGTAAYPDPCKNIFSRFFTYFQGTEVTDNCSVNIYPIGEDFYACTETNFITKVNPDTLETIKKVDLCNYLSVNGLTAHPHIEADGTVYNIGNCFGKNMSLAYNIVKIPPLQEEKSDPLAMSKVLVQFPSSERFKPSYVHSFGMTENHFVFVETPVKINLLKFLTSWSIRGSNYMDCFESNDRMGTWFHLAAKNPGKYIDHKFRTSAFNIFHHINCFED... | 3.1.1.90; 5.3.3.22 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000305|PubMed:21235714}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000305|PubMed:21235714}; | retinal metabolic process [GO:0042574]; retinoid metabolic process [GO:0001523]; zeaxanthin biosynthetic process [GO:1901827] | endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886] | all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity [GO:0052885]; beta-carotene 15,15'-dioxygenase activity [GO:0003834]; metal ion binding [GO:0046872]; retinol isomerase activity [GO:0050251] | PF03055; | null | Carotenoid oxygenase family | PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q28175}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21235714}. Cell membrane {ECO:0000269|PubMed:21235714}; Lipid-anchor {ECO:0000269|PubMed:21235714}. Note=Attached to the membrane by a lipid anchor when palmitoylated (membrane form), soluble when unpalmitoylated. {ECO:0000250|UniProtKB:Q28175}. | CATALYTIC ACTIVITY: Reaction=an all-trans-retinyl ester + H2O = 13-cis-retinol + a fatty acid + H(+); Xref=Rhea:RHEA:31779, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:45479, ChEBI:CHEBI:63410; EC=3.1.1.90; Evidence={ECO:0000269|PubMed:21235714}; CATALYTIC ACTIVITY: Reaction=lutein = (3R,3'S)-z... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.6 uM for all-trans-retinyl ester {ECO:0000269|PubMed:21235714}; Note=kcat is 0.00044 sec(-1) with all-trans-retinyl ester as substrate.; | null | null | null | FUNCTION: Specifically generates 13-cis retinol, a stereoisomeric form of retinoic acid. Capable of catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid (By similarity). {ECO:0000250|UniProtKB:Q16518, ECO:0000269|PubMed:21235714}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A9CB27 | ZPR1_PAPAN | MAASGAVEPGPPGAAVAPSPALAPPPAPDHLFRPISAEDEEQQPTEIESLCMNCYCNGMTRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRVQDQGVRYTLTVRAPEDMNREVVKTDSATTRIPELDFEIPAFSQKGALTTVEGLITRAISGLEQDQPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHAPQKDDSLVITHYNRTQHQKEMLGLQEEAPAEKPEEEDLRNEVLQFNTNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSD... | null | null | apoptotic process involved in development [GO:1902742]; axon development [GO:0061564]; Cajal body organization [GO:0030576]; cellular response to epidermal growth factor stimulus [GO:0071364]; DNA endoreduplication [GO:0042023]; DNA replication [GO:0006260]; microtubule cytoskeleton organization [GO:0000226]; mRNA proc... | axon [GO:0030424]; Cajal body [GO:0015030]; cytoplasm [GO:0005737]; Gemini of coiled bodies [GO:0097504]; growth cone [GO:0030426]; neuronal cell body [GO:0043025]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471] | protein folding chaperone [GO:0044183]; translation initiation factor binding [GO:0031369]; zinc ion binding [GO:0008270] | PF03367; | 2.60.120.1040;2.20.25.420; | ZPR1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Nucleus, gem {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Note=Localized predominantl... | null | null | null | null | null | FUNCTION: Acts as a signaling molecule that communicates proliferative growth signals from the cytoplasm to the nucleus. Plays a role for the localization and accumulation of the survival motor neuron protein SMN1 in sub-nuclear bodies, including gems and Cajal bodies. Induces neuron differentiation and stimulates axon... | Papio anubis (Olive baboon) |
