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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
D1A4G7 | ECCC_THECD | MSTVLVRRKERRQPPQMPRGEILLESPPELPEVVTNSFQNVLMYLPMAAGSAAMVFTFLNHRNTLQLVAGGMFALSMFGMMFGQLSQQSGERKTKLNSARRDYLRYLGQVRQRVRKAAKQQREALEWNNPAPGRLWSMVMSPRLWERRSSDADFAQVRIGAGPQRLAVQLIPPETKPVEDLEPMSAGALRRFLRAHSTVPDLPVAISLRSFARILPDGDPKAVYGMVRALIMQLAAFHSPDDVRITVCASRERMPQWQWMKWLPHSLHPTEYDAAGQVRLLTHSLVELESMLGPEIKDRGMFGASRAPAEPFHLVIVDGGQASYDSQIASDGIDGVCVIDLTGSVAETNEATMLRLRVTPERVYVVKRDRAGKEVLSSVGRPDQASIAEAEALARQLAPFRTSAADEPEEDVLSANMTLTSLLHIDNPYNLDPAVLWRPRPQRNRLRVPIGLDADGRPLELDIKESAQGGMGPHGLCIGATGSGKSELLRTLVLALAMTHSPEVLNFVLVDFKGGATFLGMEGLRHVSAIITNLEEELPLVDRMYDALHGEMVRRQEHLRHSGNYASLRDYEKARMEGAPLPPMPTLFIVLDEFSELLSAKPDFAELFVMIGRLGRSLGVHLLLASQRLEEGKLRGLDTHLSYRIGLRTFSAMESRVVLGVPDAYELPPSPGNGYLKFATEPLVRFKAAYVSGPVDEEPQTRSEGPQIVRQVLPYLTDYIRPQVVEQPQPEQRAEENKSSESLFDVVVRQLAGHGPEPHQIWLPPLDVPPTLDELLPPLSPSAAHGYTADGWEWRGRLHAVVGLVDRPFDQRRDPYWLDLSGGAGHVGVAGGPQTGKSTMLRTLITSLALLHTPQEVQFYCLDFGGGTLAGLAELPHVGSVATRLDADRIRRTVAEVSALLEQREQEFTERGIDSMATYRRLRATGEYAGDGFGDVFLVVDNWLTLRQDYEALEDSITQLAARGLGYGIHVVLSSNKWSEFRTSIRDLLGTKLELRLGDPYESEVDRKKAANVPENRPGRGLTRDGYHFLTALPRIDGDTSAETLTEGIATTVKTIREAWHGPTAPPVRMLPNVLPAAQLPSAAESGTRIPIGIDEDSLSPVYLDFNTDPHFLVFGDTECGKSNLLRLITAGIIERYTPQQARLIFIDYSRSLLDVATTEHQIGYAASSTAASSLVRDIKGAMEARLPPPDLTPEQLRSRSWWTGAELFLVVDDYEMVATSDNPLRPLAELLPQARDIGLHLIIARSMGGAGRALYEPIIQRIKEMASPGLVMSGNKDEGILLGNVKPHKLPQGRGYFVERRSGTRLIQTAYRES | null | null | localization [GO:0051179] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677] | PF01580; | 3.40.50.300; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Part of the ESX specialized secretion system, which exports proteins from the cell including EsxA (ESAT-6) and EsxB (CFP-10) (PubMed:25865481). Has weak intrinsic ATPase activity; probably only the first FtsK domain can hydrolyze ATP (PubMed:25865481). Might be the translocase subunit (PubMed:25865481). {ECO:0000269|PubMed:25865481}. | Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9) |
D1A7C3 | FGE_THECD | MPSFDFDIPRRSPQEIAKGMVAIPGGTFRMGGEDPDAFPEDGEGPVRTVRLSPFLIDRYAVSNRQFAAFVKATGYVTDAERYGWSFVFHAHVAPGTPVMDAVVPEAPWWVAVPGAYWKAPEGPGSSITDRPNHPVVHVSWNDAVAYATWAGKRLPTEAEWEMAARGGLDQARYPWGNELTPRGRHRCNIWQGTFPVHDTGEDGYTGTAPVNAFAPNGYGLYNVAGNVWEWCADWWSADWHATESPATRIDPRGPETGTARVTKGGSFLCHESYCNRYRVAARTCNTPDSSAAHTGFRCAADPL | 1.8.3.7 | COFACTOR: Name=Cu(+); Xref=ChEBI:CHEBI:49552; Evidence={ECO:0000269|PubMed:26403223, ECO:0000269|PubMed:27862795, ECO:0000269|PubMed:28544744}; Note=The catalytic copper is required to activate oxygen and catalyze oxidative C-H activation. {ECO:0000269|PubMed:28544744}; | post-translational protein modification [GO:0043687]; protein oxidation [GO:0018158] | null | cuprous ion binding [GO:1903136]; formylglycine-generating oxidase activity [GO:0120147] | PF03781; | 3.90.1580.10; | Sulfatase-modifying factor family | null | null | CATALYTIC ACTIVITY: Reaction=2 a thiol + L-cysteinyl-[sulfatase] + O2 = 3-oxo-L-alanyl-[sulfatase] + an organic disulfide + H(+) + H2O + hydrogen sulfide; Xref=Rhea:RHEA:51152, Rhea:RHEA-COMP:12900, Rhea:RHEA-COMP:12901, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29256, ChEBI:CHEBI:29919, ChEBI:CHEBI:29950, ChEBI:CHEBI:35489, ChEBI:CHEBI:85621; EC=1.8.3.7; Evidence={ECO:0000269|PubMed:26403223, ECO:0000269|PubMed:27862795}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=580 uM for [sulfatase]-L-cysteine (in presence of Cu(+)) {ECO:0000269|PubMed:27862795}; Note=kcat is 1.6 min(-1) in presence of Cu(+). {ECO:0000269|PubMed:26403223, ECO:0000269|PubMed:27862795}; | PATHWAY: Protein modification; sulfatase oxidation. {ECO:0000269|PubMed:26403223, ECO:0000269|PubMed:27862795}. | null | null | FUNCTION: Oxidase that catalyzes the conversion of cysteine to 3-oxoalanine on target proteins. 3-oxoalanine modification, which is also named formylglycine (fGly), occurs in the maturation of arylsulfatases and some alkaline phosphatases that use the hydrated form of 3-oxoalanine as a catalytic nucleophile. {ECO:0000269|PubMed:26403223, ECO:0000269|PubMed:27862795}. | Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9) |
D1D8L6 | CDNTP_ASPFM | MDGEMTASPPDISACDTSAVDEQTGQSGQSQAPIPKDIAYHTLTKALLFPDIDQYQHWHHVAPMLAKMLVDGKYSIHQQYEYLCLFAQLVAPVLGPYPSPGRDVYRCTLGGNMTVELSQNFQRSGSTTRIAFEPVRYQASVGHDRFNRTSVNAFFSQLQLLVKSVNIELHHLLSEHLTLTAKDERNLNEEQLTKYLTNFQVKTQYVVALDLRKTGIVAKEYFFPGIKCAATGQTGSNACFGAIRAVDKDGHLDSLCQLIEAHFQQSKIDDAFLCCDLVDPAHTRFKVYIADPLVTLARAEEHWTLGGRLTDEDAAVGLEIIRGLWSELGIIQGPLEPSAMMEKGLLPIMLNYEMKAGQRLPKPKLYMPLTGIPETKIARIMTAFFQRHDMPEQAEVFMENLQAYYEGKNLEEATRYQAWLSFAYTKEKGPYLSIYYFWPE | 2.5.1.-; 3.4.11.17 | null | alkaloid metabolic process [GO:0009820]; proteolysis [GO:0006508] | null | aminopeptidase activity [GO:0004177]; prenyltransferase activity [GO:0004659] | PF11991; | null | Tryptophan dimethylallyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + harmol = 6-(3-dimethylallyl)harmol + diphosphate; Xref=Rhea:RHEA:72983, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:192558, ChEBI:CHEBI:192559; Evidence={ECO:0000269|PubMed:35767141}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72984; Evidence={ECO:0000269|PubMed:35767141}; CATALYTIC ACTIVITY: Reaction=H2O + N-terminal L-tryptophanyl-L-alpha-aminoacyl-[peptide] = L-tryptophan + N-terminal L-alpha-aminoacyl-[peptide]; Xref=Rhea:RHEA:72999, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:18174, ChEBI:CHEBI:15377, ChEBI:CHEBI:57912, ChEBI:CHEBI:78597, ChEBI:CHEBI:192694; EC=3.4.11.17; Evidence={ECO:0000269|PubMed:18635009}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73000; Evidence={ECO:0000269|PubMed:18635009}; CATALYTIC ACTIVITY: Reaction=(R)-benzodiazepinedione + dimethylallyl diphosphate = (2S,3R,11R)-aszonalenin + diphosphate; Xref=Rhea:RHEA:73727, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:188914, ChEBI:CHEBI:192690; Evidence={ECO:0000269|PubMed:19421461}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73728; Evidence={ECO:0000269|PubMed:19421461}; CATALYTIC ACTIVITY: Reaction=(S)-benzodiazepinedione + dimethylallyl diphosphate = (2S,3R,11S)-aszonalenin + diphosphate; Xref=Rhea:RHEA:73731, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:192691, ChEBI:CHEBI:192693; Evidence={ECO:0000269|PubMed:19421461}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73732; Evidence={ECO:0000269|PubMed:19421461}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=650 uM for dimethylallyl diphosphate (DMAPP) {ECO:0000303|PubMed:17525915}; KM=300 uM for H-L-Trp-L-Gly-OH (for aminopeptidase activity) {ECO:0000269|PubMed:18635009}; KM=380 uM for L-tryptophan {ECO:0000303|PubMed:19113967}; KM=128 uM for cyclo-D-Trp-L-Tyr {ECO:0000303|PubMed:19113967}; | null | null | null | FUNCTION: Prenyltransferase that catalyzes reverse prenylation at position N-1 of tryptophan-containing cyclic dipeptides (PubMed:17525915, PubMed:18383240, PubMed:19113967, PubMed:19421461, PubMed:33643664, PubMed:35767141). Accepts only dimethylallyl diphosphate (DMAPP) as the prenyl donor but shows broad substrate specificities toward its aromatic substrates (PubMed:17525915, PubMed:18383240, PubMed:19113967, PubMed:19421461, PubMed:33643664, PubMed:35767141). Shows also tryptophan aminopeptidase activity with preference for linear peptides containing a tryptophanyl moiety at the N-terminus (PubMed:18635009). {ECO:0000269|PubMed:17525915, ECO:0000269|PubMed:18383240, ECO:0000269|PubMed:18635009, ECO:0000269|PubMed:19113967, ECO:0000269|PubMed:19421461, ECO:0000269|PubMed:33643664, ECO:0000269|PubMed:35767141}. | Aspergillus fumigatus (Neosartorya fumigata) |
D1FVF0 | BSLS_BEABA | MEPPNNANTGQLGPTLPNGTVDLPTDLSREITRHFGLEQDEIEEILPCTPFQRDVIECASDDKRRAVGHVVYEIPEDVDTERLAAAWKATVRYTPALRTCIFTSETGNAFQVVLRDYFIFARMYCPSAHLKSAIVKDEATAAVAGPRCNRYVLTGEPNSKRRVLVWTFSHSFVDSAFQGRILQQVLAAYKDGHGRVFSLQPTTDLTESENGDHLSTPASERTVVIERATQFWQEKLHGLDASVFPHLPSHKRVPAIDARADHYLPCPPFIQHEWSSTTVCRTALAILLARYTHSSEALFGVVTEQSHEEHPLLLDGPTSTVVPFRVLCALNQSVSKVMEAITTYDHDMRQFAHAGLCNISRIGDDASAACGFQTVLMVTDSRTAGDDEIHQVLEESEKFIPCTDRALLLSCQMTDEGVLLVARYDQSILEPLQMARFLRQLGFLINKLQSTDGSPCVGQLDVLAPEDRTEIEGWNSEPLQTQDCLIHSEVVRNAGDTPNKPAVCAWDGEWTYSELNNVSSRLASYISSLDLGQQLIVPIYLEKSKWVMAAILAVLKAGHAFTLIDPNDPPARTAQIIKQASASIALTSALHQSKMQAVVGRCITVDDDLVQTLTTFEGSQVASAAKPGDLAYVIFTSGSTGDPKGIMIEHRAFYSSVVKFGKALGIRSSTRALQFATHGFGAFLLEVLTTLIHGGCICVPSDHDRMHNIPGFIRQNQINWMMATPSYMTTMKPEDVPGLETLVLVGEQMSSSINDVWLSELQLLDGYGQSESSSICFVGKIDDSSRDPNNLGWAIGAHSWIINPDNPDQLVPIGAIGELLIESPGIARGYLFSQSTETPFLERAPAWYASKQPPYGVKFYRTGDLARYAPDGTVICLGRMDSQVKIRGQRVELDAIENLLRRQFPSDVTVVAEAVKRSDLPSSVVITGFLISSEYVVGAPSTEDTYILDQVVTQEINAKMRQILPAHSIPSFYICMKSLPRTATGKVDRRKLRSIGSSLLALQAQSTAPRSSQAPDASAGVTKLEEVWMDIFNLTPNSHNIGGNFFALGGDSITAIKMVNMARAAGIQLKVSDIFQNPTLASLQAAIGGSSMTVTSIPALALDGPVEQSYSQGRLWFLDQLEIGANWYTIPYAVRLRGPLDVDALNRALLALEKRHETLRTTFEDQDGVGVQIIHETLLDQLRIINADHADYVQLLKQEQTAPFNLASESGWRVSLIRLDDDDNILSIVMHHIISDGWSIDVLRRELGQLYAAALHGADLFGSALSPLPIQYRDFSVWQKQDAQVAEHERQLQYWQKQLADCSPAKLPTDFHRPALLSGKATTVPVTITSELYYRLQEFCSTFNTTSFVVLLATFRAAHYRLTGVDDAVIGTPIANRNRHELENLIGFFVNTQCMRITINEDEDTFESLVRQVRSTTTAAFEHEDVPFERVVSAMLPGSRDLSQNPLAQLVFAIHSHKDLGKFELEALESEPLQNEVYTRFDAEFHFFQAPDGLTGYINFATELFKVETIQNVVSVFLQILRHGLEHPQTLISVVPLTDGLAELRSMGLLEIKKVEYPRDSSVVDVFRTQVASYPDTLAVVDSSSRLTYAELDHQSDLLATWLRQQNLPTEALVVVLAPRSCETIITFLGILKANLAYLPLDIRSPITRMRDVLSTLPGRTIALLCSDEVAPDFQLPSIELVRIADALEEAAGMTSLNGHEHVPVPSPSPTSLAYVLYTSGSTGRPKGVMIEHRAIVRLARSDIIPDYRPACGDTMAHMFNTAFDGATYEIYTMLLNGGTLVCVDYMDTLSPKSLEAVFKKEQVNATIMAPALLKLYLADARDALKGLDVLISGGDRFDPQDAVDAQSLVRGSCYNGYGPTENGVFSTVYKVDKNDPFVNGVPLGRAVNNSGAYVVDRNQQLVGPGIIGELVVTGDGLARGYTERAFDQNRFTQLKVEGQSVRGYRTGDRVRYRVGEGLIEFFGRMDFQFKIRSNRIEAGEVEAAILSHPAVRNAAVILRVEEKLEPEIVGFVVAEHDDTAEQEEAGDQVEGWQAFFESTTYTELDTVSSSEIGKDFKGWTSMYDGNEIDKAEMQEWLDDTIHTLTDGQALGHVLEIGTGSGMVLFNLGSGLQSFVGLEPSKSAAAFVNNAIKSTPALAGKAQVFVGTATDTNKLDDLHPDLVIFNSVLQYFPTRDYLERVVDALVHLRSAKRIFFGDVRSYATNRHFLAARAIYTLGNHTTKDEVRKKMAEMEEREEEFLVEPAFFTTLVNRLPDVRHVEIIPKNMQATNELSAYRYAAVVHLRGSDELTRPVHPIKMDDWVDFQASHMHKDALREYLRLAENTKTVAISNIPYGKTIFERQVVESLDETSEDAPHASLDGAAWISAVRSDAKARSSLSVPDLVLLAKETGFRVEVSAARQWSQSGALDAVFHRYPAEPGVRTLFQFPTDNDVRMSAPLTNQPLQRLQKRRVAVQVREWLQDRIPSYMIPSHIVALDQMPLNTSGKVDRKELSRQAKAIKKVQKSAPPTAPAFPLSEVEVMLCEELTKTFEMDVNITDDFFQLGGHSLLATRLVARISHRLGARLTVKDVFDYPVFSELADIIRQQLASKNTLLPTASAGGGGQDKKESAGVAPTTDMEAMLCEEFANILGMDVGITDNFFDLGGHSLMATRLAARIGHRLNTTISVKDIFSHPVIFQLSAKLEVSQLESSSGGTDIKMPDYTAFQLIPAADAEKFMQDHIYPQINFSQDMVQDVYLATHLQQCFLRDVFGRPKPLVPFYVEFPPDSNPHTLATACTSLVDKYDIFRTIFVEAEGNLYQVVLKHLNLDIDVVETDANVHKTSSDLVDAIAKEPVRLGQPMIQVKVLKQTSSVRVLLWLSHALYDGLSWEHIVRDLHILSKERSLPPATQFSRYMQYVDHTRGPGCDFWRDVLQNAPITNLSDAGSGGRPTKAGDPRVWHAGKVISGPSQAIRSSITQATVFNAACAIVLSKETGTDNVVFGRIVSGRQGLPVRWQNIIGPCTNAVPVRAVVDAHGNHQQMLRDLQEQYLLSLPYETIGFDEIKRSCTDWPDSARNYGCCVTYQNFEYHPESEVDQQRVEMGILAKKAELIKEEPLYNVAIAGEVEPDGVHLQVTVVVDSQLFSQEGATHLMEQVCNTFQALNASL | 2.1.1.-; 6.1.2.- | null | amino acid activation for nonribosomal peptide biosynthetic process [GO:0043041]; methylation [GO:0032259]; secondary metabolite biosynthetic process [GO:0044550] | cytosol [GO:0005829] | isomerase activity [GO:0016853]; ligase activity [GO:0016874]; methyltransferase activity [GO:0008168]; phosphopantetheine binding [GO:0031177] | PF00501;PF00668;PF00550; | 3.30.300.30;3.40.50.980;1.10.1200.10;3.40.50.1820;3.30.559.10;3.40.50.12780;3.30.559.30;3.40.50.150; | NRP synthetase family | null | null | CATALYTIC ACTIVITY: Reaction=4 (R)-2-hydroxy-3-methylbutyrate + 8 ATP + 4 L-leucine + 4 S-adenosyl-L-methionine = 8 AMP + bassianolide + 8 diphosphate + 8 H(+) + 4 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:62272, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:145108, ChEBI:CHEBI:145660, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:23608474, ECO:0000269|PubMed:23727842, ECO:0000269|PubMed:29163920, ECO:0000269|PubMed:31388353, ECO:0000269|PubMed:31471217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62273; Evidence={ECO:0000269|PubMed:23608474, ECO:0000269|PubMed:23727842, ECO:0000269|PubMed:29163920, ECO:0000269|PubMed:31388353, ECO:0000269|PubMed:31471217}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.46 uM for L-phenylalanyl-N-acetyl-cysteamine thioester (by the MT domain) {ECO:0000269|PubMed:31388353}; KM=2.8 uM for L-leucyl-N-acetyl-cysteamine thioester(by the MT domain) {ECO:0000269|PubMed:31388353}; Vmax=0.41 uM/min/mg enzyme toward L-phenylalanyl-N-acetyl-cysteamine thioester (by the MT domain) {ECO:0000269|PubMed:31388353}; Vmax=0.05 uM/min/mg enzyme toward L-leucyl-N-acetyl-cysteamine thioester (by the MT domain) {ECO:0000269|PubMed:31388353}; | null | null | null | FUNCTION: Bassianolide nonribosomal synthetase that mediates the biosynthesis of bassianolide (BSL), a non-ribosomal cyclodepsipeptide that shows insecticidal and cancer cell antiproliferative activity (PubMed:19285149, PubMed:23608474, PubMed:23727842, PubMed:29163920, PubMed:31388353, PubMed:31471217). BSLS first catalyzes the iterative synthesis of an enzyme-bound dipeptidol monomer intermediate from D-2-hydroxyisovalerate and L-leucine before performing the condensation and cyclization of 4 dipeptidol monomers to yield the cyclic tetrameric ester bassianolide (PubMed:23608474, PubMed:23727842, PubMed:29163920, PubMed:31388353, PubMed:31471217). The N-methyltransferase MT domain is responsible for the methylation of the leucine residues of bassianolide (PubMed:29163920, PubMed:31388353). BSLS is flexible with both the amino acid and hydroxyl acid precursors, and produces bassianolide as the major product (containing N-methyl-L-Leu), together with small amounts of beauvericin and its analogs beauvericins A-C (containing N-methyl-L-Phe) (PubMed:31388353). {ECO:0000269|PubMed:19285149, ECO:0000269|PubMed:23608474, ECO:0000269|PubMed:23727842, ECO:0000269|PubMed:29163920, ECO:0000269|PubMed:31388353, ECO:0000269|PubMed:31471217}. | Beauveria bassiana (White muscardine disease fungus) (Tritirachium shiotae) |
D1KF50 | SRS2L_ARATH | MENLPPNRGMWNQEYSHGRISQSFRSAKPLLDRKRPIENAPNSSNPLPQRMKESMDTESVSHNINFNSTPLMELSANTPYKRLKPEIESYADGHPCGLRTPPPRFDLDKEIINGFQTDIYADVGSLSEAFVTPLKEPERVTLSNGCSTSSILDDDFDDSILEEIDLICEQSARKAACQTPTTSIYQTPSKDNKSSDPKASLDFRDVEKFEPDSNVKLKLDEETPTIAADPALLNSMPDECSKYMLSLNDRQRDAACSNISTPLMVIAGPGSGKTSTMVGRVLVLLNEGLLPSNILAMTFTKAATSEMRERIGKSAGKKAAKDITISTFHSFSLQLCRMHADKLQRTSEFSVYGHGQQRRAIIEAVRLYEEEKKNGSKTSVPCESGEGLNGAGAGAVCPEYAKDLSKKWQKFVTQGKASGKSPEQCRKMGNEIGAKILGNYNDILKACDALDYHDLISCSVTLLSDFPEVFKECQDTWKAIIVDEFQDTSTMQYKLLRMLGSHNHITIVGDDDQSIFGFNGADSSGFDSFRRDFPNYKEVRLIKNYRSSRHIVEAASSIIKNNTKRCQSKSISSENSQGSKITVKECHNEEAQCAYVIDKIIEITNDGSTPCCSHGDIAILYRRQVSGKVFQNAFRQRKIPFNVHGVAFYRKKVVQVILAMLKTTFSECDDASYRRVFKALLPFEKEEKKRIIEHIEKISTSRKCSFISAASDIFNAKISGTFKRSQLTQGRKVLQTLDMVAKLVDREQSLSAVVTCVANMIPQKYLLEQRAVVDNDGGKLLNEDNDLRSVLQYLMDDVAEFISTHCTTTEEEDAIKEKKGCNQLHSFINYISERETENFRSRRRDNENSVTLTTIHQSKGLEWDIVFIVKANENEIPLLHESNGNASESGTSLEEERRLLYVAMTRARKKLFFLYVTVDSNWQVLQPSRFLKEIPGHLLQGDMSVNDCRKVHENLPNKTEQSVSSFGTDIKHEESKLTDNDVMNIPEDYASEESIAAYALNGNNFLKRFDVEVRSVVSHLFHNWAKKQAFQEPKRLIDKVRFVIGERLAIKKNKHKDVLRALKSSLTSEEAFQYAEHVLRWEQLPADTRAHIVREKQEHFQKLRIENSMGTSEATSKQIAFLHSLGCTVVPTSRLHASRLIEQYKSL | 5.6.2.4 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19767619}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19767619}; | DNA recombination [GO:0006310]; DNA rewinding [GO:0036292]; recombinational repair [GO:0000725] | nucleus [GO:0005634] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; isomerase activity [GO:0016853] | PF00580;PF13361; | 1.10.10.160;3.40.50.300; | Helicase family, UvrD subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4; | null | null | null | null | FUNCTION: ATP-dependent 3'- to 5'-DNA helicase that could disrupt recombinogenic DNA intermediates and facilitate single strand annealing. Unwinds nicked and partial Holliday junctions in vitro. Anneals two single strands into a dsDNA molecule in vitro. {ECO:0000269|PubMed:19767619}. | Arabidopsis thaliana (Mouse-ear cress) |
D1L2X1 | DPOL2_BPK32 | MLDNFNQPKGSTIGVLKDGRTIQEAFDSLPRLESFSGSTATDKLRAAITLGVSEVAIGPVEGNGGRPYEFGDVVIPYPLRIVGCGSQGINVTKGTVLKRSAGASFMFHFTGEGQAQRPMGGGLFNINLNGDTATALGDIIKVTQWSYFKANNCAFQNMAGWGIRLKDVMESNISGNLFRRLGGPSGGGILFDDVRSAVTDNVNNLHIEDNTFALMSGPWIGSTANSNPDLIWIVRNKFEFDGTPAAPNTVDSYVLDFQQLSRAFIQDNGFTHFTTERNRYVGVLRVGATAVGTIKFEDNLLFACESAGLIAGGIVVSRGNVNNQGSATTAIKQFTNTSSKLCKLERVINVQSNGNVSVGQQILPDGYINMAELPGNTRLPSEYDADGETTSVLRVPANTQVRQWSVPKMYKDGLTVTKVTVRAKGAAAGAILSLQSGSTVLSTKSIDAGVWKNYVFYVKANQLQETLQLRNTGTADVLADGMVFGKVDYIDWDFAIAPGTLAAGAKYTTPNQSYLDVAGMRVQAVSIPMFDGPTTGLQVWVEATSANGSFVVVMKNDTGSELVTTVTRCRVRAFVS | null | null | adhesion receptor-mediated virion attachment to host cell [GO:0098671]; symbiont entry into host cell via disruption of host cell envelope [GO:0098994]; symbiont entry into host cell via disruption of host cell glycocalyx [GO:0098996] | virus tail [GO:0098015] | null | null | 2.160.20.10; | Przondovirus depolymerase 2 family; K21-specific depolymerase family | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Tail appendage (Probable). Depolymerase 1 is connected to the phage tail via an N-terminal anchor domain, while depolymerase 2 is attached to depolymerase 1 (PubMed:33947754). {ECO:0000303|PubMed:33947754, ECO:0000305}. | null | null | null | null | null | FUNCTION: Functions as a receptor binding protein (RBP) and probably mediates the attachment to the host capsular exopolysaccharides (Probable). Displays a depolymerase activity that specifically degrades the K21-type polysaccharides Klebsiella pneumoniae capsule, which allows the phage to reach the host cell membrane and bind the entry receptor (PubMed:30405575, PubMed:32386574, PubMed:33947754). {ECO:0000269|PubMed:30405575, ECO:0000269|PubMed:32386574, ECO:0000269|PubMed:33947754, ECO:0000305|PubMed:32386574, ECO:0000305|PubMed:33947754}. | Klebsiella phage KP32 (Bacteriophage KP32) |
D1LYT2 | GBRB2_MACMU | MWRVRKRGYFGIWSFPLIIAAVCAQSVNDPSNMSLVKETVDRLLKGYDIRLRPDFGGPPVAVGMNIDIASIDMVSEVNMDYTLTMYFQQAWRDKRLSYNVIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGDDNAVTGVTKIELPQFSIVDYKLITKKVVFSTGSYPRLSLSFKLKRNIGYFILQTYMPSILITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKIPYVKAIDMYLMGCFVFVFMALLEYALVNYIFFGRGPQRQKKAAEKAASANNEKMRLDVNKIFYKDIKQNGTQYRSLWDPTGNLSPTRRTTNYDFSLYTMDPHENILLSTLEIKNEMATSEAVMGLGDPRSTMLAYDASSIQYRKAGLPRHSFGRNALERHVAQKKSRLRRRASQLKITIPDLTDVNAIDRWSRIFFPVVFSFFNIVYWLYYVN | null | null | cellular response to histamine [GO:0071420]; chemical synaptic transmission [GO:0007268]; chloride transmembrane transport [GO:1902476]; inhibitory synapse assembly [GO:1904862]; nervous system process [GO:0050877]; regulation of membrane potential [GO:0042391]; signal transduction [GO:0007165] | chloride channel complex [GO:0034707]; cytoplasmic vesicle membrane [GO:0030659]; 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] | 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, GABRB2 sub-subfamily | PTM: Glycosylated. {ECO:0000250|UniProtKB:P63137}. | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P63138}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47870}. Cell membrane {ECO:0000250|UniProtKB:P47870}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P47870}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P63138}. | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P08219}; | null | null | null | null | FUNCTION: Beta subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain. GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain GABA active binding site(s) located at the alpha and beta subunit interface(s) (By similarity). When activated by GABA, GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (By similarity). Chloride influx into the postsynaptic neuron following GABAAR opening decreases the neuron ability to generate a new action potential, thereby reducing nerve transmission (By similarity). GABAARs containing alpha-1 and beta-2 or -3 subunits exhibit synaptogenic activity; the gamma-2 subunit being necessary but not sufficient to induce rapid synaptic contacts formation (By similarity). Extrasynaptic beta-2 receptors contribute to the tonic GABAergic inhibition (By similarity). Beta-containing GABAARs can simultaneously bind GABA and histamine where histamine binds at the interface of two neighboring beta subunits, which may be involved in the regulation of sleep and wakefulness (By similarity). {ECO:0000250|UniProtKB:P08219, ECO:0000250|UniProtKB:P47870, ECO:0000250|UniProtKB:P63138}. | Macaca mulatta (Rhesus macaque) |
D1MEI7 | MASTA_EUMPO | MRGTSFILFAVVVILGFLNANAEPLANPAPLANPDPLANPDPLANPEAFDLLGLVKKVASALG | null | null | defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; innate immune response [GO:0045087]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218] | toxin activity [GO:0090729] | null | null | MCD family, Mastoparan subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20096300}. Target cell membrane {ECO:0000250|UniProtKB:P0CJ38}. Note=Has an amphipathic alpha-helical conformation in hydrophobic environment. {ECO:0000305|PubMed:21184791}. | null | null | null | null | null | FUNCTION: Antimicrobial peptide. Shows activities against Gram-positive bacteria (S.aureus MIC=50 uM and 200 ug/ml, and B.subtilis MIC=200 ug/ml), Gram-negative bacterium E.coli (MIC=100 uM and 200 ug/ml) and fungi (B.cinerea MIC=5 uM, S.cerevisiae MIC=128 ug/ml, S.pombe MIC=128 ug/ml, A.nidulans MIC=128 ug/ml, and C.albicans MIC=64-100 uM) (PubMed:21184791, PubMed:36690087). Shows cytolytic activity against insect cell lines (PubMed:21184791). Its hemolytic activity is controversial, as Baek and colleagues report no activity while Bea and colleagues note an hemolytic activity (PubMed:21184791, PubMed:36690087). In vivo, peptide injection in the vicinity of the head and thorax of lepidopteran larvae induces feeding disorder followed by death due to starvation (PubMed:21184791). Is weakly lethal when tested on water flies (D.magna), but is not lethal on lady beetles (H.convergens). {ECO:0000269|PubMed:21184791}. | Eumenes pomiformis (Potter wasp) (Vespa pomiformis) |
D1ZA70 | ARO1_SORMK | MAESSSNPTRINILGKDNIIIDHGIWLNFVAQDLLQNIKSSTYILITDTNLYATYVPSFQSVFEKAAPQDVRLLTYAIPPGEYSKGRDTKAEIEDWMLSHQCTRDTVIIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDVPMGKNLIGAFWQPERIYIDLTFLNTLPVREFINGMAEVIKTAAIWDESEFTTLEENAKAILEAVRSKNKSADRLAPIRDILKRIVLGSARVKAEVVSSDEREGGLRNLLNFGHSIGHAYEAILTPQVLHGEAVAIGMVKEAELARFLGVLKPSAVARLTKCIASYDLPTSLQDKRIVKLTAGKECPVDVLLQKMAVDKKNEGRKKKIVLLSAIGKTYEPKASVVEDRAIRIVLTPCIRVHAGVPKDLKVSVTPPGSKSISNRALTLAALGEGTTRIYNLLHSDDTQVMLNAVAQLQGASFSWEDSDVLVVKGNGGRLQATSTPLYLGNAGTASRFLTSVVALCNPTDVNSTVLTGNARMKQRPIGALVDALRANGVGVKYLEKEHSLPVQVDAAGGLAGGVMELAATISSQYVSSLLMAAPYAREPVTLRLVGGKPISQPYIDMTIAMMASFGVQVQRSAEDPNTYHIPQGTYKNPETYIVESDASSATYPLAVAAITGTTCTVPNIGSKSLQGDARFAIEVLRPMGCTVEQTDASTTVTGPPVGTLKAIPHVDMEPMTDAFLTASVLAAVASGTTQITGIANQRVKECNRIKAMKDELAKFGVTCNELEDGIEVTGIPYTELKNPTEGIYCYDDHRVAMSFGVLSTISPHPVLILERECTGKTWPGWWDTMSNYFKSHLEGEEEPHSSHVSHEKPRKGNPKSIFIIGMRGAGKSTAGKWMSEVLNRPLIDLDHELERREGQTIPEIIRSERGWEGFRKAELDLLEDVIKNNPTGHIFSCGGGIVESEAARKLLISYSQNGGIVLLVHRDTDQVVEYLMRDKTRPAYSENIREVYYRRKPWFEECSNFRYYSPHPDGSKALTEPPFDFSQFLSVICGHSNHLEEAKKKPQSSFVSLTVPNVSKALDIIPKVVVGSDAVELRVDLLEDYDPEFVAKQVALLRSAARIPIVYTVRTVSQGGKFPDDDYALALKLYRTGLQAGVEYLDLEMTMPDEVIEAVTNEKGYTHIIASHHDPKATLSWKNGGWIQYYNKALQHGDVVKLVGVARELSDNFALARFKASLAAAHDKPFIGLNMGTAGKLSRVLNGFLTPVSHPALPSKAAPGQLSAAEIRQALALIGELEPRSFYLFGKPISASRSPALHNALFRDNGLPHQYSLFETDNAADVKELIRATDFGGASVTIPLKLDIMPLLDEVSDAAKVIGAVNTIIPVGSGDKVTLRGDNTDWMGMVYALRNAGVVKVSKESPAAGMVVGSGGTTRAAVYALHDLGFAPIYVVARNADRIKALAESFPADYDIRSLSTPEEVAAESTAQPSVVISTIPADKPIEQSMREVLVASLRHPSVTNGKHVLLEMAYTPRHTPLMQLAEDAHWQTIPGLEVLAAQGWYQFQLWTGITPIYTDAQAAVMGN | 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;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}. | Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell) |
D2CLZ9 | ATOH8_DANRE | MKNPHLNSPCKILNTVSGDKKMKRKAREPIKHVSEDHYPYFKLYKNPHLMAETLGDGSPQETHRSEIITSRDDSVRNDVLNTAVDMRINTITAAEVPDSKLRSVSEKTVNSKIVQASPQVSVLSAPQVFPLERVVLSQRAASQAPAGGSERAESPRKRAGEPSGVVTEIKAIQQTRRLLANARERTRVHTISAAFEALRKQVPCYSYGQKLSKLAILRIACNYILSLAQLADLDYTPDHRNMSFRECVEQCTRTLQAEGRSKKRKE | null | null | anatomical structure morphogenesis [GO:0009653]; axon development [GO:0061564]; heart development [GO:0007507]; heart looping [GO:0001947]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of neural retina development [GO:0061074]; regulation of skeletal muscle cell differentiation [GO:2001014]; sensory organ development [GO:0007423]; swim bladder formation [GO:0048797] | cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983] | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99NA2}. Nucleus speckle {ECO:0000250|UniProtKB:Q96SQ7}. Cytoplasm {ECO:0000250|UniProtKB:Q99NA2}. | null | null | null | null | null | FUNCTION: Transcription factor that binds a palindromic (canonical) core consensus DNA sequence 5'-CANNTG- 3' known as an E-box element, possibly as a heterodimer with other bHLH proteins (By similarity). During development, is required for heart looping and swim bladder formation by acting in concert with GATA4 and ZFPM1 (PubMed:23836893). During the development of both the retina and skeletal muscles is required for neural retinal cell through modulating PAX6 and NEUROG3 expression and myogenic differentiation (PubMed:20532172). {ECO:0000250|UniProtKB:Q96SQ7, ECO:0000269|PubMed:20532172, ECO:0000269|PubMed:23836893}. | Danio rerio (Zebrafish) (Brachydanio rerio) |
D2CSU4 | CM1_PETHY | METQLLRFPSHTITSSITTNSSRNTTPFLPHKKWSHFVKFQLVNSSSSIKHGIRPLQASATSLGLGNKNRVDETESYTLDGIRHSLIRQEDSIIFSLVERAQYCYNAETYDPDVFAMDGFHGSLVEYIVRETEKLHATVGRYKSPDEHPFFPKVLPEPVLPPMQYPKVLHPIADSININVKIWEMYFENLLPRLVKEGDDGNYGSTAVCDTICVQALSKRIHYGKFVAEAKYRASPEVYNAAIRAQDRNGLMDLLTYPAVEEAIKRRVEIKTRTYGQELHINGPENGGDPVYKIKPSLVAELYGDWIMPLTKEVQVQYLLRRLD | 5.4.99.5 | null | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate metabolic process [GO:0046417]; green leaf volatile biosynthetic process [GO:0010597] | chloroplast stroma [GO:0009570] | chorismate mutase activity [GO:0004106] | null | 1.10.590.10; | null | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:19811620}. | CATALYTIC ACTIVITY: Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU00516, ECO:0000269|PubMed:19811620}; | null | PATHWAY: Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1. {ECO:0000269|PubMed:19811620}. | null | null | FUNCTION: Component of the floral volatile benzenoid/phenylpropanoid (FVBPs) biosynthetic pathway (PubMed:19811620). Mediates the conversion of chorismate to prephenate, thus coupling metabolites from the shikimate pathway to the synthesis of FVBPs in the corolla (PubMed:19811620). {ECO:0000269|PubMed:19811620}. | Petunia hybrida (Petunia) |
D2CVN6 | TEB1_TETTS | MKLTKGGSYILKKVDRKQFYQDEEIVMQIKKILGQKTTDCKQYIKCECIDGLGDEALIYFEMLANQNQHLQKNDVIMIQDYLNDKTQNDKIVVLVTRFQFCKASHVQPKTAQKESIQLLNTEKTIIQKSKITKNPAEEVLKFIEVNEKDNSSNSEDMIIEQQKQEIKNNQKEKQSINGFNLEDSYSNISDITNFGGKSNFNIGSLSDQLSKQTLLISQLQVGKNRFSFKFEGRVVYKSSTFQNQQDSKYFFITAQDANNQEINLSFWQKVDQSYQTLKVGQYYYFIGGEVKQFKNNLELKFKFGDYQIIPKETLSANYVQPLALQPSKQFGNDSIGDSDYSIHNLIEKEESIAQKGYNGQKNNKYRQNNNNSKHTLLISEVLKTSKQYLSVLAQVVDIQSSDKNIRLKICDNSCNQELKVVIFPDLCYEWRDKFSINKWYYFNEFVRQIYNDEVQLKNNIHSSIKESDDQRKVITYNQEQGVFKKSISINSNDSFEIKPKISYKNNSNQEQRIYSSIEEIIQQAQASEIGQKKEFYVYGNLVSIQMKNKLYYYRCTCQGKSVLKYHGDSFFCESCQQFINPQVHLMLRAFVQDSTGTIPVMIFDQQSSQLINQIDPSIHVQEAGQYVKNCIENGQEEIIRQLFSKLDFARFIFEIQFENKEFNNEQEIAYKVLKIEKENIKEESKYLLKKLEHLINNNQNN | null | null | telomere maintenance via telomerase [GO:0007004] | chromosome, telomeric region [GO:0000781]; telomerase holoenzyme complex [GO:0005697] | single-stranded telomeric DNA binding [GO:0043047]; zinc ion binding [GO:0008270] | PF08646; | 2.20.25.10;2.40.50.140; | Replication factor A protein 1 family | null | SUBCELLULAR LOCATION: Chromosome, telomere {ECO:0000305}. | null | null | null | null | null | FUNCTION: Single-stranded DNA (ssDNA)-binding protein that mediates the recruitment of telomerase to telomeric DNA (PubMed:19941821, PubMed:20363756, PubMed:22143754, PubMed:25225329). Telomerase is an essential ribonucleoprotein (RNP) enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER (PubMed:19941821). Acts as a part of a replication protein A (RPA)-related subcomplex of the holoenzyme telomerase ribonucleoprotein complex: TEB1 specifically recognizes and binds telomeric ssDNA, thereby mediating the recruitment of the holoenzyme telomerase RNP complex to telomeres (PubMed:19941821, PubMed:25225329, PubMed:27895115). TEB1 is related to RPA1 subunit of the RPA complex but is specific to telomeric DNA, which is not the case of RPA1 (PubMed:25225329). {ECO:0000269|PubMed:19941821, ECO:0000269|PubMed:20363756, ECO:0000269|PubMed:22143754, ECO:0000269|PubMed:25225329, ECO:0000269|PubMed:27895115}. | Tetrahymena thermophila (strain SB210) |
D2EAC2 | ZBED6_MOUSE | MSVCTLSVPVSSISPGRRCSTFGDAGILGCVSINSNTDEDDVVEGKMVAEGANKETKLPAKKKRKKGLRIKGKRRRKKLILAKKFSKDLGSGRPVADAPASLASGAPEQDEESLFEGNIEKQIYLPSTRAKTSIVWHFFHVDPQYTWRAICNLCEKSVSRGKPGSHLGTSTLQRHLQARHSPHWTRANKFGVTNGEEDFTLDLSLSPPSPGSNGSFEYIPTDSVDENRMGKKRDKSASDALRAKRGRFLIKSNIVKHALIPGTRAKTSAVWNFFYTDPQHISRAVCNICKRSVSRGRPGSHLGTSTLQRHLQATHPIHWAVANKDSGAIGNGLDETETESSDLLNDTMPGEKSSGSQDLTAEDLSDSDTDEPPCLEVENRSESPIPVADQDNPVHAQERETTTHCENAAANQISQAVIQMIVEDLHPYNYFSTPAFQRFLQIVAPDYRLPSETYFFTKAVPQLYDSVREKIFLTLENVQSQKIHLTADIWTHDPSTDYFIVTVHWVSLETASSPSNGGTPNFRKWAVLCVTGLAKDCLITNILQELNDQIGLWLSPNFLTPSFIVSDNSSNVVHAIKGGGFTHVPCFLHCLNIVIQDFFCEHKSIENMLVAARKTCHHFSHSVKARQILQEFQNDHQLPWKNLKQDETGHWISTFYMLKWLLEHCYSVHHSLGRASGVVLTSLQWTLMTYVCDILKPFEEATQRVSVKTTGLNQVLPLIHHLLFSLQRLREDFQVRGITQALNLVDSLSLKLESDALLSAMLKSKHCILATLLDPCFKNSLEDFFPQGADLETYKQILAEEVCNYMESSPGACQISSSETSGPLVRLGTDSFTSIKEGTSSAGSLDSSAAGSVAVGSKSSLLPAAVAVVDEYFKEKYSELSGGDDPLVYWQRKVSIWPALTQVAIQYLSCPMCSWQSECMFTTNSHFHPKQIMNMDFDNIEQLIFLKMNLENVNYDYSTLILSWDPENKAVQSNEKEILP | null | null | blastocyst hatching [GO:0001835]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of muscle cell differentiation [GO:0051148]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]; regulation of transcription by RNA polymerase II [GO:0006357] | centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; protein dimerization activity [GO:0046983]; transcription cis-regulatory region binding [GO:0000976] | PF05699;PF02892; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20016685, ECO:0000269|PubMed:24043816, ECO:0000269|PubMed:26750727, ECO:0000269|PubMed:32557799}. Nucleus, nucleolus {ECO:0000269|PubMed:20016685}. Cytoplasm {ECO:0000269|PubMed:24043816, ECO:0000269|PubMed:26750727, ECO:0000269|PubMed:32557799}. Note=Located predominantly in the nucleolus but is also dispersed throughout the nucleus (PubMed:20016685). Mainly cytoplasmic in insulin- and glucagon-positive islet pancreatic cells, however nuclear localization is evidence in some pancreatic endocrine cells (PubMed:24043816). {ECO:0000269|PubMed:20016685, ECO:0000269|PubMed:24043816}. | null | null | null | null | null | FUNCTION: Transcriptional repressor which binds to the consensus sequence 5'-GCTCGC-3', transcription regulation may be tissue-specific (PubMed:20016685, PubMed:20134481, PubMed:24043816, PubMed:29440408, PubMed:32557799). Regulates the expression of target genes such as: IGF2, PGAP6/TMEM8, ENHO, and PIANP (PubMed:20016685, PubMed:20134481, PubMed:24043816, PubMed:29440408, PubMed:32557799). Acts as a transcriptional repressor of growth factor IGF2, thereby negatively regulating postnatal growth of muscles and internal organs, especially in females (PubMed:20016685, PubMed:29440408, PubMed:32557799). Negatively regulates myoblast differentiation and myoblast mitochondrial activity via its regulation of IGF2 transcription (PubMed:32557799). Negatively regulates the cell cycle of myoblasts, potentially via transcriptional regulation of the E2F family of transcription factors such as: E2F1 and E2F2 (PubMed:20016685, PubMed:32557799). Positively regulates the cell cycle and survival of pancreatic beta cells (PubMed:24043816). Binds to the CDH2 gene and may directly repress CDH2 transcription (PubMed:26750727). Probably by controlling CDH2 expression, regulates pancreatic beta cell adhesion, and formation of cell-to-cell junctions between pancreatic beta cells and neural crest stem cells (PubMed:26750727). May also play a role in embryonic beta cell differentiation (PubMed:24043816). May play a role in insulin sensitivity and glucose clearance (PubMed:29440408). {ECO:0000269|PubMed:20016685, ECO:0000269|PubMed:20134481, ECO:0000269|PubMed:24043816, ECO:0000269|PubMed:26750727, ECO:0000269|PubMed:29440408, ECO:0000269|PubMed:32557799}. | Mus musculus (Mouse) |
D2GXM8 | CBPC5_AILME | MELRCGGLLFSSRFDSGNLAHVEKVDSVSGDGEGGAAGASAPFSSIASSPDYEFNVWTRPDCAETEFENGNRSWFYFSVRGGTPGKLIKINIMNMNKQSKLYSQGMAPFVRTLPTRPRWERIRDRPTFEMTETQFVLSFVHRFVEGRGATTFFAFCYPFSYSDCQDLLNQLDQRFLENHPTHSSPLDTIYYHREILCYSLDGLRVDLLTITSCHGLREDREPRLQQLFPDTGTPRPFCFTGKRIFFLSSRVHPGETPSSFVFNGFLDFILRPDDPRAQTLRRLFVFKLIPMLNPDGVVRGHYRTDSRGVNLNRQYLKPDAALHPAIYGAKAVLLYHHVHSRLHPQSPSEHQHSPCLPPDAPLSDLEKANHLRNEAHLGHTSDGDSPEDWTQTRPAEQKASGVWLMPQQCADAEQPAPDTIPPKESGVAYYVDLHGHASKRGCFMYGNSFSDESTQVENMLYPKLISLNSAHFDFQGCNFSEKNMYARDRRDGQSKEGSGRVAIYKASGIIHSYTLECNYNTGRSVNSIPAACHDNGRASPPPPPAFPSRYTVELFEQVGRAMAIAALDMAECNPWPRIVLSEHSSLTNLRAWMLKHVRSSRGLSSTVSGAVNKKRGSRTPPRSNSGLPVSCSENPLSRARSFSTGTSAGGSSSSQQNSPQMKNSPSFPFHGSRPTGLPGLGSSTQKVSHRVLGPVREPRSQDRRRRQQPLTHRPTSSSLAPSPNPTSSSPASSHSTGPCLLPSAFSVSGSSCSLLSSGDKPEAVMVIGKGLLGPRIPCIRTRLQVRPRLGQGSPPTCRGMSGSSGPTSPIPRTRESSEPEPGPHSAPGLPQAGPPRPRSAPAFSPISCSLSDSQSRICYSGGPLGQPEVCFGPKSPPLTVSPRV | 3.4.17.-; 3.4.17.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00730}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730}; | C-terminal protein deglutamylation [GO:0035609]; defense response to virus [GO:0051607]; protein branching point deglutamylation [GO:0035611]; protein deglutamylation [GO:0035608]; protein side chain deglutamylation [GO:0035610]; proteolysis [GO:0006508] | cytosol [GO:0005829]; intercellular bridge [GO:0045171]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; nucleus [GO:0005634] | metallocarboxypeptidase activity [GO:0004181]; tubulin binding [GO:0015631]; zinc ion binding [GO:0008270] | PF18027;PF00246; | 2.60.40.3120;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09M02}. Nucleus {ECO:0000250|UniProtKB:Q09M02}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q8NDL9}. Midbody {ECO:0000250|UniProtKB:Q8NDL9}. Note=Mainly cytoplasmic. Slight accumulation in the nucleus is observed. Colocalizes with alpha-tubulin in the mitotic spindle and with midbody microtubules in the intercellular bridges formed during cytokinesis. {ECO:0000250|UniProtKB:Q09M02, ECO:0000250|UniProtKB:Q8NDL9}. | CATALYTIC ACTIVITY: Reaction=gamma-L-glutamyl-L-glutamyl-[protein] + H2O = L-glutamate + L-glutamyl-[protein]; Xref=Rhea:RHEA:60152, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15377, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:143622; Evidence={ECO:0000250|UniProtKB:Q09M02}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60153; Evidence={ECO:0000250|UniProtKB:Q09M02}; 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:Q09M02}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60005; Evidence={ECO:0000250|UniProtKB:Q09M02}; CATALYTIC ACTIVITY: Reaction=C-terminal L-alpha-aminoacyl-L-glutamyl-[tubulin] + H2O = C-terminal L-alpha-aminoacyl-[tubulin] + L-glutamate; Xref=Rhea:RHEA:63796, Rhea:RHEA-COMP:16436, Rhea:RHEA-COMP:16437, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90782, ChEBI:CHEBI:149556; EC=3.4.17.24; Evidence={ECO:0000250|UniProtKB:Q09M02}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63797; Evidence={ECO:0000250|UniProtKB:Q09M02}; 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:Q09M02}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63793; Evidence={ECO:0000250|UniProtKB:Q09M02}; | null | null | null | null | FUNCTION: Metallocarboxypeptidase that mediates 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. Cleaves alpha- and gamma-linked polyglutamate tubulin side-chain, as well as the branching point glutamate. Also catalyzes the removal of alpha-linked glutamate residues from the carboxy-terminus of alpha-tubulin. Mediates deglutamylation of nucleotidyltransferase CGAS, leading to CGAS antiviral defense response activation. {ECO:0000250|UniProtKB:Q09M02}. | Ailuropoda melanoleuca (Giant panda) |
D2GZV9 | ENTP5_AILME | MATTWGAAFFMLVASCVCSTVFHRDQQTWFEGVFLSSMCPINVSASTLYGIMFDAGSTGTRIHIYTFVQKIPGQLPILEGEIFESVKPGLSAFVDQPKQGAETVEELLEVAKDSVPRSHWKRTPVVLKATAGLRLLPEQKAEALLFEVREIFRKSPFLVPDDSVSIMDGSYEGILAWVTVNFLTGQLHGHSQKTVGTLDLGGASTQITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTHSYLGFGLKAARLATLGALETEGIDGHTFRSACLPRWLEAEWIFGGVKYQYGGNKEGNEGSGEVGFEPCYAEVLRVVQGKLHQPDEVRKSSFYAFSYYYDRAADTDMIDYETGGVLKVEDFERKAREVCDNLEKFTSGSPFLCMDLSYITALLKDGFGFADSTILQLSKKVNNIETGWALGATFHLLQSLGISH | 3.6.1.6 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:O75356}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O75356}; | 'de novo' post-translational protein folding [GO:0051084]; protein N-linked glycosylation [GO:0006487]; UDP catabolic process [GO:0006256]; UDP-glucose metabolic process [GO:0006011] | endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576] | ADP phosphatase activity [GO:0043262]; CDP phosphatase activity [GO:0036384]; GDP phosphatase activity [GO:0004382]; IDP phosphatase activity [GO:1990003]; UDP phosphatase activity [GO:0045134] | PF01150; | 3.30.420.40;3.30.420.150; | GDA1/CD39 NTPase family | PTM: N-glycosylated; high-mannose type. {ECO:0000250|UniProtKB:Q9WUZ9}. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9WUZ9}. Secreted {ECO:0000250|UniProtKB:O75356}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800; Evidence={ECO:0000250|UniProtKB:O75356}; CATALYTIC ACTIVITY: Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157; Evidence={ECO:0000250|UniProtKB:O75356}; CATALYTIC ACTIVITY: Reaction=H2O + UDP = H(+) + phosphate + UMP; Xref=Rhea:RHEA:64876, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877; Evidence={ECO:0000250|UniProtKB:O75356}; CATALYTIC ACTIVITY: Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208; Evidence={ECO:0000250|UniProtKB:O75356}; CATALYTIC ACTIVITY: Reaction=CDP + H2O = CMP + H(+) + phosphate; Xref=Rhea:RHEA:64880, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64881; Evidence={ECO:0000250|UniProtKB:O75356}; CATALYTIC ACTIVITY: Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=3.6.1.6; Evidence={ECO:0000250|UniProtKB:O75356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437; Evidence={ECO:0000250|UniProtKB:O75356}; | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q9WUZ9}. | null | null | FUNCTION: Hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP (By similarity). In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases. UMP can be transported back by an UDP-sugar antiporter to the cytosol where it is consumed to regenerate UDP-glucose. Therefore, it positively regulates protein reglucosylation by clearing UDP from the ER lumen and by promoting the regeneration of UDP-glucose. Protein reglucosylation is essential to proper glycoprotein folding and quality control in the ER (By similarity). {ECO:0000250|UniProtKB:O75356, ECO:0000250|UniProtKB:Q9WUZ9}. | Ailuropoda melanoleuca (Giant panda) |
D2H526 | CDK12_AILME | MPNPERHGGKKDGSGGASGTLQPSSGGGSSNSRERHRLVSKHKRHKSKHSKDMGLVTPEAAPLGTIIKPLVEYDDISSDSDTFSDDMAFKLDRRENDERRGTDRSDRLHKHRHHQHRRSRDLLKTKQTEKEKNQEVSSKSGSMKDRISGSSKRSNEENEDYGKAQISKSSSNKESRSSKLHKEKTRKERELKSGHKDRSKSHRKRETPKSYKTVDSPKRRSRSPHRKWSDSPKQDDSPSGASYGQDYDLSPPRSHTSSNYDSYKKSPGSTSRRQSISPPYKEPSAYQSSTRSPSPYSRRQRSVSPYSRRRSSSYERSGSYSGRSPSPYGRRRSSSPFMSKRSLSRSPLPSRKSMKSRSRSPAYSRHSSSHSKKKRSGSRSRHSSISPVRLPLNSSLGAELSRKKKERAAAAAAAKMDGKESKGSPIFLPRKENSLVEAKDSGLESKKLTRGVKLEKSAPDTELVNIPHLNTEVKNSLDTGKVKLDENSEKHPIKDLKAQGSRDSKPIALKEEIVTPKETETSEKETPPPVPAVTSPPPPLPTTSPPPQTPPLPPLPPLPAIPQQPPLPPPQPAFSHVLASSTSTLPPSTHPRTSTLSSQANSQPLAQVSVKTQVSVTAAIPHLKTSTLPPLPLPPLLPGDDDMDSPKETPPSKPVKKEKEQRPRHLLTDLPLPPELPGGDPSPPDSPEPKAVTPPQQPYKKRPKICCPRYGERRQTESDWGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLIHRSVVNMKEIVTDKQDALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLMEGLDYCHKKNFLHRDIKCSNILLNNSGQIKLADFGLARLYNSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANLELAQLELISRLCGSPCPAVWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPSAALDLLDHMLTLDPSKRCTAEQTLQSDFLKDVELSKMDPPDLPHWQDCHELWSKKRRRQRQSGVVIEEPPPSKASRKETTSGTSAEPVKNSSPAPPQPASGKVEPGTGDAIGLGDITQQLNQSELAVLLNLLQSQTDLSIPQMAQLLNIHSNPEMQQQLEALNQSISALTEATSQQQDSEHMAPEESLKEAPPALVVQPSAEQTTSEASSTPADMQNMLAVLLSQLMKTQEPAGSLEENNSDKNSGPQGPRRTPTMPQEEAAACPPHILPPEKRPPEPPGPPPPPPPPPLIEGDLSSAPQELNPAVTAALLQLLSQPEAEPPGHLPHEHQALRPMEYSTRPHPNRTYGNTDGPETGFSATDTDERNSGPALTESLTQTLVKNRTFSGSVSHLGESSSYQGTGSVQFPGDQDLRFARVPLPLHSVVGQPFLKAEGSSNSVVHAETKLQNYGELGPGTTGASSSGAGLNWGGSAQSSAYGKLYRGPTRVPPRGGRGRGVPY | 2.7.11.22; 2.7.11.23 | null | mRNA processing [GO:0006397]; negative regulation of stem cell differentiation [GO:2000737]; phosphorylation [GO:0016310]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; regulation of MAP kinase activity [GO:0043405]; RNA splicing [GO:0008380]; transcription by RNA polymerase II [GO:0006366] | cyclin K-CDK12 complex [GO:0002944]; cyclin/CDK positive transcription elongation factor complex [GO:0008024]; nuclear cyclin-dependent protein kinase holoenzyme complex [GO:0019908]; nuclear speck [GO:0016607] | ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353] | PF12330;PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily | PTM: Phosphorylation at Thr-894 increases kinase activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Colocalized with nuclear speckles throughout interphase. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23; 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: Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors (By similarity). {ECO:0000250}. | Ailuropoda melanoleuca (Giant panda) |
D2HBJ8 | UBP44_AILME | MLTMDKCKHIGQLRLAQDHSILNPQKWHCVDCNTTESIWACLSCSHVACGRYIEEHALKHFQESSHPVALEVNEMYVFCYLCDDYVLNDNATGDLKLLRSMLSAIKSQNYQCTTRSGRVLRSMGTSDDTYYLHDGTQSLLQNEDQMYTALWHRRRILMSKIFRTWFEQSPTGRKRQEEQFQEKIAKREVKKRRQELEYQVKAELETIHPRKSLRLQGLAQSTTVEIVPVQVPLQTPASPAKDKVVSTSEDVRLKKASDSSGKRRPIVTPGVTGLRNLGNTCYMNSVLQVLSHLLIFRQCFLKLDLNQWLAVTASDKTRSPYKHPSITDTVYQMNECQETDTGSAPSRHPSLSLGLSGGASKSRKMELIQPREPSSQYISLCHELHTLFQVMWSGKWALVSPFAMLHSVWRLIPAFRGYAQQDAQEFLCELLDKIQHELETTGTRLPALIPTSQRKLIKQVLNVVNNIFHGQLLSQVTCLACDNKSNTIEPFWDLSLEFPERYQCNGKDIASQPCRVTEMLAKFTETEALEGKIYVCDHCNSKRRRFSSKSVVLTEAQKQLMICHLPQVLRLHLKRFRWSGRNNREKIGVHVGFEEILNMEPYCCRESLKSLRPECFIYDLSAVVMHHGKGFGSGHYTAYCYNSEGGFWVHCNDSKLSMCTMDEVCKAQAYILFYTQRVTENGHSKLLPPELLSGSQHPNEEADTSSNEILS | 3.4.19.12 | null | antiviral innate immune response [GO:0140374]; cell division [GO:0051301]; chromosome segregation [GO:0007059]; negative regulation of mitotic metaphase/anaphase transition [GO:0045841]; negative regulation of ubiquitin protein ligase activity [GO:1904667]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein deubiquitination [GO:0016579]; regulation of mitotic cell cycle spindle assembly checkpoint [GO:0090266]; regulatory T cell differentiation [GO:0045066] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | cysteine-type deubiquitinase activity [GO:0004843]; zinc ion binding [GO:0008270] | PF00443;PF02148; | 3.90.70.10;3.30.40.10; | Peptidase C19 family, USP44 subfamily | PTM: Dephosphorylated by CTDP1. {ECO:0000250}.; PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination and is degraded by the proteasome. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H0E7}. Cytoplasm {ECO:0000250|UniProtKB:Q9H0E7}. Note=Peaks in interphase, with relatively low levels maintained throughout mitosis. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q9H0E7}; | null | null | null | null | FUNCTION: Deubiquitinase that plays a key regulatory role in the spindle assembly checkpoint or mitotic checkpoint by preventing premature anaphase onset. Acts by specifically mediating deubiquitination of CDC20, a negative regulator of the anaphase promoting complex/cyclosome (APC/C). Deubiquitination of CDC20 leads to stabilize the MAD2L1-CDC20-APC/C ternary complex (also named mitotic checkpoint complex), thereby preventing premature activation of the APC/C. Promotes association of MAD2L1 with CDC20 and reinforces the spindle assembly checkpoint. Promotes also the deubiquitination of histone H2A and H2B. Recruited to RNF8/RNF168-ubiquitinated chromatin surrounding double stranded breaks (DSBs), promotes hydrolysis of such ubiquitin conjugates, thus negatively regulating protein recruitment to damaged chromatin (By similarity). Participates in nucleotide excision repair (NER) pathway by deubiquitinating DDB2 to prevent its premature degradation so it can remain on damaged chromatin (By similarity). Promotes FOXP3 stabilization through 'Lys-48'-linked deubiquitination leading to increased stability and increased regulatory T-cell lineage stability. Plays also a positive role in innate immune response to DNA viruses by deubiquitinating STING1, selectively removing its 'Lys-48'-linked polyubiquitin chains and stabilizing it (By similarity). {ECO:0000250|UniProtKB:Q8C2S0, ECO:0000250|UniProtKB:Q9H0E7}. | Ailuropoda melanoleuca (Giant panda) |
D2HEW7 | KLH22_AILME | MAEEQEFTQLCKLPVQPSHPHCVNNTYRSAQHSQALLRGLLALRDSGILFDVVLVVEGRHIEAHRILLAASCDYFRGMFAGGLKEMEQEEVLIHGVSYNAMCQILHFIYTSELELSLSNVQETLVAACQLQIPEIIHFCCDFLMSWVDEENILDVYRLAELFDLSRLTEQLDTYILKNFVAFSRTDKYRQLPLEKVYSLLSSNRLEVSCETEVYEGALLYHYTLEQVQADQISLHEPPKLLETVRFPLMEAEVLQRLHDKLDPSPLRDTVANALMYHRNESLQPSLQGPHTELRSDFQCVVGFGGIHSTPSTVLSDQAKYLNPLLGEWKHFTASLAPRMSNQGIAVLNNFVYLIGGDNNVQGFRAESRCWRYDPRHNRWFQIQSLQQEHADLCVCVVGRYIYAVAGRDYHNDLNAVERYDPTTNSWAYVAPLKREVYAHAGATLEGKMYVTCGRRGEDYLKETHCYDPDSNTWHSLADGPVRRAWHGMATLLDKLYVIGGSNNDAGYRRDVHQVACYSCTSGQWSSVCPLPAGHGEPGIAVLDTRIYVLGGRSHNRGSRTGYVHIYDVEKDCWEEGPQLDNSISGLAACVLTLPRTLLLEPPRGTPDRSQADPDFASEVMSVSDWEEFDNSSED | null | null | cell division [GO:0051301]; cellular response to leucine [GO:0071233]; mitotic sister chromatid segregation [GO:0000070]; mitotic spindle assembly checkpoint signaling [GO:0007094]; negative regulation of autophagy [GO:0010507]; negative regulation of type I interferon production [GO:0032480]; positive regulation of cell growth [GO:0030307]; positive regulation of TORC1 signaling [GO:1904263]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein monoubiquitination [GO:0006513] | centrosome [GO:0005813]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intercellular bridge [GO:0045171]; lysosome [GO:0005764]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; polar microtubule [GO:0005827] | 14-3-3 protein binding [GO:0071889]; ubiquitin ligase-substrate adaptor activity [GO:1990756] | PF07707;PF00651;PF01344;PF13415;PF13964; | 1.25.40.420;2.120.10.80; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q53GT1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q53GT1}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q53GT1}. Nucleus {ECO:0000250|UniProtKB:Q53GT1}. Lysosome {ECO:0000250|UniProtKB:Q53GT1}. Note=Mainly cytoplasmic in prophase and prometaphase. Associates with the mitotic spindle as the cells reach chromosome bi-orientation. Localizes to the centrosomes shortly before cells enter anaphase After anaphase onset, predominantly associates with the polar microtubules connecting the 2 opposing centrosomes and gradually diffuses into the cytoplasm during telophase. Localizes to the nucleus upon amino acid starvation. Relocalizes to the cytosol and associates with lysosomes when amino acids are available. {ECO:0000250|UniProtKB:Q53GT1}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q53GT1}. | null | null | FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for chromosome alignment and localization of PLK1 at kinetochores. The BCR(KLHL22) ubiquitin ligase complex mediates monoubiquitination of PLK1, leading to PLK1 dissociation from phosphoreceptor proteins and subsequent removal from kinetochores, allowing silencing of the spindle assembly checkpoint (SAC) and chromosome segregation. Monoubiquitination of PLK1 does not lead to PLK1 degradation. The BCR(KLHL22) ubiquitin ligase complex is also responsible for the amino acid-stimulated 'Lys-48' polyubiquitination and proteasomal degradation of DEPDC5. Through the degradation of DEPDC5, releases the GATOR1 complex-mediated inhibition of the TORC1 pathway. It is therefore an amino acid-dependent activator within the amino acid-sensing branch of the TORC1 pathway, indirectly regulating different cellular processes including cell growth and autophagy. {ECO:0000250|UniProtKB:Q53GT1}. | Ailuropoda melanoleuca (Giant panda) |
D2HHP1 | WEE2_AILME | MDDSSINKELKQKLNFSYCEEESESEGQEAWETRDAHSQIPDRAEGQESEAKFTPPGPPLSSVHEVGTFQEKTKKSPEQVLMTPVSGFRNYPETPAQPDSRSKLLDCESPFTPKGLLSQSVISSTEKIPSRGSKHLRFTPVPFVDEMTSSALVNINPFTPESYRKQFLKSNGKRKTRGDFEEAGPGEGNVEQGLPAKRCVLQETNMASRYEKEFLEVEKIGVGEFGTVYKCIKRLDGCVYAIKRSTKPFAGLSNENLALHEVYAHAVLGHHPHVVRYYSAWAEDDHMIIQNEYCNGGSLQTAISENTKSGNHFQEPKLKDILLQISLGLKYIHSSGMVHLDIKPSNIFICHKMQSDSPVVPEEIENEADWFLSANVMYKIGDLGHVTSISKPKVEEGDSRFLANEILQEDYQHLPKADIFALGLTIAVAAGAESLPTNGAAWHHIREGKLPDIPQKLSEEFYNLLKNMIHPDPRERPSAAALARSRVLRPSLGKAEELQQQLNLEKFKTATLERELREAQQAWFSQEERGDAGVSGTPTGSRSTKRLVGGKSAKSSSFTWGKSSP | 2.7.10.2 | null | female meiotic nuclear division [GO:0007143]; female pronucleus assembly [GO:0035038]; mitotic cell cycle [GO:0000278]; negative regulation of G2/MI transition of meiotic cell cycle [GO:0110031]; negative regulation of oocyte maturation [GO:1900194]; phosphorylation [GO:0016310]; positive regulation of phosphorylation [GO:0042327]; regulation of fertilization [GO:0080154]; regulation of meiosis I [GO:0060631] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; non-membrane spanning protein tyrosine kinase activity [GO:0004715] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, WEE1 subfamily | PTM: Phosphorylation leads to increase its activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027}; | null | null | null | null | FUNCTION: Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1 and acts as a key regulator of meiosis during both prophase I and metaphase II. Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, by phosphorylating CDK1 at 'Tyr-15', leading to inhibit CDK1 activity and prevent meiotic reentry. Also required for metaphase II exit during egg activation by phosphorylating CDK1 at 'Tyr-15', to ensure exit from meiosis in oocytes and promote pronuclear formation (By similarity). {ECO:0000250}. | Ailuropoda melanoleuca (Giant panda) |
D2HKB0 | UBIA1_AILME | MAASQVPGEINIQAGETAKSGDRDLLGNDCRDQDRLPQRSWRQKCASYVLALRPWSFSASLTPVALGSALAYRSQGVLDPRLLVGCAVAVLAVHGAGNLVNTYYDFSKGIDHKKSDDRTLVDRILEPQDVVLFGVFLYTLGCVCAACLYCLSPLKLEHLALIYFGGLSGSFLYTGGIGFKYVALGDLVILITFGPLAVMFAYAVQVGSLAVFPLVYAIPLALSTEAVLHSNNTRDMESDREAGIVTLAILIGPTLSYVLYNTLLFLPYLIFSILATHCSISLALPLLTVPMAFSLERQFRSQTFNKLPQRTAKLNLLLGLFYVFGIILAPAGSLPKL | 2.5.1.-; 2.5.1.39 | null | circulatory system development [GO:0072359]; endothelial cell development [GO:0001885]; menaquinone biosynthetic process [GO:0009234]; phylloquinone biosynthetic process [GO:0042372]; ubiquinone biosynthetic process [GO:0006744]; ubiquinone biosynthetic process via 3,4-dihydroxy-5-polyprenylbenzoate [GO:0032194]; vitamin K biosynthetic process [GO:0042371] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | 4-hydroxybenzoate decaprenyltransferase activity [GO:0002083]; antioxidant activity [GO:0016209]; prenyltransferase activity [GO:0004659] | PF01040; | 1.10.357.140; | UbiA prenyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Y5Z9}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Y5Z9}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9Y5Z9}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + menadiol = diphosphate + menaquinol-4; Xref=Rhea:RHEA:74083, ChEBI:CHEBI:6746, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:193091; Evidence={ECO:0000250|UniProtKB:Q9Y5Z9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74084; Evidence={ECO:0000250|UniProtKB:Q9Y5Z9}; CATALYTIC ACTIVITY: Reaction=4-hydroxybenzoate + all-trans-decaprenyl diphosphate = 4-hydroxy-3-all-trans-decaprenylbenzoate + diphosphate; Xref=Rhea:RHEA:44564, ChEBI:CHEBI:17879, ChEBI:CHEBI:33019, ChEBI:CHEBI:60721, ChEBI:CHEBI:84503; EC=2.5.1.39; Evidence={ECO:0000250|UniProtKB:Q9Y5Z9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44565; Evidence={ECO:0000250|UniProtKB:Q9Y5Z9}; | null | PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. {ECO:0000250|UniProtKB:Q9Y5Z9}.; PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. {ECO:0000250|UniProtKB:Q9Y5Z9}. | null | null | FUNCTION: Prenyltransferase that mediates the formation of menaquinone-4 (MK-4) and coenzyme Q10. MK-4 is a vitamin K2 isoform required for endothelial cell development. Mediates the conversion of phylloquinone (PK) into MK-4, probably by cleaving the side chain of phylloquinone (PK) to release 2-methyl-1,4-naphthoquinone (menadione; K3) and then prenylating it with geranylgeranyl pyrophosphate (GGPP) to form MK-4. Also plays a role in cardiovascular development independently of MK-4 biosynthesis, by acting as a coenzyme Q10 biosynthetic enzyme: coenzyme Q10, also named ubiquinone, plays an important antioxidant role in the cardiovascular system. Mediates biosynthesis of coenzyme Q10 in the Golgi membrane, leading to protect cardiovascular tissues from NOS3/eNOS-dependent oxidative stress. {ECO:0000250|UniProtKB:Q9Y5Z9}. | Ailuropoda melanoleuca (Giant panda) |
D2HNY3 | FAN1_AILME | MSEGKSPAKKRARRSLSISKTKKNECNSIISFFNNVPPAKLACPICSKMVPRYDLNWHLDEKCANNDNITPVDLRHVGFTDSSGSTVNLTNTVLENVTPGKLSPSKASLTPDPSDSAKMGIKQQTSPYFKNNKDLVFKNQDKLRHHNVKVITLGSLSSKLSRRYTEARRSICKKNEEFASKSPQSPSSTVVRSPVDNCSEIEDKDQILENSSQKENVFTCDSLNEQRTEHSVEDTKVLEAESQEATQECGRSPLTPAFSDNAFVLFSPDLTRGNPLRSTSEDSLEWETITGIDGKDVEKCEAGSCEEVKVTVASEAKTQLSDWEAKCHSSTPDDSKGCNIQDLLLEGDSDLKNEITCRIPLEQGSSCDVPDKTVTVPPSHPYYLRSFLVVLKAVFENEEDRMLFDEHEKEIVTKFYQLSASAQKLYVRLFQRKFSWLKMNKLEYEEIAPDLTPVIGELQQAGFLQTESELQELSEVLELLSAPELKTLAKTFHLVNPNGQKQQLVDTFLKLAKQPSVCTWGKNQPGIGAVILKRAKGLAGQALRVCKGPRAVFSRVLLLFSLTDSLEDEEAACGGQGQLSTVLLVNLGRMEFPRYTINRKTQIFQDRDDLIRYAAAAHMLSDISTAMANGNWKEANELSQCAKSDWNKLKSHPSLRYHENLPLFLRCFTVGWIYTRILSRTVEILQRLHMYEEAVKELESLLSQRVYCPDSRGRWWDRLALNLHQHLKRLEPAIKCITEGLADPEVRTGHRLSLYQRALRLRESPSCQKYRHLFHQLPEVTVGDVKHVTITGRLCPQRGMGKSVFVMEAGGPTAPATVLCSVEEVALAYYRRSGFDQGIHGEGSTFSTLYGLLLWDIIFMDGIPDVFRNAYQASPLDLCTDSFFASRGPAIEARLQRIHSAPAESLRAWVAAAWQAQEGRVASIVSWDRFASLQQAQDLVSCLGGPVLSGVCRRLAADFRHCRGGLPDLVVWNSQSRHFKLVEVKGPNDRLSHKQMLWLDELQKLGADVEVCHVVAVGAKSKSLT | 3.1.21.-; 3.1.4.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9Y2M0}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9Y2M0}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250|UniProtKB:Q9I2N0, ECO:0000250|UniProtKB:Q9Y2M0}; | DNA repair [GO:0006281]; double-strand break repair via homologous recombination [GO:0000724]; interstrand cross-link repair [GO:0036297]; nucleotide-excision repair [GO:0006289] | nucleus [GO:0005634] | 5'-3' exonuclease activity [GO:0008409]; 5'-flap endonuclease activity [GO:0017108]; flap-structured DNA binding [GO:0070336]; metal ion binding [GO:0046872]; phosphodiesterase I activity [GO:0004528]; ubiquitin-dependent protein binding [GO:0140036] | PF21315;PF21169;PF21170;PF08774; | 3.40.1350.10; | FAN1 family | PTM: Ubiquitinated and degraded during mitotic exit by the APC/C-Cdh1 complex. {ECO:0000250|UniProtKB:Q9Y2M0}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y2M0}. Note=Localizes at sites of DNA damage following recruitment by monoubiquitinated FANCD2. Localizes to stalled replication forks via its UBZ4-type zinc finger. {ECO:0000250|UniProtKB:Q9Y2M0}. | CATALYTIC ACTIVITY: Reaction=Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.; EC=3.1.4.1; Evidence={ECO:0000250|UniProtKB:Q9Y2M0}; | null | null | null | null | FUNCTION: Nuclease required for the repair of DNA interstrand cross-links (ICL) recruited at sites of DNA damage by monoubiquitinated FANCD2. Specifically involved in repair of ICL-induced DNA breaks by being required for efficient homologous recombination, probably in the resolution of homologous recombination intermediates. Not involved in DNA double-strand breaks resection. Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions. Probably keeps excising with 3'-flap annealing until it reaches and unhooks the ICL. Acts at sites that have a 5'-terminal phosphate anchor at a nick or a 1- or 2-nucleotide flap and is augmented by a 3' flap. Also has endonuclease activity toward 5'-flaps. {ECO:0000250|UniProtKB:Q9Y2M0}. | Ailuropoda melanoleuca (Giant panda) |
D2HS90 | STPAP_AILME | MAAVDLDVQSLPRGGFRCCLCHVTTANRPSLDAHLGGRKHRHLVELRATRKAQGLRSVFVSGFPRDVDSAQLTQYFQAFGPVASVVMDKDKGVFAIVEMGDVGTREAVLSQPQHTLGGHRLRVRPREQKEFQSPASKSPKGAAPDSHQLTKALAEAPDVGAQMVKLVGLRELSEAERQLRNLVVALMQEVFTEFFPGCVVHPFGSSINSFDVHGCDLDLFLDLGDLEESQPAPKAPESPSLDSALASPLDPQALACTPASPPDSQPPSPQDSEALDFETPSSSLAPQTPDSALASETLASPQSLPPASPLQEDRGEGDLGKALELAEALSGEKTEGVAMLELVGSILRGCVPGVYRVQTVPSARRPVVKFCHRPSGLHGDVSLSNRLALHNSRFLSLCSELDGRVRPLVYTLRCWAQGRGLSGSGPLLSNYALTLLVIYFLQTRDPPVLPTVSQLTQKAGEGEQVEVDGWDCSFPRDASGLEPSTNKEPLSSLLAQFFSCVSCWDLRGSLLSLREGQALPVAGDLPSNRWEGLRLGPMNLQDPFDLSHNVAANVTSRVAGRLQNSCQAAANYCRSLQYQRRSSRGRDWGLLPLLQPSSPSSLLSATPIPLPPAPFTQLTAALAQVLREALGCHIEQGTKRLRSDRGGPEESPQGGTSKRLKLDGEEKSCEEGREEQQGYIRDHSEDGVEEMVVEVGEMVQDWVQSPGRPGEPPQMLREQLATGEEGQSGHAALAEQGPKGPEAAREGSQGETGRGVSLSSVSWRCALWHRVWQGRRRARRRLQQQTKERGRGSAGTAEWLAVEAQVTRELRGLSSAAQRPEAEPLLTFVASASQVNQTLTVTPIQDSQGLFPDLHHFLQVFLPQALRNL | 2.7.7.19; 2.7.7.52 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9H6E5}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9NVV4}; Note=Binds 1 divalent cation per subunit. {ECO:0000250|UniProtKB:Q9H6E5}; | co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway [GO:0180010]; mRNA polyadenylation [GO:0006378]; snRNA processing [GO:0016180]; U6 snRNA 3'-end processing [GO:0034477] | mitochondrion [GO:0005739]; mRNA cleavage and polyadenylation specificity factor complex [GO:0005847]; nuclear speck [GO:0016607]; nucleolus [GO:0005730] | ATP binding [GO:0005524]; enzyme-substrate adaptor activity [GO:0140767]; metal ion binding [GO:0046872]; mRNA 3'-UTR binding [GO:0003730]; poly(A) RNA polymerase activity [GO:1990817]; RNA binding [GO:0003723]; RNA uridylyltransferase activity [GO:0050265]; U6 snRNA binding [GO:0017070] | PF03828;PF00076;PF12874; | 1.10.1410.10;3.30.70.330;3.30.460.10; | DNA polymerase type-B-like family | PTM: Phosphorylated by CK1 in the proline-rich (Pro-rich) region. {ECO:0000250|UniProtKB:Q9H6E5}. | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H6E5}. Nucleus speckle {ECO:0000250|UniProtKB:Q9H6E5}. | CATALYTIC ACTIVITY: Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide; Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395, ChEBI:CHEBI:173116; EC=2.7.7.52; Evidence={ECO:0000250|UniProtKB:Q9H6E5}; CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000250|UniProtKB:Q9H6E5}; | null | null | null | null | FUNCTION: Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation. {ECO:0000250|UniProtKB:Q9H6E5}. | Ailuropoda melanoleuca (Giant panda) |
D2HWM5 | RFWD3_AILME | MAQEAMEYNVDEQLEHRVAEQPVPAEVVSTQGGPPPLQPLPTEVVSSQGAPPLLQPAPAEGTSSQVGPHLLQPAAQLSVDLTEEVELLGEDRVENINPGASEEHRQPSRVNRPIPVSSLDSMNSFISGLQRLHGMLEFLRPPSDHNVGPVRSRRRRGSASRRSRTVGSQRTDSARSRAPLDAYFQVSRTQPHLPSMSQDSETRNPVSEDLQVSSSSSSDSESSAEYEEVVVQAEDTRAVVSEEQGGTAAEQEVTCVGGGETLPKQSPQKTNPLLPSVSKDDEEGDTCTICFEHWTNAGDHRLSALRCGHLFGYKCISKWLKGQARKCPQCNKKAKHSDIVVLYARTLRALDTSEHERMKSSLLKEQMLRKQAELESAQCRLQLQVLTDECSKLHSRVQDLQKLTVQHRDQISQSPSGSQARSLNCLPSSQNQRKYHFQKTFTVSPTGNCRIMTYCDALSCLVVSQPSPQASFLPGFGVKMLSTANMKSSQYVPMHGKQIRGLAFSSRSKGLLLSASLDSTVKLTSLETNTVVQTYNAGRPVWSCCWCLDESNHIYAGLVNGSILVYDLRNTSSHIQELVPQKARCPLVSLSYIPRAASAAFPYGGVLAGTLENASFWELKMGFSHWPHVLPMEPGGCVDFQTESSTRHCLVTYRPDKNHNTLRSVLMEMSYKLNDAGEPVCSCRPVQTFLGGPTCKLLTKSAIFQNPENDGSILVCTGDEASNSALLWDAGSGSLLQELQADQPVLDICPFEANHSSCLATLTEKMVHIYRWE | 2.3.2.27 | null | DNA damage response [GO:0006974]; double-strand break repair via homologous recombination [GO:0000724]; interstrand cross-link repair [GO:0036297]; mitotic G1 DNA damage checkpoint signaling [GO:0031571]; protein ubiquitination [GO:0016567]; regulation of DNA damage checkpoint [GO:2000001]; replication fork processing [GO:0031297]; response to ionizing radiation [GO:0010212] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; PML body [GO:0016605]; site of DNA damage [GO:0090734]; site of double-strand break [GO:0035861] | MDM2/MDM4 family protein binding [GO:0097371]; metal ion binding [GO:0046872]; p53 binding [GO:0002039]; ubiquitin protein ligase activity [GO:0061630] | PF13639; | 2.130.10.10;3.30.40.10; | null | PTM: Phosphorylated at Ser-46 and Ser-63 upon DNA damage by ATM or ATR. ATM phosphorylation occurs at early times upon DNA damage, while ATR is the major kinase at later times. Phosphorylation by ATM and ATR is required to stabilize p53/TP53. Part of the phosphorylation depends upon RPA2 presence. {ECO:0000250|UniProtKB:Q6PCD5}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6PCD5}. Nucleus, PML body {ECO:0000250|UniProtKB:Q6PCD5}. Cytoplasm {ECO:0000250|UniProtKB:Q6PCD5}. Note=In undamaged cells, found both in the cytoplasm and in the nucleus, partially associated with PML nuclear bodies. In response to replication block, such as that caused by hydroxyurea treatment, or to DNA damage caused by ionizing radiations or doxorubicin, recruited to the nucleus, to stalled replication forks or to sites of DNA repair. This recruitment depends upon RPA2. {ECO:0000250|UniProtKB:Q6PCD5}. | 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; Evidence={ECO:0000250|UniProtKB:Q6PCD5}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q6PCD5}. | null | null | FUNCTION: E3 ubiquitin-protein ligase required for the repair of DNA interstrand cross-links (ICL) in response to DNA damage. Plays a key role in RPA-mediated DNA damage signaling and repair. Acts by mediating ubiquitination of the RPA complex (RPA1, RPA2 and RPA3 subunits) and RAD51 at stalled replication forks, leading to remove them from DNA damage sites and promote homologous recombination. Also mediates the ubiquitination of p53/TP53 in the late response to DNA damage, and acts as a positive regulator of p53/TP53 stability, thereby regulating the G1/S DNA damage checkpoint. May act by catalyzing the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome. In response to ionizing radiation, interacts with MDM2 and enhances p53/TP53 ubiquitination, possibly by restricting MDM2 from extending polyubiquitin chains on ubiquitinated p53/TP53. Required to translesion DNA synthesis across DNA-protein cross-link adducts by catalyzing ubiquitination of proteins on single-stranded DNA (ssDNA). {ECO:0000250|UniProtKB:Q6PCD5}. | Ailuropoda melanoleuca (Giant panda) |
D2HXI8 | GWL_AILME | MEPTAGSEKESEGDTVTGECVNRIPVPRPPSIEEFTIVKPISRGAFGKVYLGQKGGKLYAVKVVKKADMINKNMTHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRDINMMDILTTPSMAKPRQDYSRTPGQVLSLISSLGFFTPVAEKNKDSANILSTHVSETSQLSQGLVCPMSVDHRDTTPYSSKLLNSCLETVAPNPGMPVKCLTSHLLQSRRRLATSSASSQSHTFVSSVESECHSSPRWEKDCQESDHALGYTVMSWNIIEKPSCTDSRDAIETKGFNKKDLELALSPIHNSSTIPETGRSCVNLAKKGFPGEVSWEARELDINNIHVATDTAQSGFHQSDQWAVDSGDATEEHLGKRGFKRNFELVDSSPCQNIIQHKKNCIEHKPRNAMSDGYINQRTGLTTEVQDLKLSVCGGQQSDCANKENMVNSFIDKPQTPEKSPVPMIAKNLLCELDEDCDKNNKRDLLSSSLLCSDDERASKSICMDSDSSFPGISVMESSLERQSLDPDKSIKESSFEESNIEDLLTVSPRWQENILPKGDENPAVQDSSQKMLAPSSKVLKTLTLSKRNAVAFRSFNSHINASNNSEPSKMSLTSLDGMDISCVYSGSYPMAITPNQKGTSYIPYQQTPNQVKSGTPYRTPKSVRRGAAPVDDGRILGTPDYLAPELLLGRAHGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILKRDIPWPEGEEKLSDNSQNAVEILLTIDNAKRAGMKELKRHHLFSDVDWENLQHQTMPFIPQPDDETDTSYFEARNNAQHLTISGFSL | 2.7.11.1 | null | cell division [GO:0051301]; DNA damage response [GO:0006974]; female meiosis II [GO:0007147]; G2/M transition of mitotic cell cycle [GO:0000086]; intracellular signal transduction [GO:0035556]; mitotic cell cycle [GO:0000278]; negative regulation of phosphoprotein phosphatase activity [GO:0032515]; phosphorylation [GO:0016310] | centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein phosphatase 2A binding [GO:0051721]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family | PTM: Phosphorylation at Thr-744 by CDK1 during M phase activates its kinase activity. Maximum phosphorylation occurs in prometaphase (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus. Note=During interphase is mainly nuclear, upon nuclear envelope breakdown localizes at the cytoplasm and during mitosis at the centrosomes. {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=2.7.11.1; 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; | null | null | null | null | FUNCTION: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser-62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited (By similarity). {ECO:0000250}. | Ailuropoda melanoleuca (Giant panda) |
D2IYS2 | TORSO_BOMMO | MYSEGKLLKVFLIFAGFIIFSLCGEVVSQRYPPAPGLLKYLEQDVCYSLYYYLNWTSLADCKTNFEETGISDVPSTVKVRCQSKNSIRFETEPSEHWQLFILMEHDNFDPIPFTLIEPNNVFGELITTANKEYQIWSTYLDEYGTLQDWMEGPIVLKFDQRNQQPDDIKYNVTQEFKYIILGNDSYTINGKFVWNTTGDRDLCFDIANICQNTNMKHAKIWPTAHPSFDVENLVLNDECEIHVKGIHGTTKHKYKTPSCFELPECFLNNMEPEIPQDVAIAADQDLRGWWNINVAWAKPHFQPEIYNVTVRANMIRSIILPGNATETTFRNIPNTFLSAGKIYNVSVYAIIGQKASHTSRRAFTPGMLRWVWAGATAGAGCAAGGLLAATLLCCGHRRATSRVSQEDPDEKTPKEDDVEIIGIESGSADDHWEVRSDRVLLHEVIGEGAFGVVRRGTLAPGGKSVAVKMLKEFPSQEEVRSFRSEMELMKSVGAHPHVVSLVGCCSGRKPLIVAEYCSRGDLLSYLRSSWDIIVSKHTAKYYNNNMDSMDTSKLKVHKEHTKLVVNKLYELQGPCETELTPLDLLSFCRQIAMGMEFLASNRIVHRDLAARNVLVTEDKTLKIADFGLSRDIYEENQYKQKGNGKMPVKWMALESLTRRVYTTQSDVWSFGVVIWEIVTVGGSPYPEVPAARLVRSLRSGYRMPKPVNCSKPLYDIMRACWNASPRDRPTFPELHQKLDDLLHSACANEYITLEVDVDEAPSTPKPQRYIKMLIRGKLPWSRESYERPVNPTSNLYSSPPVIQTKTA | 2.7.10.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; | phosphorylation [GO:0016310]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF07714;PF21468; | 1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family | PTM: May be auto-phosphorylated on tyrosine residues. {ECO:0000269|PubMed:26928300}.; PTM: At least one of the 3 cysteine residues Cys-381, Cys-393 or Cys-394 is involved in the formation of interchain disulfide bonds. The disulfide bond sites in the extracellular region are not involved in homodimer formation. {ECO:0000269|PubMed:26698662}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:19965758}; Single-pass type I membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:26928300}; | null | null | null | null | FUNCTION: Probable receptor tyrosine kinase. During postembryonic development, involved in the initiation of metamorphosis probably by inducing the production of ecdysone in response to prothoracicotropic hormone (PTTH) (By similarity). Binding to PTTH stimulates activation of canonical MAPK signaling leading to ERK phosphorylation (PubMed:19965758, PubMed:26928300). {ECO:0000250|UniProtKB:P18475, ECO:0000269|PubMed:19965758, ECO:0000269|PubMed:26928300}. | Bombyx mori (Silk moth) |
D2J0Y4 | CJ090_MOUSE | MISPVVISRLIDEKKSMENGAILPQAIAQPQLCPTKPALARRDGVSMHRRFALSPDRLGILTPSDDQGLETEPLSTGDNLGKGSHSGFSSITITARRVGPPASSLVWDTFRDPLCPKCKAKDALFQEPPVLAGDAHLCQHNRPFTCTESPSNGSVEGMKVFQAHSRLSARQDYWVTHTNDNEDSFSSDNSPSRKVPLVFSSCVHFRVSQQCPNAIYYLDKSLSVPLERPQIASPKMHRSVLSLSLRCSSHQLTADGVDSSANGEPISTALSQELSEGKQDLLGPQWGQPQGGHWKESPALVPVHLGSGTCPRTGSPPLENVKFADVGRNQVPVRKEKEDHATCTSSSHTNQLSIHIPGWSYRAETKVLSGSKKQQQEAQRTLPAFPVGQKTIKHFPPEGDSSPSSDGQPSILSESNERQHPYFMIPRVPLPGFYCPLQTGCASLQEDGAVQIETHFPKDYTCCDLVVKLKECEKNEDPTVTPEPSPATPSPSTPEGAQSSDPSEDSYEPLLASSMTLQEALEVHRPQFISRSQERLQKLKRMVQQRKTQQKESLGQKQSLLPVRANKKQFTIPHPLSDNLFKPKERCISEKEMHMRSKRIYNNLPEVKKKKEEQKKRMILQSNRLRAEVFKKQLLDQLLQRNAV | 2.3.2.- | null | DNA damage response [GO:0006974]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; negative regulation of cell growth [GO:0030308]; protein polyubiquitination [GO:0000209]; protein stabilization [GO:0050821]; protein ubiquitination [GO:0016567]; regulation of centriole replication [GO:0046599]; response to ionizing radiation [GO:0010212]; response to UV [GO:0009411] | centriole [GO:0005814]; centrosome [GO:0005813]; cytosol [GO:0005829] | histone deacetylase binding [GO:0042826]; microtubule binding [GO:0008017]; ubiquitin protein ligase activity [GO:0061630] | PF15309;PF17730; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96M02}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96M02}. Note=Localizes to the actin cytoskeleton in a proportion of cells. Colocalizes with centriolar acetylated tubulin (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q96M02}. | null | null | null | null | null | FUNCTION: Tumor suppressor that is required to sustain G2/M checkpoint after DNA damage (PubMed:20154723, PubMed:20843368, PubMed:24240685). Acts as a p53/TP53 activator by inhibiting MDM2 binding to p53/TP53 and stimulating non-proteolytic polyubiquitination of p53/TP53. Exhibits ubiquitin ligase (E3) activity and assemble ubiquitin polymers through 'Lys-11'- (K11-), 'Lys-29'- (K29-) and 'Lys-63'- (K63)-linkages, independently of the ubiquitin-conjugating enzyme (E2). Promotes p53/TP53-dependent transcription of CDKN1A/p21, leading to robust checkpoint response (PubMed:24240685). Mediates CDKN1A/p21 protein stability in a ubiquitin-independent manner. Interacts with HDAC1 and prevents binding of HDAC1 to CDKN1A/p21 and facilitates the acetylation and stabilization of CDKN1A/p21 (PubMed:20154723). May have a role in the assembly of primary cilia (By similarity). {ECO:0000250|UniProtKB:Q96M02, ECO:0000269|PubMed:20154723, ECO:0000269|PubMed:20843368, ECO:0000269|PubMed:24240685}. | Mus musculus (Mouse) |
D2KC46 | PKHA8_CANLF | MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTRMDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSELRLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSELLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELNSCENGSLHMEINDGEEILMKNKSSLYLKPEIDCSISSEENTDDNITVQGEIMKEEGEDNLGNHDSSLAQPASDSSSSPPESHWEEGQEIIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCYAVVPVLDKLGPTVFAPVKMDLVGNIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLKGFLTEVKNGEKDIQTALNNAYGKTLRQHHGWVVRGVFALALRAAPSYEDFVAALTIKEGDHQKAAFSVGMQRDLSLYLPAMEKQLAILDTLYEVHGLESDEVV | null | null | ceramide transport [GO:0035627]; ER to Golgi ceramide transport [GO:0035621]; intermembrane lipid transfer [GO:0120009]; lipid transport [GO:0006869]; protein transport [GO:0015031] | cytosol [GO:0005829]; membrane [GO:0016020]; trans-Golgi network [GO:0005802] | ceramide 1-phosphate binding [GO:1902387]; ceramide 1-phosphate transfer activity [GO:1902388]; ceramide binding [GO:0097001]; glycolipid binding [GO:0051861]; glycolipid transfer activity [GO:0017089]; identical protein binding [GO:0042802]; phosphatidylinositol-4-phosphate binding [GO:0070273] | PF08718;PF00169; | 1.10.3520.10;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q96JA3}. Membrane {ECO:0000250|UniProtKB:Q96JA3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96JA3}. Note=Binds through its PH domain to PtdIns(4)P and ARF1, and subsequently localizes to TGN exit sites. {ECO:0000250|UniProtKB:Q96JA3}. | null | null | null | null | null | FUNCTION: Cargo transport protein that is required for apical transport from the trans-Golgi network (TGN). Transports AQP2 from the trans-Golgi network (TGN) to sites of AQP2 phosphorylation. Mediates the non-vesicular transport of glucosylceramide (GlcCer) from the trans-Golgi network (TGN) to the plasma membrane and plays a pivotal role in the synthesis of complex glycosphingolipids. Binding of both phosphatidylinositol 4-phosphate (PIP) and ARF1 are essential for the GlcCer transfer ability. Also required for primary cilium formation, possibly by being involved in the transport of raft lipids to the apical membrane, and for membrane tubulation. {ECO:0000269|PubMed:16103222, ECO:0000269|PubMed:19794145, ECO:0000269|PubMed:19940249}. | Canis lupus familiaris (Dog) (Canis familiaris) |
D2KX21 | PLAT1_RAT | MAVNDCFSLTYPHNPHPGDLIEVFRPCYQHWALYLGDGYVINIAPVDGIPSSFSSAKSVFSTKALVKMQLLKDVVGNDTYRINNKYDTTYPPLPVEEVIQRSEFAIGQEVTYDLLVNNCEHFVTLLRYGEGVSEQANRAIGTIGLVAAGIDIFTFLGLFPKRQGAKS | 2.3.1.-; 3.1.1.32; 3.1.1.4 | null | ether lipid metabolic process [GO:0046485]; lens fiber cell differentiation [GO:0070306]; lipid catabolic process [GO:0016042]; N-acylphosphatidylethanolamine metabolic process [GO:0070292]; organelle disassembly [GO:1903008]; peroxisome organization [GO:0007031]; phosphatidylcholine metabolic process [GO:0046470] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; lysosome [GO:0005764]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nuclear envelope lumen [GO:0005641]; nucleus [GO:0005634]; peroxisome [GO:0005777] | 1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; N-acyltransferase activity [GO:0016410]; O-acyltransferase activity [GO:0008374]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970]; phospholipase A2 activity [GO:0004623]; phospholipase activity [GO:0004620] | PF04970; | 3.90.1720.10; | H-rev107 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9QZU4}. Nucleus {ECO:0000250|UniProtKB:Q9QZU4}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:Q9QZU4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000250|UniProtKB:Q9QZU4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 2-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:40487, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40488; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41348, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73009, ChEBI:CHEBI:76091; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41349; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine = H(+) + hexadecanoyl-sn-glycero-3-phosphocholine + N-hexadecanoyl-1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:41360, ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999, ChEBI:CHEBI:74986, ChEBI:CHEBI:78097; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41361; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + a 2-acyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-2-acyl-sn-glycero-3-phosphocholine + 2-hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41364, ChEBI:CHEBI:57875, ChEBI:CHEBI:72999, ChEBI:CHEBI:76078, ChEBI:CHEBI:77369; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41365; Evidence={ECO:0000250|UniProtKB:Q9HDD0}; | null | null | null | null | FUNCTION: Exhibits both phospholipase A1/2 and acyltransferase activities (By similarity). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (By similarity). Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (By similarity). {ECO:0000250|UniProtKB:Q9HDD0, ECO:0000250|UniProtKB:Q9QZU4}. | Rattus norvegicus (Rat) |
D2W6T1 | TET1_NAEGR | MTTFKQQTIKEKETKRKYCIKGTTANLTQTHPNGPVCVNRGEEVANTTTLLDSGGGINKKSLLQNLLSKCKTTFQQSFTNANITLKDEKWLKNVRTAYFVCDHDGSVELAYLPNVLPKELVEEFTEKFESIQTGRKKDTGYSGILDNSMPFNYVTADLSQELGQYLSEIVNPQINYYISKLLTCVSSRTINYLVSLNDSYYALNNCLYPSTAFNSLKPSNDGHRIRKPHKDNLDITPSSLFYFGNFQNTEGYLELTDKNCKVFVQPGDVLFFKGNEYKHVVANITSGWRIGLVYFAHKGSKTKPYYEDTQKNSLKIHKETK | 1.14.11.80 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:24390346, ECO:0000269|PubMed:26323320}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:24390346, ECO:0000269|PubMed:26323320}; | null | null | 5-methylcytosine dioxygenase activity [GO:0070579]; double-stranded methylated DNA binding [GO:0010385]; iron ion binding [GO:0005506] | null | 3.60.130.30; | null | null | null | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-methyl-2'-deoxycytidine in DNA + O2 = a 5-hydroxymethyl-2'-deoxycytidine in DNA + CO2 + succinate; Xref=Rhea:RHEA:52636, Rhea:RHEA-COMP:11370, Rhea:RHEA-COMP:13315, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:85454, ChEBI:CHEBI:136731; EC=1.14.11.80; Evidence={ECO:0000269|PubMed:24390346, ECO:0000269|PubMed:26323320}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-hydroxymethyl-2'-deoxycytidine in DNA + O2 = a 5-formyl-2'-deoxycytidine in DNA + CO2 + H2O + succinate; Xref=Rhea:RHEA:53828, Rhea:RHEA-COMP:13315, Rhea:RHEA-COMP:13656, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:136731, ChEBI:CHEBI:137731; EC=1.14.11.80; Evidence={ECO:0000269|PubMed:24390346, ECO:0000269|PubMed:26323320}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + a 5-formyl-2'-deoxycytidine in DNA + O2 = a 5-carboxyl-2'-deoxycytidine in DNA + CO2 + H(+) + succinate; Xref=Rhea:RHEA:53832, Rhea:RHEA-COMP:13656, Rhea:RHEA-COMP:13657, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:137731, ChEBI:CHEBI:137732; EC=1.14.11.80; Evidence={ECO:0000269|PubMed:24390346, ECO:0000269|PubMed:26323320}; | null | null | null | null | FUNCTION: Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), and thereby plays a role in active DNA demethylation. Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). {ECO:0000269|PubMed:24390346, ECO:0000269|PubMed:26323320}. | Naegleria gruberi (Amoeba) |
D2WL32 | GLGB3_ARATH | MVSLSNQTRFSFHPNNLVVSEKRRLGISGVNFPRKIKLKITCFAAERPRQEKQKKKSQSQSTSDAEAGVDPVGFLTRLGIADRIFAQFLRERHKALKDLKDEIFKRHFDFRDFASGFELLGMHRHMEHRVDFMDWGPGSRYGAIIGDFNGWSPTENAAREGLFGHDDYGYWFIILEDKLREGEEPDELYFQQYNYVDDYDKGDSGVSAEEIFQKANDEYWEPGEDRFIKNRFEVPAKLYEQMFGPNSPQTLEELGDIPDAETRYKQWKEEHKDDPPSNLPPCDIIDKGQGKPYDIFNVVTSPEWTKKFYEKEPPIPYWLETRKGRKAWLQKYIPAVPHGSKYRLYFNTPDGPLERVPAWATYVQPEDEGKQAYAIHWEPSPEAAYKWKYSKPKVPESLRIYECHVGISGSEPKVSTFEEFTKKVLPHVKRAGYNAIQLIGVPEHKDYFTVGYRVTNFFAASSRYGTPDDFKRLVDEAHGLGLLVFLDIVHSYAAADQMVGLSLFDGSNDCYFHYGKRGHHKHWGTRMFKYGDLDVLHFLISNLNWWITEYQVDGYQFHSLASMIYTHNGFASFNNDLDDYCNQYVDRDALMYLILANEILHVQHPNIITIAEDATYYPGLCEPVSQGGLGFDYYVNLSASEMWVSLLDNVPDNEWSMSKIVSTLVANKEYADKMLSYAENHNQSISGGRSFAEILFGGVDNGSPGGKELLDRGISLHKMIRLITFTSGGRAYLNFMGNEFGHPERVEFPTQSNNFSFSLANRRWDLLESGVHHHLFSFDKELMDLDKSKGILSRGLPSIHHVNDANMVISFSRGPFLFIFNFHPSNSYEKYDVGVEEAGEYTMILNSDEVKYGGQGIVTEDHYLQRSISKRIDGQRNCLEVFLPSRTAQVYKLTRILRI | 2.4.1.18 | null | carbohydrate metabolic process [GO:0005975]; glycogen biosynthetic process [GO:0005978]; post-embryonic development [GO:0009791]; starch biosynthetic process [GO:0019252] | amyloplast [GO:0009501]; chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; plastid [GO:0009536] | 1,4-alpha-glucan branching enzyme activity [GO:0003844]; 1,4-alpha-glucan branching enzyme activity (using a glucosylated glycogenin as primer for glycogen synthesis) [GO:0102752]; cation binding [GO:0043169] | PF00128;PF02806; | 3.20.20.80;2.60.40.1180;2.60.40.10; | Glycosyl hydrolase 13 family, GlgB subfamily | null | SUBCELLULAR LOCATION: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:20377688}. Plastid, amyloplast {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.; EC=2.4.1.18; | null | PATHWAY: Glycan biosynthesis; starch biosynthesis. | null | null | FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages in starch by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. Essential during embryogenesis. {ECO:0000269|PubMed:17028209, ECO:0000269|PubMed:20377688}. | Arabidopsis thaliana (Mouse-ear cress) |
D2X8K2 | PA2_CONGI | GVWQFAYMIAKYTGRNPLDYWGYGCWCGLGGKGNPVDAVDRCCYVHDVCYNSITQGPRPTCSRIAPYHKNYYFTGKKCSTGWLTSKCGRAICACDIAAVKCFRRNHFNKKYRLYKKNIC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:20562011}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:20562011}; | arachidonic acid secretion [GO:0050482]; envenomation resulting in induction of edema in another organism [GO:0044398]; envenomation resulting in myocyte killing in another organism [GO:0044522]; hemostasis [GO:0007599]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; suppression of blood coagulation in another organism [GO:0035899] | extracellular region [GO:0005576]; nematocyst [GO:0042151] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0000255|PROSITE-ProRule:PRU10036, ECO:0000269|PubMed:20562011}; | null | null | null | null | FUNCTION: Sea anemone phospholipase A2 (PLA2). When incubated with plasma, this protein shows a moderate anticoagulant activity (0.15 ug of enzyme/200 uL of plasma), inhibiting clotting induced by thrombin. This enzyme also induces myotoxicity, and edema. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. {ECO:0000269|PubMed:20562011}. | Condylactis gigantea (Giant Caribbean anemone) (Condylactis passiflora) |
D2XV59 | GTPB1_RAT | MAAERSRSPVDSPVPASMFAPEPSSPGAARAAAAAARLHGGFDSDCSEDGEALNGEPELDLTSKLVLVSPTSEQYDSLLRQMWERMDEGCGETIYVIGQGSDGTEYGLSEADMEASYATVKSMAEQIEADVILLRERQESGGRVRDYLVRKRVGDNDFLEVRVAVVGNVDAGKSTLLGVLTHGELDNGRGFARQKLFRHKHEIESGRTSSVGNDILGFDSEGNVVNKPDSHGGSLEWTKICEKSSKVITFIDLAGHEKYLKTTVFGMTGHLPDFCMLMVGSNAGIVGMTKEHLGLALALNVPVFVVVTKIDMCPANILQETLKLLQRLLKSPGCRKIPVLVQSKDDVIVTASNFSSERMCPIFQISNVTGENLDLLKMFLNLLSPRTSYREEEPAEFQIDDTYSVPGVGTVVSGTTLRGLIKLNDTLLLGPDPLGNFLSIAVKSIHRKRMPVKEVRGGQTASFALKKIKRSSIRKGMVMVSPRLNPQASWEFEAEILVLHHPTTISPRYQAMVHCGSIRQTATILSMDKDCLRTGDKATVHFRFIKTPEYLHIDQRLVFREGRTKAVGTITKLLQTTNNSPMNSKPQQIKMQSTKKGPLSKREEGGPSGVPAAGPPSTGDEASSLGTTQAATSSGLQPQPKPSSGGRRRGGQRHKVKSQGACVTPASGC | null | null | cytoplasmic translation [GO:0002181]; GTP metabolic process [GO:0046039]; positive regulation of mRNA catabolic process [GO:0061014]; translational elongation [GO:0006414] | cytoplasmic exosome (RNase complex) [GO:0000177]; cytosol [GO:0005829] | alpha-aminoacyl-tRNA binding [GO:1904678]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; translation elongation factor activity [GO:0003746]; tRNA binding [GO:0000049] | PF00009;PF03144; | 3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, GTPBP1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21515746}. | null | null | null | null | null | FUNCTION: Promotes degradation of target mRNA species. Plays a role in the regulation of circadian mRNA stability. Binds GTP and has GTPase activity. {ECO:0000269|PubMed:21515746}. | Rattus norvegicus (Rat) |
D2Y1X6 | H1A01_CYRHA | MKASMFLALAGLVLLFVVCYASESEEKEFPRELISKIFAVDDFKGEERECKGFGKSCVPGKNECCSGYACNSRDKWCKVLLGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 14 (Hntx-1) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14675784}. | null | null | null | null | null | FUNCTION: Weakly blocks the rat SCN2A/SCN1B (Nav1.2/beta-1) sodium channel (IC(50)=68 uM) and the insect sodium channel para/tipE (IC(50)=4.3 uM), without altering the activation or inactivation kinetics (depressant toxin). {ECO:0000269|PubMed:14675784, ECO:0000269|PubMed:26429937}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1X7 | H1A02_CYRHA | MKASMFLALAGLVLLFVVCYASESEEKEFPRELISKIFTVDDFKGEERECKGFGKSCVPGKNECCSGYACNSRDKWCKVLLGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 14 (Hntx-1) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14675784}. | null | null | null | null | null | FUNCTION: Weakly blocks the rat SCN2A/SCN1B (Nav1.2/beta-1) sodium channel (IC(50)=68 uM) and the insect sodium channel para/tipE (IC(50)=4.3 uM), without altering the activation or inactivation kinetics (depressant toxin). {ECO:0000269|PubMed:14675784, ECO:0000269|PubMed:26429937}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1X8 | H1A03_CYRHA | MKASMFLALAGLVLLFVVCYASESEEKEFPRELISKIFAVDDFKGEVRECKGFGKSCVPGKNECCSGYACNSRDKWCKVLLGK | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 14 (Hntx-1) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14675784}. | null | null | null | null | null | FUNCTION: Weakly blocks the rat SCN2A/SCN1B (Nav1.2/beta-1) sodium channel (IC(50)=68 uM) and the insect sodium channel para/tipE (IC(50)=4.3 uM), without altering the activation or inactivation kinetics (depressant toxin). {ECO:0000269|PubMed:14675784, ECO:0000269|PubMed:26429937}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1X9 | H3A01_CYRHA | MKASMFLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state. {ECO:0000269|PubMed:23703613}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1Y0 | H3A02_CYRHA | MKASMYLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state. {ECO:0000269|PubMed:23703613}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1Y1 | H3A03_CYRHA | MKASMFLALAGLVLLFVVGYASESEEKEFPRELLSKIFALDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state. {ECO:0000269|PubMed:23703613}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1Y2 | H3A04_CYRHA | MKASMYLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFKGKERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state. {ECO:0000269|PubMed:23703613}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1Y3 | H3A05_CYRHA | MKASRFLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state. {ECO:0000269|PubMed:23703613}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1Z4 | H3A06_CYRHA | MKASMFLALAGLVLLFVVGYASESEEKESPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state. {ECO:0000269|PubMed:23703613}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1Z7 | H3A07_CYRHA | MKASMFLALAGLVLLFVVGYASESEEKEFPRELLSKVFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state. {ECO:0000269|PubMed:23703613}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y1Z8 | H3A08_CYRHA | MKASMFLALAGLVLLFVVGYASESEEKEFPRELLSKIFAVDDFTGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state. {ECO:0000269|PubMed:23703613}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y232 | H4A01_CYRHA | MKASMFLALAGLALLFVVCYASESEEKEFSNELLSSVLAVDDNSKGEERECLGFGKGCNPSNDQCCKSSNLVCSRKHRWCKYEIGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 22 (Htx-4) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12827284, ECO:0000269|PubMed:14512091}. | null | null | null | null | null | FUNCTION: Neurotoxin that selectively inhibits neuronal tetrodotoxin-sensitive voltage-gated sodium channels (Nav) (IC(50)=44.6 nM) (PubMed:12518233, PubMed:14512091). It is active on Nav1.2/SCN2A (IC(50)=22.4 nM), Nav1.6/SCN8A (IC(50)=50.1 nM) and Nav1.7/SCN9A (IC(50)=48.9 nM) (PubMed:29703751). It shows low affinity for lipid bilayers (PubMed:29703751). {ECO:0000269|PubMed:12518233, ECO:0000269|PubMed:12827284, ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:29703751}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y233 | H4A02_CYRHA | MKASMFLALAGLDLLFVVCYASESEEKEFSNELLSSVLAVDDNSKGEERECLGFGKGCNPSNDQCCKSSNLVCSRKHRWCKYEIGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 22 (Htx-4) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12827284, ECO:0000269|PubMed:14512091}. | null | null | null | null | null | FUNCTION: Neurotoxin. Selectively blocks neuronal tetrodotoxin-sensitive voltage-gated sodium channels (Nav) with an IC(50) of 44.6 nM. Does not affect tetrodotoxin-resistant voltage-gated sodium channels or calcium channels. {ECO:0000269|PubMed:12518233, ECO:0000269|PubMed:12827284, ECO:0000269|PubMed:14512091}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y2D1 | H3A09_CYRHA | MKASMFLALAGLALLFVVCYASESEEKEFPIELLSKIFAVDVFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state. {ECO:0000269|PubMed:23703613}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y2D2 | H3A10_CYRHA | MKASMFLALAGLVRLFVVGYASESEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state. {ECO:0000269|PubMed:23703613}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y2D3 | H3A11_CYRHA | MKASMFLALAGLVLLFVVGYASESEEKDFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state. {ECO:0000269|PubMed:23703613}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y2D7 | H4A03_CYRHA | MKASMFLALTGLALLFVVCYASESEEKEFSNELLSSVLAVDDNSKGEERECLGFGKGCNPSNDQCCKSSNLVCSRKHRWCKYEIGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 22 (Htx-4) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12827284, ECO:0000269|PubMed:14512091}. | null | null | null | null | null | FUNCTION: Neurotoxin. Selectively blocks neuronal tetrodotoxin-sensitive voltage-gated sodium channels (Nav) with an IC(50) of 44.6 nM. Does not affect tetrodotoxin-resistant voltage-gated sodium channels or calcium channels. {ECO:0000269|PubMed:12518233, ECO:0000269|PubMed:12827284, ECO:0000269|PubMed:14512091}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Y2I3 | H3A12_CYRHA | MKASMFLALAGLVLLFVVGYASGSEEKEFPRELLSKIFAVDDFKGEERGCKGFGDSCTPGKNECCPNYACSSKHKWCKVYLGK | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | ion channel inhibitor activity [GO:0008200]; sodium channel regulator activity [GO:0017080]; toxin activity [GO:0090729] | PF07740; | null | Neurotoxin 10 (Hwtx-1) family, 15 (Hntx-3) subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14512091, ECO:0000269|PubMed:23703613}. | null | null | null | null | null | FUNCTION: Selective antagonist of neuronal tetrodotoxin (TTX)-sensitive voltage-gated sodium channels (IC(50)=1270 nM on Nav1.1/SCN1A, 270 nM on Nav1.2/SCN2A, 491 nM on Nav1.3/SCN3A and 232 nM on Nav1.7/SCN9A). This toxin suppress Nav1.7 current amplitude without significantly altering the activation, inactivation, and repriming kinetics. Short extreme depolarizations partially activate the toxin-bound channel, indicating voltage-dependent inhibition of this toxin. This toxin increases the deactivation of the Nav1.7 current after extreme depolarizations. The toxin-Nav1.7 complex is gradually dissociated upon prolonged strong depolarizations in a voltage-dependent manner, and the unbound toxin rebinds to Nav1.7 after a long repolarization. Moreover, analysis of chimeric channels showed that the DIIS3-S4 linker is critical for toxin binding to Nav1.7. These data are consistent with this toxin interacting with Nav1.7 site 4 and trapping the domain II voltage sensor in the closed state. {ECO:0000269|PubMed:23703613}. | Cyriopagopus hainanus (Chinese bird spider) (Haplopelma hainanum) |
D2Z026 | DCSC_STRLA | MIRMRTPSTLPFTKMHGAGNDFVVLDLRDGPDPSPELCRALADRHKGVGCDLVLGIREPRSARAVAAFDIWTADGSRSAQCGNGARCVAAWAVRAGLARGPRFALDSPSGTHEVDVLDADTFRVALAVPRFAPESIPLFGHDGEQDLYEADLGDGTRVRFAAVSMGNPHAVIEVDDTATAPVARVGRAVQASGLFLPTVNVGFARVESRDRVHLRVHEYGAGETLACGSGACAAAAVLMRRGRVDRNVSVVLPGGELRISWPDDAADVLMTGPAAFVYEGTFLHASV | 5.1.1.19 | null | antibiotic biosynthetic process [GO:0017000]; lysine biosynthetic process via diaminopimelate [GO:0009089] | cytosol [GO:0005829] | diaminopimelate epimerase activity [GO:0008837]; racemase and epimerase activity, acting on amino acids and derivatives [GO:0016855] | PF01678; | null | Diaminopimelate epimerase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=O-ureido-L-serine = O-ureido-D-serine; Xref=Rhea:RHEA:36707, ChEBI:CHEBI:73389, ChEBI:CHEBI:74158; EC=5.1.1.19; Evidence={ECO:0000269|PubMed:22307920, ECO:0000269|PubMed:23529730}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17 mM for O-ureido-D-serine (at 30 degrees Celsius) {ECO:0000269|PubMed:22307920}; KM=110 mM for O-ureido-L-serine (at 30 degrees Celsius) {ECO:0000269|PubMed:22307920}; Note=kcat is 158 sec(-1) and 29 sec(-1) for O-ureido-L-serine and O-ureido-D-serine, respectively (at 30 degrees Celsius). {ECO:0000269|PubMed:22307920}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.9. {ECO:0000269|PubMed:22307920}; | null | FUNCTION: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the stereoinversion of O-ureido-L-serine to O-ureido-D-serine. {ECO:0000269|PubMed:20086163, ECO:0000269|PubMed:22307920, ECO:0000269|PubMed:23529730}. | Streptomyces lavendulae |
D2Z027 | DCSD_STRLA | MPLFNSILDTIGRTPIVRLQRMAPEHTSVYVKVESFNPGGSVKDRLALSVVLDAEAKGLLKPGDTIVECTSGNVGIALAMVAAARGYRFVAVMGDTYSVERRKLIRAYGGKLVLFPGHLGSKGGNLIADELAEKYGWFRARQFDNPANPSYHRETTASEILADFAGKRLDHFVTGFGTTGTLTGVGQMLRVARPEVRVVALEPSNAAMLARGEWSPHQIQGLAPNFVPGVLDRSVIDDLVTMDEVTARDTSRRLAAEEGIFAGISAGATVATALSIAEHAPEGTVLLAMLPDTGERYLSTFLFDGVDEGSDDAWLASLDTGSGL | 2.5.1.47; 2.6.99.3 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:23529730, ECO:0000269|PubMed:26207937, ECO:0007744|PDB:3X43}; | antibiotic biosynthetic process [GO:0017000]; cysteine biosynthetic process from serine [GO:0006535] | cytoplasm [GO:0005737] | cystathionine beta-synthase activity [GO:0004122]; cysteine synthase activity [GO:0004124]; L-cysteine desulfhydrase activity [GO:0080146] | PF00291; | 3.40.50.1100; | Cysteine synthase/cystathionine beta-synthase family | null | null | CATALYTIC ACTIVITY: Reaction=hydroxyurea + O-acetyl-L-serine = acetate + H(+) + O-ureido-L-serine; Xref=Rhea:RHEA:36263, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:44423, ChEBI:CHEBI:58340, ChEBI:CHEBI:73389; EC=2.6.99.3; Evidence={ECO:0000269|PubMed:23529730, ECO:0000269|PubMed:26207937}; CATALYTIC ACTIVITY: Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine; Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47; Evidence={ECO:0000269|PubMed:23529730, ECO:0000269|PubMed:26207937}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=200 mM for OAS {ECO:0000269|PubMed:23529730}; KM=190 mM for OAS {ECO:0000269|PubMed:26207937}; KM=0.12 mM for hydrogen sulfide {ECO:0000269|PubMed:26207937}; | null | null | null | FUNCTION: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent (PubMed:20086163). Catalyzes the addition of hydroxyurea on O-acetyl-L-serine (OAS) to yield O-ureido-L-serine. It prefers sulfide as the second substrate, followed by hydroxyurea, L-homocysteine, and thiosulfate (PubMed:26207937). {ECO:0000269|PubMed:20086163, ECO:0000269|PubMed:23529730, ECO:0000269|PubMed:26207937}. | Streptomyces lavendulae |
D2Z028 | DCSE_STRLA | MREFIPPASRFIELPDGFAMRRGGALYGARIAYETFGSLNAARDNAVLVLTGLSPDAHAASRPDDPTPGWWEAMVGPGKPVDTDLWHVICVNSLGSCKGSTGPASTDPRTGEPYRLSFPELSIEDIADAAAHTVRALGISRLACVVGASMGGMSALALLARHPELARTHISLSGAVHALPFSIAVRSLQREAIRSDPGWLQGHYDEGEGPRRGMLTARKLGMMTYRSAQEWDCRFGRTRIGERRRADQGRFGPEFEVESYLDFHAQRFADRFDPNSYLYLSHAMDQFDLGDGGGGGGGAPGALSRMRVERALVMGARTDILFPLSQQQEIADGLSAGGADVSFLPVDTPAGHDAFLVDIERFGPPVAKFLAIVA | 2.3.1.30; 2.3.1.31 | null | cysteine biosynthetic process from serine [GO:0006535]; homoserine metabolic process [GO:0009092]; methionine biosynthetic process [GO:0009086] | cytoplasm [GO:0005737] | homoserine O-acetyltransferase activity [GO:0004414]; O-succinyltransferase activity [GO:0016750]; serine O-acetyltransferase activity [GO:0009001] | PF00561; | 1.10.1740.110;3.40.50.1820; | AB hydrolase superfamily, MetX family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-serine = CoA + O-acetyl-L-serine; Xref=Rhea:RHEA:24560, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58340; EC=2.3.1.30; Evidence={ECO:0000269|PubMed:20086163}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine; Xref=Rhea:RHEA:13701, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57476, ChEBI:CHEBI:57716; EC=2.3.1.31; Evidence={ECO:0000255|HAMAP-Rule:MF_00296, ECO:0000269|PubMed:20086163}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.9 mM for L-serine (at 30 degrees Celsius and pH 8) {ECO:0000269|PubMed:23396912}; KM=98 mM for L-homoserine (at 30 degrees Celsius and pH 8) {ECO:0000269|PubMed:23396912}; Note=kcat is 95 min(-1) and 88 min(-1) for L-serine and L-homoserine, respectively (at 30 degrees Celsius and pH 8).; | PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:20086163}. | null | null | FUNCTION: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the transfer of the acetyl group from acetyl-CoA to the hydroxyl group of L-serine to yield the activated serine, O-acetyl-L-serine. It prefers L-serine over L-homoserine. {ECO:0000269|PubMed:20086163, ECO:0000269|PubMed:23396912}. | Streptomyces lavendulae |
D2Z030 | DCSG_STRLA | MGILALVTDAVSLPIDYDMPPLLEACRTVGITAEVCDWEDGTVDWSRFEAVVFRSPWTWAERQAEFLAFCERVSHVTRLITPMPLVRWALDKRYLADLAAHGVPVIPTTVVAPGSDALAAVRDFLAARPEAREFVVKPTDGCYSKDVQRYQRSLAEPASRHVARLLANGSHVILQPYVESVDRHGETDLTFFDGVYSHAIHKGAMLMPDGTVHVPTLDFRQARDADEDQRAVAAAALAASVAHLGLDLPLVCGRVDLVRGADGSPMVLEMELCEPSLNLTFSEDGALRFAQALAERLKP | 6.3.3.5 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:31793174}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:31793174}; | antibiotic biosynthetic process [GO:0017000] | null | ATP binding [GO:0005524]; cyclo-ligase activity [GO:0016882]; metal ion binding [GO:0046872] | null | 3.40.50.20;3.30.1490.20;3.30.470.20; | null | null | null | CATALYTIC ACTIVITY: Reaction=ATP + H(+) + H2O + O-ureido-D-serine = ADP + CO2 + D-cycloserine + NH4(+) + phosphate; Xref=Rhea:RHEA:36711, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:74158, ChEBI:CHEBI:75929, ChEBI:CHEBI:456216; EC=6.3.3.5; Evidence={ECO:0000269|PubMed:23529730}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.3 mM for O-ureido-D-serine (D-OUS) in the presence of 5 mM ATP {ECO:0000269|PubMed:31793174}; KM=10 mM for D-OUS in the presence of 5 mM ATP {ECO:0000269|PubMed:23529730, ECO:0000269|PubMed:26578703}; KM=19 mM for D-homocysteine {ECO:0000269|PubMed:23529730, ECO:0000269|PubMed:26578703}; KM=73 uM for ATP, in the presence of 50 mM D-OUS {ECO:0000269|PubMed:23529730, ECO:0000269|PubMed:26578703}; Note=kcat is 2200 sec(-1) with D-OUS as substrate. kcat is 0.86 sec(-1) with D-homocysteine as substrate. {ECO:0000269|PubMed:23529730, ECO:0000269|PubMed:26578703}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:23529730}; | null | FUNCTION: Involved in the biosynthesis of the antibiotic D-cycloserine (DCS), a cyclic structural analog of D-alanine, used as an antitubercular agent. Catalyzes the synthesis of D-cycloserine from O-ureido-D-serine (D-OUS). It reacts with D-OUS, D-homocysteine and beta-aminooxy-D-alanine. {ECO:0000269|PubMed:20086163, ECO:0000269|PubMed:23529730, ECO:0000269|PubMed:31793174}. | Streptomyces lavendulae |
D3DJG4 | SOXA1_HYDTT | MGKWVTIIFVLFLYAIAQQENPAEEVKKQKELLLKEMGILPGDVYAEQGRDMFNKPMGNAGKSCSSCHGQDGRYLRGAYAHMPRYYKDMDAVADLDTRIKYCMEKYMGVGNVKHDLNFKSIATYVATLSNGMKMDVKLTHPKEREMYEKGRELWYARVGKMDFSCAICHDSEAGKRVFLQTVVAVKEDKVATHWPAYRFSNDQLWTMEDRIRGCFGDMRVAPPEHFHWAVVALNLYLSYKAKGGVVRVPGFIY | 2.8.5.2 | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000250|UniProtKB:O33434}; Note=Binds 2 heme c groups covalently per subunit. {ECO:0000250|UniProtKB:O33434}; | sulfur oxidation [GO:0019417] | cytochrome complex [GO:0070069]; periplasmic space [GO:0042597] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor [GO:0016669]; transferase activity [GO:0016740] | PF21342; | 1.10.760.10; | SoxA family | PTM: Cysteine persulfide at Cys-214. {ECO:0000250|UniProtKB:O33434}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:O33434}. | CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:56720, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14328, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14691, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:29950, ChEBI:CHEBI:33542, ChEBI:CHEBI:139321; EC=2.8.5.2; Evidence={ECO:0000269|PubMed:20378963}; CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + S-sulfanyl-L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-(2-sulfodisulfanyl)-L-cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:51224, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14689, Rhea:RHEA-COMP:14690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:33542, ChEBI:CHEBI:61963, ChEBI:CHEBI:140664; EC=2.8.5.2; Evidence={ECO:0000269|PubMed:20378963}; | null | null | null | null | FUNCTION: C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation. {ECO:0000250|UniProtKB:O33434, ECO:0000269|PubMed:20378963}. | Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6) |
D3DJG5 | SOXA2_HYDTT | MRKLWFLPILLGAVGGVSLYAIAQQENPAEEVKKQKELLLKEMGILPGDVYAEQGRDMFNKPMGNAGKSCSSCHGQDGRYLRGAYAHMPRYYKDMDAVADLDTRIKYCMEKYMGVGNVKHDLNFKSIATYVATLSNGMKMDVKLTHPKEREMYEKGRELWYARVGKMDFSCAICHDTFGGQRIRLQTLAKVKEDKVATHWPAYRFSNDQLWTMEDRIRGCYNQIRVTPPPHFSWPQIALSLYMAYESKGGTIETPGFVR | 2.8.5.2 | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000250|UniProtKB:O33434}; Note=Binds 2 heme c groups covalently per subunit. {ECO:0000250|UniProtKB:O33434}; | sulfur oxidation [GO:0019417] | cytochrome complex [GO:0070069]; periplasmic space [GO:0042597] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on a sulfur group of donors, cytochrome as acceptor [GO:0016669]; transferase activity [GO:0016740] | PF21342; | 1.10.760.10; | SoxA family | PTM: Cysteine persulfide at Cys-220. {ECO:0000250|UniProtKB:O33434}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:O33434}. | CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-sulfosulfanyl-L-cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:56720, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14328, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14691, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:29950, ChEBI:CHEBI:33542, ChEBI:CHEBI:139321; EC=2.8.5.2; Evidence={ECO:0000269|PubMed:20378963}; CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + S-sulfanyl-L-cysteinyl-[SoxY protein] + thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + S-(2-sulfodisulfanyl)-L-cysteinyl-[SoxY protein]; Xref=Rhea:RHEA:51224, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, Rhea:RHEA-COMP:14689, Rhea:RHEA-COMP:14690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:33542, ChEBI:CHEBI:61963, ChEBI:CHEBI:140664; EC=2.8.5.2; Evidence={ECO:0000269|PubMed:20378963}; | null | null | null | null | FUNCTION: C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation. {ECO:0000250|UniProtKB:O33434, ECO:0000269|PubMed:20378963}. | Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6) |
D3DKC4 | GLYA_HYDTT | MRHLFNTDAEIYEAIVKEYERQFYHLELIASENFTSLAVMEAQGSVMTNKYAEGLPHKRYYGGCEFVDIAEDLAIERAKALFDAEHANVQPHSGTQANMAVYMAVLKPGDTIMGMDLSHGGHLTHGAKVNFSGKIYNAVYYGVHPETHLIDYDQLYRLAKEHKPKLIVGGASAYPRVIDWAKLREIADSVGAYLMVDMAHYAGLIAGGVYPNPVPYAHFVTSTTHKTLRGPRSGFILCKKEFAKDIDKSVFPGIQGGPLMHVIAAKAVAFKEAMSQEFKEYARQVVANARVLAEEFIKEGFKVVSGGTDSHIVLLDLRDTGLTGREVEEALGKANITVNKNAVPFDPLPPVKTSGIRLGTPAMTTRGMKEDQMRIIARLISKVIKNIGDEKVIEYVRQEVIEMCEQFPLYPELREEINHLAKIKATY | 2.1.2.1; 4.1.2.48 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_00051}; | folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; L-serine catabolic process [GO:0006565]; tetrahydrofolate interconversion [GO:0035999] | cytosol [GO:0005829] | cobalt ion binding [GO:0050897]; glycine hydroxymethyltransferase activity [GO:0004372]; L-allo-threonine aldolase activity [GO:0008732]; pyridoxal phosphate binding [GO:0030170]; serine binding [GO:0070905]; zinc ion binding [GO:0008270] | PF00464; | 3.90.1150.10;3.40.640.10; | SHMT family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051}. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1; CATALYTIC ACTIVITY: Reaction=L-threonine = acetaldehyde + glycine; Xref=Rhea:RHEA:19625, ChEBI:CHEBI:15343, ChEBI:CHEBI:57305, ChEBI:CHEBI:57926; EC=4.1.2.48; CATALYTIC ACTIVITY: Reaction=L-allo-threonine = acetaldehyde + glycine; Xref=Rhea:RHEA:26209, ChEBI:CHEBI:15343, ChEBI:CHEBI:57305, ChEBI:CHEBI:58585; EC=4.1.2.48; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.28 mM for L-serine (at pH 7.5 and 70 degrees Celsius) {ECO:0000269|PubMed:22141341}; KM=0.78 mM for glycine (at pH 7.5 and 70 degrees Celsius) {ECO:0000269|PubMed:22141341}; KM=7.64 mM for L-threonine (at pH 7.5 and 70 degrees Celsius) {ECO:0000269|PubMed:22141341}; KM=0.92 mM for L-allo-threonine (at pH 7.5 and 70 degrees Celsius) {ECO:0000269|PubMed:22141341}; KM=0.59 mM for L-allo-threonine (at pH 7.5 and 75 degrees Celsius) {ECO:0000269|PubMed:22141341}; KM=4.98 mM for DL-threo-beta-phenylserine (at pH 7.5 and 75 degrees Celsius) {ECO:0000269|PubMed:22141341}; KM=2.63 mM for DL-erythro-beta-phenylserine (at pH 7.5 and 75 degrees Celsius) {ECO:0000269|PubMed:22141341}; Note=kcat is 18.7 sec(-1) for the L-serine hydroxymethyltransferase reaction, 2.3 sec(-1) for the L-threonine cleavage, and 18.0 sec(-1) for the L-allo-threonine cleavage, at 70 degrees Celsius. In the THF-independent aldolase reaction, the rate constants for the erythro form substrates and for the substrates with beta-phenyl groups are larger than those for the threo form substrates and for the substrates with beta-methyl groups, respectively.; | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000255|HAMAP-Rule:MF_00051}.; PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00051}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.4 for the THF-independent L-allothreonine aldolase activity. More than 95% of full activity remains at pH 8.4, although the activities are reduced to about 90% at pH 6.9 and about 75% at pH 5.9. {ECO:0000269|PubMed:22141341}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Highly thermostable. Retains almost complete THF-independent L-allo-threonine aldolase activity after being incubated at 75 degrees Celsius for 10 minutes, and retains about 77% residual activity after being treated at 87 degrees Celsius for the same time. {ECO:0000269|PubMed:22141341}; | FUNCTION: Its primary function is to catalyze the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-threonine, L-allo-threonine, L-threo-beta-phenylserine and L-erythro-beta-phenylserine. This second activity is likely to be physiological in H.thermophilus, which is an organism that lacks the ortholog gene for the 'real' threonine aldolase characterized in mesophilic bacteria (LtaE), yeast and plants. {ECO:0000269|PubMed:22141341}. | Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6) |
D3GDK4 | GUN_CRYAT | MKVFVVLAAIVAIANGLTSGSGVTTRYWDCCKPSCSWGGKASVTKPVRTCKANGNTTIDSNTQSGCNGGSSYVCNDQQPFTQGNVGYGFAAASISGQPESQTCCACYEMTFTNTAISGQKMIVQVTNTGSDLNGNHFDLMIPGGGVGIFNGCQSQWGAPSNGWGQRYGGISSQSECNQLPTSLRAGCNWRFGWFKNADNPSMKFTQVRCPTILTQKSQCVRTPGP | 3.2.1.4 | null | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | cellulase activity [GO:0008810] | PF02015; | 2.40.40.10; | Glycosyl hydrolase 45 (cellulase K) family | PTM: N- and O-glycosylated. Contains hybrid- and complex-type N-glycans. {ECO:0000269|PubMed:24848382}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24848382}. | 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:0000255|PROSITE-ProRule:PRU10069, ECO:0000269|PubMed:22333528, ECO:0000269|PubMed:24848382, ECO:0000269|PubMed:28156112}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.5 (PubMed:24848382, PubMed:28156112). More than 90% of the maximal activity is maintained between pH range 3-5 (PubMed:24848382). More than 60% of the maximal activity is maintained between pH range 2-8 (PubMed:24848382, PubMed:28156112). About 80% of the maximal activity is maintained even at pH 2.5 (PubMed:28156112). {ECO:0000269|PubMed:24848382, ECO:0000269|PubMed:28156112}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is around 40-50 degrees Celsius (PubMed:24848382, PubMed:28156112). Has more than 50% of the maximal activity between 10-70 degrees Celsius, and more than 30% of activity at 0 degrees Celsius. Stable at 50 degrees Celsius for 30 minutes (PubMed:24848382). 60-80% of the maximal activity is retained between 0-10 degrees Celsius. Displays 40% of its maximal activity at as high as 80 degrees Celsius. Remains active at 60 degrees Celsius for over 8 hours. Approximately 50% of the activity is still maintained after 4-hour incubation at 70 degrees Celsius (PubMed:28156112). {ECO:0000269|PubMed:24848382, ECO:0000269|PubMed:28156112}; | FUNCTION: Hydrolyzes carboxymethylcellulose (CMC) (PubMed:24848382, PubMed:28156112). Hydrolyzes also lichenan and barley beta-1,4-D-glucan. CMC is hydrolyzed majorily to cellobiose (G2), cellotriose (G3) and cellotetraose (G4). Cellohexaose (G6) is hydrolyzed to G4 and G2 with traces of G3. Cellopentaose (G5) is completely hydrolyzed to G2 and G3, and G4 is partially hydrolyzed to G2. Does not hydrolyze G2 or G3. Does not hydrolyze crystalline cellulose, soluble starch, xylan, mannan or laminarin (PubMed:28156112). {ECO:0000269|PubMed:24848382, ECO:0000269|PubMed:28156112}. | Cryptopygus antarcticus (Antarctic springtail) |
D3GE74 | STR1_MEDTR | MARLERDGTNKSLESLMDSHKPGGTTTNLNQLRTQKSIPGYGLEFTNLSYSIIKKQKKDGVWINKETYLLHDISGQAIKGEIMAIMGPSGAGKSTFLDALAGRIAKGSLQGSVRIDGKPVTTSYMKMVSSYVMQDDQLFPMLTVFETFMFAAEVRLPPSISRDEKKKRVHELLNKLGLQSATHTYIGDEGRRGVSGGERRRVSIGIEIIHKPSLLFLDEPTSGLDSTSAYSVVEKIKDIAQGGSIVLMTIHQPSFRIQMLLDKITILARGRLIYMGRPDALHTHLSGFGRPVPDGENNIEYLLDVITEYDQATVGLDPLVQYQHDGHKPDPAAMTPVPKPPRTPYRRNTPASKHMISLRSQGFTAGTPQPDSSQFGLDDDDNDDDENFDNSLERRSVQTSRNIVTSGVYPRLASQFYQDFSAKDFSVWLYNGVVGTPRRPPSWTPARTPGWTPGKTPLSGPRSFVSNQHSASYQDPYYIQKTNTVVGQSMDYSATSYAPSYEEFEIEEVLDEPDLGPKYANPWLREVAVLSWRTVLNVIRTPELFASREIVLTVMALVLSTIFKNLGDTTFIDINRLLNFYIFAVCLVFFSSNDAVPSFIMERFIFIRETSHNAYRASSYVISSLIVYLPFFAVQGLTFAVITKLMLHLKSNLFNFWMILFASLITTNAYVMLVSALVPSYITGYAVVIATTALFFLTCGFFLKRTQIPAYWKWLHYISAIKYPFEGLLINEFKNNRGCYSGNKADLSPGPLGDVKPSKHHNASLPLNCLLGEDVLSTMDITMESLWYDILILLAWGVLYRFFFYLVLRFYSKNERK | 7.6.2.- | null | arbuscular mycorrhizal association [GO:0036377]; response to symbiotic fungus [GO:0009610]; transmembrane transport [GO:0055085] | membrane [GO:0016020]; periarbuscular membrane [GO:0085042]; plasma membrane [GO:0005886] | ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626] | PF01061;PF00005; | 3.40.50.300; | ABC transporter superfamily, ABCG family, Stunted arbuscule (STR) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20453115}; Multi-pass membrane protein {ECO:0000255}. Note=Located in the peri-arbuscular membrane of arbuscular mycorrhiza (AM). {ECO:0000269|PubMed:20453115}. | null | null | null | null | null | FUNCTION: Together with STR2, required for arbuscule development in arbuscular mycorrhizal (AM) symbiosis. {ECO:0000269|PubMed:20453115}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
D3J162 | VPY_MEDTR | MDRLIKLDPSNIVLIRVEEGQKCLGKITLNNVMYTMPVAFRIQPLIKTRYTIKPQSGIISPLASLVIEITYHPPQQQGSNNLPHSFPFSDDSFLLHSVLAPGAAIKEPSSMFDSVPSDWFTTKKKQVFIDSAIKVMFVGSQILTQLVEDGNSMDDIREVLEKSDPLWESVNSKDSQGQTLLHLAISKTRPDLVQLILEFKPDIEAINSVGSTPLEAASSSGESLIVELLLAHKANTEGSESSVFRPIHHASREGHMEILRLLLLKGARVDSLTKDGNTSLHLAVEEKRRDCARLLLANGARTDVRNMREGDTPLHIAAANGDENMVKLLLHKGATKYVRNKLGKTAFDVAAENGHSRLFDALRLGDNLCAAARKGEVRTIQKVLESGGVINGRDQNGWTSLHRAAFKGRMDAVRFLVEKGIDLDAKDEDGYTALHCAAESGHADVTEFLVKKGADVEARTNKGVSALQIVESLNYVGITRILVNGGASREGLGEKPPSAPSKIPFGRKVESGSVMTMKKKMSSRTRALRGSFDHSMPLAVL | null | null | arbuscular mycorrhizal association [GO:0036377]; nodulation [GO:0009877]; response to molecule of bacterial origin [GO:0002237]; response to symbiotic bacterium [GO:0009609]; response to symbiotic fungus [GO:0009610] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; periarbuscular membrane [GO:0085042]; plasma membrane [GO:0005886] | null | PF12796;PF00635; | 1.25.40.20;2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19912567, ECO:0000269|PubMed:21223389}. Nucleus {ECO:0000269|PubMed:19912567, ECO:0000269|PubMed:21223389}. Cell membrane {ECO:0000269|PubMed:26234213}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=In cells containing arbuscular mycorrhizal (AM) fungal hyphae and arbuscules, accumulates in small puncta that move through the cytoplasm, likely mobile spherical structures that are associated with the tonoplast referred to as 'tonospheres' (PubMed:19912567). Present in cytoplasmic strands below hyphopodia (PubMed:19912567). Observed associated with EX70I in zones adjacent to the periarbuscular membrane (PAM) around the arbuscule hyphal tips (PubMed:26234213). Occasionally observed in the nucleus of cells containing fungal hyphae (PubMed:19912567). {ECO:0000269|PubMed:19912567, ECO:0000269|PubMed:26234213}. | null | null | null | null | null | FUNCTION: Required for arbuscular mycorrhizal (AM) symbiosis with AM fungi (e.g. Glomus versiforme and Gigaspora gigantea) both during fungal passage across root epidermis and for arbuscule formation in cortical cells; this symbiosis promotes phosphorus (P) and copper (Cu) uptake (PubMed:19912567, PubMed:21223389). Essential for infection by symbiotic nitrogen-fixing rhizobial bacteria (e.g. Sinorhizobium meliloti) leading to the formation of root nodules (PubMed:21223389). {ECO:0000269|PubMed:19912567, ECO:0000269|PubMed:21223389}. | Medicago truncatula (Barrel medic) (Medicago tribuloides) |
D3K0R6 | AT2B4_BOVIN | MTNPTEHTLPSNSILESREGEFGCTVMDLRKLMELRSSDAIDQINVHYGGVMNLCSRLKTNPVEGLSGNPADLEKRKQVFGQNLIPPKKPKTFLELVWEALQDVTLIILEIAAIISLVLSFYRPPGGENEQCGLAVTSPEDEGEAEAGWIEGAAILFSVIIVVLVTAFNDWSKEKQFRGLQNRIEKEQKFSVIRNGHIIQLPVAEIVVGDIAQIKYGDLLPADGILIQGNDLKIDESSLTGESDHVKKSLERDPMLLSGTHVMEGSGRMVVTAVGINSQTGIIFTLLGASEGEEEEKKKKGKKQGVPENRNKAKTQDGVALEIQPLNSQEGIDSEEKEKKAAKLPKKEKSVLQGKLTRLAVQIGKAGLIMSAITVLILILYFVIDNFVIQRRPWLAECTPIYVQYFVKFFIIGVTVLVVAVPEGLPLAVTISLAYSVKKMMKDNNLVRHLDACETMGNATAICSDKTGTLTMNRMSVVQAYIGDTRYHQIPSPDDLVPKVLDLIVNGISINSAYTSKILPPEKEGGLPRQVGNKTECALLGFVSDLKQDYHAVRSEVPEEKLYKVYTFNSVRKSMSTVIEKPGGGYRMYSKGASEIILRKCNRILDKKGEAVPFKNKDRDEMVRTVIEPMACEGLRTLCIAYRDFNDGEPPWDNESEILTELTCIAVVGIEDPVRPEVPEAIAKCKRAGITVRMVTGDNINTARAIATKCGIVTPGDDFLCLEGKEFNRLIRNEKGEVEQEKLDKIWPKLRVLARSSPTDKHTLVKGIIDSTVGDQRQVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSISKFLQFQLTVNVVAVIVAFTGACITQDSPLKAVQMLWVNLIMDTFASLALATEPPTDSLLKRRPYGRNKPLISRTMMKNILGHAVYQLTVIFFLVFAGEKFFDIDSGRRAPLHSPPSQHYTIIFNTFVLMQLFNEINSRKIHGERNVFSGIFRNLIFCSVVLGTFISQIIIVEFGGKPFSCTKLTLSQWFWCLFIGIGELLWGQVISTIPTQSLKFLKEAGHGTTKEEITKDAEGLDEIDHAEMELRRGQILWFRGLNRIQTQIKVVKAFHSSLHESIQKPKNQNSIHNFMTHPEFTIDEEGPRTPLLDEQEEEIFEKVSKPGTKTSSLDGEVTPQTNKNNNTVDCCQVQIVASHSDSPLHSLETSV | 7.2.2.10 | null | cellular response to acetylcholine [GO:1905145]; flagellated sperm motility [GO:0030317]; intracellular calcium ion homeostasis [GO:0006874]; regulation of cytosolic calcium ion concentration [GO:0051480]; urinary bladder smooth muscle contraction [GO:0014832] | intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]; sperm flagellum [GO:0036126] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calmodulin binding [GO:0005516]; metal ion binding [GO:0046872]; P-type calcium transporter activity [GO:0005388]; PDZ domain binding [GO:0030165] | PF12424;PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIB subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21187283}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium, flagellum membrane {ECO:0000250|UniProtKB:Q6Q477}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000250|UniProtKB:P23634}; | null | null | null | null | FUNCTION: Calcium/calmodulin-regulated and magnesium-dependent enzyme that catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell (By similarity). By regulating sperm cells calcium homeostasis, may play a role in sperm motility (By similarity). {ECO:0000250|UniProtKB:P23634, ECO:0000250|UniProtKB:Q6Q477}. | Bos taurus (Bovine) |
D3K5I7 | NCAP_RVFV | MDNYQELAIQFAAQAVDRNEIEQWVREFAYQGFDARRVIELLKQYGGADWEKDAKKMIVLALTRGNKPRRMMMKMSKEGKATVEALINKYKLKEGNPSRDELTLSRVAAALAGRTCQALVVLSEWLPVTGTTMDGLSPAYPRHMMHPSFAGMVDPSLPGDYLRAILDAHSLYLLQFSRVINPNLRGRTKEEVAATFTQPMNAAVNSNFISHEKRREFLKAFGLVDSNGKPSAAVMAAAQAYKTAA | null | null | null | host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell Golgi apparatus [GO:0044177]; host cell nucleus [GO:0042025]; ribonucleoprotein complex [GO:1990904]; viral nucleocapsid [GO:0019013] | identical protein binding [GO:0042802]; RNA binding [GO:0003723] | PF05733; | null | Phlebovirus nucleocapsid protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:34960686}. Host cytoplasm {ECO:0000269|PubMed:34960686}. Host nucleus {ECO:0000269|PubMed:34960686}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:I6WJ72}. Host Golgi apparatus {ECO:0000250|UniProtKB:I6WJ72}. | null | null | null | null | null | FUNCTION: Encapsidates the genomic RNA, protecting it from nucleases (Probable) (PubMed:20547879). Displays high affinity for single-stranded nucleic acid (PubMed:23129612). The encapsidated genomic RNA is termed the nucleocapsid (NC) or ribonucleoprotein (PubMed:20547879). The ribonucleoprotein has a non-helical structure (PubMed:20547879). Serves as template for viral transcription and replication (By similarity). After replication, the nucleocapsid is recruited to the host Golgi apparatus by glycoprotein Gn for packaging into virus particles (By similarity). {ECO:0000250|UniProtKB:P21700, ECO:0000269|PubMed:20547879, ECO:0000269|PubMed:23129612, ECO:0000305|PubMed:34960686}. | Rift valley fever virus (RVFV) |
D3KCC4 | CRNS1_CHICK | MISVDRLSEEQALGMKEQEWAGPEALCPGWQEEEVSDGEGPEDSGHPDPTAHAYEVLQHTLRLEGMPLTIDRTGQPRTGSGPLDMTVCVLGSPTAFLPVLLEGGTRYPGAMVLCLAPAWASRVPSETSPGSWSLLLSRGVSFEAGGCTALEEFVPPRRATYVTGTFGSEGSWEGELARDLDCPTGGSALLTRWLEDPLLSRWLLSARAGLPVPPTLAFITGLWETLPEEPEPPGVHLVRLQDPQGQESLVRDEVGAFLEGSSMQPYDQVAVRLSGWRWRGTDPHSTHRKVEGEAVAQAVAALLKGLREEESILLEALVPTARLPTLPPRSAAPRLPMALRICTVVCRSWGDRPQLCQVACTAGRAEVPVRHGSALPLGLDSSLRQWGLADAAQRQALAGQLREAAEAAMAALLAAEGELSPAQRGGARAHTDVLGVDFLLACVDGTLELVALSANCLRCLETCLLAEGMGHDVGQPAGDVPRLLAECLLHRAQCHLVEGKDILLIGAGGVSKSFVWEAAREYGLRIHLVESDPEHFAAGLVETFLPYDSREHRRDEEHAERVLEMLRARGLRPDACLSYWDDCVVLTALLCQRLGLPGCPPAAVRLAKQKSRTHQHLQRCRRGRPPPAAFSVPCRRLRSHGDVERAAGAVPFPAVAKLEFGAGAVGVRLVENAGQCHAHAAQLWHDLRADADHPGIGLGWGNAMLLMEYVPGTEHDVDLVLFEGRLLGAWVSDNGPTRVPTFLETAATLPSCLPADRQAQLVRAALRCCRACGLRHGVFNVELKLSPAGPRLLEINPRMGGFYLRDWMRAVYGPDLLLAAVLLALGLPPVLPSRPAPRQQLAGVMCLASEHGRALRGGVMAALQGLQRRGLVRLNPLFEEAGGRYEEPCLSVACAGDGPAEACGRLLGLCQALGIDSPQYPVGHFLSHFK | 6.3.2.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409}; | carnosine biosynthetic process [GO:0035499] | null | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; carnosine synthase activity [GO:0047730]; homocarnosine synthase activity [GO:0102102]; metal ion binding [GO:0046872] | PF18130;PF15632; | 3.40.50.20;3.30.470.20; | null | null | null | CATALYTIC ACTIVITY: Reaction=ATP + beta-alanine + L-histidine = ADP + carnosine + H(+) + phosphate; Xref=Rhea:RHEA:19297, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57485, ChEBI:CHEBI:57595, ChEBI:CHEBI:57966, ChEBI:CHEBI:456216; EC=6.3.2.11; Evidence={ECO:0000269|PubMed:20097752}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19298; Evidence={ECO:0000305|PubMed:20097752}; CATALYTIC ACTIVITY: Reaction=4-aminobutanoate + ATP + L-histidine = ADP + H(+) + L-homocarnosine + phosphate; Xref=Rhea:RHEA:59568, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57595, ChEBI:CHEBI:59888, ChEBI:CHEBI:143075, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:20097752}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59569; Evidence={ECO:0000305|PubMed:20097752}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.033 mM for beta-alanine {ECO:0000269|PubMed:20097752}; KM=0.35 mM for 4-aminobutanoate {ECO:0000269|PubMed:20097752}; KM=0.1 mM for L-histidine {ECO:0000269|PubMed:20097752}; KM=1.42 mM for L-lysine {ECO:0000269|PubMed:20097752}; KM=1.62 mM for L-ornithine {ECO:0000269|PubMed:20097752}; KM=0.39 mM for N-methylhistidine {ECO:0000269|PubMed:20097752}; Vmax=119 nmol/min/mg enzyme toward beta-alanine {ECO:0000269|PubMed:20097752}; Vmax=84.1 nmol/min/mg enzyme toward gamma-aminobutyrate {ECO:0000269|PubMed:20097752}; Vmax=3.3 nmol/min/mg enzyme toward L-histidine {ECO:0000269|PubMed:20097752}; Vmax=3.43 nmol/min/mg enzyme toward L-lysine {ECO:0000269|PubMed:20097752}; Vmax=2.54 nmol/min/mg enzyme toward L-ornithine {ECO:0000269|PubMed:20097752}; Vmax=3.51 nmol/min/mg enzyme toward N-methylhistidine {ECO:0000269|PubMed:20097752}; | null | null | null | FUNCTION: Catalyzes the synthesis of carnosine and homocarnosine. Carnosine is synthesized more efficiently than homocarnosine. {ECO:0000269|PubMed:20097752}. | Gallus gallus (Chicken) |
D3KU66 | ASMT_MOUSE | MHRGRSASARQERDFRALMDLAHGFMASQVLFAGCALRVFDAAALGPVDAAALARSSGLSPRGTRLLLDACAGLGLLRRRRGAGPRGPAYTNSPLASTFLVAGSPLSQRSLLLYLAGTTYLCWGHLADGVREGRSQYARAVGVDADDPFTAIYRSEAERLLFMRGLQETWSLCGGRVLTAFDLSPFRVICDLGGGSGALARMAARLYPGSEVTVFETPDVVAAARAHFPPPADEDGAEPRVRFLSGDFFRSPLPPADLYVLARVLHDWADAACVELLRRVRGALRPGGAVLLVESVLSPGGAGPTRTLLLSLTMLLQARGRERTEAEYRALTARAGFSRLRLRRPRGPYHAMMAARGGGAGARSDGGGGDATSQTGSGTGSEVGAQD | 2.1.1.4 | null | lipid metabolic process [GO:0006629]; male gonad development [GO:0008584]; melatonin biosynthetic process [GO:0030187]; methylation [GO:0032259]; negative regulation of male gonad development [GO:2000019] | null | acetylserotonin O-methyltransferase activity [GO:0017096]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757] | PF16864;PF00891; | 3.40.50.150;1.10.10.10; | Class I-like SAM-binding methyltransferase superfamily, Cation-independent O-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=N-acetylserotonin + S-adenosyl-L-methionine = H(+) + melatonin + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15573, ChEBI:CHEBI:15378, ChEBI:CHEBI:16796, ChEBI:CHEBI:17697, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.4; Evidence={ECO:0000269|PubMed:20308563}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15574; Evidence={ECO:0000305|PubMed:20308563}; | null | PATHWAY: Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2. {ECO:0000269|PubMed:20308563}. | null | null | FUNCTION: Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine). {ECO:0000269|PubMed:20308563}. | Mus musculus (Mouse) |
D3KZG3 | TMC1_CAEEL | MQEAARRASLRKEHTPTNEKFGDLSKQDSLGERASSKLTLDDELYDILYAFGETDAFINKGDKQRETDEDGNPLTRQALLERIRQKKEVIGKLRCQAWSMTRKRRTLKLAQKYLEQHESKVSRSHLYMEEMRKRARLMKRSFSNFKTYLIPWESKIKRIESHFGSVVSSYFTFLRWIVFVNIMITLIALVFVVLPETLADSVANEGRFNRTKTRKQIPANERVHADELAVVWHYDGYLRYSPLFYGYYSDDPFLGNKIKYALPLAYFMVTLTIFAYSFFAILRKMAANARMSKLSGSKAEQYIFNWKLFTGWDYTIGNSETASNTVMAVVIKLRESIADIKKDAHGKFRLLQFSLRVFANIIICAMLGFSIYCIIFAVQKSQVQDDGNLFTKNQVPSVVSTITHVFPMIFDLIGKMENYHPRTALRAHLGRVLILYTVNYITLIFALFEKMTALRDRVNSTSTSSSHRTKRQQGGWNPNMQRPPPYASRAEVRQMSDFLAANTRRFQTVSQRTTRSVTTPFTVAPQFGPFNVNNPNAVFHNGTHSTSFESQILGPKALPIFTPPPRKYPGFTPGNVGQQFGGPDFPRNQVYTKSTPLPRVRTKPPWVYTTTHPPLVQNRAMTTTMSKSAKKGNSKNLDDDILLSNETIQMSEAALRRNHDGHNNDICWETIIGQEIVKLVTMDLIFTILSILVIDLFRGLWIKYCSSWWCWDIETTFPEYGEFKVAENVLHIINNQGMIWLGLFFAPLLPAINNIKLIILMYIRGWAVMTCNVPAREIFRASRSSNFYLGILLIWLLLCTLPVGFVIASMSPSRSCGPFARYQHFYTVVTREIEKRVDQTVLSYIRHIASPGVVIPIILFLILIIYFLFSLVRGLREANTDLQAQLVHERTEEKKKIFELAGGKKNKFEKDRDKKRSNDYIPLIEQRRREPWRQYHEMEADHALASDSSEESDINEDEDDERQPLTAYPLRAIETPPETLQVTAFHPSLGSLIENREMEDEESASGDQLPMIHKSVSFQGPSHMQMRQSISTESCSQISRSAIQVATPEEIRALLRPYLEAKYGIPYQHGIKSFPIDVHTPPNNTPSRRSSKYNSFVSLYEHTRDDHKNFVASTIKETDEDPGKSDKKQTSSKDVAPDFMPWPSADEARALREKMKSKTPLMLTKTTVEEKPKGGKSSESEFRPPVPIHRKYNIQTTEEENEEEETDSAPESSKKRFRISVSPTKTIAPASASRAQHKIVSQASSSSSIPHGRQPDPNKKASLVLPPLRAPRVQFDEDDSPRQID | null | null | detection of stimulus involved in sensory perception [GO:0050906]; monoatomic ion transmembrane transport [GO:0034220]; sensory perception of chemical stimulus [GO:0007606] | neuronal cell body [GO:0043025]; non-motile cilium [GO:0097730]; plasma membrane [GO:0005886] | mechanosensitive monoatomic ion channel activity [GO:0008381]; monoatomic ion channel activity [GO:0005216]; sodium channel activity [GO:0005272] | PF07810; | null | TMC family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23364694}; Multi-pass membrane protein {ECO:0000269|PubMed:23364694}. | null | null | null | null | null | FUNCTION: Sodium-sensor ion channel that acts specifically in salt taste chemosensation. Required for salt-evoked neuronal activity and behavioral avoidance of high concentrations of NaCl. {ECO:0000269|PubMed:23364694}. | Caenorhabditis elegans |
D3RVD4 | TSDA_ALLVD | MRGDVRVHTASPIAAAWLLAVGLVAHAEEPPTVALTVPAAALLPDGALGESIVRGRRYLSDTPAQLPDFVGNGLACRHCHPGRDGEVGTEANAAPFVGVVGRFPQYSARHGRLITLEQRIGDCFERSLNGRALALDHPALIDMLAYMSWLSQGVPVGAVVAGHGIPTLTLEREPDGVHGEALYQARCLACHGADGSGTLDADGRYLFPPLWGPRSFNTGAGMNRQATAAGFIKHKMPLGADDSLSDEEAWDVAGFVLTHPRPLFQEPTGD | 1.8.2.2 | null | null | periplasmic space [GO:0042597] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; thiosulfate dehydrogenase activity [GO:0050338] | PF13442;PF21342; | 1.10.760.10; | null | PTM: Binds 2 heme c groups covalently per subunit. {ECO:0000269|PubMed:22779704}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:16995898}. | CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c] + 2 thiosulfate = 2 Fe(II)-[cytochrome c] + 2 H(+) + tetrathionate; Xref=Rhea:RHEA:20549, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15226, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:33542; EC=1.8.2.2; Evidence={ECO:0000269|PubMed:16995898, ECO:0000269|PubMed:22779704}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=30000 umol/min/mg enzyme (with 1 mM ferricyanide) {ECO:0000269|PubMed:16995898, ECO:0000269|PubMed:22779704}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.2. {ECO:0000269|PubMed:16995898, ECO:0000269|PubMed:22779704}; | null | FUNCTION: Catalyzes the oxidation of 2 molecules of thiosulfate to tetrathionate. {ECO:0000269|PubMed:16995898, ECO:0000269|PubMed:22779704}. | Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D) (Chromatium vinosum) |
D3TTC1 | VM3KL_NAJAT | MIQALLVIICLAVFPHQGSSIILESGNVNDYEVVYPQKVPALLKGGVQNPQPETKYEDTMRYEFQVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSPPVQDHCYYHGYIQNEADSSAVISACDGLKGHFEHQGETYFIEPLKISNSEAHAIYKDENVENEDETPEICGVTETTWESDESIEKTSQFTNTPEQDRYLQDKKYIEFYVIVDNRMYRYYNNDKPAIKIRVYEMINAVNTKFRPLKIHIALIGLEIWSNKDKFEVKPAASVTLKSFGEWRETVLLPRKRNDNAQLLTGIDFNGNTVGRAYIGSLCKTNESVAIVQDYNRRISLVASTITHELGHNLGIHHDKASCICIPGPCIMLKKRTAPAFQFSSCSIREYREYLLRDRPQCILNKPLSTDIVSPPICGNYFVEVGEECDCGSPQACQSACCNAATCQFKGAETECRVAKDDCDLPELCTGQSAECPTDSLQRNGHPCQNNQSYCYNGTCPTLTNQCITLLGPHFTVSPKGCFDLNMRGDDGSFCRMEDGTKIPCAAKDVKCGRLYCTEKNTMSCLIPPNPDGIMAEPGTKCGDGMVCSKGQCVDVQTAY | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF08516;PF01562;PF01421; | 3.40.1620.60;3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom zinc metalloproteinase that cleaves the membrane-bound precursor of TNF-alpha (TNF) into its mature soluble form showing the same digestion pattern than ADAM17. {ECO:0000269|PubMed:19932752}. | Naja atra (Chinese cobra) |
D3TTC2 | VM3H_NAJAT | MIQALLVIICLAVFPHQGSSIILESGNVNDYEVVYPQKVPALLKGGVQNPQPETKYEDTMRYEFQVNGEPVVLHLERNKGLFSEDYTETHYAPDGREITTSPPVQDHCYYHGYIQNEADSSAVISACDGLKGHFEHQGETYFIEPLKISNSEAHAIYKDENVENEDETPEICGVTETTWESDESIEKTSQLTNTPEQDRYLQAKKYIEFYVVVDNIMYRHYKRDQPVIKRKVYEMINTMNMIYRRLNFHIALIGLEIWSNINEINVQSDVRATLNLFGEWREKKLLPRKRNDNAQLLTGIDFNGTPVGLAYIGSICNPKTSAAVVQDYSSRTRMVAITMAHEMGHNLGMNHDRGFCTCGFNKCVMSTRRTKPAYQFSSCSVREHQRYLLRDRPQCILNKPLSTDIVSPPICGNYFVEVGEECDCGSPADCQSACCNATTCKLQHEAQCDSEECCEKCKFKGARAECRAAKDDCDLPELCTGQSAECPTDVFQRNGLPCQNNQGYCYNGKCPIMTNQCIALRGPGVKVSRDSCFTLNQRTRGCGLCRMEYGRKIPCAAKDVKCGRLFCKRRNSMICNCSISPRDPNYGMVEPGTKCGDGMVCSNRQCVDVKTAY | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF08516;PF00200;PF01562;PF01421; | 3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Snake venom zinc metalloproteinase that seems to inhibit cell migration. This activity is dominated by the local structure of the hyper-variable region. {ECO:0000269|PubMed:19932752}. | Naja atra (Chinese cobra) |
D3UW23 | AMPE_BITRH | MDIEDKTSKMHCMKGKHVVIICGVVIAVGLILGLGLGLGLDTKACNPPEVNGQVSTKSPISNTPDVTSPSGSSVFCSAKNDENGPWTHFRLPNYVHPVHYDLHLTPEMEAEVYTGMVNISIRLEEQTTKHLWLHLRETKITEMPQLWTSSGQVIEIKRCFGYEPQEYVVIEAEEDLRPSNYFLSMRFKGYLNGSLVGFYSTTYGENGKIKYIAATDHEPTDARKSFPCFDEPNKKATYTISITHEHDYEAISNMPVEKTISLDNKWTKTIFKKSVPMSTYLVAWAVHQFKYEERISSRGIPLRIYAQPQQINTAIYAANVTKVVFDYFENYFNMNYSLPKLDKIAIPDFGTGAMENWGLITYRETNLLYDSQESAASNKQRVAAVIAHELVHQWFGNIVTMDWWDDLWLNEGFASFFEFMGVNAKEEKWQMLDQILISDLLPVLKEDSLVSSHPITVNVSSPDEITSVFDGISYSKGASILRMLEDWISPECFRAGCEKYLKEHYFKNAKTDDFWKAMEEVSGKPVKEVMDTWTRQMGYPVLKVDLNSTVTQQRFLLDPKADPSKPSSQFSYKWNIPVKWKEGNTSNIIFYNKSELAGITITRPSDLPLNSFLKVNKDHVGFYRVNYEPQVWRALTDIMMKDHQNFNLADRAGFIDDAFALARAGLLKYADALNLTRYLQNEAEYIPWQRAVVAISYIRNMFEDDKALYPKFQRYFGSLVKPIASELKWEXDEDHIKSLLRTTVLEFACKMEDPEALGNASLLFKKWMSGISLDVNLRLLVYRFGMQNSGDEQAWNYMFQKYRTATLAQEKEKLLYGLASVKNITLLNRFLSCIKNTSLIRSQDVFTVLGYISLNSYGKTMAWDWVRLNWEYLVKRYTLNDRNLGRLISRLSGTFNTELQLWQMENFFERYPDAGAGEASRKQALETTKSNIEWLKQYRDDVATWLENSEHSNFA | 3.4.11.7 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q07075}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q07075}; | peptide catabolic process [GO:0043171]; proteolysis [GO:0006508]; regulation of blood pressure [GO:0008217] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | metalloaminopeptidase activity [GO:0070006]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270] | PF11838;PF01433;PF17900; | 1.25.50.20;2.60.40.1910;1.10.390.10;2.60.40.1730; | Peptidase M1 family | PTM: N-glycosylated. Glycosylation counts for an increased mass of about 32% of the protein mass (about 48 kDa). {ECO:0000269|PubMed:20706583}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q07075}; Single-pass type II membrane protein {ECO:0000255}. Note=Found in the venom as transmembrane proteins in exosome-like vesicles. {ECO:0000250|UniProtKB:P0DQU2}. | CATALYTIC ACTIVITY: Reaction=Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide.; EC=3.4.11.7; Evidence={ECO:0000269|PubMed:20706583}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=703 uM for Glu-AMC (in presence of 1.2 mM Ca(2+)) {ECO:0000269|PubMed:20706583}; KM=2478 uM for Asp-AMC (in presence of 1.2 mM Ca(2+)) {ECO:0000269|PubMed:20706583}; KM=2235 uM for Glu-AMC (in absence of Ca(2+)) {ECO:0000269|PubMed:20706583}; KM=4119 uM for Asp-AMC (in absence Ca(2+)) {ECO:0000269|PubMed:20706583}; | null | null | null | FUNCTION: Venom protein that cleaves N-terminal acidic residues from peptides with high potency in presence of calcium (PubMed:20706583). It may have several roles in venom including alteration of blood pressure by cleaving circulating angiotensin-2, general degradation of host tissue, increase of permeability to other venom components, and/or processing of other toxins in the venom (By similarity). {ECO:0000250|UniProtKB:P0DQU2, ECO:0000269|PubMed:20706583}. | Bitis rhinoceros (West African gaboon viper) (Vipera rhinoceros) |
D3UW26 | IF4EA_SOLTU | MAAAEMERTTSFDAAEKLKAADAGGGEVDDELEEGEIVEESNDTASYLGKEITVKHPLEHSWTFWFDSPIAKSRQTAWGSSLRNVYTFSTVEDFWGAYNNIHHPSKLVMGADFHCFKHKIEPKWEDPVCANGGTWKMSFLKGKSDTSWLYTLLAMIGHQFDHGDEICGAVVSVRSKGEKIALWTKNAANETAQVSIGKQWKQFLDHSDSVGFIFHDDAKRLDRSAKNRYTV | null | null | defense response to virus [GO:0051607]; translational initiation [GO:0006413] | cytoplasm [GO:0005737]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634] | RNA 7-methylguanosine cap binding [GO:0000340]; RNA binding [GO:0003723]; translation initiation factor activity [GO:0003743] | PF01652; | 3.30.760.10; | Eukaryotic initiation factor 4E family | PTM: According to the redox status, the Cys-129-Cys-167 disulfide bridge may have a role in regulating protein function by affecting its ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:K0P2S0}. Cytoplasm {ECO:0000250|UniProtKB:K0P2S0}. | null | null | null | null | null | FUNCTION: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures (By similarity). Key component of recessive resistance to potyviruses (PubMed:21668622, PubMed:22146867, PubMed:31906869). {ECO:0000250|UniProtKB:P29557, ECO:0000269|PubMed:21668622, ECO:0000269|PubMed:22146867, ECO:0000269|PubMed:31906869}.; FUNCTION: (Microbial infection) Susceptibility host factor required for viral infection (e.g. Potato virus Y (PVY)) by recruiting viral RNAs to the host ribosomal complex via an interaction with viral genome-linked protein (VPg). {ECO:0000269|PubMed:21668622, ECO:0000269|PubMed:22146867, ECO:0000269|PubMed:31906869}. | Solanum tuberosum (Potato) |
D3VML5 | PZNA_BACVZ | MTQIKVPTALIASVHGEGQHLFEPMAARCTCTTIISSSSTF | null | null | cytolysis by symbiont of host cells [GO:0001897]; defense response to Gram-positive bacterium [GO:0050830] | extracellular region [GO:0005576]; Gram-positive-bacterium-type cell wall [GO:0009275] | null | null | null | null | PTM: Maturation of thiazole and oxazole containing antibiotics involves the enzymatic condensation of a Cys, Ser or Thr with the alpha-carbonyl of the preceding amino acid to form a thioether or ether bond, then dehydration to form a double bond with the alpha-amino nitrogen. Thiazoline or oxazoline ring are dehydrogenated to form thiazole or oxazole rings. {ECO:0000305}.; PTM: 2 forms exist: plantazolicin A and plantazolicin B. The structural difference between them is a dimethylation at Arg-28 in plantazolicin A. {ECO:0000269|PubMed:21568297}. | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:20971906, ECO:0000269|PubMed:21950656}. | null | null | null | null | null | FUNCTION: Peptide antibiotic inhibiting growth of Gram-positive bacteria in the dimethylated form plantazolicin A. The desmethyl form plantazolicin B has no antibiotic activity. The mode of action appears to be disruption of cell walls and lysis of cells. Inhibits B.subtilis strain HB0042, B.megaterium strain 7A1 and B.anthracis (MIC=2-4 ug/ml). Weakly inhibits Gram-positive bacteria B.brevis strain ATCC 8246, B.subtilis strain 168, B.cereus strain ATCC 14579 and strain CU1065, B.licheniformis strain ATCC 9789, M.luteus, B.sphaericus, P.granivorans and S.pyogenes (MIC=128 ug/ml). Does not inhibit B.pumilus, P.polymyxa, Arthrobacter sp., S.aureus, vancomycin-resistant E.faecalis, L.monocytogenes, methicillin-resistant S.aureus or Gram-negative bacteria E.coli strain K12, K.terrigena, Pseudomonas sp. and E.carotovora. {ECO:0000269|PubMed:20971906, ECO:0000269|PubMed:21950656}. | Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42) (Bacillus amyloliquefaciens subsp. plantarum) |
D3W0D1 | KLRF2_HUMAN | MENEDGYMTLSFKNRCKSKQKSKDFSLYPQYYCLLLIFGCIVILIFIMTGIDLKFWHKKMDFSQNVNVSSLSGHNYLCPNDWLLNEGKCYWFSTSFKTWKESQRDCTQLQAHLLVIQNLDELEFIQNSLKPGHFGWIGLYVTFQGNLWMWIDEHFLVPELFSVIGPTDDRSCAVITGNWVYSEDCSSTFKGICQRDAILTHNGTSGV | null | null | natural killer cell degranulation [GO:0043320]; positive regulation of cytokine production [GO:0001819] | plasma membrane [GO:0005886] | carbohydrate binding [GO:0030246]; protein homodimerization activity [GO:0042803] | PF00059; | 3.10.100.10; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:20194751}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20194751}; Single-pass type II membrane protein {ECO:0000269|PubMed:20194751}. | null | null | null | null | null | FUNCTION: C-type lectin-like receptor involved in natural killer cell mediated cytotoxicity and cytokine secretion in keratinocytes via its interaction with CLEC2A. {ECO:0000269|PubMed:20194751}. | Homo sapiens (Human) |
D3WYW0 | LSC_LACGS | MLENKKHKKMSLSGKSLLMGTLSTAAIVLSASTVNAATNTDTVDNANASQVTTVKASASVNKNDNSGLKENATNDKVAGTETNLNSSLNSGKETSSQVNDSKEDSSSTQVGSTPISSAIINNGKASSDLNQDSDNISDHFKDNNSQGQSSTSSEKTELKGKIKEIVNNSGIDVTKLTNDQINNLNKVNFDNDPQDGTKLTLNDLDAIGQALIRRDPKYAVPYFNAKEIKNMDAAETKDAQTGKTETLEIWDSWPVQDPITGYVSNYKGYQLVIAMMGMPKKNDNHIYLLYNKYNDNEFSHWRNAGSIFGYNETPDLQEWSGSAIVNKDGSVQLFYTKNDTSNGKLNDQQLATANLKLNVDNNGVSIASVDNDHVIFIGDGKHYQTYDQFSNGKNRNRDNYTLRDPHVVEEENGDRYLVFEANTGSNNYQGEDQVYRWANYGGNDKFNVNNFLSYFGNNDDQALASVANGALGILKLSGDQNNPTVKLDDVYSPLVTSLMVSDEMERPDIVKVGNKYYLFSATRLSRGTKGEITRLANKVVGDNVAMIGFVSDSLTHGYVPLNGSGVVLTASVPANWRTATYSYYAVPIEGKENQLLITAYMTNRGEVAGKGNNSTWAPSFILQLNPDNTTTVLAKLTNQGVWVWNGDSENKNMIGSLEKDSPNSAALDGEWGKFIDWDAINSYSLKPHQPVTPNVPTTPEKPENPTTPNTPDTPRTPEVPTTPVKKTTQSELPKAGAKDGIAATILGAISSMLGVIGLAGISKRKRNN | 2.4.1.10 | null | carbohydrate utilization [GO:0009758] | cell surface [GO:0009986]; extracellular region [GO:0005576] | levansucrase activity [GO:0050053]; metal ion binding [GO:0046872] | PF02435;PF00746; | null | Glycosyl hydrolase 68 family | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. Cell surface {ECO:0000269|PubMed:20075040}. | CATALYTIC ACTIVITY: Reaction=[6)-beta-D-fructofuranosyl-(2->](n) alpha-D-glucopyranoside + sucrose = [6)-beta-D-fructofuranosyl-(2->](n+1) alpha-D-glucopyranoside + D-glucose; Xref=Rhea:RHEA:13653, Rhea:RHEA-COMP:13093, Rhea:RHEA-COMP:13094, ChEBI:CHEBI:4167, ChEBI:CHEBI:17992, ChEBI:CHEBI:134464; EC=2.4.1.10; Evidence={ECO:0000269|PubMed:20075040}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 3.5-4.5. {ECO:0000269|PubMed:20075040}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. Activity drastically decreases at 60 degrees Celsius. {ECO:0000269|PubMed:20075040}; | FUNCTION: Fructosyltransferase that catalyzes the polymerization of the fructose moiety of sucrose to produce levan polymer and the fructo-oligosaccharide (FOS) 1-kestose. Is also able to convert raffinose into a fructan polymer and a single oligosaccharide (most likely Gal-Glc-Frc-Frc) in vitro; however, L.gasseri strain DSM 20077 is unable to ferment raffinose. Also displays sucrose hydrolase activity. {ECO:0000269|PubMed:20075040}. | Lactobacillus gasseri |
D3XDS2 | UL97_MUHVS | MSVELTPPRSDGSVGFAPVVVPPAPRKPLRRRAVSDLEKLYKVKRRLVFGADDGAVDNDTSNNNSGSSSTTSRSRRKTAADVVSDSPKRTDDSSTAGEDGYTHCVHSCACTPGERHLLCCELVSIGDSVSVARCPLCSLGISTTYLSRGCCRGRSKVTGGDEDEEDEDEEENSQDEDRDEEEAASASSSGGLEWSDDSNSALSWSDENIIISPFPGLKCYVTTFEDIRQPVLLETGSAYLPVYVPYDESFCRNRCLERGGDDDDERDATLIGKGSFGQVWRLSDKKTALKAAASESINETLLTVWISGVVRSRAQDAGYRGELDDSVYCNILVATGSCLRHNLVSFASFDRDLYNYRGWHYAGLASYRRAFSGIADALRFLNLRCGVGHFDVTPMNVLINYDRADDRQIARAVICDFSLSQCHTEGTTGHCVVVFQQTKTVRALPKSAYYLTDIYHPAFKPLMLQKLCAIEPRKQFPKPSANRFCVSDLCALGHVAAFCLVRVLDERGQLKVRSTSEDALFGVARKTCDALARHSVDEVANFCSLLITRQLAYTATLLGSDDMREPMARLCDYFETVSDKDAPDRFRSVYKRARREIDGSYMVRLLLAASETEDGRYLLDNIRATCLMVDSEDLDVDPYKIFP | 2.7.11.1 | null | phosphorylation [GO:0016310]; viral process [GO:0016032] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; virion component [GO:0044423] | ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674] | PF06734; | 1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, HCMV ganciclovir subfamily | null | SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P16788}. Host nucleus {ECO:0000269|PubMed:32973148}. Host cytoplasm {ECO:0000269|PubMed:32973148}. Note=Present in host nucleus at early times but redistributes to a predominantly cytoplasmic localization pattern at 24 hours post infection. {ECO:0000269|PubMed:32973148}. | 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:P16788}; 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:31548683}; | null | null | null | null | FUNCTION: Serine/threonine protein kinase that plays important roles in several processes including viral morphogenesis, nuclear viral egress, viral replication or regulation of host cell cycle progression (PubMed:17910700, PubMed:32973148). Participates in the acquisition of tegument during virion morphogenesis in the nucleus (By similarity). Phosphorylates host SAMHD1 and thereby counteracts its antiviral effect by reducing its dNTP hydrolase activity (PubMed:31548683). Inhibits host DNA synthesis by cyclin A/CDKN2A sequestration to the cytoplasm (PubMed:32973148). {ECO:0000250|UniProtKB:P16788, ECO:0000269|PubMed:17910700, ECO:0000269|PubMed:31548683, ECO:0000269|PubMed:32973148}. | Murid herpesvirus 1 (strain Smith) (MuHV-1) (Mouse cytomegalovirus) |
D3YN49 | GEMC1_XENLA | MNTILTCQDEYFAGGLGYDCPYFSSTSASTVDVSKETWVSLWASGLLDNRSSNHGPHTQGQLYNMGNSLQEDYLFGDQLSSQISANKQLQDTLLQKEEELSRLHEENNKLKEFLNSAFVKTLAEKTKKLLHQNGQSSFCTNPNSRVPFSSNSTPGSKAKRARRNLYGELTACEAQSSPVVEKWVLQTLGLKDVDTIDDSALANYSAMSLQPKQDSPSSGYSSAHLTPGHSQAATSCSLSPSQCSSASLPESETASPLSSPTYHTPDVAPNKTEVAFSTSLHPHCNVKTHSFPQGQAFVRRDTQGGWKFTWVPKQSE | null | null | cell cycle [GO:0007049]; DNA replication initiation [GO:0006270]; negative regulation of cell cycle [GO:0045786]; negative regulation of DNA replication [GO:0008156] | nucleus [GO:0005634] | chromatin binding [GO:0003682] | null | null | GEMC1 family | PTM: Highly phosphorylated by cdk2; stimulates initiation of DNA replication. {ECO:0000269|PubMed:20383140}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20383140}. Note=Associates with chromatin during pre-replication complex (pre-RC) formation following interaction with topbp1. | null | null | null | null | null | FUNCTION: Regulator of DNA replication. Promotes initiation of chromosomal DNA replication by mediating topbp1- and cdk2-dependent recruitment of cdc45l onto replication origins. {ECO:0000269|PubMed:20383140}. | Xenopus laevis (African clawed frog) |
D3YUJ3 | CCYL1_MOUSE | METRIRAAQLKGRGGAFPKLGRRAGPAEPDYESEVYEAAAGDAVAVAPAPAAAVEPAELDFGAGEGHHLQHISDREMPEDLALESNPSDHPRASTIFLSKSQTDVREKRKSNHLNHVSPGQLTKKYSSCSTIFLDDSTVSQPNLRTTIKCVTLAIYYHIKNRDANRSLDIFDERSHPLTREKVPEEYFKHDPEHKFIYRFVRTLFSAAQLTAECAIVTLVYLERLLTYAEIDICPTNWKRIVLGAILLASKVWDDQAVWNVDYCQILKDITVEDMNEMERHFLELLQFNINVPASVYAKYYFDLRSLADDNNLNFLFAPLSKERAQNLEAISRLCEDKYKDLCRAAMRRSLSADNFIGIQRSNAILS | null | null | flagellated sperm motility [GO:0030317]; neurogenesis [GO:0022008]; regulation of canonical Wnt signaling pathway [GO:0060828]; regulation of protein phosphorylation [GO:0001932]; spermatogenesis [GO:0007283]; Wnt signaling pathway [GO:0016055] | membrane [GO:0016020]; plasma membrane [GO:0005886] | cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]; protein kinase binding [GO:0019901] | PF00134; | 1.10.472.10; | Cyclin family, Cyclin Y subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26305884, ECO:0000269|PubMed:26590424}. | null | null | null | null | null | FUNCTION: Key regulator of Wnt signaling implicated in various biological processes including male fertility, embryonic neurogenesis and cortex development (PubMed:26305884, PubMed:26590424, PubMed:34431536). Activates the cyclin-dependent kinase CDK16, and promotes sperm maturation (PubMed:26305884, PubMed:26590424). {ECO:0000269|PubMed:26305884, ECO:0000269|PubMed:26590424, ECO:0000269|PubMed:34431536}. | Mus musculus (Mouse) |
D3YVF0 | AKAP5_MOUSE | METSVSEIQVETKDEKGPVAASPQKERQERKTATLCFKRRKKANKTKPKAGSRTAEETKKHTPEAGGSGQRQPAGAWASIKGLVTHRKRSEPAKKQKPPEAEVQPEDGALPKKKAKSRLKFPCLRFSRGAKRSRHSKLTEDSGYVRVQGEADDLEIKAQTQPDDQAIQAGSTQGLQEGVLVRDGKKSQESHISNSVTSGENVIAIELELENKSSAIQMGTPELEKETKVITEKPSVQTQRASLLESSAAGSPRSVTSAAPPSPATTHQHSLEEPSNGIRESAPSGKDDRRKTAAEEKKSGETALGQAEEAAVGQADKRALSQAGEATAGHPEEATVIQAESQAKEGKLSQAEETTVAQAKETVLSQAKEGELSQAKKATVGQAEEATIDHTEKVTVDQAEETTVGQAEEATVGQAGEAILSQAKEATVVGQAEEATVDRAEEATVGQAEEATVGHTEKVTVDQAEEATVGQAEEATVGQAEEATVDWAEKPTVGQAEEATVGQAEEATVGHTEKVTVDQAEEATVGQAEEATVGHTEKVTVDHAEEATVGQAEEATVGQAEKVTVDHAEEATVGQAEEATVGQAEKVTVDHAEEATVGQAEEATVGQAEKVTVDQAEEPTVDQAEEAISSHAPDLKENGIDTEKPRSEESKRMEPIAIIITDTEISEFDVKKSKNVPKQFLISMENEQVGVFANDSDFEGRTSEQYETLLIETASSLVKNAIELSVEQLVNEMVSEDNQINTLFQ | null | null | amylase secretion [GO:0036394]; cellular response to calcium ion [GO:0071277]; cellular response to xenobiotic stimulus [GO:0071466]; clustering of voltage-gated calcium channels [GO:0070073]; clustering of voltage-gated potassium channels [GO:0045163]; establishment of localization in cell [GO:0051649]; gene expression [GO:0010467]; negative regulation of adenylate cyclase activity [GO:0007194]; negative regulation of monoatomic ion transport [GO:0043271]; negative regulation of potassium ion transport [GO:0043267]; positive regulation of calcineurin-NFAT signaling cascade [GO:0070886]; positive regulation of calcium ion import across plasma membrane [GO:1905665]; positive regulation of calcium ion transport into cytosol [GO:0010524]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein phosphorylation [GO:0001934]; postsynaptic neurotransmitter receptor cycle [GO:0099630]; protein-containing complex disassembly [GO:0032984]; receptor clustering [GO:0043113]; regulation of postsynaptic neurotransmitter receptor internalization [GO:0099149]; synapse assembly [GO:0007416] | asymmetric synapse [GO:0032279]; basolateral plasma membrane [GO:0016323]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendrite membrane [GO:0032590]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; dendritic spine membrane [GO:0032591]; excitatory synapse [GO:0060076]; filopodium membrane [GO:0031527]; glutamatergic synapse [GO:0098978]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic density, intracellular component [GO:0099092]; postsynaptic recycling endosome [GO:0098837]; postsynaptic recycling endosome membrane [GO:0098944]; protein serine/threonine phosphatase complex [GO:0008287] | actin binding [GO:0003779]; adenylate cyclase binding [GO:0008179]; beta-2 adrenergic receptor binding [GO:0031698]; cadherin binding [GO:0045296]; calmodulin binding [GO:0005516]; G protein-coupled receptor binding [GO:0001664]; GABA receptor binding [GO:0050811]; glutamate receptor binding [GO:0035254]; kinase binding [GO:0019900]; molecular adaptor activity [GO:0060090]; protein domain specific binding [GO:0019904]; protein kinase A regulatory subunit binding [GO:0034237]; protein kinase binding [GO:0019901]; protein phosphatase 2B binding [GO:0030346]; protein-containing complex binding [GO:0044877]; scaffold protein binding [GO:0097110]; SH3 domain binding [GO:0017124] | PF03832; | null | null | PTM: Palmitoylated. Palmitoylation at Cys-36 and Cys-123 play a key role in the targeting of AKAP5 to lipid rafts. Palmitoylation by ZDHHC2 is required for AKAP5 function in LTP-stimulated recycling endosome exocytosis. {ECO:0000250|UniProtKB:P24588}. | SUBCELLULAR LOCATION: Postsynaptic recycling endosome membrane {ECO:0000250|UniProtKB:P24588}; Lipid-anchor {ECO:0000250|UniProtKB:P24588}. Note=Associates with lipid rafts. {ECO:0000250|UniProtKB:P24588}. | null | null | null | null | null | FUNCTION: Multivalent scaffold protein that anchors the cAMP-dependent protein kinase/PKA to cytoskeletal and/or organelle-associated proteins, targeting the signal carried by cAMP to specific intracellular effectors. Association with the beta2-adrenergic receptor (beta2-AR) not only regulates beta2-AR signaling pathway, but also the activation by PKA by switching off the beta2-AR signaling cascade. Plays a role in long term synaptic potentiation by regulating protein trafficking from the dendritic recycling endosomes to the plasma membrane and controlling both structural and functional plasticity at excitatory synapses. Associates with ORAI1 pore-forming subunit of CRAC channels in Ca(2+) signaling microdomains where it recruits NFATC2/NFAT1 and couples store-operated Ca(2+) influx to calmodulin and calcineurin signaling and activation of NFAT-dependent transcriptional responses. {ECO:0000250|UniProtKB:P24588}. | Mus musculus (Mouse) |
D3YVL2 | CFA70_MOUSE | MDQTSSTTKIVHITVTNGYDLKGFKGDTPVTFVRAEFNQTVLGDSSKVTVSPEGTAKYNFTSNIDLSPDGGGALDDLAHKPLFLTVTEVLPKEKKQKDEKTLILGQAVVDLLPLLEGEESFETTVPLHPVPGSPLETPLPGSKQCSLDVKVFVAEPLLTPAQVSASNLLKVTLEAAYSVPESFIPVGPQQNYMVGLQVPSVGEKDYTMIFKNGNLKLGGEKEPVPRPKKWPIANILAPGASNIPDEFIVGGPYEEEEGELNHPEDREFRNQAECTKKRIVWDLESRCFLHPFAVASFQKRIADCRLWPVEITRVPLVVMPKAKPGKLEKIDDENQLSFHGVAYINMVPLLYPGVKKIRGAFHVYPYLDGTVFEKTKCLFSLFRDTGHHLVQNNKAGGLNSPLSKPLSKNLKEEKPGKDKDTEGRPRLGELQAPSIKSQSSDTPLESEAPLSHNLEGQQYIEAGTYIVLEIQLEKALVPKRMPEELARRVKEMIPPRPPLTRRTGGAQKAVSDYHTQIKSISRAILNEYYRMFGKQGPKLESDIDNETMEERKCQLNYELNCSGKYFAFKEQLKHAVVKIVREKYLKTTAFESQEELQTFISELYVFLVDQMHVALNQAVPDDVPSSTSTIQTSSEQLRLFAFEAEVNEKFEIAAMYYEERLVREPQNLENWLDYGAFCLLTEDNIKAQECFRKALSLNESHVDSLLLCGVLAILLENYEQAEIFFEDATCLEPTNVIAWTLLGLFYEIQNNDIRMEMAFHEAFKQLQARTLQTKLKSTVTIENMEEGVKVEPSFGPWGVVQESTTAIKTEGLSGMRPQSSHQLSPHTNMELHPQPQGPNTALSSLDEFLEESPKAQSESQEPMATGQPLEPSLVQRSSNALLKELTSKKDISKCQDSSAFSPPTQHVIAQPPVTIFMETIRFLMKVNAVQFVHRVLAHELLCPQGGPSCEYYLVLAQTHLLKKDFAKTEEYLQQAAQMDYLNPNVWGVKGHLYFLSGNHAEAKECYERTISFVVDASEMHFIFLRLGHIYLEEKEYENAKRTYMHACKRSPSCLTWLGLGIACYRLEELTEAEDALSEANALNNCNAEVWAYLALVCLKVGRQLEAEQAYKYTIKLKLKDQALLEEIHTVQEMVGFGNPSF | null | null | cilium assembly [GO:0060271]; cilium movement [GO:0003341] | axoneme [GO:0005930]; extracellular exosome [GO:0070062]; motile cilium [GO:0031514]; outer dynein arm [GO:0036157]; sperm flagellum [GO:0036126] | null | PF13181; | 1.25.40.10; | CFAP70 family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000269|PubMed:30158508}. Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000250|UniProtKB:Q5T0N1}. Cell projection, cilium {ECO:0000269|PubMed:30158508}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:30158508}. Note=Present all along the flagellum, with a marked signal at the base of the flagellum. {ECO:0000250|UniProtKB:Q5T0N1}. | null | null | null | null | null | FUNCTION: Axoneme-binding protein that plays a role in the regulation of ciliary motility and cilium length. {ECO:0000269|PubMed:30158508}. | Mus musculus (Mouse) |
D3YWP0 | EFMT3_MOUSE | MASSRTDPETEPESVFPREIRLFTDSYSESSRFCFCGHELSITQNFGSRLGVAARVWDAALSLCDYFESQNVDFRGKKVIELGAGTGIVGILAALQGGDVTITDLPVALEQIQDNVHANVPPGGRARVCALSWGIDQHVFPGNYDLVLGADIVYLEPTFPLLLGTLRHLCGPHGTIYLASKMRAEHGAETFFRRLLPQHFHLELAQRDEDVNVNIYRARHREVAPAGQHPFC | 2.1.1.- | null | peptidyl-lysine methylation [GO:0018022] | centrosome [GO:0005813]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; protein-containing complex [GO:0032991] | heat shock protein binding [GO:0031072]; histone methyltransferase activity [GO:0042054]; methyltransferase activity [GO:0008168]; protein-lysine N-methyltransferase activity [GO:0016279] | PF10294; | 3.40.50.150; | Methyltransferase superfamily, METTL21 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96AZ1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96AZ1}. | CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; Evidence={ECO:0000250|UniProtKB:Q96AZ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193; Evidence={ECO:0000250|UniProtKB:Q96AZ1}; CATALYTIC ACTIVITY: Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; Evidence={ECO:0000250|UniProtKB:Q96AZ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51737; Evidence={ECO:0000250|UniProtKB:Q96AZ1}; CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54196, Rhea:RHEA-COMP:13053, Rhea:RHEA-COMP:13827, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000250|UniProtKB:Q96AZ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54197; Evidence={ECO:0000250|UniProtKB:Q96AZ1}; CATALYTIC ACTIVITY: Reaction=N(6),N(6)-dimethyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:54200, Rhea:RHEA-COMP:13826, Rhea:RHEA-COMP:13827, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; Evidence={ECO:0000250|UniProtKB:Q96AZ1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54201; Evidence={ECO:0000250|UniProtKB:Q96AZ1}; | null | null | null | null | FUNCTION: Protein-lysine methyltransferase that selectively mono-, di- and trimethylates 'Lys-165' of the translation elongation factors EEF1A1 and EEF1A2 in an aminoacyl-tRNA and GTP-dependent manner (By similarity). EEF1A1 methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation (PubMed:28108655). {ECO:0000250|UniProtKB:Q96AZ1, ECO:0000269|PubMed:28108655}. | Mus musculus (Mouse) |
D3YWQ0 | DGKI_MOUSE | MDAAGRGCHLLPLPAARGPARAPAASSALSPTGLCSGTTSASFAAAGAVAMNPSSSAGEERGATGGSSSSGSGAGSCCLGAEGGADPRGAGAAAAAALEEPAAAGQKEKEEALEEKLRDLTFRKQVSYRKAISRTGLQHLAPAHPLGLPVANGPAKEPRATLDWSENAVNGEHLWLETNVSGDLCYLGEENCQVRFAKSALRRKCAVCKIVVHTACIEQLEKINFRCKPTFREGGSRSPRENFVRHHWVHRRRQEGKCKQCGKGFQQKFSFHSKEIVAISCSWCKQAFHNKVTCFMLHHIEEPCSLGAHAAVIVPPTWIIKVKKPQNSLKASNRKKKRTSFKRKASKRGTEQETKGRPFVIKPISSPLMKPLLVFVNPKSGGNQGTKVLQMFMWYLNPRQVFDLSQEGPKDALEMYRKVPNLRILACGGDGTVGWILSILDELQLSPQPPVGVLPLGTGNDLARTLNWGGGYTDEPVSKILCQVEDGTIVQLDRWNLHVERNPDLPPEELEDGVCKLPLNVFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGAAFSDFLQRSSRDLSKHVKVVCDGTDLTPKIQDLKFQCIVFLNIPRYCAGTMPWGNPGDHHDFEPQRHDDGYIEVIGFTMASLAALQVGGHGERLHQCREVMLLTYKSIPMQVDGEPCRLAPAMIRISLRNQANMVQKSKRRTSMPLLNDIHQVQAADLRRVSAPPGSFTIPQSVPDRLRIRVNKISLQDYEGLHYDKDKLREASIPLGILVVRGDCDLETCRMYIDRLQEDLQSVSSGSQRVHYQDQETSFPRALSAQRLSPRWCFLDATSADRFYRIDRSQEHLHFVMEISHDEIFILDPDMVVSQQAGTPPGMPDLVVEQASGLSDWWNPALRKRMLSDSGMITPHYEDSDLKDFSHSRVLQSPVSSEDHAILQAVLTGDLMKLMESYKNGGSLLIQGPGHCSLLHYAAKTGNGDIVKYILDHGPAELLDMADSETGETALHKAACQRNRAVCQLLVDAGASLRQTDSKGKTPQERAQQAGDPDLAAYLESRQNYKIIGHEDLETAV | 2.7.1.107 | null | diacylglycerol metabolic process [GO:0046339]; excitatory postsynaptic potential [GO:0060079]; habituation [GO:0046959]; intracellular signal transduction [GO:0035556]; lipid phosphorylation [GO:0046834]; neurotransmitter secretion [GO:0007269]; phosphatidic acid biosynthetic process [GO:0006654]; positive regulation of Ras protein signal transduction [GO:0046579]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; Ras protein signal transduction [GO:0007265]; regulation of long-term synaptic depression [GO:1900452]; regulation of synaptic transmission, glutamatergic [GO:0051966] | axon terminus [GO:0043679]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; excitatory synapse [GO:0060076]; extrinsic component of postsynaptic density membrane [GO:0099147]; extrinsic component of presynaptic active zone membrane [GO:0098891]; glutamatergic synapse [GO:0098978]; guanyl-nucleotide exchange factor complex [GO:0032045]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; postsynaptic density [GO:0014069]; presynaptic active zone [GO:0048786]; protein-containing complex [GO:0032991]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202]; synaptic membrane [GO:0097060]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672] | ATP binding [GO:0005524]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; GTPase inhibitor activity [GO:0005095]; metal ion binding [GO:0046872]; small GTPase binding [GO:0031267] | PF12796;PF00130;PF00609;PF00781; | 2.60.200.40;3.30.60.20;1.25.40.20; | Eukaryotic diacylglycerol kinase family | null | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000250|UniProtKB:F1MAB7}. Cell projection, dendrite {ECO:0000250|UniProtKB:F1MAB7}. Presynapse {ECO:0000250|UniProtKB:F1MAB7}. Postsynapse {ECO:0000250|UniProtKB:F1MAB7}. Postsynaptic density {ECO:0000250|UniProtKB:F1MAB7}. Synaptic cell membrane {ECO:0000250|UniProtKB:F1MAB7}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:F1MAB7}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O75912}. Nucleus {ECO:0000250|UniProtKB:O75912}. Note=Excluded from inhibitory synapses (By similarity). Localization between cytoplasm and nucleus is regulated by protein kinase C (By similarity). Both in the detergent soluble and particulate fractions (By similarity). {ECO:0000250|UniProtKB:F1MAB7, ECO:0000250|UniProtKB:O75912}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107; Evidence={ECO:0000250|UniProtKB:O75912}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273; Evidence={ECO:0000250|UniProtKB:O75912}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O75912}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328; Evidence={ECO:0000250|UniProtKB:O75912}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O75912}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324; Evidence={ECO:0000250|UniProtKB:O75912}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + ATP = 1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40339, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77097, ChEBI:CHEBI:77098, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:F1MAB7}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40340; Evidence={ECO:0000250|UniProtKB:F1MAB7}; | null | PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000250|UniProtKB:O75912}. | null | null | FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Has probably no preference for any of the diacylglycerols in terms of the acyl chain composition, especially for the acyl chain at the sn-2 position (By similarity). By controlling the diacylglycerol/DAG-mediated activation of RASGRP3, negatively regulates the Rap1 signaling pathway (PubMed:15894621). May play a role in presynaptic diacylglycerol/DAG signaling and control neurotransmitter release during metabotropic glutamate receptor-dependent long-term depression (PubMed:21119615). {ECO:0000250|UniProtKB:O75912, ECO:0000269|PubMed:15894621, ECO:0000269|PubMed:21119615}. | Mus musculus (Mouse) |
D3YXG0 | HMCN1_MOUSE | MIAQEVVHTVFLVALFRSSLAGDGTPQSESRAEEIPEGASTLAFVFDVTGSMYDDLVQVIEGASKILETSLKRPKRPLYNFALVPFHDPEIGPVTITTDPKKFQYELRELYVQGGGDCPEMSIGAIKIALEISLPGSFIYVFTDARSKDYRLTHEVLQLIQQKQSQVVFVLTGDCDDRNHIGYKVYEEIASTSSGQVFHLDKKQVNEVLKWVEEAVQASKVHLLSTDHLEHAVNTWKIPFDPSLKEVTVSLSGPSPVIEIRNPFGKLIKKGFGLNELLNIHNSAKVVNVKEPEAGMWTVKTSSSGRHSVRITGLSTIDFRAGFSRKPTLDFKKTMSRPVQGIPTYVLLNTSGISSPARVDRLELLSISGGSLKTIPVKHYPDRKPYGIWNISDFIPPDEAFFLKVTGYDKDGYLFQRVSSVSFSSIVPDAPKVTMPTRTLGYYLQPGQILCSVESFLPFTLSFMRDGIALGVDQYLRESASVNWDFTKVTLSDEGFYDCIAVSSAGTGRAQTFFDVSEPPPIIQLPNNVTVTPGERAVLACLVISAVDYNLTWQRSGRDIRLADSARIRTLANLSLELRSVKIGDAGEYRCVVSSEGGSAAASVFLTVQEKPKVTVMPKNQSFTGGSEISIMCSATGYPKPKIVWTMNEMFIMGSHRYRMTSEGTLFIKNAVPKDAGTYACLASNAAGTDKQTSTLRYIEAPKLVVEQSELLVALGDTTVMECKTSGIPPPQVKWFKGDLELRPSTFLSIDPLVGLLKIQETQDLDAGDYTCVAINEAGRATGRLTLDVGSPPVFIQEPSDVAVEIGSNVTLPCYVQGYPEPKIKWRRLDNMPVFSRPFSVSFISQLRTGALFISNLWASDKGTYICEAENQFGKIQSQTTVTVTGLVAPLIGISPSMASVIEGQPLTLPCTLLAGNPIPERRWMKNSAMLVQNPYITVRSDGSLHIERVRLQDGGKYTCVASNVAGTNNKTTSVAVHVLPSIQHGQQILSTIEGVPVTLPCRASGIPKPSITWSKKGELISTSSAKFSAGADGSLYVVSPGSEESGEYICTATNAAGYAKRKVQLTVYVRPRVFGDQRGLSQDKPVEISVLAGEEAILPCEAKSLPPPIITWAKDSQLISPFSPRHTFLPSGSMKITETRVSDSGMYLCVATNIAGNVTQSVKLSVHVPPKIQHGNRHIKVQVGQRVDILCNAHGSPPPVITWFKSGRPFLDGAQHPGSPDGTLSIEQAVISDAGVYTCAATNIAGSDEAEVTLHVQEPPSVEDLQPPFNTPFQERLANQRIEFPCPAKGTPKPTIKWLHNGREVTGQEPGVSILEDGALLVIASVTPHNNGEYICVAVNEAGTTERKYNLKVHVPPVIRDKEHVTNVSVLTSQLASLYCEVEGTPSPVITWYKDDIQVTESSTVQIVNNGKILKLFKVSAEDAGRYSCKAINIAGTSQKDFSVNVLVPPSILGASSPSEVSVVLNHNVTLQCPGTGVPFPAIHWFKDGKPLFLGDPNIELSDRGQSLHLRNARRSDKGRYQCTVSNAAGKQAKDIKLTVYVPPSIKGGNITTEISALLNSIVKLECETRGLPVPAITWYKDGQVVTSSSQALYIDKGQLLHIQRAQVSDSATYTCHAANVAGTAEKSFHVDIYVPPTIEGDLTAPSNKQVIIGQSLILECKAAGNPPPILTWLKDGVPVKASDNIHIEAGGKKLEILSALEVDRGQYICVATSVAGEREIKYEVDVLVPPAVEGGEETSYFIVLANNLLELDCQVSGSPPPTIMWLKGGQLIDERDGFKILLNGRKLVIAQAQVSDTGLYQCVATNIAGDHRKEFEVTVHVPPTIKSSDLPEKTVVRYKPVTLQCIANGIPNPSITWLKDDQPVNTAHGNLKIQSSGRVLQIAKALLEDAGRYTCVATNAAGEAHQHTQLHVHEPPSLDDAGKMRNETVVVNNPIQLECKATGKPLPVITWYKDSHPLSGSASAAFLKRGQVLEIGSAQISDAGIYKCVAINSAGATELFYSLQVHVPPSISGSSSMVEVVVNNLARLECEARGIPAPSLTWLKDGSPVSSFSNGIQILSGGRILALTSAQMSDAGRYTCVAVNAAGEKQRDIDLRVYAPPNIMGEEQNVSVLIGQAVELFCQSDAVPPPTLMWLKDGRPLLKRPGLSISENGSVLKIEDAQAGDTGRYTCEATNVAGKTEKNYNVNVWVPPSIYGSDELVQLTAIEGNLITLLCESSGIPPPDLTWKKKGSLVLADSAGRVHILSGGRRLQISIAEKADAGLYTCVASNVAGVAKKEYNLQVYIRPSITNSGGHRPEITVIRGKSISLECEVQGIPQPTVTWMKDGRPLTKGKGVEILDEGRILQLKNVHVSDTGRYVCVAVNVAGMTDKRYDLSVHAPPSIIGNHGVPENVSVVEKSSVSLTCEASGIPLPSITWLKDGWPVNLGSSVKILSGGRMLRLMQTRPEDAGQYTCIVRNAAGEDRKMFGLSVLVPPHIVGENTLEDVKIKEKQSVTLTCEVRGNPVPQITWHKDGQLLQEDEAHHMMSGGRFLQITNAQVSHTGRYTCLASNIAGDKSKSFRLNVFVSPTIAGVDSDGSPEDVIVILNSPTSLVCEAYSYPPATITWFKDGTPLESNRNIRILPGGRTLQILNAQEDNAGRYSCVATNEAGEKIKHYEVKVYIPPIIKKGDLLGPGLSPKEVKIRVNSSLTLECEAYAIPSASLRWYKDGQPLKSDDHVTIAASGHTLQIKEAQISDTGRYTCVASNLAGEDELDFDVNIQVPPSFQKLWEIGNMLDTGRSGEAKDVIINNPLSLHCETNAAPPPTLTWYKDGRPLTSSDRVLILPGGRVLQIPRAKVEDAGRYTCVAVNEAGEDSLRYDVHVLLPPVIKGANSDLPEEVTVLVNKSTQMECSSSGNPAPRNYWQKDGQILLEDEHHKFQSDGRSLQILNAQITDTGRYVCVAENTAGSAKKYFNLNVHVPPSVIGPNHEHLSVVVNHFISLNCEVSGFPPPDLSWLKNEEPIKPNTNVLTVPGGRTLQIIRAKISDGGDYTCIAINQAGESKKKVSLTVHVPPSIKDHGSQSLSIVNVREGTSVSLECESNAVPPPVITWSKNGRMIPDSTNVEILTGGQTLHIRRAEVSDTGQYVCRAINVAGRDDKNFHLNVYVPPTIEGPETEVIVETISNPVTLTCDATGIPPPTITWLKNHKPIENSDPLEVHILSGGSKLQIARPQRSNSGNYTCVASNMEGKAQKNFILFIQVPPSVAGAEVPSEVSVLLGENVELVCNADGIPTPHLQWLRDGKPIVNGETERVRVTTDGSTLNIYRALTSDMGKYTCVATNPAGEEDRIFNLNVYVPPKIRGNKEEAEKLMALVDTSINIECKATGTPPPQINWLKNGLPLPISSHIRLLSAGQVVRIVRAQVSDIAVYTCVASNRAGVDSKHYSLQVFVPPNMDNAMGTEEITIVKGSSTSMTCFTDGTPAPSMSWLRDGQPLAPDAHLTVSTQGMVLQLIKAETEDTGKYTCVATNEAGEVSKHFVLKVLEPPHINGSEGPGEVSVIVNNPLELSCIASGIPAPKISWMKDGRPFLQTEQVQTLEGGAILRVSSAQVEDTGRYTCLASSPAGDDDKEYLVRVHVPPNIAGMDEAQDFTVLRNRQVTLECKSDAVPPPVIMWLKNREQLQATPRVRILSGGRYLQINNADLGDTANYTCVASNIAGKTTREFNLTVNVPPSIGGGPQSLVTLLNKSIALECRAEGVPAPRITWRKDGVVLAESHARYSILENGFLHIESAHVTDTGRYLCMATNVAGTDRRRIDLQVHVPPSIAMGPTNVTVTVNVQTTLACEATGIPKPSVTWRKNGHLLNVDQNQNSYRLLSSGSLVIISPSVDDTASYECTVTSDAGEDKRAVDLTVQVPPTIADEPMDFLVTRQAPAVMTCSASGVPVPSIHWTKNGLRLLPRGDGYRILSSGAIEIPTTQLNHAGRYTCVARNAAGSAHRHVTLRVQEPPVIQPQPSELDVILNNPILLPCEATGIPTPFITWQKEGINVITSGKSLAILPSGSLQISRAVRGDAGTYMCVAQNPAGTALGKVKLNVQVPPVISSHQKEYVVTMDKPVSLLCETEGSPPPDITWHKDGHALTESIRQRILNSGALQIAFAQPDDAGQYTCMAANMAGSSSVSSTLTVHVPPRIQSTEVHFTVNENSQAVLPCVADGIPTPAIHWEKDGVLIANLLGKYTAQPYGELILENVVLEDSGTYTCVANNAAGEDTRIVTLAVHTLPTFTELPGDLSLNKGEQLRLSCKAVGIPLPKLTWTFNNNIIPAHFDSINGHSELVIEKVSKEDSGTYVCTAENSVGFVKAIGFVYVKEPPVFKGDYPSNWIEPLGGNAILNCEVKGDPAPTIQWSRKGADIEISHRIRQLGNGSLAIYGTVNEDAGDYTCVAANEAGMVERSMSLTLQSSPIITLEPVETVVDAGGRVILDCQAAGEPQPTITWSRQGQPISWDNRLSMLPNSSLYIAAARKEDTSEYECVARNLMGSVLVRVPVIVQVHGGFSLWSAWRPCSVTCGKGIQKRSRLCDNPPPANGGRPCQGADSEARHCHNKLCPVDGHWSEWSFWEDCSRSCGHGNQTRTRTCSNPPAQHGGRPCEGHAVETIMCNIRPCPVHGVWNAWQPWSACSKSCGKGSQTRMRLCNNPPPSFGGAHCSGAETQMQVCNERHCPVDGRWATWSSWSACTVSCGGGARKRTRDCSDPVPQYGGNKCEGTGVQSDFCNSDPCPTHGNWSPWSGWGTCSRTCNGGQMRRYRTCDNPRPSNGGRACGGPDTQIQRCNTDMCPVDGSWGTWHSWSHCSVSCGGGERTRKRLCDNPVPTKGGRSCPGDATQVSRCNMQACPGGPQRARGSVIGNINDIEFGIAFLNATITDSPNTDTRVIQAKITNVPRSLGPAMRKIISILNPIYWTTAKEIGEAVNGFTLTNAVFKRETQVEFATGEVLRMTHVARGLDSDGALLLDVIVSGQVLQLHSPAEVGVKDYTEDYIQTGPGQLYAYSTRLFTIDGISIPYTWNHTIFYDQAWGKMPFLVETLHASSIESDYNQLEETLGFKIHASISKGDRSNQCPSGFILDSVGPFCADEDECTAGNPCSHTCHNAIGAYYCSCPKGLTIAADGRTCQDIDECALGGHTCRAGQDCDNTIGSYRCVVHCGTGFRRTSDGLSCQDINECQESSPCHQRCFNVIGSFHCGCEAGYQLKGRKCIDVNECRQNVCRPDQHCKNTRGGYKCIDLCPSGMTKAENGTCIDIDECKDGTHQCRYNQICENTRGSYRCACPRGYRSQGVGRPCIDINECEQVPKPCAHQCSNSPGSFKCICLPGQQLLGDGKSCAGLERLSNYGTQYSSYTLERFSPVRSDYQPSQHYRQYSQLYSSYSEYRNSRASFSRNRRTIRKTCPEGSEANHETCVDIDECQNRDTCQHECKNTIGSYQCVCPPGYRLMLNGKTCQDVDECLEQNVRCGPNRMCFNMRGSYQCIDTPCPPNYQRDPVLGFCLKNCPPNDLECTLSPYALEYKLVSLPFGIAANQDLIRLVAYTQDGVMHPRTTFLMIDEEPAVPFALRDENLKGVVYTTRPLREAETYRMKVGALSYSANGTIEYQTTFIVYIAVSAYPY | null | null | actin cytoskeleton organization [GO:0030036]; basement membrane organization [GO:0071711]; cell cycle [GO:0007049]; cell division [GO:0051301]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; response to bacterium [GO:0009617]; synapse organization [GO:0050808] | adherens junction [GO:0005912]; axon [GO:0030424]; basement membrane [GO:0005604]; cell cortex [GO:0005938]; cell junction [GO:0030054]; cleavage furrow [GO:0032154]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; muscle tendon junction [GO:0005927]; neuronal cell body [GO:0043025] | axon guidance receptor activity [GO:0008046]; calcium ion binding [GO:0005509] | PF12662;PF07645;PF07474;PF07679;PF13927;PF00090; | 2.40.155.10;2.60.40.10;2.10.25.10;2.20.100.10;3.40.50.410; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:17015624, ECO:0000269|PubMed:24951538, ECO:0000269|PubMed:29488390, ECO:0000269|PubMed:32035013, ECO:0000269|PubMed:34504132}. Cytoplasm {ECO:0000269|PubMed:17015624, ECO:0000269|PubMed:29488390}. Cell junction {ECO:0000269|PubMed:17015624}. Cleavage furrow {ECO:0000269|PubMed:21215633}. Note=Has been detected in the glomerular basement membrane in one study (PubMed:29488390). However, another study found expression in the glomerular mesangial matrix but not in the glomerular basement membrane (PubMed:32035013). The antibody used in PubMed:17015624 and PubMed:21215633 to determine subcellular location does not distinguish between HMCN1 and HMCN2 (PubMed:17015624, PubMed:21215633). {ECO:0000269|PubMed:17015624, ECO:0000269|PubMed:21215633, ECO:0000269|PubMed:29488390, ECO:0000269|PubMed:32035013}. | null | null | null | null | null | FUNCTION: Involved in transforming growth factor beta-mediated rearrangement of the podocyte cytoskeleton which includes reduction of F-actin fibers and broadening, flattening and elongation of podocytes (By similarity). Plays a role in basement membrane organization (PubMed:34504132). May promote cleavage furrow maturation during cytokinesis in preimplantation embryos (PubMed:21215633). May play a role in the architecture of adhesive and flexible epithelial cell junctions (PubMed:17015624). May play a role during myocardial remodeling by imparting an effect on cardiac fibroblast migration (PubMed:24951538). {ECO:0000250|UniProtKB:Q96RW7, ECO:0000269|PubMed:17015624, ECO:0000269|PubMed:21215633, ECO:0000269|PubMed:24951538, ECO:0000269|PubMed:34504132}. | Mus musculus (Mouse) |
D3YXJ0 | DGKH_MOUSE | MAGAGSQHHPQGVAGGAVAGASAVSPTAAGPGEDSSDSEAEQEGPQKLIRKVSTSGQMRTKTSIKEGQLLKQTSSFQRWKKRYFKLRGRTLYYAKDSKSLIFDEVDLSDASVAEASTKNANNSFTIITPFRRLMLCAENRKEMEVWISSLKSVQSREPYEVAQFNVEHFSGMHNWYACSHARPTFCNVCRESLSGVTSHGLSCEVCKFKAHKRCAVRATNNCKWTTLASIGKDIIEDEDGVAMPHQWLEGNLPVSAKCAVCDKTCGSVLRLQDWKCLWCKTMVHTACKDVYHPVCPLGQCKVSIIPPIALNSTDSDGFCRATFSFCVSPLLVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPYLGLRLFQKFDNFRILVCGGDGSVGWVLSEIDKLNLHKQCQLGVLPLGTGNDLARVLGWGGSYDDDTQLPQILEKLERASTKMLDRWSIMTYELKLPAKSSLLPEPVAATEEFYMTIYEDSVANHLTKIVNSDEHAVVISSAKILCETVKDFVAKVEKAQDRTLENTVVAEAVASKCSVLNEKLEQLLQALHADSQASRVPPGIGPAIPEEDTVESASDESLGESKDQLVNDIGKPSSQKAVKPREIMLRANSLKKAVRQVIEEAEKVMDEPAVQPSEPVSPSCDYDTETDEAKEDDAKESLSAKTTSQSPDAQASCGHPQTDSVAGPAMATTKENLPVLNTRIICPGLRAGLAASIAGSSIINKMLLANIDPFGATPFIDPDLDSLDGYSEKCVMNNYFGIGLDAKISLEFNNKREEHPEKCRSRTKNLMWYGVLGTRELLQRSYKNLEQRVQLECDGQYIPLPSLQGIAVLNIPSYAGGTNFWGGTKEDDIFAAPSFDDKILEVVAVFDSVQMAVSRVIKLQHHRIAQCRTVKITIFGDEGVPVQVDGEAWVQPPGIIKIVHKNRAQMLTRDRAFESTLKSWEDKQKCDSGKPVLRTNLYIHPAPDLATEEVSQMRLCSQAAEELITRICDAATIHCLLEQELAHAVNACSHALNKANPRFPESLTRDTATEIAINVKALYNETEALLVGRVPLHLESPHEERVSSALHSVEMELQKLTEIPWLYYILRPSEDEEPPLDCTKRNNKSTVFRIVPKFKKEKAQKQKTSSQPVQNWGTEEVAAWLDLLNLGEYKEIFIRHDVRGAELLHLERRDLKDLGIPKVGHMKRILQGIKELERNPPNLV | 2.7.1.107 | null | diacylglycerol metabolic process [GO:0046339]; intracellular signal transduction [GO:0035556]; lipid phosphorylation [GO:0046834]; phosphatidic acid biosynthetic process [GO:0006654]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205] | actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; endosome [GO:0005768]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803] | PF00130;PF00609;PF00781;PF00169;PF07647; | 2.60.200.40;3.30.60.20;2.30.29.30;1.10.150.50; | Eukaryotic diacylglycerol kinase family | PTM: Phosphorylated. Phosphorylation does not inhibit catalytic activity. {ECO:0000250|UniProtKB:Q86XP1}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27643686}. Cell membrane {ECO:0000269|PubMed:27643686}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:27643686}. Note=Translocated from the cytoplasm to endosomes in response to stress stimuli. Isoform 2 is rapidly relocated back to the cytoplasm upon removal of stress stimuli, whereas isoform 1 exhibits sustained endosomal association. Translocates from the cytoplasm to the cell membrane in the presence of active GTP-bound form of HRAS. {ECO:0000250|UniProtKB:Q86XP1}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107; Evidence={ECO:0000269|PubMed:27643686}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273; Evidence={ECO:0000305|PubMed:27643686}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:27643686}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328; Evidence={ECO:0000305|PubMed:27643686}; | null | PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000305|PubMed:27643686}. | null | null | FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids (PubMed:27643686). Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (Probable). Plays a key role in promoting cell growth. Activates the Ras/B-Raf/C-Raf/MEK/ERK signaling pathway induced by EGF. Regulates the recruitment of RAF1 and BRAF from cytoplasm to membranes and their heterodimerization (By similarity). {ECO:0000250|UniProtKB:Q86XP1, ECO:0000269|PubMed:27643686, ECO:0000305}. | Mus musculus (Mouse) |
D3YXK1 | SAMD1_MOUSE | MAGPPALPPPETAAAATTAAAASSSAASPHYQEWILDTIDSLRSRKARPDLERICRMVRRRHGPEPERTRAELEKLIQQRAVLRVSYKGSISYRNAARVQPPRRGATPPAPPRVPRGGPAAPPPTPAPPPAPVAAPTRAPRAAAATAPPSPGPAQPGPRAQRAAPLAAPPPAPAAPPAAAPPAGPRRAPPPAVAAREPPAPPQQQQPPPPQPQPPPEGGAARAGGPARPVSLREVVRYLGGSGGASGRLTRGRVQGLLEEEAARGRLERTRLGALALPRGDRPGRAPPAASARAARSKRGGEERVFEKEEEDEDEDEEEEEEDNVSEGSEVPESDRPAGAQHHQINGERGPQSAKERVKEWSPCGPYQGQDEGRGPAPGSCTRQVFPMTAVNKEGGSACVGAAPDSPSPVPLPPGKPALPGADGTPFGCPPGRKEKPTDPVEWTVMDVVEYFTEAGFPEQATAFQEQEIDGKSLLLMQRTDVLTGLSIRLGPALKIYEHHIKVLQQGHFEDDDPDGLLG | null | null | chromatin organization [GO:0006325]; foam cell differentiation [GO:0090077]; lipoprotein lipid oxidation [GO:0034439]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein homooligomerization [GO:0051260]; regulation of DNA methylation-dependent heterochromatin formation [GO:0090308] | chromosome [GO:0005694]; extracellular space [GO:0005615]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; low-density lipoprotein particle binding [GO:0030169] | PF00536;PF21524; | 1.10.150.50; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33980486}. Chromosome {ECO:0000269|PubMed:33980486}. Secreted {ECO:0000269|PubMed:34006929}. Note=In atherosclerotic lesions, it is found in the extracellular compartment and in foam cells cytoplasm. {ECO:0000269|PubMed:34006929}. | null | null | null | null | null | FUNCTION: Unmethylated CpG islands (CGIs)-binding protein which localizes to H3K4me3-decorated CGIs, where it acts as a transcriptional repressor (PubMed:33980486, PubMed:34006929). Tethers L3MBTL3 to chromatin and interacts with the KDM1A histone demethylase complex to modulate H3K4me2 and H3K4me3 levels at CGIs (PubMed:33980486). Plays a role in atherogenesis by binding with LDL on cell surface and promoting LDL oxidation which leads to the formation of foam cell (PubMed:34006929). {ECO:0000269|PubMed:33980486, ECO:0000269|PubMed:34006929}. | Mus musculus (Mouse) |
D3YXK2 | SAFB1_MOUSE | MAETLSGLGDASAAGAAAVSSAASETGTRRLSDLRVIDLRAELKKRNLDSSGNKSVLMERLKKAIEDEGGNPDEIEVTSECNKKMPKRPSKGRKPEDEGVEDNGLEENSGDGQEDVETSLENLQDMDMMDISVLDEADIDNGSVADCVEEEEEATLPEGLADSTELVEGDLKGLPEQLQEHAIDDKDTVNNVDTSSSDFTMLQEMEEASLEPENEKILDILGETCKSEPVKEEGSELEQPFAQATSSVGPDRKLAEEEDLFESCGHPEEEEEEEEEDQEEEQEEEGDLALASSSKSESPSTRCQWSEADAPLAVVKREPADAPGGGTGMDREPVGLEEPVEQSSTAAQLPEATSQELVRAPTAALSPEPQDSKEDVKKFAFDACNDVPAPPKESSASEGADQKMSSVEEDSDTKRLSREEKGRSSCGRNFWVSGLSSTTRATDLKNLFSRYGKVVGAKVVTNARSPGARCYGFVTMSTAEEATKCISHLHKTELHGKMISVEKAKSEPTGKRVPDRRDGDSKKEKASTSDRSANLKREEKGERKDDAKKTDDGSTEKSKDADDQKPGPSERSRTTKSGSRGTERTVVMDKSKGVPVISVKTSGSKERASKSQDRKSASREKRSVVSFDKVKESRKSRDSESRRERERSEREQRLQAQWEREERERLEIARERLAFHRHRLERERMERERLERERMHVEQERRREQERIHREREELRRQQELRYEQERRPAVRRPYEVDGRRDDAYWPEAKRAALDDRYHSDFSRQDRFHDFDHRDRGRYPNHSVDRREGSRSMMGDREGQHYPERHGGPERHGRDSRDGWGYGSNKRLSEGRGLPPPPRRDWGEHGRRLEDDRAWQGTADGGMMERDHKRWQGGERSMSGHSGPGHMMNRGGMSGRGSFAPGGASRGHVIPRGGMQAGFGGQSRGSRPSDARFTRRY | null | null | hormone metabolic process [GO:0042445]; intracellular estrogen receptor signaling pathway [GO:0030520]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of growth [GO:0040008]; regulation of mRNA processing [GO:0050684]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | chromatin binding [GO:0003682]; RNA binding [GO:0003723]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF00076;PF02037; | 3.30.70.330;1.10.720.30; | null | PTM: Sumoylated by PIAS1 with SUMO1 and SUMO2/3, desumoylated by SENP1. Sumoylation is required for transcriptional repressor activity. {ECO:0000250|UniProtKB:Q15424}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15424}. | null | null | null | null | null | FUNCTION: Binds to scaffold/matrix attachment region (S/MAR) DNA and forms a molecular assembly point to allow the formation of a 'transcriptosomal' complex (consisting of SR proteins and RNA polymerase II) coupling transcription and RNA processing (By similarity). Functions as an estrogen receptor corepressor and can also bind to the HSP27 promoter and decrease its transcription (By similarity). Thereby acts as a negative regulator of cell proliferation (By similarity). When associated with RBMX, binds to and stimulates transcription from the SREBF1 promoter (PubMed:19403048). {ECO:0000250|UniProtKB:Q15424, ECO:0000269|PubMed:19403048}. | Mus musculus (Mouse) |
D3YYI7 | RN217_MOUSE | MGEEQSTVSGSGGARASGGGSAGQPESPRPRGDRVRTAGPRAAASSSRPNGGGGGRDPGCVDASVQEPASNRAPAGQPARLPLSGPLDPQSLELQLEREAEGAGPREAPPGQQPPDGLLLDVLAQRHPPPAKPQVLCSVYCVESDLPEAPSAESPSPSESPPQAPLGPIPASPPPSFPSSPLSLPADPLSPDGGSIELEFYLAPEPFSVPGLLGAPPYSGLGGVGDPYAPLMVLMCRVCLEDKPIKPLPCCKKAVCEECLKIYLSSQVQLGQVEIKCPVTECFEFLEETTVVYNLTHEDSIKYKYFLELGRIDSSTKPCPQCKHFTTFKKKGHIPTPSRSESRYKIQCPTCQLIWCFKCHSPWHEGVNCKEYKKGDKLLRHWASEIEHGQRNAQKCPKCKIHIQRTEGCDHMTCSQCNTNFCYRCGERYRQLRFFGDHTSNLSIFGCKYRYLPERPHLRRLVRGSVCAGKLFIAPLILVLGLALGAIAVVIGLFVFPIYCLCKKQRKRSRTGMHW | 2.3.2.31 | null | positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein polyubiquitination [GO:0000209]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; membrane [GO:0016020]; ubiquitin ligase complex [GO:0000151] | ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF01485; | 1.20.120.1750;3.30.40.10; | RBR family, RNF217 subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q8TC41}. | CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000269|PubMed:33895792}; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates the degradation of the iron exporter ferroportin/SLC40A1 and thus regulates iron homeostasis. {ECO:0000269|PubMed:33895792}. | Mus musculus (Mouse) |
D3YZU1 | SHAN1_MOUSE | MTHSPATSEDEERHSASECPEGGSESDSSPDGPGRGPQGTRGRGSGAPGNLASTRGLQGRSMSVPDDAHFSMMVFRIGIPDLHQTKCLRFNPDATIWTAKQQVLCALSESLQDVLNYGLFQPATSGRDANFLEEERLLREYPQSFEKGVPYLEFRYKTRVYKQTNLDEKQLAKLHTKTGLKKFLEYVQLGTSDKVARLLDKGLDPNYHDSDSGETPLTLAAQTEGSVEVIRTLCLGGAHIDFRARDGMTALHKAACARHCLALTALLDLGGSPNYKDRRGLTPLFHTAMVGGDPRCCELLLYNRAQLGIADENGWQEIHQACQRGHSQHLEHLLFYGAEPGAQNASGNTALHICALYNKETCARILLYRGANKDVKNNNGQTPFQVAVIAGNFELGELIRNHREQDVVPFQESPKYAARRRGPPGAGLTVPPALLRANSDTSMALPDWMVFSAPGASSSGTPGPTSGSQGQSQPSAPSTKLSSGTLRSASSPRGARARSPSRGRHPEDAKRQPRGRPSSSGTPRDGPAGGTGGSGGPGGSLGSRGRRRKLYSAVPGRSFMAVKSYQAQGEGEISLSKGEKIKVLSIGEGGFWEGQVKGRVGWFPSDCLEEVANRSQEGRQESRSDKAKRLFRHYTVGSYDSFDAPSLIDGIDSGSDYIIKEKTVLLQKKDSEGFGFVLRGAKAQTPIEEFTPTPAFPALQYLESVDEGGVAWRAGLRMGDFLIEVNGQNVVKVGHRQVVNMIRQGGNTLMVKVVMVTRHPDMDEAVHKKASQQAKRLPPPAISLRSKSMTSELEEMVSPWKKKIEYEQQPAAVPSMEKKRTVYQMALNKLDEILAAAQQTISASESPGPGGLASLGKHRPKGFFATESSFDPHHRSQPSYDRPSFLPPGPGLMLRQKSIGAAEDDRPYLAPPAMKFSRSLSVPGSEDIPPPPTTSPPEPPYSTPPAPSSSGRLTPSPRGGPFNPGSGGPLPASSPSSFDGPSPPDPRSGGREKSLYHSGALPPAHHHPPHHHHHHAPPPQPHHHHAHPPHPPEMETGGSPDDPPPRLALGPQPSLRGWRGGGPSPTSGAPSPSHHSSSGGSSGPAQAPALRYFQLPPRAASAAMYVPARSGRGRKGPLVKQTKVEGEPQKGSLPPASSPTSPALPRSEPPPAGPSEKNSIPIPTIIIKAPSTSSSGRSSQGSSTEAEPPTQPDGAGGGGSSPSPAPATSPVPPSPSPVPTPASPSGPATLDFTSQFGAALVGAARREGGWQNEARRRSTLFLSTDAGDEDGGDSGLGPGAPPGPRLRHSKSIDEGMFSAEPYLRLESGGSSGGYGAYAAGSRAYGGSGSSSAFTSFLPPRPLVHPLTGKALDPASPLGLALAARERALKESSEGGVTPQPPPRPPSPRYDAPPPTLHHHSPHSPHSPHARHEPVLRLWGDPARRELGYRAGLGSQEKALTASPPAARRSLLHRLPPTAPGVGPLLLQLGPEPPTPHPGVSKAWRTAAPEEPERLPLHVRFLENCQARPPPAGTRGSSTEDGPGVPPPSPRRVLPTSPTSPRGNEENGLPLLVLPPPAPSVDVDDGEFLFAEPLPPPLEFSNSFEKPESPLTPGPPHPLPDPPSPATPLPAAPPPAVAAAPPTLDSTASSLTSYDSEVATLTQGAPAAPGDPPAPGPPAPAAPAPPAPQPGPDPPPGTDSGIEEVDSRSSSDHPLETISSASTLSSLSAEGGGNTGGVAGGGAGVASGTELLDTYVAYLDGQAFGGSGTPGPPYPPQLMTPSKLRGRALGTSGNLRPGPSGGLRDPVTPTSPTVSVTGAGTDGLLALSACSGPSTAGVAGGPVAVEPEVPPVPLPTASSLPRKLLPWEEGPGPPPPPLPGPLSQPQASALATVKASIISELSSKLQQFGGASTAGGALPWARGGSGGSTDSHHGGASYIPERTSSLQRQRLSEDSQTSLLSKPSSSIFQNWPKPPLPPLPTGSGVSSSTAAAPGATSPSASSASASTRHLQGVEFEMRPPLLRRAPSPSLLPASDHKVSPAPRPSSLPILPSGPLYPGLFDIRSSPTGGAGGSADPFAPVFVPPHPGISGGLGGALSGASRSLSPTRLLSLPPDKPFGAKPLGFWTKFDVADWLEWLGLSEHRAQFLDHEIDGSHLPALTKEDYVDLGVTRVGHRMNIDRALKFFLER | null | null | adult behavior [GO:0030534]; associative learning [GO:0008306]; dendritic spine morphogenesis [GO:0060997]; determination of affect [GO:0050894]; habituation [GO:0046959]; long-term memory [GO:0007616]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of actin filament bundle assembly [GO:0032232]; neuromuscular process controlling balance [GO:0050885]; olfactory behavior [GO:0042048]; positive regulation of dendritic spine development [GO:0060999]; positive regulation of excitatory postsynaptic potential [GO:2000463]; protein localization to synapse [GO:0035418]; protein-containing complex assembly [GO:0065003]; regulation of AMPA receptor activity [GO:2000311]; righting reflex [GO:0060013]; social behavior [GO:0035176]; synapse maturation [GO:0060074]; vocalization behavior [GO:0071625] | cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; excitatory synapse [GO:0060076]; glutamatergic synapse [GO:0098978]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202] | ankyrin repeat binding [GO:0071532]; G protein-coupled receptor binding [GO:0001664]; identical protein binding [GO:0042802]; ionotropic glutamate receptor binding [GO:0035255]; protein-containing complex binding [GO:0044877]; scaffold protein binding [GO:0097110]; SH3 domain binding [GO:0017124]; signaling receptor complex adaptor activity [GO:0030159]; somatostatin receptor binding [GO:0031877]; structural constituent of postsynaptic density [GO:0098919]; synaptic receptor adaptor activity [GO:0030160] | PF12796;PF17820;PF00536;PF07653; | 2.30.42.10;1.25.40.20;2.30.30.40;1.10.150.50; | SHANK family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Synapse {ECO:0000250}. Postsynaptic density {ECO:0000250}. Note=Colocalizes with alpha-latrotoxin receptor 1. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Seems to be an adapter protein in the postsynaptic density (PSD) of excitatory synapses that interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors, and the actin-based cytoskeleton. Plays a role in the structural and functional organization of the dendritic spine and synaptic junction. Overexpression promotes maturation of dendritic spines and the enlargement of spine heads via its ability to recruit Homer to postsynaptic sites, and enhances presynaptic function (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
D3YZZ2 | TGR3L_MOUSE | MVGTALLLLALLPGTSSKHGTPRAPLLPGAPGPWLRRPLFSLELSDAEDAFPRRAGPLEVPADSHVFVQAALARPSPRWGLALHRCSVTPSSRPTLGPALVLLRGGCPADDSVSFSPPPRPDAASVSRFSFRLRPVFNASVQFLHCQISRCRRRSSHHRRAVRLTPVPLTPPAPLRCLPQDEACAGSSLSLGTDSPHLHMLTQPIVVTIPRPSPRPSKSLPGRSVHPEPPAPAPAALEPAPVVALVLAAFVLGAALAAGLGLVCAHSAPPPPGPPPRASLSGPQLQRPPVGRDGTTQ | null | null | cell migration [GO:0016477]; epithelial to mesenchymal transition [GO:0001837]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; transforming growth factor beta receptor signaling pathway [GO:0007179] | cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | glycosaminoglycan binding [GO:0005539]; transforming growth factor beta binding [GO:0050431]; transforming growth factor beta receptor activity [GO:0005024]; type II transforming growth factor beta receptor binding [GO:0005114] | PF00100; | 2.60.40.4100; | null | PTM: Glycosylated. {ECO:0000269|PubMed:34910520}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:34910520}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Expressed in gonadotrope cells, acts as an inhibin B coreceptor and regulates follicle-stimulating hormone (FSH) levels and female fertility. {ECO:0000269|PubMed:34910520}. | Mus musculus (Mouse) |
D3Z120 | FOXI3_MOUSE | MALYCGDNFVYSQPAAAPGAPPTSRAPYGLSDYAAPPAAAANPYLWLNGPGVGGPASAASYLGAPPPPPGAAPGPFLQPPAAPGTFAGAQRGFAQPSASAPASPAGSAAPGELGWLSMASREDLMKMVRPPYSYSALIAMAIQSAPERKLTLSHIYQFVADNFPFYQRSKAGWQNSIRHNLSLNDCFKKVPRDEDDPGKGNYWTLDPNCEKMFDNGNFRRKRRRRAEASSNLTVPSGTSKSEGQSSRLRVSGKLEGDSPSSILRPSQSPEPPEGTKSTASSPGASTLTSTPCLNTFLSTFNTLNVNSSSSMGNQRTLPGSRRHLGGTQLPSSTFPNTSVPDSSPDSMQLSTVGGSNQLSSYYNPFSGGSSGDQSSPFSSPFYNFSMVNSLIYPRDGSDI | 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 (PubMed:30467319). Dephosphorylation by protein phosphatase 2A (PP2A) reduces its activity (PubMed:30467319). {ECO:0000269|PubMed:30467319}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:30467319, 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:24650709, PubMed:26550799, PubMed:26992132, PubMed:30467319). May act as a pioneer transcription factor during pharyngeal arch development (PubMed:26550799, PubMed:26992132). Required for epithelial cell differentiation within the epidermis (PubMed:26450968). Acts at multiple stages of otic placode induction: necessary for preplacodal ectoderm to execute an inner ear program (PubMed:26550799). Required for hair follicle stem cell specification (PubMed:26992132). Acts downstream of TBX1 for the formation of the thymus and parathyroid glands from the third pharyngeal pouch (PubMed:31412026). {ECO:0000269|PubMed:24650709, ECO:0000269|PubMed:26450968, ECO:0000269|PubMed:26550799, ECO:0000269|PubMed:26992132, ECO:0000269|PubMed:30467319, ECO:0000269|PubMed:31412026}. | Mus musculus (Mouse) |
D3Z1Q2 | MRAP2_MOUSE | MEMSAQRLASNRTSPQSPSNSDYTWEYEYYEIGPVSFEGLKAHKYSIVIGFWVGLAVFVIFMFFVLTLLTKTGAPHQDNAESSERRFRMNSFVSDFGKPLESDKVFSRQGNEESRSLFHCYINEVEHLDRVKVCHQTTAIDSDVHLQEASRSSGRPEEELARFMKFDIPNFVNTEQSSFGEDDLLISEAPVLLENKPVSQTSRIDLD | null | null | energy homeostasis [GO:0097009]; energy reserve metabolic process [GO:0006112]; feeding behavior [GO:0007631]; negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106072]; negative regulation of protein localization to plasma membrane [GO:1903077]; positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106071]; protein localization to plasma membrane [GO:0072659]; regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106070] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886] | corticotropin hormone receptor binding [GO:0031780]; identical protein binding [GO:0042802]; signaling receptor regulator activity [GO:0030545]; type 1 melanocortin receptor binding [GO:0070996]; type 3 melanocortin receptor binding [GO:0031781]; type 4 melanocortin receptor binding [GO:0031782]; type 5 melanocortin receptor binding [GO:0031783] | PF15183; | null | MRAP family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=The formation of antiparallel homo- and heterodimers suggest that N- and C-terminus can both localize in the cytoplasmic and extracellular parts, depending on the context. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Modulator of melanocortin receptor 4 (MC4R), a receptor involved in energy homeostasis. Plays a central role in the control of energy homeostasis and body weight regulation by increasing ligand-sensitivity of MC4R and MC4R-mediated generation of cAMP. May also act as a negative regulator of MC2R: competes with MRAP for binding to MC2R and impairs the binding of corticotropin (ACTH) to MC2R. May also regulate activity of other melanocortin receptors (MC1R, MC3R and MC5R); however, additional evidence is required in vivo. {ECO:0000269|PubMed:20371771, ECO:0000269|PubMed:23869016}. | Mus musculus (Mouse) |
D3Z291 | CAHM1_MOUSE | MDKFRMIFQFLQSNQESFMNGICGIMALASAQMYSAFDFNCPCLPGYNVVYSLGILLTPPLVLFLLGLVMNNNISMLAEEWKRPAGRRAKDPAVLRYMFCSMAQRALIAPVVWVAVTLLDGKCFLCAFCTAVPVATLGNGSLVPGLPAPELARLLARVPCPEIYDGNWLLAREVAVRYLRCISQALGWSFVLLTTLLAFVVRSVRPCFTQVAFLKSKYWSHYIDIERKLFDETCTEHAKAFAKVCIQQFFEAMNHDLELGHTHGVLATATATATATEAVQSPSDRTEEEREKLRGITDQGTMNRLLTSWHKCKPPLRLGQEAPLMSNGWAGGEPRPPRKEVATYFSKV | null | null | ATP transport [GO:0015867]; monoatomic cation transport [GO:0006812]; protein heterooligomerization [GO:0051291]; protein homooligomerization [GO:0051260]; regulation of monoatomic ion transmembrane transport [GO:0034765]; response to stimulus [GO:0050896]; sensory perception of bitter taste [GO:0050913]; sensory perception of sweet taste [GO:0050916]; sensory perception of taste [GO:0050909]; sensory perception of umami taste [GO:0050917] | basolateral plasma membrane [GO:0016323]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886] | calcium-activated cation channel activity [GO:0005227]; identical protein binding [GO:0042802]; monoatomic cation channel activity [GO:0005261]; voltage-gated calcium channel activity [GO:0005245]; voltage-gated monoatomic ion channel activity [GO:0005244] | PF14798; | null | CALHM family | PTM: N-glycosylated. Assembly with CALHM3 is associated with N-glycan remodeling and formation of hybrid complex- and high mannose-type glycochains. This N-glycan processing regulates channel trafficking and gating kinetics. {ECO:0000269|PubMed:33788965}.; PTM: Palmitoylated by ZDHHC3, ZDHHC20 and possibly ZDHHC7. Palmitoylation regulates voltage-dependent gating of the channel by shifting it toward more depolarized potentials. {ECO:0000269|PubMed:28734079}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IU99}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IU99}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IU99}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IU99}. Basolateral cell membrane {ECO:0000269|PubMed:30804437}; Multi-pass membrane protein. Note=Localizes to the basolateral membrane of epithelial cells including taste cells (PubMed:30804437). Colocalizes with HSPA5 at the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q8IU99, ECO:0000269|PubMed:30804437}. | CATALYTIC ACTIVITY: Reaction=ATP(in) = ATP(out); Xref=Rhea:RHEA:75687, ChEBI:CHEBI:30616; Evidence={ECO:0000269|PubMed:23467090, ECO:0000269|PubMed:28734079, ECO:0000269|PubMed:29681531, ECO:0000269|PubMed:33788965}; CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:29681531}; CATALYTIC ACTIVITY: Reaction=Mg(2+)(in) = Mg(2+)(out); Xref=Rhea:RHEA:29827, ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8IU99}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:29681531}; CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:29681531}; CATALYTIC ACTIVITY: Reaction=Li(+)(in) = Li(+)(out); Xref=Rhea:RHEA:78551, ChEBI:CHEBI:49713; Evidence={ECO:0000250|UniProtKB:Q8IU99}; CATALYTIC ACTIVITY: Reaction=Rb(+)(in) = Rb(+)(out); Xref=Rhea:RHEA:78547, ChEBI:CHEBI:49847; Evidence={ECO:0000250|UniProtKB:Q8IU99}; CATALYTIC ACTIVITY: Reaction=Cs(+)(in) = Cs(+)(out); Xref=Rhea:RHEA:78555, ChEBI:CHEBI:49547; Evidence={ECO:0000250|UniProtKB:Q8IU99}; CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:29681531}; | null | null | null | null | FUNCTION: Pore-forming subunit of gustatory voltage-gated ion channels required for sensory perception of sweet, bitter and umami tastes (PubMed:23467090). With CALHM3 forms a fast-activating voltage-gated ATP-release channel in type II taste bud cells, ATP acting as a neurotransmitter to activate afferent neural gustatory pathways (PubMed:23467090, PubMed:29681531). Acts both as a voltage-gated and calcium-activated ion channel: mediates neuronal excitability in response to membrane depolarization and low extracellular Ca(2+) concentration. Has poor ion selectivity and forms a wide pore (around 14 Angstroms) that mediates permeation of small ions including Ca(2+), Na(+), K(+) and Cl(-), as well as larger ions such as ATP(4-) (PubMed:22711817, PubMed:28734079, PubMed:29681531, PubMed:33788965). Mediates Ca(2+) influx and downstream activation of the ERK1 and ERK2 cascade in neurons (By similarity). Triggers endoplasmic reticulum stress by reducing the calcium content of the endoplasmic reticulum (By similarity). May indirectly control amyloid precursor protein (APP) proteolysis and aggregated amyloid-beta (Abeta) peptides levels in a Ca(2+) dependent manner (By similarity). {ECO:0000250|UniProtKB:Q8IU99, ECO:0000269|PubMed:22711817, ECO:0000269|PubMed:23467090, ECO:0000269|PubMed:29681531, ECO:0000269|PubMed:33788965}. | Mus musculus (Mouse) |
D3Z2R5 | SELN_MOUSE | MGQARPAARRPHSPDPGAQPAPPRRRARALALLGALLAAAAAVAAARACALLADAQAAARQESALKVLGTDGLFLFSSLDTDQDMYISPEEFKPIAEKLTGSVPVANYEEEELPHDPSEETLTIEARFQPLLMETMTKSKDGFLGVSRLALSGLRNWTTAASPSAAFAARHFRPFLPPPGQELGQPWWIIPGELSVFTGYLSNNRFYPPPPKGKEVIIHRLLSMFHPRPFVKTRFAPQGTVACLTAISDSYYTVMFRIHAEFQLSEPPDFPFWFSPGQFTGHIILSKDATHIRDFRLFVPNHRSLNVDMEWLYGASETSNMEVDIGYVPQMELEAVGPSVPSVILDEDGNMIDSRLPSGEPLQFVFEEIKWHQELSWEEAARRLEVAMYPFKKVNYLPFTEAFDRARAEKKLVHSILLWGALDDQSCUGSGRTLRETVLESPPILTLLNESFISTWSLVKELEDLQTQQENPLHRQLAGLHLEKYSFPVEMMICLPNGTVVHHINANYFLDITSMKPEDMENNNVFSFSSSFEDPSTATYMQFLREGLRRGLPLLQP | null | null | calcium ion homeostasis [GO:0055074]; cellular response to caffeine [GO:0071313]; cellular response to oxidative stress [GO:0034599]; lung alveolus development [GO:0048286]; mitochondrion organization [GO:0007005]; multicellular organismal response to stress [GO:0033555]; positive regulation of response to oxidative stress [GO:1902884]; positive regulation of skeletal muscle cell proliferation [GO:0014858]; regulation of ryanodine-sensitive calcium-release channel activity [GO:0060314]; respiratory system process [GO:0003016]; response to muscle activity involved in regulation of muscle adaptation [GO:0014873]; skeletal muscle fiber development [GO:0048741]; skeletal muscle satellite cell differentiation [GO:0014816]; skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration [GO:0014834]; skeletal muscle tissue regeneration [GO:0043403] | endoplasmic reticulum membrane [GO:0005789] | calcium ion binding [GO:0005509]; oxidoreductase activity [GO:0016491] | null | null | null | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9NZV5}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NZV5}. | null | null | null | null | null | FUNCTION: Plays an important role in cell protection against oxidative stress and in the regulation of redox-related calcium homeostasis. Regulates the calcium level of the ER by protecting the calcium pump ATP2A2 against the oxidoreductase ERO1A-mediated oxidative damage. Within the ER, ERO1A activity increases the concentration of H(2)O(2), which attacks the luminal thiols in ATP2A2 and thus leads to cysteinyl sulfenic acid formation (-SOH) and SEPN1 reduces the SOH back to free thiol (-SH), thus restoring ATP2A2 activity (PubMed:25452428). Acts as a modulator of ryanodine receptor (RyR) activity: protects RyR from oxidation due to increased oxidative stress, or directly controls the RyR redox state, regulating the RyR-mediated calcium mobilization required for normal muscle development and differentiation (By similarity). Essential for muscle regeneration and satellite cell maintenance in skeletal muscle (PubMed:21131290). {ECO:0000250|UniProtKB:Q9NZV5, ECO:0000269|PubMed:21131290, ECO:0000269|PubMed:25452428}. | Mus musculus (Mouse) |
D3Z3K2 | CIP1_MOUSE | MSLCEDMLLCNYRKCRIKLSGYAWVTACSHIFCDQHGSGEFSRSPAICPACNSTLSGKLDIVRTELSPSEEYKAMVLAGLRPEVVLDISSRALAFWTYQVHQERLYQEYNFSKAENHLKQMEKMYMQQIQSKNIELTSMKGEVISMKKVLEEYKKKFSDISEKLMERNRQYQKLQGLYDSLRLRNITIASQEGSLEPGMIPQSGVFGFPPGNNSKFSLDHIPVGNQGGGDEDVQFRPFFVCSPTAPEPINNFFSFASPSHEAEQQVCSRAFKAKRI | 2.3.2.27 | null | blastocyst formation [GO:0001825]; chiasma assembly [GO:0051026]; protein ubiquitination [GO:0016567]; reciprocal meiotic recombination [GO:0007131]; spermatid development [GO:0007286] | condensed nuclear chromosome [GO:0000794]; synaptonemal complex [GO:0000795] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842] | PF14634; | null | null | PTM: Ubiquitinated; autoubiquitinated. {ECO:0000250}.; PTM: Phosphorylated by CDK1 on serine or threonine residues (in vitro). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24390283}. Chromosome {ECO:0000269|PubMed:24390283}. Note=Associates to the synaptonemal complex. | 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; Evidence={ECO:0000250|UniProtKB:Q9NPC3}; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Ubiquitin E3 ligase that acts as a limiting factor for crossing-over during meiosis: required during zygonema to limit the colocalization of RNF212 with MutS-gamma-associated recombination sites and thereby establish early differentiation of crossover and non-crossover sites. Later, it is directed by MutL-gamma to stably accumulate at designated crossover sites. Probably promotes the dissociation of RNF212 and MutS-gamma to allow the progression of recombination and the implementation of the final steps of crossing over. Modulates cyclin-B levels and participates in the regulation of cell cycle progression through the G2 phase. Overexpression causes delayed entry into mitosis. {ECO:0000269|PubMed:17784788, ECO:0000269|PubMed:24390283}. | Mus musculus (Mouse) |
D3Z4I3 | RBM24_MOUSE | MHTTQKDTTYTKIFVGGLPYHTTDASLRKYFEVFGDIEEAVVITDRQTGKSRGYGFVTMADRAAAERACKDPNPIIDGRKANVNLAYLGAKPRIMQPGFAFGVQQLHPALIQRPFGIPAHYVYPQAFVQPGVVIPHVQPTAAAASTTPYIDYTGAAYAQYSAAAAAAAAAAAYDQYPYAASPAAAGYVTTGGYSYAVQQPITAAAPGTAAAAAAAAAAAAAFGQYQPQQLQTDRMQ | null | null | 3'-UTR-mediated mRNA destabilization [GO:0061158]; cell differentiation [GO:0030154]; DNA damage response [GO:0006974]; endocardial cushion development [GO:0003197]; mRNA destabilization [GO:0061157]; mRNA processing [GO:0006397]; mRNA stabilization [GO:0048255]; negative regulation of cytoplasmic translation [GO:2000766]; positive regulation of 3'-UTR-mediated mRNA stabilization [GO:1905870]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of myotube differentiation [GO:0010831]; positive regulation of skeletal muscle fiber differentiation [GO:1902811]; positive regulation of stem cell differentiation [GO:2000738]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of mRNA stability [GO:0043488]; regulation of myotube differentiation [GO:0010830]; RNA splicing [GO:0008380] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; mRNA CDS binding [GO:1990715]; pre-mRNA intronic binding [GO:0097157]; sequence-specific mRNA binding [GO:1990825] | PF00076; | 3.30.70.330; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6GQD3}. Cytoplasm {ECO:0000269|PubMed:25217815}. | null | null | null | null | null | FUNCTION: Multifunctional RNA-binding protein involved in the regulation of pre-mRNA splicing, mRNA stability and mRNA translation important for cell fate decision and differentiation (PubMed:25313962, PubMed:26844700). Plays a major role in pre-mRNA alternative splicing regulation (PubMed:25313962, PubMed:26844700). Mediates preferentially muscle-specific exon inclusion in numerous mRNAs important for striated cardiac and skeletal muscle cell differentiation (PubMed:25313962, PubMed:26844700). Binds to intronic splicing enhancer (ISE) composed of stretches of GU-rich motifs localized in flanking intron of exon that will be included by alternative splicing (PubMed:25313962). Involved in embryonic stem cell (ESC) transition to cardiac cell differentiation by promoting pre-mRNA alternative splicing events of several pluripotency and/or differentiation genes. Plays a role in the regulation of mRNA stability. Binds to 3'-untranslated region (UTR) AU-rich elements in target transcripts, such as CDKN1A and MYOG, leading to maintain their stabilities. Involved in myogenic differentiation by regulating MYOG levels. Binds to multiple regions in the mRNA 3'-UTR of TP63, hence inducing its destabilization. Promotes also the destabilization of the CHRM2 mRNA via its binding to a region in the coding sequence. Plays a role in the regulation of mRNA translation. Mediates repression of p53/TP53 mRNA translation through its binding to U-rich element in the 3'-UTR, hence preventing EIF4E from binding to p53/TP53 mRNA and translation initiation. Binds to a huge amount of mRNAs (By similarity). Required for embryonic heart development, sarcomer and M-band formation in striated muscles (PubMed:25313962, PubMed:29358667). Together with RBM20, promotes the expression of short isoforms of PDLIM5/ENH in cardiomyocytes (By similarity). {ECO:0000250|UniProtKB:M0R7T6, ECO:0000250|UniProtKB:Q9BX46, ECO:0000269|PubMed:25313962, ECO:0000269|PubMed:26844700, ECO:0000269|PubMed:29358667}. | Mus musculus (Mouse) |
D3Z5L6 | S18B1_MOUSE | MDEAGSPAPAGTGGGDDPGGSTRETSRRLSREQIFVLVSAASMNLGCMMTYSILGPFFPKEAEKKGASNTMIGMIFGCYALFELLASLVFGKYLVHIGAKFMFIAGMFVSGGVTILFGVLDQLPEGPIFIAMCFLVRIVDAIGFGAAITASSSILAKAFPNNVATVMGSLEVFSGLGLVAGPPLGGLLYQSFGYEVPFIFLGCIVLLMIPLNLYILPSYAQESDPGKQSFWKLVTLPKMGLLAFVIISLSSCFGFLDPTLSLFVMEKFSLSTGYVGLVFLGLSLSYAISSPLFGLLSDKMPTLRKWLLVFGNLITAGCYMLLGPVPLLHIKSQLWLLVLVLVVNGISAGMSIIPTFPEMLSCAYANGFEDSISTLGLVSGLFGAMWSVGAFMGPILGGFLCEKIGFEWAAAMQGLWTLLSGVSMALFYLWEDSTARRRSKAQNSLGTEEERAALLPNDT | null | null | serotonin uptake [GO:0051610]; spermidine transport [GO:0015848]; spermine transport [GO:0000296] | secretory granule membrane [GO:0030667]; synaptic vesicle membrane [GO:0030672] | monoamine:proton antiporter activity [GO:0015311]; polyamine:proton antiporter activity [GO:0015312]; transmembrane transporter activity [GO:0022857] | PF07690; | 1.20.1250.20; | Major facilitator superfamily | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:28082679}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:D4A9K4}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with VAMP3 and VAMP8 in mast cell secretory granules, which are distinct from histamine- and serotonin-containing granules (PubMed:28082679). Partly colocalizes with SYP in synaptic vesicles in hippocampal neurons. Colocalizes with SYP and VAMP2 in secretory vesicles of astrocytes (By similarity). {ECO:0000250|UniProtKB:D4A9K4, ECO:0000269|PubMed:28082679}. | CATALYTIC ACTIVITY: Reaction=n H(+)(out) + spermine(in) = n H(+)(in) + spermine(out); Xref=Rhea:RHEA:74263, ChEBI:CHEBI:15378, ChEBI:CHEBI:45725; Evidence={ECO:0000250|UniProtKB:Q6NT16}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74264; Evidence={ECO:0000250|UniProtKB:Q6NT16}; CATALYTIC ACTIVITY: Reaction=n H(+)(out) + spermidine(in) = n H(+)(in) + spermidine(out); Xref=Rhea:RHEA:74267, ChEBI:CHEBI:15378, ChEBI:CHEBI:57834; Evidence={ECO:0000250|UniProtKB:Q6NT16}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74268; Evidence={ECO:0000250|UniProtKB:Q6NT16}; CATALYTIC ACTIVITY: Reaction=n H(+)(out) + serotonin(in) = n H(+)(in) + serotonin(out); Xref=Rhea:RHEA:74295, ChEBI:CHEBI:15378, ChEBI:CHEBI:350546; Evidence={ECO:0000250|UniProtKB:Q6NT16}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74296; Evidence={ECO:0000250|UniProtKB:Q6NT16}; | null | null | null | null | FUNCTION: Proton-coupled polyamine antiporter involved in the translocation of polyamines from cytosol into secretory vesicles prior to their release via exocytosis. Uses the electrochemical proton gradient generated by a V-type proton-pumping ATPase to couple the efflux of protons with the uptake of a polyamine molecule (By similarity). Facilitates vesicular storage of spermine and spermidine in astrocytes with an impact on glutamatergic neuronal transmission and memory formation (By similarity) (PubMed:31800589). Upon antigen stimulation, regulates polyamine accumulation and release in mast cell secretory granules, which in turn potentiates mast cell degranulation and histamine secretion (PubMed:28082679). {ECO:0000250|UniProtKB:D4A9K4, ECO:0000250|UniProtKB:Q6NT16, ECO:0000269|PubMed:28082679, ECO:0000269|PubMed:31800589}. | Mus musculus (Mouse) |
D3Z5S8 | TET5A_MOUSE | MHQRYFWTDQGQVAFGGHYMAEGEGYFAMAEDELTGGPYIPLGGDFGGGGSSFGDRCSDYCESPTAHCNVLNWEQVQRLDGILSETIPIHGRGNFPTLELQPSLIVKVVRRRLEEKGIGVRDVRLNGSAASHVLHQDSGLGYKDLDLIFCADLRGEEEFQTVKDVVLDCLLDFLPEGVNKEKITPLTLKEAYVQKMVKVCNDSDRWSLISLSNNSGKNVELKFVDSLRRQFEFSVDSFQIKLDSLLLFYECSENPMTETFHPTIIGESVYGDFHEAFDHLCNKIIATRNPEEIRGGGLLKYCNLLVRGFRPASEEIKTLQRYMCSRFFIDFSDIGEQQRKLESYLQNHFVGLEDRKYDYLMTLHGVVNESTVCLMGHERRQTLNLITMLAIRVLADQNVIPNVANVTCYYQPAPYVADANFSNYYIAQVQPVFTCQQQTYSTWLPCN | 2.7.7.19 | null | mRNA stabilization [GO:0048255]; positive regulation of bone mineralization [GO:0030501]; positive regulation of osteoblast differentiation [GO:0045669]; regulation of ossification [GO:0030278]; response to bacterium [GO:0009617] | cytoplasm [GO:0005737] | poly(A) RNA polymerase activity [GO:1990817]; RNA binding [GO:0003723] | PF07984; | null | TENT family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:33882302}. | CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000269|PubMed:33882302}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333; Evidence={ECO:0000269|PubMed:33882302}; | null | null | null | null | FUNCTION: Cytoplasmic non-canonical poly(A) RNA polymerase that catalyzes the transfer of one adenosine molecule from an ATP to an mRNA poly(A) tail bearing a 3'-OH terminal group and participates in the cytoplasmic polyadenylation (PubMed:33882302). Polyadenylates mRNA encoding extracellular matrix constituents and other genes crucial for bone mineralization and during osteoblast mineralization, mainly focuses on ER-targeted mRNAs (PubMed:26803617, PubMed:33882302). {ECO:0000269|PubMed:26803617, ECO:0000269|PubMed:33882302}. | Mus musculus (Mouse) |
D3Z6P0 | PDIA2_MOUSE | MDKQLLPVLLLLLGVSGSWGQGEEPGGPSEVLPEEPTGEEVPKEDGILVLNHRTLSLALQEHSALMVEFYAPWCGHCKELAPEYSKAAALLAAESAVVTLAKVDGPAEPELTKEFEVVGYPTLKFFQNGNRTNPEEYAGPKTAEGIAEWLRRRVGPSATHLEDEEGVQALMAKWDMVVIGFFQDLQGKDMATFLALAKDALDMTFGFTDQPQLFEKFGLTKDTVVLFKKFDEGRADFPVDKETGLDLGDLSRFLVIHSMHLVTEFNSQTSPKIFAAKILNHLLLFVNQTLAQHRELLTDFREAAPPFRGQVLFVMVDVAADNSHVLNYFGLKAEEAPTLRLINVETTKKYAPTGVIAITAASVAAFCQAVLHGEIKHYLLSQEIPPDWDQGPVKTLVSKNFEQVAFDETKNVFVKFYAPWCSHCKEMAPAWEALAEKYKDREDIVIAELDATANELEAFSVLGYPTLKFFPAGPDRKVIDYKSTRDLETFSKFLDSGGHLPKEEPKEPAASAPEAQANSTLGPKEEL | 5.3.4.1 | null | platelet aggregation [GO:0070527]; protein folding [GO:0006457]; response to endoplasmic reticulum stress [GO:0034976] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788] | protein disulfide isomerase activity [GO:0003756]; protein-disulfide reductase activity [GO:0015035]; steroid binding [GO:0005496] | PF00085;PF13848; | 3.40.30.10; | Protein disulfide isomerase family | PTM: Glycosylated. {ECO:0000269|PubMed:9115635}. | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q13087, ECO:0000255|PROSITE-ProRule:PRU10138}. | CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; Evidence={ECO:0000305}; | null | null | null | null | FUNCTION: Acts as an intracellular estrogen-binding protein. May be involved in modulating cellular levels and biological functions of estrogens in the pancreas. May act as a chaperone that inhibits aggregation of misfolded proteins (By similarity). {ECO:0000250|UniProtKB:Q13087}. | Mus musculus (Mouse) |
D3Z752 | SPXN_MOUSE | MKGPSVLAVTAVVLLLVLSALENSSGAPQRLSEKRNWTPQAMLYLKGAQGRRFLSDQSRRKELADRPPPERRNPDLELLTLPEAAALFLASLEKSQKDEGGNFDKSELLEDRLFNW | null | null | long-chain fatty acid import into cell [GO:0044539]; negative regulation of appetite [GO:0032099]; negative regulation of heart rate [GO:0010459]; negative regulation of renal sodium excretion [GO:0035814]; positive regulation of gastro-intestinal system smooth muscle contraction [GO:1904306]; positive regulation of systemic arterial blood pressure [GO:0003084]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of sensory perception of pain [GO:0051930] | cytoplasm [GO:0005737]; dense core granule [GO:0031045]; extracellular space [GO:0005615]; transport vesicle [GO:0030133] | neuropeptide hormone activity [GO:0005184]; type 2 galanin receptor binding [GO:0031765]; type 3 galanin receptor binding [GO:0031766] | PF15171; | null | Spexin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24550067}. Secreted, extracellular space {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Note=Secreted via the classical ER/Golgi-dependent pathway into the extracellular medium largely as a full-length protein without the signal peptide, and not as a hydrolyzed and amidated peptide. Localized extracellularly surrounding the villous trophoblastic cells (By similarity). Detected in the serum. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Plays a role as a central modulator of cardiovascular and renal function and nociception. