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 | MWAQLLLGMLALSPAIAEELPNYLVTLPARLNFPSVQKVCLDLSPGYSDVKFTVTLETKDKTQKLLEYSGLKKRHLHCISFLVPPPAGGTEEVATIRVSGVGNNISFEEKKKVLIQRQGNGTFVQTDKPLYTPGQQVYFRIVTMDSNFVPVNDKYSMVELQDPNSNRIAQWLEVVPEQGIVDLSFQLAPEAMLGTYTVAVAEGKTFGTFSVEEYVLPKFKVEVVEPKELSTVQESFLVKICCRYTYGKPMLGAVQVSVCQKANTYWYREVEREQLPDKCRNLSGQTDKTGCFSAPVDMATFDLIGYAYSHQINIVATVVEEGTGVEANATQNIYISPQMGSMTFEDTSNFYHPNFPFSGKIRVRGHDDSFLKNHLVFLVIYGTNGTFNQTLVTDNNGLAPFTLETSGWNGTDVSLEGKFQMEDLVYNPEQVPRYYQNAYLHLRPFYSTTRSFLGIHRLNGPLKCGQPQEVLVDYYIDPADASPDQEISFSYYLIGKGSLVMEGQKHLNSKKKGLKASFSLSLTFTSRLAPDPSLVIYAIFPSGGVVADKIQFSVEMCFDNQVSLGFSPSQQLPGAEVELQLQAAPGSLCALRAVDESVLLLRPDRELSNRSVYGMFPFWYGHYPYQVAEYDQCPVSGPWDFPQPLIDPMPQGHSSQRSIIWRPSFSEGTDLFSFFRDVGLKILSNAKIKKPVDCSHRSPEYSTAMGAGGGHPEAFESSTPLHQAEDSQVRQYFPETWLWDLFPIGNSGKEAVHVTVPDAITEWKAMSFCTSQSRGFGLSPTVGLTAFKPFFVDLTLPYSVVRGESFRLTATIFNYLKDCIRVQTDLAKSHEYQLESWADSQTSSCLCADDAKTHHWNITAVKLGHINFTISTKILDSNEPCGGQKGFVPQKGRSDTLIKPVLVKPEGVLVEKTHSSLLCPKGKVASESVSLELPVDIVPDSTKAYVTVLGDIMGTALQNLDGLVQMPSGCGEQNMVLFAPIIYVLQYLEKAGLLTEEIRSRAVGFLEIGYQKELMYKHSNGSYSAFGERDGNGNTWLTAFVTKCFGQAQKFIFIDPKNIQDALKWMAGNQLPSGCYANVGNLLHTAMKGGVDDEVSLTAYVTAALLEMGKDVDDPMVSQGLRCLKNSATSTTNLYTQALLAYIFSLAGEMDIRNILLKQLDQQAIISGESIYWSQKPTPSSNASPWSEPAAVDVELTAYALLAQLTKPSLTQKEIAKATSIVAWLAKQHNAYGGFSSTQDTVVALQALAKYATTAYMPSEEINLVVKSTENFQRTFNIQSVNRLVFQQDTLPNVPGMYTLEASGQGCVYVQTVLRYNILPPTNMKTFSLSVEIGKARCEQPTSPRSLTLTIHTSYVGSRSSSNMAIVEVKMLSGFSPMEGTNQLLLQQPLVKKVEFGTDTLNIYLDELIKNTQTYTFTISQSVLVTNLKPATIKVYDYYLPDEQATIQYSDPCE | 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 traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity). Displays inhibitory activity against chymotrypsin, papain, thermolysin, subtilisin A and, to a lesser extent, elastase but not trypsin. May play an important role during desquamation by inhibiting extracellular proteases. {ECO:0000250|UniProtKB:P01023, ECO:0000269|PubMed:16298998}. | 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 | MGPFKSSVFILILHLLEGALSNSLIQLNNNGYEGIVVAIDPNVPEDETLIQQIKDMVTQASLYLLEATGKRFYFKNVAILIPETWKTKADYVRPKLETYKNADVLVAESTPPGNDEPYTEQMGNCGEKGERIHLTPDFIAGKKLAEYGPQGRAFVHEWAHLRWGVFDEYNNDEKFYLSNGRIQAVRCSAGITGTNVVKKCQGGSCYTKRCTFNKVTGLYEKGCEFVLQSRQTEKASIMFAQHVDSIVEFCTEQNHNKEAPNKQNQKCNLRSTWEVIRDSEDFKKTTPMTTQPPNPTFSLLQIGQRIVCLVLDKSGSMATGNRLNRLNQAGQLFLLQTVELGSWVGMVTFDSAAHVQNELIQINSGSDRDTLAKRLPAAASGGTSICSGLRSAFTVIRKKYPTDGSEIVLLTDGEDNTISGCFNEVKQSGAIIHTVALGPSAAQELEELSKMTGGLQTYASDQVQNNGLIDAFGALSSGNGAVSQRSIQLESKGLTLQNSQWMNGTVIVDSTVGKDTLFLITWTMQPPQILLWDPSGQKQGGFVVDKNTKMAYLQIPGIAKVGTWKYSLQASSQTLTLTVTSRASNATLPPITVTSKTNKDTSKFPSPLVVYANIRQGASPILRASVTALIESVNGKTVTLELLDNGAGADATKDDGVYSRYFTTYDTNGRYSVKVRALGGVNAARRRVIPQQSGALYIPGWIENDEIQWNPPRPEINKDDVQHKQVCFSRTSSGGSFVASDVPNAPIPDLFPPGQITDLKAEIHGGSLINLTWTAPGDDYDHGTAHKYIIRISTSILDLRDKFNESLQVNTTALIPKEANSEEVFLFKPENITFENGTDLFIAIQAVDKVDLKSEISNIARVSLFIPPQTPPETPSPDETSAPCPNIHINSTIPGIHILKIMWKWIGELQLSIA | 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) activation activity. {ECO:0000269|PubMed:23112050, ECO:0000269|PubMed:9828122}. | 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 predominantly localized to microvilli. | 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 the innate immune response. May play a role as a tumor suppressor. Induces MUC5AC. {ECO:0000269|PubMed:11445004, ECO:0000269|PubMed:11842292, ECO:0000269|PubMed:11956057, ECO:0000269|PubMed:23112050, ECO:0000269|PubMed:9828122}. | 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 | MKNLLTEKCISSHNFHQKVIKQRMEKKVDSRYFKDGAVKKPYSAKTLSNKKSSASFGIRRELPSTSHLVQYRGTHTCTRQGRLRELRIRCVARKFLYLWIRMTFGRVFPSKARFYYEQRLLRKVFEEWKEEWWVFQHEWKLCVRADCHYRYYLYNLMFQTWKTYVRQQQEMRNKYIRAEVHDAKQKMRQAWKSWLIYVVVRRTKLQMQTTALEFRQRIILRVWWSTWRQRLGQVRVSRALHASALKHRALSLQVQAWSQWREQLLYVQKEKQKVVSAVKHHQHWQKRRFLKAWLEYLQVRRVKRQQNEMAERFHHVTVLQIYFCDWQQAWERRESLYAHHAQVEKLARKMALRRAFTHWKHYMLLCAEEAAQFEMAEEHHRHSQLYFCFRALKDNVTHAHLQQIRRNLAHQQHGVTLLHRFWNLWRSQIEQKKERELLPLLHAAWDHYRIALLCKCIELWLQYTQKRRYKQLLQARADGHFQQRALPAAFHTWNRLWRWRHQENVLSARATRFHRETLEKQVFSLWRQKMFQHRENRLAERMAILHAERQLLYRSWFMWHQQAAARHQEQEWQTVACAHHRHGRLKKAFCLWRESAQGLRTERTGRVRAAEFHMAQLLRWAWSQWRECLALRGAERQKLMRADLHHQHSVLHRALQAWVTYQGRVRSILREVAARESQHNRQLLRGALRRWKENTMARVDEAKKTFQASTHYRRTICSKVLVQWREAVSVQMYYRQQEDCAIWEAQKVLDRGCLRTWFQRWWDCSRRSAQQRLQLERAVQHHHRQLLLEGLARWKTHHLQCVRKRLLHRQSTQLLAQRLSRTCFRQWRQQLAARRQEQRATVRALWFWAFSLQAKVWATWLAFVLERRRKKARLQWALQAYQGQLLQEGATRLLRFAASMKASRQQLQAQQQVQAAHSLHRAVRRCATLWKQKVLGRGGKPQPLAAIAPSRKVTFEGPLLNRIAAGAGDGTLETKRPQASRPLGALGRLAAEEPHALELNTAHSARKQPRRPHFLLEPAQSQRPQKPQEHGLGMAQPAAPSLTRPFLAEAPTALVPHSPLPGALSSAPGPKQPPTASTGPELLLLPLSSFMPCGAAAPARVSAQRATPRDKPPVPSSLASVPDPHLLLPGDFSATRAGPGLSTAGSLDLEAELEEIQQQLLHYQTTKQNLWSCRRQASSLRRWLELNREEPGPEDQEVEQQVQKELEQVEMQIQLLAEELQAQRQPIGACVARIQALRQALC | 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 | MGPPLAPRPAHVPGEAGPRRTRESRPGAVSFADVAVYFSPEEWECLRPAQRALYRDVMRETFGHLGALGFSVPKPAFISWVEGEVEAWSPEAQDPDGESSAAFSRGQGQEAGSRDGNEEKERLKKCPKQKEVAHEVAVKEWWPSVACPEFCNPRQSPMNPWLKDTLTRRLPHSCPDCGRNFSYPSLLASHQRVHSGERPFSCGQCQARFSQRRYLLQHQFIHTGEKPYPCPDCGRRFRQRGSLAIHRRAHTGEKPYACSDCKSRFTYPYLLAIHQRKHTGEKPYSCPDCSLRFAYTSLLAIHRRIHTGEKPYPCPDCGRRFTYSSLLLSHRRIHSDSRPFPCVECGKGFKRKTALEAHRWIHRSCSERRAWQQAVVGRSEPIPVLGGKDPPVHFRHFPDIFQECG | 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 | MDPTRPPFRGSPFHTPLGVRPPVLETKEEGPHGRAVLLPRGRALLGASAPSSDTTQRDPSDSRNVLPALFRGMGIETKPSGIPGRGGPVFGRGFLSTMSSGDGPDQPLSEPSIRPSLSTRVQQASDFSTERVALGRARFPIPPVSMEKPHVPTGRGLLFPSVLPTLTSDPVPKESPIATLQIEKEEKWEPLPKKGSKGSPCQLGLNLIKINFQNEAVYQYHVTFTPIVECRSMRFGMMKDHRSVTGPVTAFDGSILYLPVKLAQTVELESERRTDGQKIKITIQMTKILDPSSDLCLPFYNVVMRRVFKILDLKLVGRNFYDPASSTVLQQYRLQVWPGYAANIRKTDGGLFLLVDITHKIIRSDSVLDIMNILYQQSPENFQDEVTKQLVGSIVITRYNNRTYRIDDIEWNMSPKDSFSMSDGSKISFIDYYSKNYGITVKELDQPLLLHRPSERKAPKGKALDIVLLLPELAFMTGIPEKMRKDFRAMKDLTQQIHLSPKQHHISLGKLLKRIESSADAKNELQRWGLFLDTDIHMTTGRILPIEKINLRNNSFPAGEDLNWNREVTREACRSSVHLLYWAMIYPKRASAQAQELSSMLERIGGPIGIRVNHPNCVELRDDRVETYARSIKSLLEGEGKVQLLVCLISGTRDDLYGAIKKLCCVQNPVPSQVINTRTISQPQKLRSIAQKILLQINCKLGGELWGVDIPLKSVMVIGMDVYHDPSRGMRSVLGFVASINSCLTAWYSRVVFQLPNQEIMDSLKLCLVAALQKFFEVNHSLPEKIVVYRDGVSDGQLNTVENYEIPQLQTCFQTFDNYNPRMVVIVVQKRVSTNLYSTATGQFLTPQPGTVIDHTVTNRKWIDFFLMSHHVRQGCGIPTHYICVMNTANLGPDHLQRLTFKLCHMYWNWPGTIRVPAPCKYAHKLAFLSGQFLHHEPSIKLCDKLFFL | 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]; rhythmic process [GO:0048511]; siRNA-mediated retrotransposon silencing by heterochromatin formation [GO:0141007]; spermatogenesis [GO:0007283] | 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 spermatogonial stem cells. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. During piRNA biosynthesis, plays a key role in the piRNA amplification loop, also named ping-pong amplification cycle, by acting as a 'slicer-competent' piRNA endoribonuclease that cleaves primary piRNAs, which are then loaded onto 'slicer-incompetent' piwil4. Piwil2 slicing produces a pre-miRNA intermediate, which is then processed in mature piRNAs, and as well as a 16 nucleotide by-product that is degraded. Required for piwil4/miwi2 nuclear localization and association with secondary piRNAs antisense. Represses circadian rhythms by promoting the stability and activity of core clock components BMAL1 and CLOCK (By similarity). {ECO:0000250|UniProtKB:Q8CDG1}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A8KBH6 | KPCB_XENTR | MADPAACEPGEDTTTRFARKGALRQKNVHEVKEHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCETCMMNVHKRCVMNVPSLCGTDHTERRGRIHIKAEIREEVLTVTVGDARNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPTWNESFKFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELLKAGVDGWFKLLSQEEGEYFNVPVPPEGEEGNEELRQKFERAKIGPGTKAVEEKVVNPMPKVDNNETRDRMKVSDFNFLKVLGKGSFGKVILAERKGTDELYAIKILKKDVVIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYQIQQVGRFKEPHAVFYAAEIAIGLLFLHSKGIVYRDLKLDNVMLDSEGHIKIADFGMCKENMWDGVTTKTFCGTPDYIAPEIIAYQPYAKSVDWWAFGILLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKDHAFFRYIDWEKLERNEIQPPYKPKACGRNAENFDKFFTRHPPVLTPPDHEVIRNIDQSEFEGFSYVNSDFAKEEEKD | 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-translational protein modification [GO:0043687]; regulation of transcription by RNA polymerase II [GO:0006357] | 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 kinase activity [GO:0106310]; zinc ion binding [GO:0008270] | 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-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; | 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 B-cell survival. Required for recruitment and activation of the IKK kinase to lipid rafts and mediates phosphorylation of card11/carma1, leading to activate the NF-kappa-B signaling. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates isoform p66Shc of shc1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (andr)-dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation (By similarity). {ECO:0000250}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A8MPH9 | FOSLD_DROME | MIALKATEMQHNNNALQQQQQLQHQLLQQHQQQHQQQLQQQLNSPDNNYIWATTHNANISRNNAMLQLQQQQLRAPWITDCNKQHHINNNNSMNVNYNQQLTQQPQQQQQQTQYMQHNYNNYTQQQQQQHLVPATTSQSNSHFYQCNQQQQQQQFLAPTTTTAAVVVAAAHQQHQTQQQHQSQQQQQHQRQDYASLQMGRQLGNFETGQSVLTLTTPTLTPTTTRNIEDTLGHLLSDTQTDRVAGCAGFAVPKVLPNAIDVLGMGIPTGVSSLPLQQTFDLSLGQGSESEDSNASYNDTQMNEEQDTTDTSSAHTDSTSYQAGHIMAGSVNGGGVNNFSNVLAAVSSSRGSASVGSSNANTSNTPARRGGGRRPNRSTNMTPEEEQKRAVRRERNKQAAARCRKRRVDQTNELTEEVEQLEKRGESMRKEIEVLTNSKNQLEYLLATHRATCQKIRSDMLSVVTCNGLIAPAGLLSAGSSGSGASSHHNHNSNDSSNGTITGMDATLNSTGRSNSPLDLKPAANIDSLLMHIKDEPLDGAIDSGSSLDQDGPPPSKRITLPPMSTMPHVHLSTILTPTGASSGSLQTPITSTAPGGFGSAFPVTSNGSSINNINSIGNNMNSPTLNAHNKVPKERPNTLAFQRPLGQMHLTMANNKAGGPTQIQGVPIQTPSTGTFNFDSLMDGGTGLTPVSGPLVPNSSSTNKHPLELPTPTAEPSKLVSL | 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 disc fusion, thorax closure [GO:0046529]; locomotor rhythm [GO:0045475]; positive regulation of border follicle cell migration [GO:1903688]; positive regulation of transcription by RNA polymerase II [GO:0045944]; R3/R4 cell fate commitment [GO:0007464]; regulation of transcription by RNA polymerase II [GO:0006357]; response to wounding [GO:0009611]; synaptic assembly at neuromuscular junction [GO:0051124]; wound healing [GO:0042060] | 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 cis-regulatory region sequence-specific DNA binding [GO:0000978] | 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 Jra. {ECO:0000269|PubMed:2116361}. | Drosophila melanogaster (Fruit fly) |
A8MPR5 | FTSI2_ARATH | MACRFPLHSSSPSQFLSPENRQRLPRNYPSISCQNNSATNVVHEDGDDNDKAKTNQVNLLAIPITLTIISASLAKPSFAAAKVTERKRTQKKPQEALTLEQLKAWSKDLPVVSNRIPYTDILSLKAEGKLKHVIKPPNLSLRQKAEPVLVVLEDSRVLRTVLPSLEGNKRFWEQWDELGIDVQCVNAYTPPVKRPPVPSPYLGFLWKVPAYMLTWVKPKKESKRAAELKRMREDFKRQRKEEIETMKEERVMMEKTMKAQKKQQERKKRKAVRKKKYEESLREARKNYRDMADMWARLAQDPNVATALGLVFFYIFYRVVVLNYRKQKKDYEDRLKIEKAEADERKKMRELEREMEGIEEEDEEVEEGTGEKNPYLQMAMQFMKSGARVRRASNKRLPEYLERGVDVKFTDVAGLGKIRLELEEIVKFFTHGEMYRRRGVKIPGGILLCGPPGVGKTLLAKAVAGEAGVNFFSISASQFVEIYVGVGASRVRALYQEARENAPSVVFIDELDAVGRERGLIKGSGGQERDATLNQLLVSLDGFEGRGEVITIASTNRPDILDPALVRPGRFDRKIFIPKPGLIGRMEILQVHARKKPMAEDLDYMAVASMTDGMVGAELANIVEIAAINMMRDGRTELTTDDLLQAAQIEERGMLDRKDRSLETWRQVAINEAAMAVVAVNFPDMKNIEFLTINPRAGRELGYVRVKMDHIKFKEGMLSRQSILDHITVQLAPRAADELWYGEDQLSTIWAETSDNARSAARSLVLGGLSDKHHGLNNFWVADRINDIDVEALRILNMCYERAKEILGRNRTLMDEVVEKLVQKKSLTKQEFFTLVELYGSSKPMPPSILELRKIKRLELEEMVLKLDMTTARNSS | 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 | MVLAFQLVSFTYIWIILKPNVCAASNIKMTHQRCSSSMKQTCKQETRMKKDDSTKARPQKYEQLLHIEDNDFAMRPGFGGSPVPVGIDVHVESIDSISETNMDFTMTFYLRHYWKDERLSFPSTANKSMTFDHRLTRKIWVPDIFFVHSKRSFIHDTTMENIMLRVHPDGNVLLSLRITVSAMCFMDFSRFPLDTQNCSLELESYAYNEDDLMLYWKHGNKSLNTEEHMSLSQFFIEDFSASSGLAFYSSTGWYNRLFINFVLRRHVFFFVLQTYFPAILMVMLSWVSFWIDRRAVPARVSLGITTVLTMSTIITAVSASMPQVSYLKAVDVYLWVSSLFVFLSVIEYAAVNYLTTVEERKQFKKTGKISRMYNIDAVQAMAFDGCYHDSEIDMDQTSLSLNSEDFMRRKSICSPSTDSSRIKRRKSLGGHVGRIILENNHVIDTYSRILFPIVYILFNLFYWGVYV | 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 of rho subunits, where GABA molecules bind at the rho intersubunit interfaces (By similarity). When activated by GABA, rho-GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (By similarity). {ECO:0000250|UniProtKB:P24046, ECO:0000250|UniProtKB:P50573}. | 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 | MGNTVHRTLPDPSPPARLLATRPCCGPGPERRPVLGEAPRFHAQAKGKNVRLDGHSRRATRRNSFCNGVTFTQRPIRLYEQVRLRLVAVRPGWSGALRFGFTAHDPSLMSAQDIPKYACPDLVTRPGYWAKALPENLALRDTVLAYWADRHGRVFYSVNDGEPVLFHCGVAVGGPLWALIDVYGITDEVQLLESAFADTLTPARLSQARFSACLPPSSHDAANFDNNELENNQVVAKLGHLALGRAPGPPPADAAAAAIPCGPRERPRPASSPALLEADLRFHATRGPDVSLSADRKVACAPRPDGGRTLVFSERPLRPGESLFVEVGRPGLAAPGALAFGITSCDPGVLRPNELPADPDALLDRKEYWVVARAGPVPSGGDALSFTLRPGGDVLLGINGRPRGRLLCVDTTQALWAFFAVRGGVAGQLRLLGTLQSSPATTTPSGSLSGSQDDSDSDMTFSVNQSSSASESSLVTAPSSPLSPPVSPVFSPPEPAGIKNGECTVCFDGEVDTVIYTCGHMCLCHSCGLRLKRQARACCPICRRPIKDVIKIYRP | 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 | MAEAVDEDSGVGRSLEESSNGQHSQAGEALSEWRSSGQVENGTPSTSPSYWDIDDDDDYGLKPSELYGQYTWKIPKFSEITKREHRSNVFEAGGYKWYILIYPQGCDVCNHLSLFLCVANYDKLLPGSFAILEAGWSQFAQFTISVLSQDLKKSKFSDTLHRFWKKEHDWGWKKFMELPKLKDGFIDESGCLTIEAKVQVIRERVDRPFRCLDCGYRRELVRVYFQNVEQICRRFVEEKRSKLGRLIEDKARWTSFGVFWLGMDQNSRRRMCREKVDVILKGVVKHFFVEKEVSSTLVMDSLYSGLKALEGQTKNMKARSRLLDAKQLPAPIVSVDKDMFVLVDDVLLLLERAALEPLPPKDEKGRQNRTKDGNDGEEVNKEADERDERRLTELGRRTVEIFILSHIFSTKIEVAHQEAIALKRQEELIREEEEAWLAETEQRAKRGAAEREKKSKKKQAKQKRNKNKGKDKRKEEKVSFATHAKDLEENQNQNQNDEEEKDSVTEKAQSSAEKPDTLGDVSDISDSVDGSADILQPDLEDRDSSSVLWDTDALEIHPPSSEGSSRGRGISISTPNGITEGKSHSTMDDSSSTCSNDSIRSGVTNGSYQGNSLNFRNQKSPNKGKNQQVKAMTDAHSLASETDDQPSTLGTDPKGQNYSSEASNVGESDWVVVSHIQEPEGSRNRIPVGRERKTVQSIVNSVDMDRPKEKSTAVLSSPRNVAKNPSPLTQTKPEKKSISTADGIPNRKVLATGPPSSSQVVLPSDIQSQTVGLRADMQKLSAPKQPPATTISRPSSAPIIPAMRPSPITVSSSVQTTTSLPRSVSSAGRLGPDPSLHNQQTYTPQSYKNAIVGNSLGSSSSSFNHHPSSHGVVPTTLPSSSYSQAPTSSYQSSFPYSQDGLLWTGRSPSSVNMGMYNNTYSPAVTSNRSLNHMDVQIAQQQAQSMMTDEFPHLDIINDLLEDEQCSNMVYNGSIFNPQPQVFNGQYSSYHGELLSGGRTRSFGEEGLHYMARGPYGTDGMMPRQWQMTNMDLSLPAMRSNGMEDGTSSAANYHHSYFGLDASNPSFTSGINGYTEFRPSNGH | 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 autophagosomes in continuous darkness (PubMed:28351989). {ECO:0000269|PubMed:26867179, ECO:0000269|PubMed:28351989}. | 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 subsequent degradation of NB-LRR immune sensors to maintain their homeostasis (PubMed:26867179). Functions redundantly with TRAF1A in the regulation of autophagosome formation. Required for SINAT1- and SINAT2-mediated ubiquitination and destabilization of ATG6. Functions as a molecular adapter that helps to regulate autophagy by modulating ATG6 stability (PubMed:28351989). {ECO:0000269|PubMed:26867179, ECO:0000269|PubMed:28351989}. | Arabidopsis thaliana (Mouse-ear cress) |
A8MQN2 | LNK1_ARATH | MSDLYIHELGDYLSDEFHGNDDGIVPDSAYEDGGQFPILVSNRKKRRNDDMGSGTNHLKSNTFIKREANMLGKNPWPEKDSGGSSVSRDTGTGKDVQDMTLEDTNTSDHGFNGGHVDVVENFSTGDPMLCDTSAATNDGVYNYSLNSIPDAENDLSFFDNGDKEKNDLFYGWGDIGNFEDVDNMLRSCDSTFGLDSLNNEGDLGWFSSAQPNEETAGAMTDDLKPDKMLENQRTAMLQVEDFLNNSEPNHAVEDEYGYTIEDDSAQGKSSQNVFDTSLQKKDILMLDVEANLEKKQTDHLHHLDGKSDGFSENSFTLQHSGISREIMDTNQYYPPSAFQQRDVPYSHFNCEQPSVQVSACESKSGIKSENKPSPSSASNESYTSNHAQSIESLQGPTVDDRFRKVFETRANLLPGQDMPPSFAANTKKSSKTDSMVFPDAAPIQKIGLENDHRKAATELETSNMQGSSCVSSVVDDISLEATSFRQLQQVIEQLDVRTKLCIRDSLYRLAKSAEQRHHGGNRPEKGAGSHLVTGEADKYAGFMDIETDTNPIDRSIAHLLFHRPSDSSLSSDNNVLSYKSHPMIPQPNSSPSLRIEKQEETTELRPEAEVVTSDNN | 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 afternoon peak (PubMed:23818596). Mediates light inhibition of hypocotyl elongation (PubMed:23818596). {ECO:0000269|PubMed:23818596, ECO:0000269|PubMed:25012192, ECO:0000269|PubMed:25848001, ECO:0000269|PubMed:25848708}. | Arabidopsis thaliana (Mouse-ear cress) |
A8MQY1 | NAC68_ARATH | MMKGLIGYRFSPTGEEVINHYLKNKLLGKYWLVDEAISEINILSHKPSKDLPKLARIQSEDLEWYFFSPIEYTNPNKMKMKRTTGSGFWKPTGVDREIRDKRGNGVVIGIKKTLVYHEGKSPHGVRTPWVMHEYHITCLPHHKRKYVVCQVKYKGEAAEISYEPSPSLVSDSHTVIAITGEPEPELQVEQPGKENLLGMSVDDLIEPMNQQEEPQGPHLAPNDDEFIRGLRHVDRGTVEYLFANEENMDGLSMNDLRIPMIVQQEDLSEWEGFNADTFFSDNNNNYNLNVHHQLTPYGDGYLNAFSGYNEGNPPDHELVMQENRNDHMPRKPVTGTIDYSSDSGSDAGSISTTSYQGTSSPNISVGSSSRHLSSCSSTDSCKDLQTCTDPSIISREIRELTQEVKQEIPRAVDAPMNNESSLVKTEKKGLFIVEDAMERNRKKPRFIYLMKMIIGNIISVLLPVKRLIPVKKL | 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 or signal, is processed into a transcriptionally active and nuclear form after a proteolytic cleavage through regulated intramembrane proteolysis (RIP). {ECO:0000269|PubMed:17098812}. | 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 with HFR1 and LAF1 in the nucleus in response to FR conditions (PubMed:16045472, PubMed:19482971). Contributes to inhibition of hypocotyl elongation in continuous blue light (B) (PubMed:16045472). {ECO:0000250|UniProtKB:Q8S4Q6, ECO:0000269|PubMed:16045472, ECO:0000269|PubMed:17566111, ECO:0000269|PubMed:19482971, ECO:0000269|PubMed:21969386, ECO:0000269|PubMed:22374392}. | Arabidopsis thaliana (Mouse-ear cress) |
A8MR93 | ALG12_ARATH | MPTDSKMAKFLQSYGYDLILGSVAAIYVVMAPYTKVEESFNVQSMHDILYHRHHLDSYDHLEFPGVVPRTFIGAFIVSVFASPVVSIISCLGFPKVYSLVAARLVLGCIILSTLRFFRIQIKKKFGNQVETFFVLFTSLQFHFLFYCTRPLPNILALGLVNLAYGNWLKGNFYPALSFLIFATVIFRCDTMLLLGPIGLELLLTKSISFWKALKYCVGTALLAVGLTIFVDSIMWKKFVWPEFEVFWFNSILNRSSDWGTHSIHWYFTSALPRSLLVAYPLSLLGTLVDRRVPFFIVPVLSFVILYSKLPHKELRFIISSVPMFNLSAAVAASRIYNNRKKTIWKLVNMVMLAFFAISAGCTVVTFMASYYNYPSGYALKRLHQIGHPANVAGEEWVHIDTFGAMNGISRFCEDDFPWRYSKEEEIVVEELRNRNFTYLVNEHSSVDGYKCLFYEEGFERLELRRGFPPIVLVKKAKVYLHREMKKEDPFHKKWPGC | 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)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+); Xref=Rhea:RHEA:29535, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:12629, Rhea:RHEA-COMP:12630, ChEBI:CHEBI:15378, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132517, ChEBI:CHEBI:132519; EC=2.4.1.260; Evidence={ECO:0000269|PubMed:20023196}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29536; Evidence={ECO:0000305|PubMed:20023196}; | 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 lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the eighth mannose residue in an alpha-1,6 linkage onto Man(7)GlcNAc(2)-PP-dolichol to produce Man(8)GlcNAc(2)-PP-dolichol. {ECO:0000269|PubMed:20023196}. | Arabidopsis thaliana (Mouse-ear cress) |
A8MRD9 | PDS5D_ARATH | MTAIVGFDQLSKALIDAGTNLLSPPSSTDDLLTLLDETESLLKNVEQDQPLSMQSALIPSRNALVSVDLLSHPDSDVRVSVVSCLTEIVRITAPETPYSDDLMKEIFRLTIEAFEKLADASSRSYKKAEFVLDNVAKVKSCLVMLDLECYDLILQMFRNFFKFIRSDHPQLVFSSMELIMIAIIDETEQVSTDLLDSLLATVKKENQNVSPMSWSLAEKVLSRCARKLKPYIIEALKSRGTSLDMYSPVVSSICQSVFNTPKVHSPVNTKEHEEKLDLGHSRKENLSKSSSKRPARHETRGINEKEKVRNGNKSSLLKQSLKQVRSESTDAEITGKRGRKPNSLMNPEDYDISWLSGKRDPLKTSSNKKIQKKGSGGVSSLGKVPAKKTPLPKENSPATSSRSLTGSLKRSRVKMDESDYDSDSLSSPRLKKLASCFRDEEPNQEDDRKIGNSSKQTRSKNGLEKSQKTAKKKPVVEAKIVNSSGKRLSARSVAKRRNLERAPLDTLVPQSSKRKKMVSQVAARQLANESEEETPKSHPTRRRTVRKEVESDGFGEDLVGKRVNIWWPLDKTFYEGVIDSYCTRKKMHRVIYSDGDSEELNLTEERWELLEDDTSADEDKEIDLPESIPLSDIMQRQKVKKSKNVAVSVEPTSSSGVRSSSRTLMKKDCGKRLNKQVEKTREGKNLRSLKELNAETDRTAEEQEVSLEAESDDRSEEQEYEDDCSDKKEQSQDKGVEAETKEEEKQYPNSEGESEGEDSESEEEPKWRETDDMEDDEEEEEEEIDHMEDEAEEEKEEVDDKEASANMSEIEKEEEEEEEDEEKRKS | 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 (PubMed:26648949). May couple sister chromatid cohesion during mitosis to DNA replication (By similarity). Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair (PubMed:26648949). {ECO:0000250|UniProtKB:Q29RF7, ECO:0000269|PubMed:26648949}. | Arabidopsis thaliana (Mouse-ear cress) |
A8MRX0 | GSOX5_ARATH | MAPARTRVNSLNVAVIGAGAAGLVAARELRRENHTVVVFERDSKVGGLWVYTPNSEPDPLSLDPNRTIVHSSVYDSLRTNLPRECMGYRDFPFVPRPEDDESRDSRRYPSHREVLAYLEDFAREFKLVEMVRFKTEVVLVEPEDKKWRVQSKNSDGISKDEIFDAVVVCNGHYTEPRVAHVPGIDSWPGKQIHSHNYRVPDQFKDQVVVVIGNFASGADISRDITGVAKEVHIASRSNPSKTYSKLPGSNNLWLHSMIESVHEDGTIVFQNGKVVQADTIVHCTGYKYHFPFLNTNGYITVEDNCVGPLYEHVFPPALAPGLSFIGLPWMTLQFFMFELQSKWVAAALSGRVTLPSEEKMMEDVTAYYAKREAFGQPKRYTHRLGGGQVDYLNWIAEQIGAPPGEQWRYQEINGGYYRLATQSDTFRDKWDDDHLIVEAYEDFLRQKLISSLPSQLLES | 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:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:136434, ChEBI:CHEBI:136435; EC=1.14.13.237; Evidence={ECO:0000269|PubMed:18799661}; | 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 | MFSSTTLHHLPRPNLLLPRKVISRRMSTNPAIEPKVRKFESVEGVDIGSRNKSDGFFAIPLYLSKLVALYNCISLSRIGTSNENFVFSGIRFRLVSYNILAQVYVKSALLPHSPPACLKWKARSHAILSVLKNLQADFFCLQEVDEYDSFYRNNMDSLGYSGIYIQRTGQRKRDGCAIFYKPSCAELVTKERIEYNDLVDSIKADSVSCSEQKIETSNEGKDSRKDSRDLNDPLVRLKRDCVGIMAAFRINKPFQHIVIVANTHLYWDPELADVKLAQAKYLLSRLAQFKTLISDEFECTPSLLLAGDFNSIPGDMVYSYLVSGNAKPTETIEEEEAPVPLSSVYEVTRGEPKFTNCTPGFTNTLDYIFISPSDFIKPVSILQLPEPDSPDVVGFLPNHHHPSDHLPIGAEFEIRRE | 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 the expression and rhythmicity of the clock core oscillator genes TOC1 and CCA1 (PubMed:26619288). Deadenylation may be a mechanism involved in the regulation of the circadian clock (PubMed:26619288). May play a negative role in response against oxidative stress (PubMed:26619288). Possesses magnesium-dependent poly(A)-specific exoribonuclease activity in vitro and is almost inactive with poly(U), poly(C) and poly(G) as substrates (PubMed:26619288). {ECO:0000250|UniProtKB:P31384, ECO:0000269|PubMed:26619288}. | Arabidopsis thaliana (Mouse-ear cress) |
A8MS68 | PLPD1_ARATH | MQSAMALSFSQTSFTRPNHVLGSSGSVFSTPRSLRFCGLRREAFGFSTSNQLAIRSNRIQFLSRKSFQVSASASSNGNGAPPKSFDYDLIIIGAGVGGHGAALHAVEKGLKTAIIEGDVVGGTCVNRGCVPSKALLAVSGRMRELQNEHHMKSFGLQVSAAGYDRQGVADHANNLATKIRNNLTNSMKAIGVDILTGFGSVLGPQKVKYGKDNIITAKDIIIATGSVPFVPKGIEVDGKTVITSDHALKLESVPEWIAIVGSGYIGLEFSDVYTALGSEVTFIEALDQLMPGFDPEISKLAQRVLINPRKIDYHTGVFASKITPARDGKPVLIELIDAKTKEPKDTLEVDAALIATGRAPFTNGLGLENVNVVTQRGFIPVDERMRVIDGKGTLVPNLYCIGDANGKLMLAHAASAQGISVVEQVSGRDHVLNHLSIPAACFTHPEISMVGLTEPQAKEKGEKEGFKVSVVKTSFKANTKALAENEGEGIAKMIYRPDNGEILGVHIFGLHAADLIHEASNAIALGTRIQDIKLAVHAHPTLSEVLDELFKAAKVESHATTRTGDAKIKLNTNQEDRKGRRRGGDDEKQPSVSKDLKDISTRPSSFFENISVGVLSLLSLIFV | 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 | MARNAISDDEEDHELEDDDGEPVHGDPAEHDENDDEEDDDDVGNEYENDGFIVNDEDEEEEEEEDEERKDSDEERQKKKKKRKKKDEGLDEDDYLLLQDNNVKFKKRQYKRLKKAQREQGNGQGESSDDEFDSRGGTRRSAEDKIKDRLFDDVDVDDPPDDVGDEEDLVVEEDVVGSEDEMADFIVDEDDEHGPPKRGNSKKKKYRQGSDITAMRDANEIFGDVDELLTIRKKGLASNQRMERRLEDEFEPTVLSEKYMTGNDDEIRQLDIPERMQISEESTGSPPVDEISIEEESNWIYAQLASQLRESDGTFDGRGFSVNKDDIAKFLELHHVQKLEIPFIAMYRKEQCRSLLDTGDFDGANQGKKPETKWHKVFWMIHDLDKKWLLLRKRKMALHGYYTKRYEEESRRVYDETRLNLNQYLFESVIKSLKVAETEREVDDVDSKFNLHFPPGEIGVDEGQYKRPKRKSQYSICSKAGLWEVANKFGYSAEQLGLALSLEKLVDELEDAKETPEEMAKNFVCAMFENSLAVLKGARHMAAVEISCEPSVKKYVRGIYMENAVVSTSPTADGNTVIDSFHQFSGIKWLREKPLSKFEGAQWLLIQKGEEEKLLQVTFKLPENYMNRLISDCNEHYLSVGVSKYAQLWNEQRKLILEDALHAFLLPSMEKEARSLLTSRAKSRLLSEYGQALWNKVSAGPYQKKEMDINLDEEAAPRVMACCWGPGKPPNTFVMLDSSGEVLDVLYAGSLTSRSQNVNDQQRKKSDQDRVLKFMMDHQPHVVALGAVNLSCTRLKDDIYEVIFQMVEEKPRDVGHGMDDLSIVYVDESLPRLYENSRISGEQLPQQSGNVRRAVALGRYLQNPLAMVATLCGPGREILSWKLHPLENFLQLDEKYGMVEQVMVDITNQVGIDINLAASHDWFFSPLQFISGLGPRKAASLQRSLVRAGSIFVRKDLIMHGLGKKVFVNAAGFLRIRRSGLAASSSQFIDLLDDTRIHPESYSLAQELAKDIYDEDVRGDSNDDEDAIEMAIEHVRDRPASLRKVVLDEYLASKKRENKKETYSNIIRELSCGFQDWRIPFKEPSPDEEFYMISGETEDTIAEGRIVQASVRRLQNGRAICVLDSGLTGMLMKEDFSDDGRDIVDLADQLKEGDILTCKIKSIQKQRYQVFLICKESEMRNNRHQHNQNVDAYYHEDRNSLQLVKEKARKEKELVRKHFKSRMIVHPRFQNITADQATEYLSDKDFGESIVRPSSRGLNFLTLTLKIYDGVYAHKEIAEGGKENKDITSLQCIGKTLTIGEDTFEDLDEVMDRYVDPLVSHLKTMLNYRKFRKGTKSEVDDLLRIEKGENPSRIVYCFGISHEHPGTFILSYIRSTNPHHEYIGLYPKGFKFRKRMFEDIDRLVAYFQRHIDDPLQESAPSIRSIAAKVPMRSPADHGSSGGSGWGSSQSEGGWKGNSDRSGSGRGGEYRNGGGRDGHPSGAPRPYGGRGRGRGRGRRDDMNSDRQDGNGDWGNNDTGTADGGWGNSGGGGWGSESAGKKTGGGSTGGWGSESGGNKSDGAGSWGSGSGGGGSGGWGNDSGGKKSSEDGGFGSGSGGGGSDWGNESGGKKSSADGGWGSESGGKKSDGEGGWGNEPSSRKSDGGGGGW | 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. {ECO:0000250|UniProtKB:Q7KZ85}. | 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 subunits CENPT and CENPW at centromeres occurs through a dynamic exchange mechanism. Although exchange is continuous in the cell cycle, de novo assembly starts principally during mid-late S phase and is complete by G2. CENPX being less stably bound at the kinetochore than CENPS. {ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:24522885}. | 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, PubMed:20347429). In complex with CENPS (MHF heterodimer), crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. Stabilizes FANCM. In complex with CENPS and FANCM (but not other FANC proteins), rapidly recruited to blocked forks and promotes gene conversion at blocked replication forks (PubMed:20347428, PubMed:20347429). In complex with CENPS, CENPT and CENPW (CENP-T-W-S-X heterotetramer), involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression (PubMed:19620631). As a component of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like structure (PubMed:20347428, PubMed:20347429). DNA-binding function is fulfilled in the presence of CENPS, with the following preference for DNA substates: Holliday junction > double-stranded > splay arm > single-stranded. Does not bind DNA on its own (PubMed:20347429). {ECO:0000269|PubMed:19620631, ECO:0000269|PubMed:20347428, ECO:0000269|PubMed:20347429}. | 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 | MGSGISSESKESAKRSKELEKKLQEDAERDARTVKLLLLGAGESGKSTIVKQMKIIHKNGYSEQECMEFKAVIYSNTLQSILAIVKAMTTLGIDYVNPRSAEDQRQLYAMANTLEDGGMTPQLAEVIKRLWRDPGIQACFERASEYQLNDSAAYYLNDLDRITASGYVPNEQDVLHSRVKTTGIIETQFSFKDLHFRMFDVGGQRSERKKWIHCFEGVTCIIFCAALSAYDMVLVEDEEVNRMHESLHLFNSICNHKYFSTTSIVLFLNKKDIFQEKVTKVHLSICFPEYTGPNTFEDAGNYIKNQFLDLNLKKEDKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF | 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-surface receptors with a cGMP-phosphodiesterase; Activation of phosphodiesterase lowers intracellular levels of cAMP and cGMP which may open a cyclic nucleotide-suppressible cation channel leading to influx of calcium, ultimately leading to release of neurotransmitter. Indeed, denatonium and strychnine induce transient reduction in cAMP and cGMP in taste tissue, whereas this decrease is inhibited by GNAT3 antibody. Gustducin heterotrimer transduces response to bitter and sweet compounds via regulation of phosphodiesterase for alpha subunit, as well as via activation of phospholipase C for beta and gamma subunits, with ultimate increase inositol trisphosphate and increase of intracellular Calcium. GNAT3 can functionally couple to taste receptors to transmit intracellular signal: receptor heterodimer TAS1R2/TAS1R3 senses sweetness and TAS1R1/TAS1R3 transduces umami taste, whereas the T2R family GPCRs act as bitter sensors. Functions also as lumenal sugar sensors in the gut to control the expression of the Na+-glucose transporter SGLT1 in response to dietaty sugar, as well as the secretion of Glucagon-like peptide-1, GLP-1 and glucose-dependent insulinotropic polypeptide, GIP. Thus, may modulate the gut capacity to absorb sugars, with implications in malabsorption syndromes and diet-related disorders including diabetes and obesity. {ECO:0000269|PubMed:11917125, ECO:0000269|PubMed:17724330}. | Homo sapiens (Human) |
A8MTJ6 | FOXI3_HUMAN | MALYCGDNFGVYSQPGLPPPAATAAAPGAPPAARAPYGLADYAAPPAAAANPYLWLNGPGVGGPPSAAAAAAAAYLGAPPPPPPPGAAAGPFLQPPPAAGTFGCSQRPFAQPAPAAPASPAAPAGPGELGWLSMASREDLMKMVRPPYSYSALIAMAIQSAPERKLTLSHIYQFVADSFPFYQRSKAGWQNSIRHNLSLNDCFKKVPRDEDDPGKGNYWTLDPNCEKMFDNGNFRRKRKRRSEASNGSTVAAGTSKSEEGLSSGLGSGVGGKPEEESPSTLLRPSHSPEPPEGTKSTASSPGGPMLTSTPCLNTFFSSLSSLSVSSSVSTQRALPGSRHLGIQGAQLPSSGVFSPTSISEASADTLQLSNSTSNSTGQRSSYYSPFPASTSGGQSSPFSSPFHNFSMVNSLIYPREGSEV | 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 system development [GO:0060037]; regulation of transcription by RNA polymerase II [GO:0006357]; thymus development [GO:0048538] | 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 similarity). Acts at multiple stages of otic placode induction: necessary for preplacodal ectoderm to execute an inner ear program (By similarity). Required for hair follicle stem cell specification (By similarity). Acts downstream of TBX1 for the formation of the thymus and parathyroid glands from the third pharyngeal pouch (By similarity). {ECO:0000250|UniProtKB:D3Z120, ECO:0000269|PubMed:37041148}. | 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]; regulation of cilium assembly [GO:1902017]; regulation of transcription by RNA polymerase II [GO:0006357] | 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 expression of various components important for axonemal assembly and function. Plays a role in regulating axial versus paraxial cell fate. Activates the transcription of ciliary proteins C11orf97 homolog, FAM183B and SPACA9 in the embryonic ventral node (By similarity). {ECO:0000250|UniProtKB:Q5TIS6}. | 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 factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. Required for primary cilia assembly and BBSome stability. Regulates cytoplasmic microtubule stability and acetylation. {ECO:0000269|Ref.4}. | Homo sapiens (Human) |
A8MU46 | SMTL1_HUMAN | MEQKEGKLSEDGTTVSPAADNPEMSGGGAPAEETKGTAGKAINEGPPTESGKQEKAPAEDGMSAELQGEANGLDEVKVESQREAGGKEDAEAELKKEDGEKEETTVGSQEMTGRKEETKSEPKEAEEKESTLASEKQKAEEKEAKPESGQKADANDRDKPEPKATVEEEDAKTASQEETGQRKECSTEPKEKATDEEAKAESQKAVVEDEAKAEPKEPDGKEEAKHGAKEEADAKEEAEDAEEAEPGSPSEEQEQDVEKEPEGGAGVIPSSPEEWPESPTGEGHNLSTDGLGPDCVASGQTSPSASESSPSDVPQSPPESPSSGEKKEKAPERRVSAPARPRGPRAQNRKAIVDKFGGAASGPTALFRNTKAAGAAIGGVKNMLLEWCRAMTKKYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPAKRRHNFTLAFSTAEKLADCAQLLDVDDMVRLAVPDSKCVYTYIQELYRSLVQKGLVKTKKK | 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). Phosphorylation at Ser-301 promotes translocation to the nucleus (By similarity). {ECO:0000250}. | 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; Evidence={ECO:0000269|PubMed:28887308}; CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl-[citrate synthase] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl-[citrate synthase] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:55548, Rhea:RHEA-COMP:14213, Rhea:RHEA-COMP:14214, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:28887308}; CATALYTIC ACTIVITY: Reaction=N(6),N(6)-dimethyl-L-lysyl-[citrate synthase] + S-adenosyl-L-methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[citrate synthase] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:55552, Rhea:RHEA-COMP:14214, Rhea:RHEA-COMP:14215, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:28887308}; | 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:28887308). {ECO:0000269|PubMed:28391595, ECO:0000269|PubMed:28887308}. | Homo sapiens (Human) |
A8MV65 | VGLL3_HUMAN | MSCAEVMYHPQPYGASQYLPNPMAATTCPTAYYQPAPQPGQQKKLAVFSKMQDSLEVTLPSKQEEEDEEEEEEEKDQPAEMEYLNSRCVLFTYFQGDIGSVVDEHFSRALGQAITLHPESAISKSKMGLTPLWRDSSALSSQRNSFPTSFWTSSYQPPPAPCLGGVHPDFQVTGPPGTFSAADPSPWPGHNLHQTGPAPPPAVSESWPYPLTSQVSPSYSHMHDVYMRHHHPHAHMHHRHRHHHHHHHPPAGSALDPSYGPLLMPSVHAARIPAPQCDITKTEPTTVTSATSAWAGAFHGTVDIVPSVGFDTGLQHQDKSKESPWY | 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 | MGQDAFMEPFGDTLGVFQCKIYLLLFGACSGLKVTVPSHTVHGVRGQALYLPVHYGFHTPASDIQIIWLFERPHTMPKYLLGSVNKSVVPDLEYQHKFTMMPPNASLLINPLQFPDEGNYIVKVNIQGNGTLSASQKIQVTVDDPVTKPVVQIHPPSGAVEYVGNMTLTCHVEGGTRLAYQWLKNGRPVHTSSTYSFSPQNNTLHIAPVTKEDIGNYSCLVRNPVSEMESDIIMPIIYYGPYGLQVNSDKGLKVGEVFTVDLGEAILFDCSADSHPPNTYSWIRRTDNTTYIIKHGPRLEVASEKVAQKTMDYVCCAYNNITGRQDETHFTVIITSVGLEKLAQKGKSLSPLASITGISLFLIISMCLLFLWKKYQPYKVIKQKLEGRPETEYRKAQTFSGHEDALDDFGIYEFVAFPDVSGVSRIPSRSVPASDCVSGQDLHSTVYEVIQHIPAQQQDHPE | 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 {ECO:0000269|PubMed:19358830, ECO:0000269|PubMed:22864114}. Midbody {ECO:0000269|PubMed:22864114}. Note=In interphase, localizes to the Golgi apparatus. Localizes to centrosomes and spindles during prophase, prometaphase, and metaphase of mitosis, and to midbodies at telophase. Translocation to mitotic centrosomes is the result of poly-ADP-ribosylation (PARsylation). {ECO:0000269|PubMed:19358830, ECO:0000269|PubMed:22864114}. | 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 of the gamma-tubulin ring complex and promotes centrosome maturation. {ECO:0000269|PubMed:22864114}. | Homo sapiens (Human) |
A8MW92 | P20L1_HUMAN | MSKKPPNRPGITFEIGARLEALDYLQKWYPSRIEKIDYEEGKMLVHFERWSHRYDEWIYWDSNRLRPLERPALRKEGLKDEEDFFDFKAGEEVLARWTDCRYYPAKIEAINKEGTFTVQFYDGVIRCLKRMHIKAMPEDAKGQVKSQHPLSWCCPIDPAGSCNQSMGSEDWIALVKAAAAAAAKNKTGSKPRTSANSNKDKDKDERKWFKVPSKKEETSTCIATPDVEKKEDLPTSSETFGLHVENVPKMVFPQPESTLSNKRKNNQGNSFQAKRARLNKITGLLASKAVGVDGAEKKEDYNETAPMLEQAISPKPQSQKKNEADISSSANTQKPALLSSTLSSGKARSKKCKHESGDSSGCIKPPKSPLSPELIQVEDLTLVSQLSSSVINKTSPPQPVNPPRPFKHSERRRRSQRLATLPMPDDSVEKVSSPSPATDGKVFSISSQNQQESSVPEVPDVAHLPLEKLGPCLPLDLSRGSEVTAPVASDSSYRNECPRAEKEDTQMLPNPSSKAIADGRGAPAAAGISKTEKKVKLEDKSSTAFGKRKEKDKERREKRDKDHYRPKQKKKKKKKKKSKQHDYSDYEDSSLEFLERCSSPLTRSSGSSLASRSMFTEKTTTYQYPRAILSVDLSGENLSDVDFLDDSSTESLLLSGDEYNQDFDSTNFEESQDEDDALNEIVRCICEMDEENGFMIQCEECLCWQHSVCMGLLEESIPEQYICYICRDPPGQRWSAKYRYDKEWLNNGRMCGLSFFKENYSHLNAKKIVSTHHLLADVYGVTEVLHGLQLKIGILKNKHHPDLHLWACSGKRKDQDQIIAGVEKKIAQDTVNREEKKYVQNHKEPPRLPLKMEGTYITSEHSYQKPQSFGQDCKSLADPGSSDDDDVSSLEEEQEFHMRSKNSLQYSAKEHGMPEKNPAEGNTVFVYNDKKGTEDPGDSHLQWQLNLLTHIENVQNEVTSRMDLIEKEVDVLESWLDFTGELEPPDPLARLPQLKRHIKQLLIDMGKVQQIATLCSV | 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|PubMed:24492612, ECO:0000269|PubMed:29358331}. | Homo sapiens (Human) |
A8MW95 | BECN2_HUMAN | MSSIRFLCQRCHQALKLSGSSESRSLPAAPAPTSGQAEPGDTREPGVTTREVTDAEEQQDGASSRSPPGDGSVSKGHANIFTLLGELGAMHMLSSIQKAAGDIFDIVSGQAVVDHPLCEECTDSLLEQLDIQLALTEADSQNYQRCLETGELATSEDEAAALRAELRDLELEEARLVQELEDVDRNNARAAADLQAAQAEAAELDQQERQHYRDYSALKRQQLELLDQLGNVENQLQYARVQRDRLKEINCFTATFEIWVEGPLGVINNFRLGRLPTVRVGWNEINTAWGQAALLLLTLANTIGLQFQRYRLIPCGNHSYLKSLTDDRTELPLFCYGGQDVFLNNKYDRAMVAFLDCMQQFKEEAEKGELGLSLPYGIQVETGLMEDVGGRGECYSIRTHLNTQELWTKALKFMLINFKWSLIWVASRYQK | 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 | MDVQKWYLRTSKLALALAIIRSKPADKSSREYTEHLAMLLSEEQSKWRSKVEILEAEVMQLRQKLLVSRLCSGSFKSGYVSSQLEAQEPKSSESTLTSMEDSGCDLSNEQRTESSDLSQHFVESCTPTHFPPLPLVKRPCAILQNPLSSHMQFLQYLLELKNLTESGNLKRDLTHFEKDSSTVSDSVFQLLDGLITFYRNPKLPFSRFWTEAVGTLASLISDYNLSSHILKKCSKKLEEFEKTLLHAILGNNHINQFQVQHYVSQSLVTLGNCSLLRKSIISLLLSEVNGFADDLGAINQEQASYDVSRYENIFYLFWVLEQLLQKETEEGNTSSIGHDDQEIKKFLQKHDETIFQLSDAFPLFTFYLWRVGILLSSAQIETLRK | 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 subsequent stages. {ECO:0000250|UniProtKB:Q8BRM6}. | 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 | MSSSLRPGPSRWRRAASIVLAAGWSRPETATPPSRPPPAEGFRLLLLQRSPHQGFMPGAHVFSGGVLDAADRSADWLGLFAPHHGPPRFGLGPAPFSRTAFPSLPDTDDHKTDNTGTLPEDVAFRICAVREAFEEAGVLLLRPRTSPPGPAPGPGLALEPPPGLASWRDRVRQDPRHFLRLCAHLDCTPDIWALHNWSAWLTPFLRGTTRRFDTAFFLCCLREPPPVYPDLAEVVGYQWSSPSEATESFLSKEIWLPPPQFYEVRRLANFASLSDLHKFCLGRALEGLERWLPIILLTADGMVHLLPGDELYLEDSDFLENLMSTEKKTEEIMKEGKQFHRIVTYHRHLYDIHVTVQPKYKHVYPKNSVVRKSHL | 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:1901289] | 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; Xref=Rhea:RHEA:50045; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=CoA + H2O = (R)-4'-phosphopantetheine + adenosine 3',5'-bisphosphate + 2 H(+); Xref=Rhea:RHEA:64988, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:58343, ChEBI:CHEBI:61723; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64989; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=H2O + hexanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) + hexanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:49980, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58343, ChEBI:CHEBI:62620, ChEBI:CHEBI:132012; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49981; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=H2O + octanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) + S-octanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50016, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57386, ChEBI:CHEBI:58343, ChEBI:CHEBI:132013; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50017; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=butanoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S-butanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:49976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57371, ChEBI:CHEBI:58343, ChEBI:CHEBI:132011; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49977; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=H2O + propanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) + propanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:67464, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57392, ChEBI:CHEBI:58343, ChEBI:CHEBI:172362; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67465; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=H2O + malonyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) + malonyl-4'-phosphopantetheine; Xref=Rhea:RHEA:67468, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57384, ChEBI:CHEBI:58343, ChEBI:CHEBI:172363; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67469; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=H2O + succinyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) + succinyl-4'-phosphopantetheine; Xref=Rhea:RHEA:67472, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57292, ChEBI:CHEBI:58343, ChEBI:CHEBI:172364; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67473; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=choloyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S-choloyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50036, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57373, ChEBI:CHEBI:58343, ChEBI:CHEBI:132020; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50037; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=4,8-dimethylnonanoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S-(4,8-dimethylnonanoyl)-4'-phosphopantetheine; Xref=Rhea:RHEA:67524, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58343, ChEBI:CHEBI:77061, ChEBI:CHEBI:172385; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67525; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S-(9Z,12Z,15Z-octadecatrienoyl)-4'-phosphopantetheine; Xref=Rhea:RHEA:67532, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58343, ChEBI:CHEBI:74034, ChEBI:CHEBI:172386; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67533; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S-(9Z,12Z-octadecadienoyl)-4'-phosphopantetheine; Xref=Rhea:RHEA:67536, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57383, ChEBI:CHEBI:58343, ChEBI:CHEBI:172387; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67537; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S-(9Z-hexadecenoyl)-4'-phosphopantetheine; Xref=Rhea:RHEA:67540, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58343, ChEBI:CHEBI:61540, ChEBI:CHEBI:172388; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67541; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=(9Z)-tetradecenoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S-(9Z-tetradecenoyl)-4'-phosphopantetheine; Xref=Rhea:RHEA:67544, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58343, ChEBI:CHEBI:65060, ChEBI:CHEBI:172389; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67545; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=(6Z)-octenoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S-(6Z-octenoyl)-4'-phosphopantetheine; Xref=Rhea:RHEA:67528, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58343, ChEBI:CHEBI:172383, ChEBI:CHEBI:172384; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67529; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) + S-hexadecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50032, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57379, ChEBI:CHEBI:58343, ChEBI:CHEBI:132018; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50033; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) + tetradecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385, ChEBI:CHEBI:58343, ChEBI:CHEBI:132017; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50029; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S-dodecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50024, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57375, ChEBI:CHEBI:58343, ChEBI:CHEBI:132015; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50025; Evidence={ECO:0000250|UniProtKB:P11930}; CATALYTIC ACTIVITY: Reaction=a 5'-end CoA-ribonucleoside in mRNA + H2O = (R)-4'-phosphopantetheine + a 5'-end phospho-adenosine-phospho-ribonucleoside in mRNA + 2 H(+); Xref=Rhea:RHEA:67592, Rhea:RHEA-COMP:15719, Rhea:RHEA-COMP:17276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:61723, ChEBI:CHEBI:144051, ChEBI:CHEBI:172371; Evidence={ECO:0000250|UniProtKB:P11930}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67593; Evidence={ECO:0000250|UniProtKB:P11930}; | 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 concentrations medium and long-chain fatty-acyl-CoA esters are the primary substrates (By similarity). Highest activity seen with medium-chain acyl-CoA esters and higher rates of activity seen with the unsaturated acyl-CoA esters compared with the saturated esters (By similarity). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity). {ECO:0000250|UniProtKB:P11930}. | Homo sapiens (Human) |
A8MYU2 | KCNU1_HUMAN | MFQTKLRNETWEDLPKMSCTTEIQAAFILSSFVTFFSGLIILLIFRLIWRSVKKWQIIKGTGIILELFTSGTIARSHVRSLHFQGQFRDHIEMLLSAQTFVGQVLVILVFVLSIGSLIIYFINSADPVGSCSSYEDKTIPIDLVFNAFFSFYFGLRFMAADDKIKFWLEMNSIVDIFTIPPTFISYYLKSNWLGLRFLRALRLLELPQILQILRAIKTSNSVKFSKLLSIILSTWFTAAGFIHLVENSGDPWLKGRNSQNISYFESIYLVMATTSTVGFGDVVAKTSLGRTFIMFFTLGSLILFANYIPEMVELFANKRKYTSSYEALKGKKFIVVCGNITVDSVTAFLRNFLRDKSGEINTEIVFLGETPPSLELETIFKCYLAYTTFISGSAMKWEDLRRVAVESAEACLIIANPLCSDSHAEDISNIMRVLSIKNYDSTTRIIIQILQSHNKVYLPKIPSWNWDTGDNIICFAELKLGFIAQGCLVPGLCTFLTSLFVEQNKKVMPKQTWKKHFLNSMKNKILTQRLSDDFAGMSFPEVARLCFLKMHLLLIAIEYKSLFTDGFCGLILNPPPQVRIRKNTLGFFIAETPKDVRRALFYCSVCHDDVFIPELITNCGCKSRSRQHITVPSVKRMKKCLKGISSRISGQDSPPRVSASTSSISNFTTRTLQHDVEQDSDQLDSSGMFHWCKPTSLDKVTLKRTGKSKYKFRNHIVACVFGDAHSAPMGLRNFVMPLRASNYTRKELKDIVFIGSLDYLQREWRFLWNFPQIYILPGCALYSGDLHAANIEQCSMCAVLSPPPQPSSNQTLVDTEAIMATLTIGSLQIDSSSDPSPSVSEETPGYTNGHNEKSNCRKVPILTELKNPSNIHFIEQLGGLEGSLQETNLHLSTAFSTGTVFSGSFLDSLLATAFYNYHVLELLQMLVTGGVSSQLEQHLDKDKVYGVADSCTSLLSGRNRCKLGLLSLHETILSDVNPRNTFGQLFCGSLDLFGILCVGLYRIIDEEELNPENKRFVITRPANEFKLLPSDLVFCAIPFSTACYKRNEEFSLQKSYEIVNKASQTTETHSDTNCPPTIDSVTETLYSPVYSYQPRTNSLSFPKQIAWNQSRTNSIISSQIPLGDNAKENERKTSDEVYDEDPFAYSEPL | 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 osmoregulation required for the acquisition of normal morphology and motility when faced with osmotic challenges, such as those experienced after mixing with seminal fluid and entry into the vagina. {ECO:0000269|PubMed:23129643, ECO:0000269|PubMed:34980136, ECO:0000269|PubMed:35551387}. | 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), present in the promoters of target genes activated in early embryos (PubMed:27578796, PubMed:30479355). {ECO:0000269|PubMed:27578796, ECO:0000269|PubMed:30479355}.; FUNCTION: [Isoform 2]: Inactive transcriptional activity. {ECO:0000269|PubMed:27578796}. | Homo sapiens (Human) |
A8NCG7 | LP9_COPC7 | MKSFASLLFLAATAAAHATWQQIWVNGVDGGTSCLRRAANNNPIDVGAKELACNAHTLSPNVCTIKPGDKVTVEMHAQHGDRSCAQEAIGGNHYGPVMVYMAKVDDARTADANAADWFKVSEMGMASNNPVYWAVQVLNDNCGHWTFTVPDLAPGNYLIRSEVIALHVAGSIGGAQFYPGCFQVNVVGNGSGRPTETVKFPGAYKATDPGVLFDMYRPQSTYIIPGPRPYGTSPATVANTPYPTTATWNTALQPTTVPTVTPPVGGGTNPPPVTTVAPPVVTSQPPVPPTTQQPPVVTPTAPPSGPLQTQYGQCGGQGWNGPTQCQPPYTCTASNQWYHQCL | 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) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (PubMed:37463979). Shows only weak binding properties to cellulose, and low cellulolytic oxidative activity which questions the involvement of X282 extension-containing AA9 proteins in the degradation of plant cell wall and opens new avenues as to the divergence of function of some AA9 members (PubMed:37463979). {ECO:0000269|PubMed:37463979}. | Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003) (Inky cap fungus) (Hormographiella aspergillata) |
A8NMB4 | ARO1_COPC7 | MAVADDTKADLLKVSILGKESIHCGFHLTPYIVQTVLTTLPSSTYVLITDDNIAKLHLNKFEEAFAKGIEKSAANPKPRFLSHVIPPGETSKSREGKARIEDFLLFHKCTRDSVILALGGGVIGDLVGFVAATFMRGVRFCQIPTTLLAMVDSSVGGKTAIDTPHGKNLIGAFWQPEYIFIDAAYLETLPTREFSNGMAEVVKTAAIWDEKEFTSLESRSAELFAAIQTPSTNYAGRTLETRSEAQKLLLSTIAASIGVKAHIVTIDERETGLRNLVNFGHSIGHAIEAVLTPTILHGECVSIGMILEAELSRQLGILTQVGVGRLTRCLKAYNLPTSLSAPLIASLPQASLLTVPRLLDIMRIDKKNSGTNKKIVLLKRIGETYEQKASIVEDKAIEKTLAEAVTVVPSIPTGNVKGSPGEVRMSTPGSKSISNRALVLAALAKGTCRLRNLLHSDDTQGAVFTWEDGGETLVVEGGEGTLTVPTPGKELYLGNAGTAARFLTTVCALAQPAPASVQPPSTNTVITGNARMKQRPIGPLVDALRANGCSIGYRESEGCLPLSIPPNSFKGGKIQLAASVSSQYVSSILLCAPYAQDANGVTLELVGGEVISQPYIDMTIAMMKTFGVEVTRRTDASGKLLDIYDIPRGTYVNPPVYNIESDASSATYPLAVAAITGTKCTIENIGSSSLQGDAKFAVEVLQKMGCEVHQTADETTVQGPPLGQLKAIEEVDMEVMTDAFLTASVLAAVANGGENKAMKITGIANQRVKECNRIRAMMDELAKFGVHTTEQELGLTIYAVPISQLKKNVSVHCYDDHRVAMAFSVLSTVVEGAIIEEKRCVEKTWPGWWDDLENKIGIKVEGVDLAGLRAESSSAGVKESKPIDNSSILLIGMRGTGKTHIGQLAAASLPGWSFVDADHYFESKLKTGVKDFVKNEGWEKFREEELAVLAELIGLGVDGKAVSSPSSYSKNHVISLGGGIVETPAARSLLKAYLAKGGRVVHITRPIDEIVRYLNVETARPAYEEPILDVWKRREPWYKECSGWEFGNVVVEAPQGQAQAANVEAGPGKTKCVKTLAGRNEVKRFFGHLAGINPNFTHGGSVEGQQRRTYFLCLTYPDVRHAFPYIDELTEGADALELRVDLLKDAKAPEAPFPSVAYVKDQVTALRRVTGLPIIYTVRTKAQGGAFPDGNAKEYKELVEAGVRLGVEYLDVEVASIFSDKEVADLSKRTKKAGSTLVIASWHDWSGKMQWDGEDVKRKYDEARKFGDLVKIVGKAEKLEDNFKLLSFVKSATSLPNSPPIIAINMSTLGQSSRILNTTFTPVSHPLLPTKAAPGQLSFKQIQQALHLLGLLPSKHFHLFGTPIAHSMSPTLHNTGFELLGLPFKYGLLESKEVDCKEVRDVISDKEGFGGASVTIPFKVDVIELLDELTESAKEIGAVNTIIPVHRSSINAQGQEETTRVLVGDNTDWVGIRVCITQRVSEGELRNENTSGLVIGAGGTARAAIYALQDLGVPVIYLFNRTKEKAEDLAKAFVGGADKKWNGQLVVLDKLGGGWGDVGVAPRVIVSTVPASATALPSASTAAIAGQVDKSTNQIVLPADVFAYTSGSAVVVDMAYKPAETPLLKLAKELKEEGNWACVQGLEVLLEQGYIQFEKWTGRRCPKEQVSTRVWEKYGEV | 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:0004765] | 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; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | 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: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | 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 | MTETVTDQGKQRSSKLQKNEAAKDEQVEGKGKETLESGTDKSAEQNSSLLVGQPDVIDNDNVQTVDDFKNLMYKMQETRRAIVFALLNEKDLTKDDVEILKRAYEKLTDNQTHSFQREMCTLTTKLSVNIGDETRGLEKDLKYLDALMNIRREEPNLLWPIIMSRVDLFSILANYHPKGKETFLKEYEDTVKFLKTFISSEAITGKKPIFITDWDGTMKDYCSQYATNLQPVYSAVGMTRFAASFTRISAVLTAGPLRGPGILDLTAMPIDGPVMFSGSWGREWWLSGKRVVHQDGITDEGFNALQRLDDEMKDLLHTSDYAPFALVGSGVQRKVDRLTLGVQTVCHHVTSELSNRYQMAVKERMHRVDPNSQILVFDPSTELEVEVVAHNSGIIWNKGNGVERLIKSLGDSLQSPGKILICGDTLSDIPMVRQAVKQNPDGVLAIFVGAKMSLREEVKQVIGDESRCCFVSCPDVIHAAMSQILNEHCIGK | 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:25955297, ECO:0000269|PubMed:26199121, ECO:0000269|PubMed:26239010, ECO:0000269|PubMed:26365206, ECO:0000269|PubMed:27130210, ECO:0000269|PubMed:27571030}; CATALYTIC ACTIVITY: Reaction=a diacylglycerol + H2O = a fatty acid + a monoacylglycerol + H(+); Xref=Rhea:RHEA:32731, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17408, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; Evidence={ECO:0000269|PubMed:17460728, ECO:0000269|PubMed:24556587, ECO:0000269|PubMed:25837472, ECO:0000269|PubMed:25955297, ECO:0000269|PubMed:26239010, ECO:0000269|PubMed:26365206, ECO:0000269|PubMed:27130210, ECO:0000269|PubMed:27571030}; | 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 does not exhibit regio-selective production of diacylglycerols (PubMed:17460728, PubMed:22750000, PubMed:25837472, PubMed:25955297, PubMed:26239010, PubMed:26365206, PubMed:27130210). Able to hydrolyze diacylglycerols such as distearin, dilinolein, dipalmitoylglycerol and dipalmitolein (PubMed:27130210). Cleaves oleic acid from 1,2 isomers of diolein on both the 1 and the 2 position of the glycerol backbone, resulting mainly in free fatty acids but no monoolein is detected (PubMed:27130210). Shows activity on monoolein and liberates mostly free fatty acids, but can also perform the reverse reaction and produce diolein (PubMed:27130210). {ECO:0000269|PubMed:17460728, ECO:0000269|PubMed:18000048, ECO:0000269|PubMed:22750000, ECO:0000269|PubMed:25837472, ECO:0000269|PubMed:25955297, ECO:0000269|PubMed:26239010, ECO:0000269|PubMed:26365206, ECO:0000269|PubMed:27130210}. | Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated fungus) |
A8QCB2 | ARO1_MALGO | MSQVSGGKVPSYHAPPFDSPLSGATIHELRCLDTKVQLGFHLVPHIAKTLITELPSSAYVLVTDTNLAKLGAIDKFRKAFEAIPGARLLVYELAPGEESKSRETKAAIEDWMLEHRLTRDTVVLACGGGVIGDLVGFVAATFMRGLKYVQIPTTLLAMVDSSVGGKTAIDHPHGKNLIGAFHQPRYVFIDAAWLLTLPEREFSNGMAEVIKTAAIWDAADFEKLESESASIRAAVMGDEARQQSAAQGHTLATRTSSQSLLLDVIRGSVGVKAHIVTIDEKETGLRNLVNFGHSVGHAIEAVLTPDILHGECVAVGMVLEAEIARLVHGLPQVAIGRLVRCLRLYNLPVTLADARIMALSKVRELTTARVLDIMRVDKKNAGAQKKIVLLSRIGATVEERASTVSDAMIERVLAPAMLVRESVSAPRPPLTIHTPGSKSVSNRALVLAALSGGTCRLRHLLHSDDTQVMMQALAQLRAADFAWEDNGATLVVHGQGGRVLASDEPVYLQNAGTAARFVTAVACLASSASCSGSDESSCHGVVHLTGNARMKQRPIGPLVDALRSNGARIDYVEQSNCLPLNVTASGALQGGRIELAADVSSQYVSAVLLCAPYAQNDVELALVGGKVISQPYIDMTIAMMQSFGVRVERVAEHVYRIPRTTYVAPSTYEVECDASSATYPLAIAAITGTTVTVPSLGRASLQGDAAFARKVLAPMGCQVEQNDVSTTVTGPPVGMLKALGAIDMESMTDAFITAAMLFAVATAPCDEYASSSTSASPSSTRITGIANQRVKECDRLRAVVTELAKLGVRAVEHDDGIEVFSTPISQLLPHASIYCYDDHRIAMAFSVLACVVPGAGTEIQEKRCVEKTWPSWWDVLGGPLNVPIAGARLNDALVSLVARSRQRGPPTPTTLYGRDASIVLIGMRASGKSHVGRSLAKLLHRTFVDADVVFSDMYDIGAFVQDHGWDAFRAEESRILESLLTQCSVGHVIALGGGVIESAASRALLARFREHVGPVVHIVRDFALIESFLATSDRPAYGEPLADVYARRLPLYAESSCMEAVNTGNDAALALSRQLRTPLGTPVPISPAFFLSLTFPRVQDAWSILDHASAGVDVLELRVDLLHADGQPSIDDVREQVALLRQYTSLPILYTVRSVSQGGRLPDEANEAYFALTRLGLRMGCEYVDIELTRPSDGIEELAQAKGQTRIVASFHDTSGTMHWMAPAMRRLYTRACVLGDIAKLVGFARTWQDSLDLESFRTRVAQEAPFPLIAINMQAAGQLSRIVNPLLTPVTHPALPVPAAPGQMSVRDIHHARHLLGLLPKRHFFLFGSPITHSQSPLIHNTAFELLGLPHVYARHETDSVDASVEALVRAGDFGGASVTIPHKLSIMQLLDSVSPHAQVIGAVNTIVPHRDETTGHMALHGENTDWRAIVDLVAKHDGGRTRACTALVIGAGGSARAALYAMHKLGASRILLYNRTFEKAVNLAEQVPVEWRVEPVDSLALAAKAKPNVIVSNVPAQGTSFTPGGADIVLPLDLLSSDGGVAIDMAYRPEITPLLTLAQQHQSWHGVRGIEILLAQAFHQFRLWTGLPPPCLDIETTVYAAYRAAAASM | 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:0004765] | 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; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; | 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: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}. | 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 | MNVFSIFSLVFLAAFGSCADDRRSALEECFREADYEEFLEIARNGLKKTSNPKHVVVVGAGMAGLSAAYVLAGAGHRVTLLEASDRVGGRVNTYRDEKEGWYVNMGPMRLPERHRIVRTYIAKFGLKLNEFFQENENAWYFIRNIRKRVWEVKKDPGVFKYPVKPSEEGKSASQLYRESLKKVIEELKRTNCSYILDKYDTYSTKEYLIKEGNLSRGAVDMIGDLLNEDSSYYLSFIESLKNDDLFSYEKRFDEISDGFDQLPKSMHQAIAEMVHLNAQVIKIQRDAEKVRVAYQTPAKTLSYVTADYVIVCATSRAVRRISFEPPLPPKKAHALRSIHYKSATKIFLTCTRKFWEADGIHGGKSTTDLPSRFIYYPNHNFTSGVGVIVAYVLADDSDFFQALDIKTSADIVINDLSLIHQLPKNEIQALCYPSLIKKWSLDKYTMGALTSFTPYQFQDYIETVAAPVGRIYFAGEYTATVHGWLDSTIKSGLTAARNVNRASQKPSRIHLINDNQL | 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 + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938, ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:19393676}; CATALYTIC ACTIVITY: Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938, ChEBI:CHEBI:58095; Evidence={ECO:0000269|PubMed:19393676}; CATALYTIC ACTIVITY: Reaction=H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+); Xref=Rhea:RHEA:61244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938, ChEBI:CHEBI:57912; Evidence={ECO:0000269|PubMed:19393676}; CATALYTIC ACTIVITY: Reaction=H2O + L-methionine + O2 = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:61236, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723, ChEBI:CHEBI:28938, ChEBI:CHEBI:57844; Evidence={ECO:0000269|PubMed:19393676}; CATALYTIC ACTIVITY: Reaction=H2O + L-isoleucine + O2 = (S)-3-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:61232, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35146, ChEBI:CHEBI:58045; Evidence={ECO:0000269|PubMed:19393676}; CATALYTIC ACTIVITY: Reaction=H2O + L-arginine + O2 = 5-guanidino-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:51404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32682, ChEBI:CHEBI:58489; Evidence={ECO:0000269|PubMed:19393676}; CATALYTIC ACTIVITY: Reaction=H2O + L-aspartate + O2 = H2O2 + NH4(+) + oxaloacetate; Xref=Rhea:RHEA:19025, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991; Evidence={ECO:0000269|PubMed:19393676}; CATALYTIC ACTIVITY: Reaction=H2O + L-histidine + O2 = 3-(imidazol-5-yl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61228, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57595, ChEBI:CHEBI:58133; Evidence={ECO:0000269|PubMed:19393676}; CATALYTIC ACTIVITY: Reaction=H2O + L-asparagine + O2 = 2-oxosuccinamate + H2O2 + NH4(+); Xref=Rhea:RHEA:61224, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57735, ChEBI:CHEBI:58048; Evidence={ECO:0000269|PubMed:19393676}; CATALYTIC ACTIVITY: Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; Evidence={ECO:0000269|PubMed:19393676}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine + O2 = 2-oxoglutaramate + H2O2 + NH4(+); Xref=Rhea:RHEA:61260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16769, ChEBI:CHEBI:28938, ChEBI:CHEBI:58359; Evidence={ECO:0000269|PubMed:19393676}; CATALYTIC ACTIVITY: Reaction=H2O + L-alanine + O2 = H2O2 + NH4(+) + pyruvate; Xref=Rhea:RHEA:61264, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57972; Evidence={ECO:0000269|PubMed:19393676}; CATALYTIC ACTIVITY: Reaction=H2O + L-lysine + O2 = 6-amino-2-oxohexanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:14437, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32551, ChEBI:CHEBI:58183; Evidence={ECO:0000269|PubMed:19393676}; CATALYTIC ACTIVITY: Reaction=H2O + L-glutamate + O2 = 2-oxoglutarate + H2O2 + NH4(+); Xref=Rhea:RHEA:20728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985; Evidence={ECO:0000269|PubMed:19393676}; | 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=1.44 mM for L-Glu {ECO:0000269|PubMed:19393676}; KM=4.84 mM for L-His {ECO:0000269|PubMed:19393676}; KM=1.64 mM for L-Ile {ECO:0000269|PubMed:19393676}; KM=60.69 mM for L-Leu {ECO:0000269|PubMed:19393676}; KM=21.49 mM for L-Lys {ECO:0000269|PubMed:19393676}; KM=15.03 mM for L-Met {ECO:0000269|PubMed:19393676}; KM=0.13 mM for L-Phe {ECO:0000269|PubMed:19393676}; KM=0.27 mM for L-Trp {ECO:0000269|PubMed:19393676}; KM=0.05 mM for L-Tyr {ECO:0000269|PubMed:19393676}; | 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 moderately active against L-Lys, L-Arg, L-Ala and L-Asn (PubMed:19393676). Exhibits diverse biological activities, such as edema, inflammatory cell infiltration, cytotoxicity and apoptosis, as well as induction of platelet aggregation (PubMed:19393676). Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. This protein may also induce hemorrhage, hemolysis, and have antibacterial and antiparasitic activities. {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:19393676}. | 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 | MVLISEDSRELLQAHVELWNQTYSFMKSVALAVALDLHIADAIHRRGGAATLSQILGEIGVRPCKLPGLHRIMRVLTVSGTFTIVQPSAETMSSESDGREPVYKLTTASSLLVSSESSATASLSPMLNHVLSPFRDSPLSMGLTAWFRHDEDEQAPGMCPFTLMYGTTLWEVCRRDDAINALFNNAMAADSNFLMQILLKEFSEVFLGIDSLVDVAGGVGGATMAIAAAFPCLKCTVLDLPHVVAKAPSSSIGNVQFVGGDMFESIPPANVVLLKWILHDWSNDECIKILKNCKQAIPSRDAGGKIIIIDVVVGSDSSDTKLLETQVIYDLHLMKIGGVERDEQEWKKIFLEAGFKDYKIMPILGLRSIIELYP | 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:CHEBI:59789; EC=2.1.1.n7; Evidence={ECO:0000269|PubMed:17998204}; | 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=23 uM for 5-n-heptyl-resorcinol {ECO:0000269|PubMed:17998204}; KM=67.5 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:17998204}; Vmax=4.3 pmol/sec/mg enzyme with 5-n-propyl-resorcinol as methyl acceptor {ECO:0000269|PubMed:17998204}; Vmax=9.2 pmol/sec/mg enzyme with 5-n-butyl-resorcinol as methyl acceptor {ECO:0000269|PubMed:17998204}; Vmax=10.9 pmol/sec/mg enzyme with 5-n-pentyl-resorcinol as methyl acceptor {ECO:0000269|PubMed:17998204}; Vmax=7 pmol/sec/mg enzyme with 5-n-hexyl-resorcinol as methyl acceptor {ECO:0000269|PubMed:17998204}; Vmax=2.9 pmol/sec/mg enzyme with 5-n-heptyl-resorcinol as methyl acceptor {ECO:0000269|PubMed:17998204}; | 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|PubMed:17998204}. | Sorghum bicolor (Sorghum) (Sorghum vulgare) |
A8R3S4 | QEDH_PSEPU | MTIRSLPAALSPLSMAVQAVLLVSSLALAPAANAKPVTWEDIANDHLNTQNVLQYGMGTNAQRWSPLAMVNDKNVFKLTPAWSYSFGDERQRGQESQAIINDGVIYVTGSYSRVFALDAKTGRRLWTYNHRLPDNIRPCCDVVNRGAAIFGDKIYFGTLDARVIALNKDTGKVVWNKKFGDHSAGYTMTGAPTLIKDQKSGKVLLIHGSSGDEFGVVGQLYARDPETGEEVWMRPFVEGHMGRLNGKDSTPTGDVKAPSWPDDPTTETGKVESWSHGGGAPWQSASFDPETNTIIVGAGNPGPWNTWARTSKDGNPHDFDSLYTSGQVGVDPTTGEVKWFYQHTPNDAWDFSGNNELVLFDYKDKDGKQYKATAHADRNGFFYVVDRTNGKLKNAFPFVDNITWASHIDLKTGRPVENEGQRPAKPLPGETKGKPVEVSPPFLGGKNWNPMAYSQDTGLFYVPANHWKEEYWTEEVNYKKGSAYLGIGFRIKRMYEDHVGSLRAMDPTTGKVVWEHNERLPLWAGVLATKGNLVFTGTGDGYFKAFNAKTGEELWKFQTGSGIVSPPITWEQDGEQYIGVTVGYGGAVPLWGGDMAELTKPVAQGGSFWVFKIPAWDTKTAKR | 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:7730276}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q9Z4J7}; Note=Binds 2 calcium ions per subunit. One is located in the active-site cavity near PQQ and the second calcium binds at the N-terminus and contributes to the stability of the native enzyme. {ECO:0000250|UniProtKB:Q9Z4J7}; | 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|PubMed:18218017, ECO:0000305|PubMed:7730276}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51021; Evidence={ECO:0000269|PubMed:18218017}; CATALYTIC ACTIVITY: Reaction=ethanol + 2 Fe(III)-[cytochrome c] = acetaldehyde + 2 Fe(II)-[cytochrome c] + 2 H(+); Xref=Rhea:RHEA:62200, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378, ChEBI:CHEBI:16236, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; Evidence={ECO:0000305|PubMed:18218017, ECO:0000305|PubMed:7730276}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62201; Evidence={ECO:0000269|PubMed:18218017}; CATALYTIC ACTIVITY: Reaction=A + ethanol = acetaldehyde + AH2; Xref=Rhea:RHEA:33567, ChEBI:CHEBI:13193, ChEBI:CHEBI:15343, ChEBI:CHEBI:16236, ChEBI:CHEBI:17499; Evidence={ECO:0000269|PubMed:7730276}; CATALYTIC ACTIVITY: Reaction=1-propanol + 2 Fe(III)-[cytochrome c] = 2 Fe(II)-[cytochrome c] + 2 H(+) + propanal; Xref=Rhea:RHEA:62204, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:17153, ChEBI:CHEBI:28831, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; Evidence={ECO:0000305|PubMed:7730276}; | 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 umol/min/mg enzyme with butan-1-ol as substrate {ECO:0000269|PubMed:7730276}; Vmax=12.3 umol/min/mg enzyme with propane-1,2-diol as substrate {ECO:0000269|PubMed:7730276}; | 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 and energy metabolism during growth of P.putida on ethanol as the sole carbon and energy source (PubMed:18218017). Displays lower activity on secondary alcohols, aldehydes and diols. Is not active with sugar alcohols such as glycerol and D-sorbitol (PubMed:7730276). In vitro, reacts well with phenazine methosulfate (PMS) as an electron acceptor but not with NAD(P), potassium ferricyanide, or molecular oxygen (PubMed:7730276). {ECO:0000250|UniProtKB:Q9Z4J7, ECO:0000269|PubMed:18218017, ECO:0000269|PubMed:7730276}. | Pseudomonas putida (Arthrobacter siderocapsulatus) |
A8R7E6 | CERK1_ARATH | MKLKISLIAPILLLFSFFFAVESKCRTSCPLALASYYLENGTTLSVINQNLNSSIAPYDQINFDPILRYNSNIKDKDRIQMGSRVLVPFPCECQPGDFLGHNFSYSVRQEDTYERVAISNYANLTTMESLQARNPFPATNIPLSATLNVLVNCSCGDESVSKDFGLFVTYPLRPEDSLSSIARSSGVSADILQRYNPGVNFNSGNGIVYVPGRDPNGAFPPFKSSKQDGVGAGVIAGIVIGVIVALLLILFIVYYAYRKNKSKGDSFSSSIPLSTKADHASSTSLQSGGLGGAGVSPGIAAISVDKSVEFSLEELAKATDNFNLSFKIGQGGFGAVYYAELRGEKAAIKKMDMEASKQFLAELKVLTRVHHVNLVRLIGYCVEGSLFLVYEYVENGNLGQHLHGSGREPLPWTKRVQIALDSARGLEYIHEHTVPVYVHRDIKSANILIDQKFRAKVADFGLTKLTEVGGSATRGAMGTFGYMAPETVYGEVSAKVDVYAFGVVLYELISAKGAVVKMTEAVGEFRGLVGVFEESFKETDKEEALRKIIDPRLGDSYPFDSVYKMAELGKACTQENAQLRPSMRYIVVALSTLFSSTGNWDVGNFQNEDLVSLMSGR | 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]; detection of peptidoglycan [GO:0032499]; innate immune response [GO:0045087]; intracellular signal transduction [GO:0035556]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; response to chitin [GO:0010200] | 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:0106310]; protein serine/threonine kinase activity [GO:0004674]; transmembrane receptor protein kinase activity [GO:0019199] | 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:0000269|PubMed:20610395}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:18042724, ECO:0000269|PubMed:20610395}; | 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-acetylglucosamine (NAG)-containing ligands. Involved in the resistance to pathogenic fungi Alternaria brassicicola and Erysiphe cichoracearum, probably by sensing microbe-associated molecular patterns (MAMP) and pathogen-associated molecular patterns (PAMP). Plays an essential role in detecting peptidoglycans (e.g. PGNs) and restricting bacterial growth. Target of the bacterial type III effector E3-ligase protein hopAB2/avrPtoB of Pseudomonas syringae pv. tomato DC3000 that mediates ubiquitination and subsequent proteolysis, thus blocking all defense responses by suppressing PAMP-triggered immunity (PTI). Mediates chitin-induced phosphorylation of PBL27 (PubMed:24750441). {ECO:0000269|PubMed:18042724, ECO:0000269|PubMed:18263776, ECO:0000269|PubMed:19249211, ECO:0000269|PubMed:19816132, ECO:0000269|PubMed:20610395, ECO:0000269|PubMed:22106285, ECO:0000269|PubMed:22461667, ECO:0000269|PubMed:22891159, ECO:0000269|PubMed:24750441}. | Arabidopsis thaliana (Mouse-ear cress) |
A8R7K9 | VP35C_ARATH | MIADDDEKWLAAAIAAVKQNAFYMQRAIDSNNLKDALKFSAQMLSELRTSKLSPHKYYELYMRVFNELGTLEIFFKEETGRGCSIAELYELVQHAGNILPRLYLLCTIGSVYIKSKDVTATDILKDLVEMCRAVQHPLRGLFLRSYLAQVTRDKLPSIGSDLEGDGDAHMNALEFVLQNFTEMNKLWVRMQHQGPSREKEKREKERNELRDLVGKNLHVLSQLEGVDLGIYRDTVLPRILEQVVNCKDELAQCYLMDCIIQVFPDDFHLQTLDVLLGACPQLQPSVDIKTVLSGLMERLSNYAASSVEALPNFLQVEAFSKLNYAIGKVVEAQADLPAAASVTLYLFLLKFTLHVYSDRLDYVDQVLGSCVTQLSATGKLCDDKAAKQIVAFLSAPLEKYNNVVTILKLTNYPLVMEYLDRETNKAMAIILVQSVFKNNTHIATADEVDALFELAKGLMKDFDGTIDDEIDEEDFQEEQNLVARLVNKLYIDDPEEMSKIIFTVRKHIVAGGPKRLPLTIPPLVFSALKLIRRLRGGDENPFGDDASATPKRILQLLSETVEVLSDVSAPDLALRLYLQCAQAANNCELETVAYEFFTKAYLLYEEEISDSKAQVTALRLIIGTLQRMRVFNVENRDTLTHKATGYSARLLRKPDQCRAVYECAHLFWADECENLKDGERVVLCLKRAQRIADAVQQMANASRGTSSTGSVSLYVELLNKYLYFLEKGNQQVTGDTIKSLAELIKSETKKVESGAEPFINSTLRYIEFQRQQEDGGMNEKYEKIKMEWFE | 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 specific cargos from endosome to the plasma membrane. {ECO:0000250}. | Arabidopsis thaliana (Mouse-ear cress) |
A8T644 | PCSK9_PANTR | MGTVSSRRSWWPLPLLLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGTTATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAVARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSIHTAPPAEAGMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPMLRPRGQPNQCVGHREASIHASCCRAPGLECKVKEHGIPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDNTCVVRSRDVSTAGSTSEEAVAAVAICCRSRHLAQASQELQ | 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 and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein (By similarity). {ECO:0000250}.; PTM: Phosphorylation protects the propeptide against proteolysis. {ECO:0000250}. | 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 apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation (By similarity). {ECO:0000250}. | 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 degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity). {ECO:0000250}. | Pan troglodytes (Chimpanzee) |
A8T650 | PCSK9_GORGO | MGTVSSRRSWWPLPLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGTTATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAVARCAPDEELLSCSSFSRSGKRRGEHMEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAEAGMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYGIDNTCVVRSRDVSTTGRTSEEALAAVAICCRSRHLVQASQELQ | 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 and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein (By similarity). {ECO:0000250}.; PTM: Phosphorylation protects the propeptide against proteolysis. {ECO:0000250}. | 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 apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation (By similarity). {ECO:0000250}. | 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 degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity). {ECO:0000250}. | Gorilla gorilla gorilla (Western lowland gorilla) |
A8T655 | PCSK9_PANPA | MGTVSSRRSWWPLPLLLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGTTATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAAHRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVRPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAVARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAEAGMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCRAPGLECKVKEHGIPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDNTCVVRNRDVSTAGSTSEEAVAAVAICCRSRHLAQASQELQ | 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 and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein (By similarity). {ECO:0000250}.; PTM: Phosphorylation protects the propeptide against proteolysis. {ECO:0000250}. | 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 apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation (By similarity). {ECO:0000250}. | 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 degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity). {ECO:0000250}. | Pan paniscus (Pygmy chimpanzee) (Bonobo) |
A8T658 | PCSK9_PONPY | MGTVSSRRSWWPLPLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGATATFHRCAKDPWRLPGTYVVVLKEETHRSQSERTARRLQAQAARRGYLTKILHVFHDLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLMPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSVEPELTLAELRQRLIHFSAKDVINEVWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAIARCAPDEELLSCSSFSRSGKRRGERMEAQGGKLVCRAHNAFGGEGVCAIARCCLLPQANCSVHTAPPAGSGMGTRVLCHQQVHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCRAPGLECKVKEHGIPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDNTCVVRSRDISTTGSTSEEAMAAVAICCRRRHLAQASQELQ | 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 and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein (By similarity). {ECO:0000250}.; PTM: Phosphorylation protects the propeptide against proteolysis. {ECO:0000250}. | 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 apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation (By similarity). {ECO:0000250}. | 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 degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity). {ECO:0000250}. | Pongo pygmaeus (Bornean orangutan) |
A8T662 | PCSK9_MACNE | MGTVSSRRSWWPLPLPLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLADAPEHGATATFHRCAKDPWRLPGTYVVVLKEETHRSQSERTARRLQAQAARRGYLTKILHVFHHLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPKGGSLVEVYLLDTSIQSDHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGAGLRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVFNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSRSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHRAGWQLFCRTVWSAHSGPTRMATAVARCAQDEELLSCSSFSRSGKRRGERIEAQGGKRVCRAHNAFGGEGVYAIARCCLLPQVNCSVHTAPPAGASMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVIVACEDGWTLTGCSALPGTSHVLGAYAVDNTCVVRSRDVSTTGSTSEEAVAAVAICCRSRHLVQASQELQ | 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 and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein (By similarity). {ECO:0000250}.; PTM: Phosphorylation protects the propeptide against proteolysis. {ECO:0000250}. | 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 apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation (By similarity). {ECO:0000250}. | 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 degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity). {ECO:0000250}. | Macaca nemestrina (Pig-tailed macaque) |
A8T666 | PCSK9_MACMU | MGTVSSRRSWWPLPLPLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLADAPEHGATATFHRCAKDPWRLPGTYVVVLKEETHRSQSERTARRLQAQAARRGYLTKILHVFHHLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPKGGSLVEVYLLDTSIQSDHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGAGLRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVFNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSRSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHRAGWQLFCRTVWSAHSGPTRMATAVARCAQDEELLSCSSFSRSGKRRGERIEAQGGKRVCRAHNAFGGEGVYAIARCCLLPQVNCSVHTAPPAGASMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVIVACEDGWTLTGCSPLPGTSHVLGAYAVDNTCVVRSRDVSTTGSTSKEAVAAVAICCRSRHLVQASQELQ | 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 and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein (By similarity). {ECO:0000250}.; PTM: Phosphorylation protects the propeptide against proteolysis. {ECO:0000250}. | 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 apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation (By similarity). {ECO:0000250}. | 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 degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity). {ECO:0000250}. | Macaca mulatta (Rhesus macaque) |
A8T672 | PCSK9_COLGU | MGTVSSRRSWWPLPLPLLLLLLLGLAGARAQEDEDGDYEELVLALRSEEDGLADAPEHGATATFHRCAKDPWRLPGTYVVVLKEETHRSQSERTARRLQAQAARRGYLTKILHVFHHLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPKGGSLVEVYLLDTSIQSDHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGAGLRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVFNAACQRLARAGVVLVTAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSRSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHRAGWQLFCRTVWSAHSGPTRMATAVVRCAPDEELLSCSSFSRSGKRRGERIEAQGGKRVCRAHNAFGGEGVYAIARCCLLPQVNCSVHTAPPAGASMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRGQPNQCVGHREASIHASCCHAPGLECKVKEHGIPAPQEQVIVACEDGWTLTGCNALPGTSHVLGAYAVDNTCVVRSRDVSTTGSTSEEAMAAVAICCRSRHLVQASQELQ | 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 and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein (By similarity). {ECO:0000250}.; PTM: Phosphorylation protects the propeptide against proteolysis. {ECO:0000250}. | 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 apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation (By similarity). {ECO:0000250}. | 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 degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity). {ECO:0000250}. | Colobus guereza (Mantled guereza) (Eastern black-and-white colobus monkey) |
A8T677 | PCSK9_PLEMO | MGTVSSRRLWWPLPLLLLLLLGPPGARAQEDDDGDYEELVLALRSEEDGPADALQHGATATFHRCAKDPWRLPGTYVVVLKDSDAHRSQPERTARRLQAQAARRGYLIKLLHVFHHLLPGFLVKMSRDLLELALRLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSSHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLHVLNCQGKGTVSSALIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACRRLAGAGVVLVAAAGNFRDDACLYSPASAPEVITVGATNAQDQPLTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSRSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVATLPPSTHGAGWQLFCRTVWSAHSGPTRMATAMARCAPDEELLSCSSFSRSGKRRGERIEAQGGRRVCLAPNAFGGEGVYAVARCCLLPQANCSVHTAPPAGAGMGTRAHCHQQGHVLTGCSSHWEMKDLGTHKPPVLKPRGQPDQCMGHSGASTHASCCYAPGLECKVKEHGLPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDDTCVVRSRDVSTTGSTSEEAVAAVAICCRSRHLA | 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 and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein (By similarity). {ECO:0000250}.; PTM: Phosphorylation protects the propeptide against proteolysis. {ECO:0000250}. | 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 apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation (By similarity). {ECO:0000250}. | 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 degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity). {ECO:0000250}. | Plecturocebus moloch (Dusky titi monkey) (Callicebus moloch) |
A8T682 | PCSK9_SAGLB | MGTVSSRRLWWPLPLLLLLLLGPAGTRAQEDDDDDYEELVLALRSEEEGLADALQNGATATFHRCAKDPWRLPGTYVVVLKEETHRSQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALRLPHVDYIEEDSSVFAQSIPWNLERITPARYQADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFGSVPKEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLHSLRVLNCQGKGTVSSTLIGLEFICKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARARVVLVAAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSRSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGEGWQLFCRTVWSAHSGPTRMATAMARCAPDEELLSCSSFSRSGKRRGERIEAQGGRRVCLAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAGAGMGTRAHCHQQGHILTGCSSHWEVEDLGTHKPPVLRPEGQHNQCMGHRGASTHASCCHAPGLECKVKEHGLPAPQEQVTVTCEEGWTLTGCSALPGTSHVLGAYAVDDTCVVRSRDVSTTGSTSEETVAAIAICCRSQHLAQAS | 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 and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein (By similarity). {ECO:0000250}.; PTM: Phosphorylation protects the propeptide against proteolysis. {ECO:0000250}. | 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 apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation (By similarity). {ECO:0000250}. | 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 degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity). {ECO:0000250}. | Saguinus labiatus (Red-chested mustached tamarin) |
A8T688 | PCSK9_CALJA | MGTVSSRRLWWPLPLLLLLLLGPTGTRAQEEDDDDYEELVLALRSEEDGLVDALQHGATATFHRCAKDSWRLPGTYVVVLKEETHRSQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALRLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFGSVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLRVLNCQGKGTVSSTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVAAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSRSGTSQAAAHVAGIAAMMLSAKPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAMARCAPDEELLSCSSFSRSGRRRGERIEAQGGRRVCLAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAGAGMGTRAHCHQQGHILTGCSSHWEVEDLGTHKPPVLRPGGQHDQCMGHRGASTHASCCHAPGLECKVKEHGLPAPQEQVTVTCEEGWTLTGCSALPGTSHILGAYAVDDTCVVRSRDVSTTSSTSEETVATVAICCRSQHLAQASQELQ | 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 and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein (By similarity). {ECO:0000250}.; PTM: Phosphorylation protects the propeptide against proteolysis. {ECO:0000250}. | 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 apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation (By similarity). {ECO:0000250}. | 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 degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity). {ECO:0000250}. | Callithrix jacchus (White-tufted-ear marmoset) |
A8T695 | PCSK9_SAIBB | MGTVSSRRLWWPLPLLLLLLLLGPAGARAQEDDDGDYEELVLALRSEEDGLADALQHGATATFHRCAKEPWRLPGTYVVVLKEETHRSQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFGSVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLRVLNCQGKGTVSSTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVAAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSRSGTSQAAAHVAGIAAVMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAMARCAPDEELLSCSSFSSSGKRRGERIEAQGGRRVCLAHNAFGGKGVYAIARCCLLPQANCSIHTAPPAGASMGTRAHCHQQGHVLTGCSAHWEVEELGTHKPPVLRPGGQPSQCMGHSGASTHATCCHAPGLECKVKEHGLPAPQEQVTVACEEGWTLTGCSALPGTSHILGAYAVDDTCVVRSQDVSTTGSTSEEAVAAVAICCRSRHLAQASQELQ | 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]; low-density lipoprotein particle receptor catabolic process [GO:0032802]; lysosomal transport [GO:0007041]; negative regulation of low-density lipoprotein particle clearance [GO:0010989]; negative regulation of receptor internalization [GO:0002091]; negative regulation of receptor recycling [GO:0001920]; negative regulation of receptor-mediated endocytosis involved in cholesterol transport [GO:1905601]; neuron differentiation [GO:0030182]; phospholipid metabolic process [GO:0006644]; positive regulation of low-density lipoprotein particle receptor catabolic process [GO:0032805]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of receptor internalization [GO:0002092]; protein autoprocessing [GO:0016540]; regulation of neuron apoptotic process [GO:0043523]; triglyceride metabolic process [GO:0006641] | 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]; PCSK9-LDLR complex [GO:1990666]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | 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 activity [GO:0030547]; sodium channel inhibitor activity [GO:0019871]; very-low-density lipoprotein particle binding [GO:0034189]; very-low-density lipoprotein particle receptor binding [GO:0070326] | 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 and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein (By similarity). {ECO:0000250}.; PTM: Phosphorylation protects the propeptide against proteolysis. {ECO:0000250}. | 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 apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation (By similarity). {ECO:0000250}. | 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 degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity). {ECO:0000250}. | Saimiri boliviensis boliviensis (Bolivian squirrel monkey) |
A8T6A1 | PCSK9_ATEGE | MGTVRSRRLWWPLPLLLLLLRGPAGARAQEDDDGDYEELVLALRSEEDGLAEAPQHGATATFHRCAKDPWRLPGTYVVVLKEETQRSQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALRLPHVDYIEEDSYVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLRVLNCQGKGTVSSTLIGLEFIRKNQLVQPVGPLVVLLPLAGGYSRVLNAACQRLAKAGVVLVAAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSRSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAMARCAPDEELLSCSSFSRSGKRRGERIKAQGGRRVCLAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAGAGMGTRVHCHHQGHVLTGCSSHWEVEDLGTHKPSVLRPRVQPDQCMGHSGASTHASCCHAPGLECKVKEHGLPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDDTCVVRSRDVSTTGNTSEQAVAAVAICCRSRHLAQASQELQ | 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 and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein (By similarity). {ECO:0000250}.; PTM: Phosphorylation protects the propeptide against proteolysis. {ECO:0000250}. | 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 apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation (By similarity). {ECO:0000250}. | 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 degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity). {ECO:0000250}. | Ateles geoffroyi (Black-handed spider monkey) (Geoffroy's spider monkey) |
A8T6A6 | PCSK9_LAGLA | MGTVRSRRLWWPLPLLLLLLLGPAGARAQEDDDGDYEELVLALRSEEDGLAEALQHGATATFHRCAKDPWRLPGTYVVVLKEETQRLQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALRLPHVDYIEEDSYVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFESVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLRVLNCQGKGTVSSTLIGLEFIRKNQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVAAAGNFRDDACLYSPASAPEVITVGATNAQDQPVTLGTLGTNFGRCVDLFAPGEDIIGASSDCSTCFVSQSGTSQAAAHVAGIAAMMLSAEPELTLAELRQRLIHFSAKDVINEAWFPEDQRVLTPNLVAALPPSTHGAGWQLFCRTVWSAHSGPTRMATAMARCAPDEELLSCSSFSRSGKRRGERIEAQGGKLVCRAHNAFGGEGVYAIARCCLLPQANCSVHTAPPAGTGMGTRVHCHQQGHVLTGCSSHWEVEDLGTHKPPVLRPRVQPDQCMGHSGASTHASCCHAPGLECKVKEHGLPAPQEQVTVACEEGWTLTGCSALPGTSHVLGAYAVDDTCVVRSRDVGTTGNISEEAVTAVAICCRSWHLAQASQELQ | 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 and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein (By similarity). {ECO:0000250}.; PTM: Phosphorylation protects the propeptide against proteolysis. {ECO:0000250}. | 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 apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and colocalizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation (By similarity). {ECO:0000250}. | 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 degradation in intracellular acidic compartments. Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation. Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway. Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways (By similarity). {ECO:0000250}. | Lagothrix lagotricha (Brown woolly monkey) (Humboldt's woolly monkey) |
A8TX70 | CO6A5_HUMAN | MKILLIIFVLIIWTETLADQSPGPGPVYADVVFLVDSSDHLGPKSFPFVKTFINKMINSLPIEANKYRVALAQYSDEFHSEFHLSTFKGRSPMLNHLKKNFQFIGGSLQIGKALQEAHRTYFSAPINGRDRKQFPPILVVLASAESEDEVEEASKALQKDGVKIISVGVQKASEENLKAMATSHFHFNLRTIRDLSTFSQNMTQIIKDVTKYKEGAVDADMQVHFPISCQKDSLADLVFLVDESLGTGGNLRHLQTFLENITSSMDVKENCMRLGLMSYSNSAKTISFLKSSTTQSEFQQQIKNLSIQVGKSNTGAAIDQMRRDGFSESYGSRRAQGVPQIAVLVTHRPSDDEVHDAALNLRLEDVNVFALSIQGANNTQLEEIVSYPPEQTISTLKSYADLETYSTKFLKKLQNEIWSQISTYAEQRNLDKTGCVDTKEADIHFLIDGSSSIQEKQFEQIKRFMLEVTEMFSIGPDKVRVGVVQYSDDTEVEFYITDYSNDIDLRKAIFNIKQLTGGTYTGKALDYILQIIKNGMKDRMSKVPCYLIVLTDGMSTDRVVEPAKRLRAEQITVHAVGIGAANKIELQEIAGKEERVSFGQNFDALKSIKNEVVREICAEKGCEDMKADIMFLVDSSWSIGNENFRKMKIFMKNLLTKIQIGADKTQIGVVQFSDKTKEEFQLNRYFTQQEISDAIDRMSLINEGTLTGKALNFVGQYFTHSKGARLGAKKFLILITDGVAQDDVRDPARILRGKDVTIFSVGVYNANRSQLEEISGDSSLVFHVENFDHLKALERKLIFRVCALHDCKRITLLDVVFVLDHSGSIKKQYQDHMINLTIHLVKKADVGRDRVQFGALKYSDQPNILFYLNTYSNRSAIIENLRKRRDTGGNTYTAKALKHANALFTEEHGSRIKQNVKQMLIVITDGESHDHDQLNDTALELRNKGITIFAVGVGKANQKELEGMAGNKNNTIYVDNFDKLKDVFTLVQERMCTEAPEVCHLQEADVIFLCDGSDRVSNSDFVTMTTFLSDLIDNFDIQSQRMKIGMAQFGSNYQSIIELKNSLTKTQWKTQIQNVSKSGGFPRIDFALKKVSNMFNLHAGGRRNAGVPQTLVVITSGDPRYDVADAVKTLKDLGICVLVLGIGDVYKEHLLPITGNSEKIITFQDFDKLKNVDVKKRIIREICQSCGKTNCFMDIVVGFDISTHVQGQPLFQGHPQLESYLPGILEDISSIKGVSCGAGTEAQVSLAFKVNSDQGFPAKFQIYQKAVFDSLLQVNVSGPTHLNAQFLRSLWDTFKDKSASRGQVLLIFSDGLQSESNIMLENQSDRLREAGLDALLVVSLNTTAHHEFSSFEFGKRFDYRTHLTIGMRELGKKLSQYLGNIAERTCCCTFCKCPGIPGPHGTRGLQAMKGSQGLKGSRGHRGEDGNPGVRGDTGPQGDKGIAGCPGAWGQKGLKGFSGPKGGHGDDGIDGLDGEEGCHGFPGIKGEKGDPGSQGSPGSRGAPGQYGEKGFPGDPGNPGQNNNIKGQKGSKGEQGRQGRSGQKGVQGSPSSRGSRGREGQRGLRGVSGEPGNPGPTGTLGAEGLQGPQGSQGNPGRKGEKGSQGQKGPQGSPGLMGAKGSTGRPGLLGKKGEPGLPGDLGPVGQTGQRGRQGDSGIPGYGQMGRKGVKGPRGFPGDAGQKGDIGNPGIPGGPGPKGFRGLALTVGLKGEEGSRGLPGPPGQRGIKGMAGQPVYSQCDLIRFLREHSPCWKEKCPAYPTELVFALDNSYDVTEESFNKTRDIITSIVNDLNIRENNCPVGARVAMVSYNSGTSYLIRWSDYNRKKQLLQQLSQIKYQDTTEPRDVGNAMRFVTRNVFKRTYAGANVRRVAVFFSNGQTASRSSIITATMEFSALDISPTVFAFDERVFLEAFGFDNTGTFQVIPVPPNGENQTLERLRRCALCYDKCFPNACIREAFLPEDSYMDVVFLIDNSRNIAKDEFKAVKALVSSVIDNFNIASDPLISDSGDRIALLSYSPWESSRRKMGTVKTEFDFITYDNQLLMKNHIQTSFQQLNGEATIGRALLWTTENLFPETPYLRKHKVIFVVSAGENYERKEFVKMMALRAKCQGYVIFVISLGSTRKDDMEELASYPLDQHLIQLGRIHKPDLNYIAKFLKPFLYSVRRGFNQYPPPMLEDACRLINLGGENIQNDGFQFVTELQEDFLGGNGFIGQELNSGRESPFVKTEDNGSDYLVYLPSQMFEPQKLMINYEKDQKSAEIASLTSGHENYGRKEEPDHTYEPGDVSLQEYYMDVAFLIDASQRVGSDEFKEVKAFITSVLDYFHIAPTPLTSTLGDRVAVLSYSPPGYMPNTEECPVYLEFDLVTYNSIHQMKHHLQDSQQLNGDVFIGHALQWTIDNVFVGTPNLRKNKVIFVISAGETNSLDKDVLRNVSLRAKCQGYSIFVFSFGPKHNDKELEELASHPLDHHLVQLGRTHKPDWNYIIKFVKPFVHLIRRAINKYPTEDMKATCVNMTSPNPENGGTENTVLLLPGIYEIKTENGDLFDEFDSQAQHLLVLGNNHSSGSETATDLMQKLYLLFSTEKLAMKDKEKAHLEEISALVVDKQQEKEDKEMEATDI | 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 | MADTACLALRLLAALREEEARAVEELLRLGADPNLVLDDGAAAVHLAARASHPRALHCLRMLLRWGADPNARSAEGLTPVHVAAAWGCCGALELLLSRGGDPTLRDQDGLRPLDWALQQRHHNCARVLQELDTPTQPDETREPTETFHVAQGSFETETCQGPALAESSGVSQDSELHVHRAELEVEAVEVAVHPQSSEATENSDYSSDASFVTAVEDSLQPGRPGGALELVAGLWVTRGAVSAGKGAPNCQPQVLTLTARDTDKPVLPGDGDLGALHPHSSVPPMSDLQLLQALRALGYSPGPVTPFTRGHYLRRLQEAQASRADVGHSQELAEALRTGTIPDCQVDEEALAQCFQRLDPLKKWREGITKSSFTYLLLDPRLTKDLPARASSLTLAECLQCFVRAIFYVGKGTRARPDAHLWEAFGYHDQPRKQVCPKVRRILDIWASGRGIISLHCFQHVVAMEAYTREACLLDALGLQTLTNQKQGHYYGVVAHWPPSRRRRLGVHLLQRALLVFLAEGERELRPQDIQARG | 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 of meiotic recombination intermediates [GO:0000712] | 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 vesicle docking [GO:0016081] | 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, ECO:0000269|PubMed:26212709}. | 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 | MNGTGSVGHRWNSLSPEPHSGTESTASTPFVKSEFPFDDDLFGIDQVNNVKPHPMDMPCNLPIQPIEYNRRFSKDADHSTFVKNEIEENILNFNVNPEIAQDNGLDTQQIDIYRDLILRHLIQDISTTCAKLGLPNDFYLWSSEHGARWINEMCMQFNLQPPRNCSITGIDLLGMSQKDFEMILPAGGDTLHAQLQVWKTGTSDYVKAFENYHPPVTVQSSGMTAAENNMQSKTNWLASTNNQTNNMAAAENPNHPFFNGNGGYPNMSMSSFFQQGTVLPSPSNSDTSSNGSSQDMNDDDIDLHMNNSNCGFSNFFHNQGYMNSPIDAMCNGSEGDDDERAYTRHQGTVHLWQFIRELLDQPKQYSACVRWVDRDEGTFKIESSLLLARYWGQRKNRSQMNYDKLSRSLRQYYKKGIIQKPEKKQRLVYKFLPPYNL | 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 (PubMed:20862312). Regulates the expression of genes such as svh-2 in response to axon injury and in addition, may function downstream of the cAMP signaling pathway to promote axon regeneration (PubMed:26484536). Regulates the expression of lipid metabolism genes and may also control the expression of the RNA-binding protein rege-1 which too has been implicated in the control of fat accumulation (PubMed:27746047). {ECO:0000269|PubMed:20862312, ECO:0000269|PubMed:26484536, ECO:0000269|PubMed:27746047}. | Caenorhabditis elegans |
A8WFU8 | KIF22_DANRE | MAQRVAVNDGAAGSKRTSRVRVAVRLRPYMDKQDEKSEGSCVRGLGPQKLEIINWRNATETLQYQFDVFHGEETTQQEVFLTSVKPILPHILNGQNASVFAYGPTGAGKTHTMLGSQEQPGVIPRAVKEVFNLVGAQKKEQDGWEYSIGMSYLEIYNEKVLDLLSPGSQDLPIREDKDRNILIPGLTHTPLSSFADFDTHFIPASLNRTTASTKLNQRSSRSHAILLIKVVKSQRGPPHRQQTGKLYLVDLAGSEDNRRTGNQGIRLKESGAINLSLFTLSKVVDALNTGAGGRVPYRDSKLTRLLQDSLGGSAHSVMITNIAPEYKYYFDTFSALNFAAKSKQIVNRPFVRETVLAPTIAPGKRTREEQEAGGSGEPQNKRSKEGKKAEHSPSPPLHPQSSPDSSVLDRLLALEKMMMGSAERERLNLLKTVAQSRKEIQMLKEKQKELEDKANMFNKQKETTEKESKDALLFKTDLPPLHRKQSTAAKPRKQQAVVTPLQVSQVQPLQQCAVVCKPSQTLVKKKRVQTEVCDGKENIGVDLPPVEDVNWESRLDPALLEQSRKKILQTLNSGSLKELKSLQQIGDKKAKLIMGWREINGDFTQVEDLKKIEGVTVKRFSSFIKANILSSMGK | 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 | MALQSTILHMARKNLLQESCRQLLIQTHGLHKSVASGSLEIAAHSQADLKEESAVSPAEEVQKAARVKSLKEMPGPSTVANLLEFFYRDGFSRIHEIQMEHAKKYGKIFKSRFGPQFVVSIADRDMVAQVLRSESATPQRGNMESWKEYRDLRGRSTGLISAEGDEWLKMRSVLRQLIMRPRDVAVFSSDVNDVVADLVKRVKTLRSQQDDSQTVLNINDLFFKYAMEGVATILYETRLGCLENEIPKMSQEYITALHLMFSSFKTTMYAGAIPKWLRPIIPKPWEEFCSSWDGLFKFSQIHVDKRLSEIKKQMEKSEEIKGGLLTHMLVTREMNLEEIYANMTEMLLAGVDTTSFTLSWSTYLLARHPTIQQQIFEEVDRVLGGRVPTGEDVPYLPLIRGLVKETLRLFPVLPGNGRVTHDDLIVGGYLIPKGTQLALCHYSTSMDEENFPRPEEFRPDRWIRKDASDRVDNFGSIPFGYGIRSCIGRRIAELEMHLALTQLLQNFHIEVSPQTTEVHAKTHGLLCPGASINLRFTDRK | 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 acid binding [GO:0001972] | 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:CHEBI:33738, ChEBI:CHEBI:132246; EC=1.14.19.53; Evidence={ECO:0000269|PubMed:26549260}; | 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 chromophore in photopigments with 11-cis 3,4-didehydroretinal enhances sensitivity to long-wavelength light. This may improve vision in fresh water which is often turbid. {ECO:0000269|PubMed:26549260}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8WGB1 | CCBE1_DANRE | MIYPGRGASLSVAVALVLFSSGAPWTFREEKEDVDREVCSESKIATTKYPCVKSTGEVTTCYRKKCCEGFKFVLGQCIPEDYDVCAGAPCEQQCTDHFGRVVCTCYDGYRYDRERHRNREKPYCLDIDECANNNETVCSQMCVNTPGSYRCDCHSGFYLEDDGKTCTKGERAPLFEKSDNVMKEGTCSATCEDFHQMKMTVLQLKQKMSLLSSNTEINKQMTNEKMMMTTNSFLPGPPGPPGPAGTPGAKGSSGSPGQMGPPGLPGPRGDMGPIGPSPDLSHIKQGRRGPVGPPGAPGRDGMKGERGFPGPSGPPGPPGSFDFLLLMMADIRNDIAELQSKVFSRPLHSSFEDFPSAPDSWRDTPENLDFGSGEDYKSQSPPKSSRKRKLPRNLKNPDWPV | 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 vessel development [GO:0060855] | 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 pathways. {ECO:0000269|PubMed:19287381, ECO:0000269|PubMed:37097004}. | 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-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; | 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 | MDQYSILGRIGEGAHGIVFKAKHIETGETVALKKVALRRLEDGIPNQALREIKALQEIEDNQYVVKLKDVFPHGTGFVLVFEYMLSDLSEVIRNSQRPLTASQVKSYMMMLLKGVAFCHENSIMHRDLKPANLLISSTGHLKIADFGLARLFSNEGDRLYSHQVATRWYRAPELLYGARKYDEGVDLWAVGCIFGELLNNSPLFPGENDIEQLCCVLRVLGTPNQKVWPEITELPDYNKITFKENPPIPLEEIVPDTSPQAVDLLKKFLVYPSKQRISARQALLHPYFFTDPLPAHHSELPIPQRGGKHSRQRMQPPHEFTVDRPLHESVVDPSLIQKHAMSCS | 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-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; | 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 of the ciliary membrane and axoneme, allowing gli2 to be properly activated in response to SHH signaling. {ECO:0000250, ECO:0000269|PubMed:20159594}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A8WJR8 | MBK2_CAEBR | MAALASFTRNSRSYGQQPIDVTQQGQRDRSVMSLDAQGRSKMSNINYTRPAALSTSDSTIGVFRRAPSSFSGASSSSSNHHHPVYHSHNSLPPTLIGGSPHSASSNSLAQGHRNPALGSGNTLTRSYHQPSSTNSSTSNLHGPLGTYSRDLKQAIRDISPPVINSSANPHLVNYIHTSSFDNGSYEFPSGQAQQQRRLGGSQQHLAPLQQTSSSLYSNPQSSSSQLLGQQAVRSNYAYQQSLPRQQHINSHQTQAFFGTIRAPGNSTNIVTPLRASKTMIDVLAPVRDSVAAQATTGALPSVGTSSSNGSSNSSSGVGSGGSGSLMTQSIGGPNKHLSASHSTLNTASTHDSMMHTKIPKSPSNESLSRSHTSSSGGSQGGHNSNSGSNSGFRPEDAVQTFGAKLVPYEKNEIYNYTRVFFVGSHAKKQPGVIGGANNGGYDDENGSYQLVVHDHIAYRYEVLKVIGKGSFGQVIKAFDHKYQQYVALKLVRNEKRFHRQADEEIRILDHLRRQDSDGTHNIIHMLDYFNFRNHKCITFELLSINLYELIKRNKFQGFSLMLVRKFAYSMLLCLDLLQKNRLIHCDLKPENVLLKQQGRSGIKVIDFGSSCFDDQRIYTYIQSRFYRAPEVILGTKYGMPIDMWSLGCILAELLTGYPLLPGEDENDQLALIIELLGMPPPKSLETAKRARTFITSKGYPRYCTATSMPDGSVVLAGARSKRGKMRGPPESRSWSTALKNMGDELFVDFLKRCLDWDPETRMTPAQALKHKWLRRRLPNPPRDGMDSMGGLADHDKKADLPNIDSNANILMRKKF | 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|UniProtKB:Q9XTF3}. | 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}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.1; Evidence={ECO:0000250|UniProtKB:Q9XTF3}; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1; Evidence={ECO:0000250|UniProtKB:Q9XTF3}; | 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 the anterior cytoplasm during zygote polarization, and thus plays a role in P granule distribution and segregation in early stage embryos following meiosis (By similarity). Functions in both spindle positioning and in the posterior localization of cytoplasmic determinants, including pie-1, pos-1, and pgl-1, in early embryos. Involved in the asymmetric distribution of plk-1 at the 2-cell embryonic stage. {ECO:0000250|UniProtKB:Q9XTF3}. | Caenorhabditis briggsae |
A8WUG4 | KPC3_CAEBR | MSSPTSVEEDGDIKLKTRFHGQVVVLYARPPLILDDFFALLRDACKQHAKQDITVKWIDEDGDPISIDSQMELDEAVRCLNVSQEAELNIHVFVGKPELPGLPCQGEDKTVYRRGARRWKKIYLYNGHRFQGKRLNRRIQCFICHDYIWGIGRQGFRCVDCRLCVHKKCHRHVRTHCGQTPQGPNVPVAPSSGVGSLRGGRLDTSSSTTRSGGGIDNGAFHEHEIESPGSAKDMSRSTNGNGASKWAVSLNDFRLLTVIGRGSYAKVVQAEHIATRQIYAIKIIKKEMFNEDEDIDWVQTEKSVFEAASNYPFLVGLHSCFQTESRLFFVIEFVPGGDLMFHMQQQRRLPEEHARFYSGEIILALHFLHSRGIIYRDLKLDNVLIDAEGHIKLTDYGMCKENINAGDLTSTFCGTPNYIAPEILRGDEYGFSVDWWALGVLMFEMMAGRSPFDIVGMQNSEENTEDYLFQIILERQIRIPRSLSVRASNILKGFLNKDPSQRLGCKLDINDGLNDMKEHDFFRGFIDWEALEQKAVAPPYHPAVESDRDLTHFDHQFTDEPPQLSPDNSAVIARIDQSEFDGFEYVNPLQMSREDSV | 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 signal transduction [GO:0035556]; phosphorylation [GO:0016310]; protein localization [GO:0008104]; response to wounding [GO:0009611]; single fertilization [GO:0007338] | 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 organelles/cytoskeleton in six of the seven developmental stages. Accumulation in cytoplasm is restricted to L1 larvae and adults. Colocalized with par-3 at the anterior cortex of the 1-cell embryo (By similarity). {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; Evidence={ECO:0000250|UniProtKB:Q19266}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000250|UniProtKB:Q19266}; | 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. Phosphorylates serine residues of num-1. Required for the expression of antimicrobial peptide nlp-29 in response in response to fungal infection or physical injury. {ECO:0000250|UniProtKB:Q19266}. | 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 guidance [GO:1905488]; regulation of multicellular organism growth [GO:0040014]; synaptic transmission, cholinergic [GO:0007271]; synaptic vesicle fusion to presynaptic active zone membrane [GO:0031629]; ventral cord development [GO:0007419]; vesicle docking [GO:0048278] | 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 with unc-18 (By similarity). Through binding to unc-18 mediates the release of the neurotransmitter acetylcholine from cholinergic motor neurons, and thereby promotes locomotory behaviors (By similarity). Essential for embryonic viability and development (By similarity). Has a role in dauer formation and adult life span. Required for locomotion (By similarity). Probably by regulating neuronal transmission downstream of lin-3 and receptor lin-23 and phospholipase plc-3 and upstream of innexin unc-7 and egl-4/PKG in ALA neurons, involved in the decrease in pharyngeal pumping during the quiescent state that precedes each larval molt (By similarity). {ECO:0000250|UniProtKB:O16000}. | Caenorhabditis briggsae |
A8WVU9 | ROCK_CAEBR | MEQDELLHQLVDPKSPINIESLLDTITALVNDCKIPVLMRMKSVDNFISRYERIVESVAALRMKATDFRQLKVIGRGAFGEVHLVRHTRTNTVYAMKMLNKDDMIKRADSAFFWEERDIMAHANSEWIVRLQYAFQDPRHLYMVMEYMPGGDLVNLMTSYEVSEKWTRFYTAEIVEALAALHNMGYIHRDVKPDNMLISRSGHIKLADFGTCVKMNSNGVVRCSTAVGTPDYISPEVLRNQGKDSEFGKEVDWWSVGVFIYEMLVGETPFYAEALVSTYANIMNHQTSLRFPDEPLISTQAKDIIKKFLSAAPERLGKNNVDEIRNHKFFKNDEWTFETLKDATPPIVPSLKSDDDTTHFEEIETRDRDNASDFQLPKTFNGNQLPFIGFTYSNEYSPVKKLLNGASSNGVQNGVENKPVVVQQPLTNGHSTGIPEEQYEEVVIELDSKKRELESLKDSISRTEIRAKLIETEKNSLSSKINDLERELKDNKERLRLGADSDTKVNELSVELRMSKEYNGEMENELSKFRDKCEQLKEDLRKKSGELAQEKNETQRVLQQKKNAEEAFAEIKRDHEMLQTREAEKSLQLKKALDERKENGAYQQSVAKATDAEWERKMQYYEKQLEQATDDRKREEQKRTAAEFDQSRVARKLAGIEANYELLQNDYTNMKEARKDLERDLQDVIAEKRRLEIRVEQLMDSRNTDERVLNLCQEELLESQEEAKYKEDGLRGKIDGIRNELENEKMKSQTLEENLIVADKERGMLKMEVQELMQRHKWEMANKEQNLKHIENQLEELKEHSRIESTEQESNDKKTIADLNKKLELEKAHKKAVINKLEEEMAKRQPLKKGDKGITKSALIKKEREIVGFKKCRTGRILMSLQQENQHLQQKMTEMYMDSEKQGEHFSYQMQEMSQLIETLRDELKEYKDEYPQRHSVNRYEDKRSLDSREGIPTSISHQNIQIDGWLSLRDMTKKSRKPKVVFKKKSDHQLTLFFQWTNYFVILNEYAFTIYTDEKHLNSVVLTIEAGAMAHVRHVTSADLRNVDDNQLPKIFHIMYDDTSSNSSRHASNSDLSICEPREEGWKRHDFQELSYHTRTYCDDCGKKLSDFIRPTPAFECKNCHYKTHKEHIAQGTITMCRYTGLSRELVLMGTHKEVCNQWVSQLRRFIEASRPANVSVSRVSSRRHVGGPGSSA | 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:0007266] | 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}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13464}; | 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 morphogenesis. Required for P-cell migration. May also play a role in oocyte cellularization (By similarity). {ECO:0000250|UniProtKB:P92199}. | Caenorhabditis briggsae |
A8WWH5 | POP1_CAEBR | MMADEELGDEVKVFRRDEDADDDPMISGETSEQQLADDKKDAVMEAELDGAGRVPLIGGLKAEIKAEPSPSFPMPSMLPCGPYSPFSGLPIMFPMVVPQYLSPNPNINMMNMMTMRAAMAGAPLSPAFPAMFSPNPLFPFPGVVAKQHLENTMPMHMRAGPLSSLNHMKMPPYMPHQMMPQHNERRGHGGGKVKKEDHIKKPLNAFMWYMKENRPKLLEEVGNDQKQSAELNKELGKRWHDLPKEEQQKYFEMAKKDRESHKEKYPQWSARENYAVNKKKPKRKRDKSVVSGSENNDQKKCRARFGVTNTSMWCKPCQRKKKCIYATDRSGSELNDGHDGRGTSGGCSSSSESSSPNNNQPMPMNAPQTVAAMHAMLMGMQIGQSAHLASSHSTGSSGTSPPVANPSDSESDVDEDEDIDPTITQQTQEYIMQESVCTL | 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]; negative regulation of cell division [GO:0051782]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; negative regulation of stem cell proliferation [GO:2000647]; polarity specification of proximal/distal axis [GO:0010085]; positive regulation of gene expression [GO:0010628]; positive regulation of vulval development [GO:0040026]; regulation of asymmetric cell division [GO:0009786]; regulation of cell fate specification [GO:0042659]; regulation of defecation rhythm [GO:2000746]; regulation of neuroblast migration [GO:0061853]; regulation of transcription by RNA polymerase II [GO:0006357] | 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 [GO:0019901]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription corepressor activity [GO:0003714]; transcription corepressor binding [GO:0001222] | 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 telophase, pop-1 levels decrease in the posterior nucleus, in contrast to the anterior nucleus (By similarity). There is a ~2-fold nuclear enrichment of pop-1 in the anterior compared with posterior daughter cells at the time of cytokinesis (By similarity). {ECO:0000250|UniProtKB:Q10666}. | 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 asymmetrical division of seam cells, a stem cell-like lineage (By similarity). Represses expression of target genes via its interaction with hda-1 histone deacetylase (By similarity). Required for specification of the M lineage-derived coelomocyte and sex myoblast fate (By similarity). Regulates coelomocyte fate by positively regulating proliferation and ceh-34 and possibly eya-1 expression in M.dlpa and M.drpa precursors (By similarity). {ECO:0000250|UniProtKB:Q10666}. | Caenorhabditis briggsae |
A8X181 | FICD_CAEBR | MSVRRRTHSDDFSFRLERTRRPSKLDVLRESPTLPVQQGYSLTTVVLVSLVVTLVCQNVAPPAFSYLNQLIKNSPKRKIPGQSNRLNIGFISTNSPEKFAPAVQKPTFLVDPIYDEKWKGVHTAVPVMTTEPEEKRDNNHAKVKEAILAAKAASRSRRDGNLERAVTIMEHAMALAPNNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRARTNPLVSAIDRKMLKTVHDLRNEFAHLQHSTALRRMMRETYFLYVYHTVAIEGNTLSLGQTRAILESGMVIPGKSIREHNEVIGMDAALRFLNCSLLSKEHHEISIDDILEMHRRVLGNADPVEAGKIRTTQVYVGKFTPVAPEYVLEQLADMVDWLNDESTMAMDPIERAAIAHYKLVLVHPFTDGNGRTARLLLNLIMMRSGFPPVILPVETRAEYYASLHVANLGDLRPFVRYVAKHSEASIQRYIGAMKTSSGNVINGEEPNLTAEESKVSEKIETECRAGS | 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 the nucleus. {ECO:0000250|UniProtKB:Q23544}. | 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 ACTIVITY: Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.108; Evidence={ECO:0000250|UniProtKB:Q8SWV6}; CATALYTIC ACTIVITY: Reaction=3-O-(5'-adenylyl)-L-threonyl-[protein] + H2O = AMP + H(+) + L-threonyl-[protein]; Xref=Rhea:RHEA:55932, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13847, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:138113, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q8SWV6}; | 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 opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins. In vivo target proteins include the heat-shock 70 family proteins hsp-1 and hsp-3 and the translation elongation factors eef-1A, eef-1G and eef-2. Can AMPylate core histone H3 in vitro (By similarity). Can also act as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from target proteins (By similarity). Decreases susceptibility to P.aeruginosa-mediated killing and might therefore play a role in the innate immune response (By similarity). {ECO:0000250|UniProtKB:A0A061I403, ECO:0000250|UniProtKB:Q23544, ECO:0000250|UniProtKB:Q8SWV6}. | Caenorhabditis briggsae |
A8X3A7 | PAT2_CAEBR | MREGSFPRRTRLLCLLAAVVLISTVTSFNIDTKNVVLHHMANNYFGYSLDFYNEQKGMPVLVVGAPEAETTNPNLSGIRRPGAVYACSVNRPTCREVHVDKMKGNLKKLNGSHLVPIEDKAYQFFGATVKSNDKHDKLLMCAPKYKYFYSKFEVIEPVGTCFYAENGFEKTEEFSSCKQEPARHGRHRLGYGQCGFSGAIPGKKNQDRVFLGAPGVWYWQGAIFSQNTKNQTDRPNTEYGSKEYDHDMMGYATATGDFDGDGIDDIVAGVPRGNDLHGKLVLYTSKLKMMINLTDEVSTQHGQYCGGALAVADVNKDGRDDIIMGCPFYTDYGSVKDAKTQERKPQYDVGKVIVFLQTAPGVFGKQLAVVGDDQWGRFGHSLAAAGDLNLDGYNDVIVGAPYAGKNKQGAVYVIHGSKDGVREKPTQKIEASQIGHGTARAFGFAVAGGVDVDGNGMPDIAVGAWKSGNAAVLLTKPVVTVTGATEPESALINVEEKNCDVDGKLGKQACRHINTCFKYEGKGDTPNDLEFDLRFNLDDHSPEPRAYFLQKDVKSDRSIKVASGSKTRDHPSSIEQRVRLEKGRQKCFRHRFFASSTMKDKLSPIHWSVNYTYVESKSGKLRGDKLEPAIDTTVPLSFQNKINIANNCGKDDLCVPDLKVTAVADREKFLLGTQDNTMLINVTVQNGGEDSYETKLYFDVPQGFEYGGIESVGADGSAPACSPTSDEPDSDGKWTFACDLGNPLPANKVVSSVVRVTASSDKPPLAPISINAHVNSSNDEEAHTIADNKVTFTIPVDFKNQLSLNGRSNPEQVDFSMTNKTRSDVFDDNEIGPVVSHLYQISNRGPSEIDAATLDIFWPSFSTEGGHLLYIITEPVVNPPNKGRCRVKQLQNVNPLNLRITNEHVPTEPPVAKTPNEYSREEDDESYEDETTTQSQTHHQTRTEHTQHHQGPVHVYERDEDKIRQNTGNWQYVEDKKKKGDYEYIPDDQEYDGDDFEDDDEDFDRAGSKRVKRAPVPKKKKKEGSRSGEPRSDKARFSDLREAVKLSKEAGGVVDYKGPLSRASVDCNGLRCTHIECDIYDLKEDEFVLVEIFSRLYTNTLVDERNPGGDISSLALARVTSTKYNWPHKPTLITAVSTNMNAIASEEGRDLPWWLYLLAILIGLAILILLILLLWRCGFFKRNRPPTEHAELRAEKQPAAHYADTQSRYAPQDQYSQGRHGQML | 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 pathway [GO:0042059]; positive regulation of engulfment of apoptotic cell [GO:1901076]; positive regulation of locomotion [GO:0040017]; positive regulation of sarcomere organization [GO:0060298]; regulation of distal tip cell migration [GO:1903354]; regulation of vulval development [GO:0040028]; vulval cell fate specification [GO:0072327] | 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 tip cell migration and dorsal pathfinding. Required for egg-laying. May play a role in cell motility and cell-cell interactions. {ECO:0000250|UniProtKB:P34446, ECO:0000250|UniProtKB:P53708}. | Caenorhabditis briggsae |
A8X5H5 | GSK3_CAEBR | MNKQLLSCSLKSGKQVTMVVASVATDGVDQQVEISYYDQKVIGNGSFGVVFLAKLSTTNEMVAIKKVLQDKRFKNRELQIMRKLNHPNIVKLKYFFYSSGDKKDELYLNLILEYVPETVYRVARHYSKQRQSIPMIYVKLYMYQLLRSLAYIHSIGICHRDIKPQNLLIDPETGILKLCDFGSAKYLVRNEPNVSYICSRYYRAPELIFGATNYTNSIDVWSAGTVIAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIQSMNPNYKEFKFPQIKAHPWNKVFRVHTPAEAIDLISKIIEYTPTSRPTPQAACQHAFFDELRSPDARLPSGRALPQLEMDGPNEVSATGGDMAGPSA | 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 specification [GO:0070986]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; phosphorylation [GO:0016310]; positive regulation of distal tip cell migration [GO:1903356]; positive regulation of engulfment of apoptotic cell [GO:1901076]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; regulation of microtubule cytoskeleton organization [GO:0070507]; regulation of neuron projection development [GO:0010975]; signal transduction [GO:0007165]; Wnt signaling pathway, regulating spindle positioning [GO:0060069] | 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}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703, Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, 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 EMS blastomeres. Thought to be a branch point in these processes as proteins downstream are not required. Negatively regulates Wnt signaling in vulval precursor cells and acts as a Wnt-independent repressor of med-1 and med-2 in the C lineage inhibiting mesoderm development. Required for normal lifespan and LiCl-induced lifespan extension (By similarity). {ECO:0000250|UniProtKB:Q9U2Q9}. | Caenorhabditis briggsae |
A8X633 | APR1_CAEBR | MSSSSSDENETTIHSSSNPGSSGIYSQLKAGSSKRPSVRHDVSDAEDDEEPYEGFRKDMNMEVDERITTLLSSLHFEHKRDVVTADEDDNKLRELHENIFSLITTEPDFHRRRRLKKALPASNCIREQVYYLRRKPITPPDSYYHRLNAALHTIVKESFGEEYRKVATVLGLVEALAEVLILEVHAFGIPETNAVEHRNIRKLIANALTNLTYGQILSKRRLCSYDGFIRCVVRIIIESPNITQVYAGLIRNLSWNADSGMSEALQPTVHALSLAAVYAHTHRFDVTAILSALWNLAGHSVENKRTICETPNCLKVLANILSPDARFTTLVDSASGILKYVSQYLATNSSHLELRSLLITRMLTLLKSSSFTCVTNTLGAIAHLIAKDPHMQQLIRQDAAAVQQLNVLRNSNREDIRKAVKEVLNTLNQPCSHRYGDMSHSVGGASGMLSEPQLQMQTSHHGYHGTASPRLLSLRATRASPGKYIHPSQQQHMQVPAPDQRSSSLPRHFAVQRNGFMMAQSFNQQMDPHQQQQQQQQQMIFQMQQQQMMIQTDDQQMRYLNQQQQQQQQQHYQQQIQRNQNVEPVLPVDDDLDIPTSTVMGTRSNSERSLGSMNPGSVMTTGGWNSTLDTAANSSRALSPVSFSDIPASPTMCAQVFNLPVHPEDNQMTTPPNHPSTQNTTHYSSGSANTMTRSDGTTVPIDNLITPTYATLNVTNNAARKTSEDLESPDDILPGPSLEVEEEGDYAIITGAEQKSDDDLLTRSIQEEMPTSSSTPKLKVSPRLNGFFSPSQKTTSSPAWSHPDTSPILKQTQRPKHHEMTTDSDRLLMESIMSEMPRSRVISPRLASGGQQYLDPEPDRSSHSKNEEADRRDAIIASHEPSDQGMNVGRGSSPQQQQLHRMESLESQASSEDSFGLNGYQEEHNTSSSAAHTMRIDKDDVVDASLPMDCVDDEDYDYTDDHFDDNYEEDYEDSNATQFDEGIDPQLTIDCSMISSGSGSSLQKAETTAGSRDSGALATSTPIGSVSSLPGVRRAKKVSINGKTRLPVPKTNGSLVDRVRKPVIEASRPRLPPKPSLLKGKQYHEEDLIENQTRDDTIYVNAPIVEAEQERIYMNALKHSQGSPSVNGTPPKSAIVSPYNYQKPPFTERSNGEINEKNVTPNPKQMLVTIV | 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]; negative regulation of microtubule depolymerization [GO:0007026]; negative regulation of Wnt signaling pathway [GO:0030178]; nervous system development [GO:0007399]; pattern specification process [GO:0007389]; positive regulation of protein catabolic process [GO:0045732]; protein transport [GO:0015031]; regulation of cell differentiation [GO:0045595]; Wnt signaling pathway [GO:0016055] | 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 and nucleus (By similarity). {ECO:0000250|UniProtKB:Q21227}. | 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 preventing hmp-2 nuclear translocation. During larval development, apr-1 is required for expression of lin-39 in P3-8.p. Shown to negatively regulate Wnt signaling in vulval precursor cells. Has a role in cell division by establishing the polarity of the mother cell which forms the asymmetries of the daughter nuclei. Thought to regulate export of wrm-1 from the nucleus possibly as part of a complex involving pry-1. {ECO:0000250|UniProtKB:Q21227}. | Caenorhabditis briggsae |
A8X811 | WRM1_CAEBR | MEERGPDIEKYGSQPCTPLSFDPMLPSTSRVATPVRPSSTLSARQAPASPFRAQPQNMEPSISRVHELREGAAVKRSYTNDWMQGNYIPPNPQQQQYQRPPSMIGSTISNMSNLSHMTKFSALSVNTQCGQFDNWIYQSQPALSKVSHSSVENQDPMKRRERMSIPEIVQSLASYEMSDQVAAIRELEPLAKAEALESTYCQADLGKIINALFEVLVPRPQENENVIRKVFEILHRAAVPKHVRMTEKIFHSLNLELMNTNSSKHSFQVPRPYSIYELVIERASRLDTAYDQAAMLLLAQICCKPFFMKYVFSEKEQSAGHRRLHEVVMQFAIKNLQQQETKRKSKGFCVSIIKNLSRRNRSIWSIVYELHVIPIFHDIIKDEYSDEDLLWPTMQALTTFCSIERVGEDFVKLGGAQDLCNLLYHGSTRLLHELLACMQRLSLLQEIGNQDMEESIRRVIQVVGSDDATIAERATGVLRNIGQPNKQNKVIMVRNGVTAHAIAVLRTSMRFQSQLREQQNARTPKNQIDAAKNQILSIYENCLSILNNVTKMGKDDILDSAIQACRMISANPDAAIVLLHFLNAGAPKCRKLAVNVMKRVIENVPAFAEPFVDLPGTTQETLPILLLKRAYESLDEWKKAVVEVMRSEPNTQQFRDAIEKRQDHEDIVWKSVSLLSNLCRNGNPRFFERVKVEMLYTRPTNPFTSLFPEMSDVILYEWLDFILAICGTEWSLQNCLMYHFLKQANITHEYLLHYRRPNPQICDKIKNIIDTGMRQQQQHNQLEQMAMMHAQQQHQQLPM | 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 fate specification [GO:0001714]; endodermal digestive tract morphogenesis [GO:0061031]; establishment of mitotic spindle orientation [GO:0000132]; left/right axis specification [GO:0070986]; negative regulation of cell division [GO:0051782]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; nematode pharyngeal muscle development [GO:0160096]; polarity specification of anterior/posterior axis [GO:0009949]; polarity specification of proximal/distal axis [GO:0010085]; positive regulation of asymmetric protein localization involved in cell fate determination [GO:1904787]; positive regulation of cell division [GO:0051781]; positive regulation of endodermal cell differentiation [GO:1903226]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of embryonic development [GO:0045995]; regulation of mesodermal cell fate specification [GO:0042661]; Wnt signaling pathway involved in dorsal/ventral axis specification [GO:0044332] | 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 activity [GO:0043539]; transcription coactivator activity [GO:0003713] | 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|UniProtKB:Q10953}. | 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 signaling during endoderm specification (By similarity). Component of the beta-catenin-lit-1 complex which promotes phosphorylation, down-regulation and subcellular relocation of pop-1 (By similarity). Within the complex, activates lit-1-dependent kinase activity (By similarity). Can substitute for bar-1 indicating functional redundancy (By similarity). Appears to have a role in centrosome positioning (By similarity). Involved in the development of distal tip cells (DTC) by regulating the asymmetric distribution of cye-1 and cki-1 between the daughters of Z1.a and Z4.p cells (By similarity). {ECO:0000250|UniProtKB:Q10953}. | Caenorhabditis briggsae |
A8Y987 | VP2_POVSM | MGALLAVLAEVVELASVTGLSVESFISGEAFATAELLEAHIANLVTVGGLTEAEALAATEVPAEAYAALTSLSSTFPQAFTAVAATELATTGTLTVGATVAAALYPYYYDYSTPVANLNRGLNPEMALQLWFPEIDYEFPGLMPFVRFINYIDPTQWATNLFETIGRYSWESAQRYGQNLIAHEVRSASRELATRTAQGFSEAVARYFENARWAVSTLPRSLYSGLQSYYEQLPSLNPMQVRDLHRRLGQPIPNRIALEEQAIKSAEYVQKVDPPGGANQRIAPDWLLPLILGLYGDISPSWESTLEDIEEEEDAPQKKKRKRTKKNTPRSA | 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 reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus in particular through a DNA-binding domain located in the C-terminal region. A N-terminal myristoylation suggests a scaffold function for virion assembly (By similarity). {ECO:0000250}.; FUNCTION: [Isoform VP3]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic reticulum membrane. Heterooligomer VP2-VP3 may create a viroporin for transporting the viral genome across the endoplasmic reticulum membrane to the cytoplasm. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2 or VP3 nuclear localization signal (shared C-terminus). Plays a role in virion assembly within the nucleus (By similarity). {ECO:0000250}. | 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]: has a vasorelaxant activity in rat aortic strips and a diuretic potency in anesthetized rats (By similarity). May act by activating natriuretic receptors (NPR1 and/or NPR2). {ECO:0000250|UniProtKB:P0C7P5}. | 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 and vasodepressor activity. Acts by activating natriuretic receptors (NPR1 and/or NPR2 and/or NPR3) (By similarity). {ECO:0000250}. | 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:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969, ChEBI:CHEBI:131709; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950, ChEBI:CHEBI:131710; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965, ChEBI:CHEBI:141553; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969, ChEBI:CHEBI:141554; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950, ChEBI:CHEBI:141555; EC=3.5.1.124; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) + lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate; Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate; Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate; Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate + H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP + H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate + H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP + H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269, ChEBI:CHEBI:141580; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445, ChEBI:CHEBI:141578; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269, ChEBI:CHEBI:141581; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; CATALYTIC ACTIVITY: Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O = a 2'-deoxyguanosine in DNA + glycolate + H(+); Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:85445, ChEBI:CHEBI:141579; Evidence={ECO:0000255|HAMAP-Rule:MF_01046}; | 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 proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Plays an important role in protecting cells from carbonyl stress. {ECO:0000255|HAMAP-Rule:MF_01046}. | Staphylococcus aureus (strain USA300 / TCH1516) |
A9BHI9 | GPGS_PETMO | MKDNILKRSFHHSKFENIKELVKLKEKQDVKISLAFPSLNEEKTIGKEIIIMKSELMEKYPLLDEIAVIDSGSEDETVSIAKEYGAKVFYSSDILPEYGFYKGKGENLWKSLYALDGDIIVWVDSDIENIHPKFVYGLVGALLNYPEIGYVKAFYDRPIVGKSAMQPTGGGRVTELVARPLFSLFYPELSTIIQPLSGEYAGRREILEKLPFFVGYGVEIAHLIDIAEKFGSEIIAQVDLELRIHDNQPLHSLSKMAFELTKVVLKRLEKYGKLDLNTELTDKHIMIQKKENEKVLVPTEILSVERPPMITIPEYKEKFSKEEKV | 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}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:20061481}; Note=Requires divalent cations for activity. {ECO:0000269|PubMed:20061481}; | 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:0000269|PubMed:20061481}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47245; Evidence={ECO:0000305|PubMed:20061481}; CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + UDP-alpha-D-glucose = (2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + H(+) + UDP; Xref=Rhea:RHEA:31319, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58272, ChEBI:CHEBI:58885, ChEBI:CHEBI:62600; EC=2.4.1.266; Evidence={ECO:0000269|PubMed:20061481}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31320; Evidence={ECO:0000305|PubMed:20061481}; CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + ADP-alpha-D-glucose = (2R)-2-O-(alpha-D-glucopyranosyl)-3-phospho-glycerate + ADP + H(+); Xref=Rhea:RHEA:31311, ChEBI:CHEBI:15378, ChEBI:CHEBI:57498, ChEBI:CHEBI:58272, ChEBI:CHEBI:62600, ChEBI:CHEBI:456216; EC=2.4.1.266; Evidence={ECO:0000269|PubMed:20061481}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31312; Evidence={ECO:0000305|PubMed:20061481}; | 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 degrees Celsius) {ECO:0000269|PubMed:20061481}; Vmax=43.9 umol/min/mg enzyme toward 3-PGA (at 60 degrees Celsius) {ECO:0000269|PubMed:20061481}; Vmax=65 umol/min/mg enzyme toward 3-PGA (at 70 degrees Celsius) {ECO:0000269|PubMed:20061481}; Vmax=44 umol/min/mg enzyme toward UDP-glucose (at 60 degrees Celsius) {ECO:0000269|PubMed:20061481}; Vmax=49.5 umol/min/mg enzyme toward UDP-glucose (at 70 degrees Celsius) {ECO:0000269|PubMed:20061481}; | 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-glucose is the preferred substrate, but it can be partially replaced by ADP-glucose. {ECO:0000269|PubMed:20061481}. | Petrotoga mobilis (strain DSM 10674 / SJ95) |
A9C3R8 | RP65C_DANRE | MVSRLEHPAGGYKKVFESCEELAEPIPAHVSGEIPAWLSGSLLRMGPGLFEVGDEPFYHLFDGQALLHKFDLKDGRVTYHRRFIRTDAYVRAMTEKRVVITEFGTTAYPDPCKNIFSRFFTYFQGIEVTDNCLVNIYPIGEDFYACTETNFITKVDPDTLETVKKVDLCNYLSVNGLTAHPHIEADGTVYNIGNCFGKNMSLAYNIVKIPPLQEDKSDQFEKSKILVQFPSSERFKPSYVHSFGITENHFVFVETPVKINLLKFLTSWSIRGSNYMDCFESNDKMGTWFHLAAKNPGKYIDHKFRTSAFNIFHHINCFEDQGFIVVDLCTWKGHEFVYNYLYLANLRQNWEEVKKAALRAPQPEVRRYVLPLDIHREEQGKNLVSLPYTTATAVMRSDGTVWLEPEVLFSGPRQAFEFPQINYSKFNGKDYTFAYGLGLNHFVPDRICKLNVKSKETWIWQEPDAYPSEPLFVQSPDAEDEDDGVLLSIVVKPGVSQRPAFLLILKATDLTEIARAEVDVLIPVTLHGIYKP | 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)-zeaxanthin; Xref=Rhea:RHEA:12729, ChEBI:CHEBI:28838, ChEBI:CHEBI:138919; EC=5.3.3.22; Evidence={ECO:0000250|UniProtKB:Q16518}; CATALYTIC ACTIVITY: Reaction=an all-trans-retinyl ester + H2O = 11-cis-retinol + a fatty acid + H(+); Xref=Rhea:RHEA:31771, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16302, ChEBI:CHEBI:28868, ChEBI:CHEBI:63410; EC=3.1.1.64; Evidence={ECO:0000269|PubMed:21676174}; CATALYTIC ACTIVITY: Reaction=all-trans-retinyl hexadecanoate + H2O = 11-cis-retinol + H(+) + hexadecanoate; Xref=Rhea:RHEA:31775, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16302, ChEBI:CHEBI:17616; EC=3.1.1.64; Evidence={ECO:0000250|UniProtKB:Q16518}; | 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:21676174}; | 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 catalyzing the isomerization of lutein to meso-zeaxanthin an eye-specific carotenoid (By similarity). {ECO:0000250|UniProtKB:Q16518, ECO:0000269|PubMed:21676174}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
A9C3R9 | RP65B_DANRE | MVSRLEHPAGGYKKVFESCEELAEPIPAHVSGKIPAWLSGSLLRMGPGLFEIGDEPFNHLFDGQALIHKFDLKDGRVTYHRKFIRTDAYVRAMTEKRVVITELGTAAYPDPCKNIFSRFFTYFQGTEVTDNCSVNIYPIGEDFYACTETNFITKVNPDTLETIKKVDLCNYLSVNGLTAHPHIEADGTVYNIGNCFGKNMSLAYNIVKIPPLQEEKSDPLAMSKVLVQFPSSERFKPSYVHSFGMTENHFVFVETPVKINLLKFLTSWSIRGSNYMDCFESNDRMGTWFHLAAKNPGKYIDHKFRTSAFNIFHHINCFEDQGFIVVDLCTWKGHEFVYNYLYLANLRQNWEEVKKAALRAPQPEVRRYVLPLDIHREEQGKNLVSLPYTTATAVMCSDGTVWLEPEVLFSGPRQAFEFPQINYSKFNGKDYTFAYGLGLNHFVPDRICKLNVKSKETWIWQEPDAYPSEPLFVQSPDAEDEDDGVLLSIVVKPGVSQRPAFLLILKATDLTEIARAEVDVLIPLTLHGIYKP | 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)-zeaxanthin; Xref=Rhea:RHEA:12729, ChEBI:CHEBI:28838, ChEBI:CHEBI:138919; EC=5.3.3.22; Evidence={ECO:0000250|UniProtKB:Q16518}; | 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 | MAASGAVEPGPPGAAVAPSPALAPPPAPDHLFRPISAEDEEQQPTEIESLCMNCYCNGMTRLLLTKIPFFREIIVSSFSCEHCGWNNTEIQSAGRVQDQGVRYTLTVRAPEDMNREVVKTDSATTRIPELDFEIPAFSQKGALTTVEGLITRAISGLEQDQPARRANKDATAERIDEFIVKLKELKQVASPFTLIIDDPSGNSFVENPHAPQKDDSLVITHYNRTQHQKEMLGLQEEAPAEKPEEEDLRNEVLQFNTNCPECNAPAQTNMKLVQIPHFKEVIIMATNCENCGHRTNEVKSGGAVEPLGTRITLHITDPSDMTRDLLKSETCSVEIPELEFELGMAVLGGKFTTLEGLLKDIRELVTKNPFTLGDSSNPCQKERLQEFSQKMDQIIEGNMKAHFIMDDPAGNSYLQNVYAPEDDPEMKVERYKRTFDQNEELGLNDMKTEGYEAGLASQR | 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 processing [GO:0006397]; negative regulation of motor neuron apoptotic process [GO:2000672]; positive regulation of gene expression [GO:0010628]; positive regulation of growth [GO:0045927]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of RNA splicing [GO:0033120]; pre-mRNA catabolic process [GO:1990261]; protein folding [GO:0006457]; regulation of myelination [GO:0031641]; RNA splicing [GO:0008380]; spinal cord development [GO:0021510]; trophectodermal cell proliferation [GO:0001834] | 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 predominantly in the cytoplasm in serum-starved cells growth arrested in G0 of the mitotic cell cycle. Localized both in the nucleus and cytoplasm at the G1 phase of the mitotic cell cycle. Accumulates in the subnuclear bodies during progression into the S phase of the mitotic cell cycle. Diffusely localized throughout the cell during mitosis. Colocalized with NPAT and SMN1 in nuclear bodies including gems (Gemini of coiled bodies) and Cajal bodies in a cell cycle-dependent manner. Colocalized with EGFR in the cytoplasm of quiescent cells. Translocates from the cytoplasm to the nucleus in a epidermal growth factor (EGF)-dependent manner. Translocates together with EEF1A1 from the cytoplasm to the nucleolus after treatment with mitogens. Colocalized with SMN1 in Gemini of coiled bodies (gems), Cajal bodies, axon and growth cones of neurons (By similarity). {ECO:0000250}. | 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 axonal growth and formation of growth cone in spinal cord motor neurons. Plays a role in the splicing of cellular pre-mRNAs. May be involved in H(2)O(2)-induced neuronal cell death (By similarity). {ECO:0000250}. | 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 degrees Celsius). kcat is 270 min(-1) for epimerase activity with D-tagatose as substrate (at pH 8 and 50 degrees Celsius). {ECO:0000269|PubMed:16461638}; | 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-ribulose, D-xylulose, and D-sorbose. It shows a higher level of activity for cis ketoses than for trans-ketoses. {ECO:0000269|PubMed:16461638}. | Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58)) |
A9CH39 | PHRB_AGRFC | MSQLVLILGDQLSPSIAALDGVDKKQDTIVLCEVMAEASYVGHHKKKIAFIFSAMRHFAEELRGEGYRVRYTRIDDADNAGSFTGEVKRAIDDLTPSRICVTEPGEWRVRSEMDGFAGAFGIQVDIRSDRRFLSSHGEFRNWAAGRKSLTMEYFYREMRRKTGLLMNGEQPVGGRWNFDAENRQPARPDLLRPKHPVFAPDKITKEVIDTVERLFPDNFGKLENFGFAVTRTDAERALSAFIDDFLCNFGATQDAMLQDDPNLNHSLLSFYINCGLLDALDVCKAAERAYHEGGAPLNAVEGFIRQIIGWREYMRGIYWLAGPDYVDSNFFENDRSLPVFYWTGKTHMNCMAKVITETIENAYAHHIQRLMITGNFALLAGIDPKAVHRWYLEVYADAYEWVELPNVIGMSQFADGGFLGTKPYAASGNYINRMSDYCDTCRYDPKERLGDNACPFNALYWDFLARNREKLKSNHRLAQPYATWARMSEDVRHDLRAKAAAFLRKLD | 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-ribityllumazine (DMRL) as antenna chromophore. {ECO:0000269|PubMed:23589886}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:23589886, ECO:0000305|PubMed:22066008}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000269|PubMed:23589886}; | 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 | MSLKTAPVIVWFRKDLRLSDNLALLAAVEHGGPVIPVYIREKSAGPLGGAQEWWLHHSLAALSSSLEKAGGRLVLASGDAERILRDLISETGADTVVWNRRYDPTGMATDKALKQKLRDDGLTVRSFSGQLLHEPSRLQTKSGGPYRVYTPFWRALEGSDEPHAPADPPKSLTAPKVWPKSEKLSNWKLLPTKPDWAKDFSDIWTPGETGALDKLDDFIDGALKGYEEGRDFPAKPATSLLSPHLAAGEISPAAVWHATKGLSRHIASNDISRFRKEIVWREFCYHLLFHFPELGEKNWNDSFDAFSWRDDEKSFKAWTRGMTGYPIVDAGMRQLWQHGTMHNRVRMIVASFLIKHLLIDWRKGEKWFRDTLVDADPASNAANWQWVAGSGADASPFFRIFNPILQGEKFDGDGDYVRRFVPELEKLERKYIHKPFEAPKDALKKAGVELGKTYPLPIVDHGKARERALAAYAAVKKTT | 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) per subunit, that serves as photoantenna. {ECO:0000269|PubMed:22066008}; | 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 well as in dsDNA. {ECO:0000269|PubMed:22066008}. | 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:0000269|PubMed:16142903}; | 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-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q8TC26}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q8TC26}; Multi-pass membrane protein {ECO:0000255}. Note=Glutamatergic synaptic vesicles. {ECO:0000269|PubMed:17623043}. | 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 similarity). Plays a role in central nervous system development and is required for myelination, and survival and proliferation of oligodendrocytes (By similarity). {ECO:0000250|UniProtKB:B0UY98, ECO:0000250|UniProtKB:Q8TC26, ECO:0000269|PubMed:21668449}. | Rattus norvegicus (Rat) |
A9FDB7 | CP260_SORC5 | MDFPLANLFFVPSEDATAFGRRLRAAAQQAPIVFDTAFGMPILLRKSHITTAYRDTATFSTRMFQAGILNGGLAAMQGDEHARMRRVYNMFFLPRAVSQYEERFVRPISEQVVDRLAGKPRVDLLEDFAMELPRRVIGELFGFPAEKLHETDERVRAMLRGLVRMHDPAAVAESQRAYGETLGLITEVVERESRDTSDTLLGEILRTLKAEHMDTIEASRQIVLSLILGGYETTSWLVANTIHALLAHPDTLARVRQDPSLLPAAIEEGMRWCPSSFGVLRMVERDVRLDDQALSAGTVVCLAGIAGNYDETAYPSPEVYDIDRKPLPAANVFGGGAHFCVGAPLARMEARVGLQALLARFPGLRAVPEERPSFMYGAKDSVAHGPDKLPVLLH | 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, ChEBI:CHEBI:33738, ChEBI:CHEBI:132358; EC=1.14.15.19; Evidence={ECO:0000269|PubMed:26478560, ECO:0000269|PubMed:29509407}; CATALYTIC ACTIVITY: Reaction=androst-4-ene-3,17-dione + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 1alpha-hydroxyandrost-4-ene-3,17-dione + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:50812, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16422, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:133778; EC=1.14.15.19; Evidence={ECO:0000269|PubMed:26478560, ECO:0000269|PubMed:29509407}; | 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 androstenedione {ECO:0000269|PubMed:26478560}; KM=25 uM for 11-deoxycorticosterone {ECO:0000269|PubMed:27878817}; KM=124 uM for progesterone {ECO:0000269|PubMed:29509407}; Note=kcat is 0.70 sec(-1) with nootkatone as substrate (in the presence of FdR_B and Fdx2). kcat is 0.96 sec(-1) with nootkatone as substrate (in the presence of FdR_B and Fdx8). {ECO:0000269|PubMed:19696019}; | 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 conversion of nootkatone (PubMed:19696019). {ECO:0000269|PubMed:19696019}.; FUNCTION: In addition, acts as a steroid 1alpha-hydroxylase, when associated in vitro with the surrogate redox partners bovine adrenodoxin (Adx) and adrenodoxin reductase (Adr) (PubMed:26478560, PubMed:27878817, PubMed:29509407). Acts on several C-19 steroid substrates, including testosterone and androstenedione, which are hydroxylated to 1alpha-hydroxytestosterone and 1alpha-hydroxyandrostenedione, respectively (PubMed:26478560, PubMed:29509407). Can use their derivatives testosterone-acetate and 11-oxoandrostenedione, but not vitamin D3 and 25-hydroxyvitamin D3 (PubMed:26478560). Also catalyzes the hydroxylation of the C-21 steroid 11-deoxycorticosterone to 1alpha-hydroxy-11-deoxycorticosterone (PubMed:27878817). Catalyzes the hydroxylation of the C-21 steroid progesterone, leading to the formation of seven products: two major (1alpha-hydroxyprogesterone and 17alpha-hydroxyprogesterone) and five minor products (PubMed:29509407). {ECO:0000269|PubMed:26478560, ECO:0000269|PubMed:27878817, ECO:0000269|PubMed:29509407}. | Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So ce56)) |
A9JRL3 | CBPC1_XENTR | MSKAKATADKCLSNNSRIQSLLSQLEKVNAEPLLFDSDNTRYVTAKILHLAQTQEKTRKEIAAKGSTGMEVILCTLENTRDLQTILNILNILNELASTAGGRRINALISKGGSRILLQLLLSASKESSSNEELMMVLHSLLAKVGPKDKKFGIKARVSGALNISLNLVKQNLQNPRLILPCLQVLRVCCMNSVNSVYLGKNGAVEILFKLIGPFTRRNTGLIKVSLDTFAALLKSKTNARKAVDRGYVQALLSIYTDWHRHDTRHRHMLIRKGILQCLKSITNIKIGRKAFIDANGMKTLYNTSQECQAVRTLDPLVNTSSLIMRKCFPKNRLPLPTIKSAFQFQLPIMPTSGPVALLYSMPPEVDDVVDESDDNDDTEAETEAEAENEESDQLCKNDDIETDITKLIPGQELGRTLEDLKMYERFFPELTEDFQEFDLVSNEPKPGAKLGPIIVPTAGEEQPEVPNNFMKDLEKRSCNISLEDECNKRPTFLDMPKNVTNKGNDGLGQQVHGDIDRSCYYFSSDIVKDLEKLSLRKPSGNHPCRNGCVSAKDKPIFLPHPCNKSTSNSGSCSNNLFEKHSMHLSPLCCSGITPDDDESSPLDELAMREITDFDNLLPLHDPDLYIEIVKNTKSVPEYSEVAYPDYFGHVPPFFKERLLERPYGVQRSKIFQDIERMIHPNDIIDRVVYDLDNSSCSAQDESEVLKFNSKFESGNLRKVIQIRKNEYDLILNSDINSNHYHQWFYFEVSGMRTGVAYRFNIINCEKSNSQFNYGMQPLMYSVQEALASRPWWYRVGMDICYYKNHFSRSSIATGGQKGKSYYTITFTVTFPHRDDVCYFAYHYPYTYSTLKMHLKKLESLHNPQQVYFRQEVLCETLGGNGCPVITITAMPESNYYEHVYQFRNRPYIFLSSRVHPGETNASWVMKGTLEFLMGSSTSAQSLRESYIFKIVPMLNPDGVINGNHRCSLSGEDLNRQWQNPNVDLHPTIYHTKGLLQYLAAIRRTPLVYCDYHGHSRKKNVFMYGCSIKETVWHTNANAASCDMVEDSGYRTLPKVLNQLAPAFSMSSCSFVVEKSKESTARVVVWREIGVQRSYTMESTLCGCDQGKYKDLQIGTKELEEMGAKFCVGLLRLKRLTSPMELTLPPSLIDIENELIESSCKVASPTTYVLEDDEPRFLEEVDYSAESNDDADPDLPDTIGDFENTALEEEGFSDSEITRTHTSGQST | 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:0035610]; proteolysis [GO:0006508] | 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:Q641K1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000250|UniProtKB:Q641K1}; CATALYTIC ACTIVITY: Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + L-glutamate; Xref=Rhea:RHEA:63792, Rhea:RHEA-COMP:16435, Rhea:RHEA-COMP:16436, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:149555, ChEBI:CHEBI:149556; EC=3.4.17.24; Evidence={ECO:0000250|UniProtKB:Q641K1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793; Evidence={ECO:0000250|UniProtKB:Q641K1}; | 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-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of alpha-tubulin as well as non-tubulin proteins. {ECO:0000250|UniProtKB:Q641K1}. | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
A9JTM7 | OTOP3_XENTR | MLSKEEPACRQFHSREKTWGNEHNGKTVTQANNKEHKVPAVRRGDIGQREPAAHPASHIQGTMASENTGEQATCKDQYMDLDAPGNNLEHSWLHRHCEIPTTLHQRAKKTGRLFSGLFGLNLMFLGGTVVSSVALSNKAVPERDSQSFLCILMLLSSVWALYHLLFIRNQNGAVHHDHHAGAMWLKASLAIFGVCSIILSIFEIGHALLLQNCEILMDIVFFSIEIVFVSVQTVLLWVSCKDCVQMHHSVTRYGIMLTLATDILLWLTAVIDDSLEQDLEILQSNSTQDESNEMAQCQCPTDSMCWGLKQGYVTMFPFNIEYSLICATLLFIMWKNVGRREKLHSDPPRHTFQLRGIIYGPLIGGAALLVGISVFVQYQVEATSGMVSILSYHMYYGYKMIILAPMIVCSVAGIIAHSLREKEKKGQKETGRSDQDWLHMEDVGSENKNTDYSSGQYQSSQGDEKIQGYSLAQFALDNEKEKLEHRQGNTTKKHNTHQGKMKNYTRKLDVTLLFVSAVGQLGISYFSIIATVVTTPWTMLSALNFSNSLLLILQYLSQTMFIIESMRSIHEEEKEKPGHHEESHRRMSVQEMHKAPPSCLDAGHLGLSRRVVKEMAMFLMICNIMCWILGAFGAHPLYMNGLERQLYGSGIWLAILNIGLPLSVFYRMHSVGILLEVYLHA | 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) |
Subsets and Splits
No saved queries yet
Save your SQL queries to embed, download, and access them later. Queries will appear here once saved.