A9CH28 | DPES_AGRFC | MKHGIYYSYWEHEWSAKFGPYIEKVAKLGFDIIEVAAHHINEYSDAELATIRKSAKDNGIILTAGIGPSKTKNLSSEDAAVRAAGKAFFERTLSNVAKLDIHTIGGALHSYWPIDYSQPVDKAGDYARGVEGINGIADFANDLGINLCIEVLNRFENHVLNTAAEGVAFVKDVGKNNVKVMLDTFHMNIEEDSFGDAIRTAGPLLGHFHTGESNRRVPGKGRMPWHEIGLALRDINYTGAVIMEPFVKTGGTIGSDIKVWRDLSGGADIAKMDEDARNALAFSRFVLGG | 5.1.3.30 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16461638, ECO:0000269|PubMed:16876192}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:16461638}; Note=Binds 1 Mn(2+) or Co(2+) ion per subunit. {ECO:0000269|PubMed:16461638, ECO:0000269|PubMed:16876192}; | null | null | cobalt ion binding [GO:0050897]; manganese ion binding [GO:0030145]; racemase and epimerase activity, acting on carbohydrates and derivatives [GO:0016857] | PF01261; | 3.20.20.150; | Hyi family | null | null | CATALYTIC ACTIVITY: Reaction=D-allulose = keto-D-fructose; Xref=Rhea:RHEA:42360, ChEBI:CHEBI:27605, ChEBI:CHEBI:48095; EC=5.1.3.30; Evidence={ECO:0000269|PubMed:16461638}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12 mM for D-psicose (at pH 8 and 50 degrees Celsius) {ECO:0000269|PubMed:16461638}; KM=762 mM for D-tagatose (at pH 8 and 50 degrees Celsius) {ECO:0000269|PubMed:16461638}; Note=kcat is 2381 min(-1) for epimerase activity with D-psicose as substrate (at pH 8 and 50... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:16461638}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. The activity of D-psicose 3-epimerase is very stable below 45 degrees Celsius but decreases above 50 degrees Celsius with increasing reaction time. {ECO:0000269|PubMed:16461638}; | FUNCTION: Involved in the biosynthesis of D-psicose. Catalyzes the reversible epimerization of D-fructose at the C3 position to yield D-psicose. The enzyme is highly specific for D-psicose and shows very low activity with D-tagatose. The substrate specificity decreases in the following order: D-fructose, D-tagatose, D-... | Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58)) |
A9CH39 | PHRB_AGRFC | MSQLVLILGDQLSPSIAALDGVDKKQDTIVLCEVMAEASYVGHHKKKIAFIFSAMRHFAEELRGEGYRVRYTRIDDADNAGSFTGEVKRAIDDLTPSRICVTEPGEWRVRSEMDGFAGAFGIQVDIRSDRRFLSSHGEFRNWAAGRKSLTMEYFYREMRRKTGLLMNGEQPVGGRWNFDAENRQPARPDLLRPKHPVFAPDKITKEVIDTVERLFPDNFGKLENFGFAVTRTDAERALSAFIDDFLCNFGATQDAMLQDDPNLNHSLLSFYINCGLLDALDVCKAAERAYHEGGAPLNAVEGFIRQIIGWREYMRGIYWL... | 4.1.99.13 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:22066008, ECO:0000269|PubMed:23589886}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:23589886}; COFACTOR: Name=6,7-dimethyl-8-(1-D-ribityl)lumazine; Xref=ChEBI:CHEBI:58201; Evidence={ECO:0000269|PubMed:23589886}; Note=Binds 6,7-dimethyl-8-rib... | photoreactive repair [GO:0000719] | null | 4 iron, 4 sulfur cluster binding [GO:0051539]; DNA (6-4) photolyase activity [GO:0003914]; DNA binding [GO:0003677]; FAD binding [GO:0071949]; metal ion binding [GO:0046872] | PF04244; | 1.25.40.80;1.10.10.1710;1.10.579.10;3.40.50.620; | Iron-sulfur bacterial cryptochrome/photolyase (FeS-BCP) family | null | null | CATALYTIC ACTIVITY: Reaction=(6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA).; EC=4.1.99.13; Evidence={ECO:0000269|PubMed:23589886}; | null | null | null | null | FUNCTION: Photolyase involved in the repair of UV-induced (6-4) lesions in DNA. Catalyzes the photoreactivation of (6-4) pyrimidine-pyrimidone photoproducts by using blue-light energy. Can repair (6-4) photoproducts in ssDNA as well as in dsDNA. {ECO:0000269|PubMed:23589886}. | Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58)) |
A9CJC9 | PHRA_AGRFC | MSLKTAPVIVWFRKDLRLSDNLALLAAVEHGGPVIPVYIREKSAGPLGGAQEWWLHHSLAALSSSLEKAGGRLVLASGDAERILRDLISETGADTVVWNRRYDPTGMATDKALKQKLRDDGLTVRSFSGQLLHEPSRLQTKSGGPYRVYTPFWRALEGSDEPHAPADPPKSLTAPKVWPKSEKLSNWKLLPTKPDWAKDFSDIWTPGETGALDKLDDFIDGALKGYEEGRDFPAKPATSLLSPHLAAGEISPAAVWHATKGLSRHIASNDISRFRKEIVWREFCYHLLFHFPELGEKNWNDSFDAFSWRDDEKSFKAWTR... | 4.1.99.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:22066008}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:22066008}; COFACTOR: Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate; Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000269|PubMed:22066008}; Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) ... | circadian regulation of gene expression [GO:0032922]; entrainment of circadian clock by photoperiod [GO:0043153]; photoreactive repair [GO:0000719] | cytoplasm [GO:0005737] | deoxyribodipyrimidine photo-lyase activity [GO:0003904]; DNA binding [GO:0003677]; FAD binding [GO:0071949] | PF00875;PF03441; | 1.25.40.80;1.10.579.10;3.40.50.620; | DNA photolyase class-3 family | null | null | CATALYTIC ACTIVITY: Reaction=cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA).; EC=4.1.99.3; Evidence={ECO:0000269|PubMed:22066008}; | null | null | null | null | FUNCTION: Photolyase involved in the repair of UV radiation-induced DNA damage. By using blue-light energy, catalyzes the photoreactivation of cyclobutane pyrimidine dimers (CPDs), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation. Can repair CPD lesions in ssDNA as w... | Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58)) |
A9CK16 | TADA_AGRFC | MAERTHFMELALVEARSAGERDEVPIGAVLVLDGRVIARSGNRTRELNDVTAHAEIAVIRMACEALGQERLPGADLYVTLEPCTMCAAAISFARIRRLYYGAQDPKGGAVESGVRFFSQPTCHHAPDVYSGLAESESAEILRQFFREKRLDD | 3.5.4.33 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00972, ECO:0000269|PubMed:16142903}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00972, ECO:0000269|PubMed:16142903}; | cytidine metabolic process [GO:0046087]; cytosine metabolic process [GO:0019858]; pyrimidine-containing compound salvage [GO:0008655]; tRNA wobble adenosine to inosine editing [GO:0002100] | null | cytosine deaminase activity [GO:0004131]; tRNA-specific adenosine-34 deaminase activity [GO:0052717]; zinc ion binding [GO:0008270] | PF14437; | 3.40.140.10; | Cytidine and deoxycytidylate deaminase family | null | null | CATALYTIC ACTIVITY: Reaction=adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+); Xref=Rhea:RHEA:43168, Rhea:RHEA-COMP:10373, Rhea:RHEA-COMP:10374, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.33; Evidence={ECO:0000255|HAMAP-Rule:MF_00972, ECO:000... | null | null | null | null | FUNCTION: Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2). {ECO:0000255|HAMAP-Rule:MF_00972, ECO:0000269|PubMed:16142903}. | Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58)) |
A9CMA6 | TM163_RAT | MERAPGSERRSPPGPGVPRPPPRGHAPSTAAPAPNPAPLSSSMQPDEERQPRISESGQFSDGFEDRGLLESSTRLKPHEAQNYRKKALWVSWLSIIVTLALAVAAFTVSVMRYSASAFGFAFDAILDVLSSAIVLWRYSNAAAVHSAHREYIACVILGVIFLLSSICIVVKAIHDLSTRLLPEVDDFLFSVSILSGILCSVLAVLKFMLGKVLTSRALITDGFNSLVGGVMGFSILLSAEVFKHNAAVWYLDGSIGVLIGLTIFAYGVKLLIDMVPRVRQTRHYEMFE | null | null | myelination [GO:0042552]; zinc export across plasma membrane [GO:0140882]; zinc ion import into synaptic vesicle [GO:0099180] | early endosome membrane [GO:0031901]; intracellular vesicle [GO:0097708]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; plasma membrane [GO:0005886]; synaptic vesicle membrane [GO:0030672] | zinc ion binding [GO:0008270] | null | 1.20.1510.10; | TMEM163 family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:17623043}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:21668449}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q8TC26}; Multi... | CATALYTIC ACTIVITY: Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351, ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q8TC26}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29352; Evidence={ECO:0000250|UniProtKB:Q8TC26}; | null | null | null | null | FUNCTION: Zinc ion transporter that mediates zinc efflux and plays a crucial role in intracellular zinc homeostasis (By similarity). Binds the divalent cations Zn(2+), Ni(2+), and to a minor extent Cu(2+) (PubMed:21668449). Is a functional modulator of P2X purinoceptors, including P2RX1, P2RX3, P2RX4 and P2RX7 (By simi... | Rattus norvegicus (Rat) |
A9FDB7 | CP260_SORC5 | MDFPLANLFFVPSEDATAFGRRLRAAAQQAPIVFDTAFGMPILLRKSHITTAYRDTATFSTRMFQAGILNGGLAAMQGDEHARMRRVYNMFFLPRAVSQYEERFVRPISEQVVDRLAGKPRVDLLEDFAMELPRRVIGELFGFPAEKLHETDERVRAMLRGLVRMHDPAAVAESQRAYGETLGLITEVVERESRDTSDTLLGEILRTLKAEHMDTIEASRQIVLSLILGGYETTSWLVANTIHALLAHPDTLARVRQDPSLLPAAIEEGMRWCPSSFGVLRMVERDVRLDDQALSAGTVVCLAGIAGNYDETAYPSPEVY... | 1.14.15.19 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:27878817, ECO:0000269|PubMed:29509407}; | cholesterol catabolic process [GO:0006707] | null | cholest-4-en-3-one 26-monooxygenase activity [GO:0036199]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; steroid hydroxylase activity [GO:0008395] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | null | CATALYTIC ACTIVITY: Reaction=2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] + testosterone = 1alpha-hydroxytestosterone + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:50340, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17347, ChEBI:CHEBI:33737... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.12 uM for nootkatone (in the presence of FdR_B and Fdx2) {ECO:0000269|PubMed:19696019}; KM=0.54 uM for nootkatone (in the presence of FdR_B and Fdx8) {ECO:0000269|PubMed:19696019}; KM=40 uM for testosterone {ECO:0000269|PubMed:26478560}; KM=31 uM for androstenedi... | null | null | null | FUNCTION: Hydroxylase that can catalyze the in vitro conversion of the sesquiterpenoid nootkatone, a natural organic compound produced by some plants, to at least five hydrophilic products (PubMed:19696019). The native ferredoxin reductase FdR_B and either Fdx2 or Fdx8 ferredoxins can act as the redox partners for the ... | Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So ce56)) |
A9JRL3 | CBPC1_XENTR | MSKAKATADKCLSNNSRIQSLLSQLEKVNAEPLLFDSDNTRYVTAKILHLAQTQEKTRKEIAAKGSTGMEVILCTLENTRDLQTILNILNILNELASTAGGRRINALISKGGSRILLQLLLSASKESSSNEELMMVLHSLLAKVGPKDKKFGIKARVSGALNISLNLVKQNLQNPRLILPCLQVLRVCCMNSVNSVYLGKNGAVEILFKLIGPFTRRNTGLIKVSLDTFAALLKSKTNARKAVDRGYVQALLSIYTDWHRHDTRHRHMLIRKGILQCLKSITNIKIGRKAFIDANGMKTLYNTSQECQAVRTLDPLVNTS... | 3.4.17.-; 3.4.17.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | C-terminal protein deglutamylation [GO:0035609]; cerebellar Purkinje cell differentiation [GO:0021702]; eye photoreceptor cell differentiation [GO:0001754]; mitochondrion organization [GO:0007005]; neuromuscular process [GO:0050905]; olfactory bulb development [GO:0021772]; protein side chain deglutamylation [GO:003561... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | metallocarboxypeptidase activity [GO:0004181]; tubulin binding [GO:0015631]; zinc ion binding [GO:0008270] | PF18027;PF00246; | 2.60.40.3120;1.25.10.10;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UPW5}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q641K1}. Nucleus {ECO:0000250|UniProtKB:Q641K1}. Mitochondrion {ECO:0000250|UniProtKB:Q641K1}. | CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + H2O = (L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + L-glutamate; Xref=Rhea:RHEA:60004, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:143623; Evidence={ECO:0000250|UniProtKB:Q6... | null | null | null | null | FUNCTION: Metallocarboxypeptidase that mediates protein deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of alpha- and beta-tubulin. Specifically cleaves tubulin long-side-c... | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A9JTM7 | OTOP3_XENTR | MLSKEEPACRQFHSREKTWGNEHNGKTVTQANNKEHKVPAVRRGDIGQREPAAHPASHIQGTMASENTGEQATCKDQYMDLDAPGNNLEHSWLHRHCEIPTTLHQRAKKTGRLFSGLFGLNLMFLGGTVVSSVALSNKAVPERDSQSFLCILMLLSSVWALYHLLFIRNQNGAVHHDHHAGAMWLKASLAIFGVCSIILSIFEIGHALLLQNCEILMDIVFFSIEIVFVSVQTVLLWVSCKDCVQMHHSVTRYGIMLTLATDILLWLTAVIDDSLEQDLEILQSNSTQDESNEMAQCQCPTDSMCWGLKQGYVTMFPFNI... | null | null | proton transmembrane transport [GO:1902600] | plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; proton channel activity [GO:0015252] | PF03189; | null | Otopetrin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30973323}; Multi-pass membrane protein {ECO:0000269|PubMed:30973323}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000269|PubMed:30973323}; | null | null | null | null | FUNCTION: Proton-selective channel gated by extracellular protons. {ECO:0000269|PubMed:30973323}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
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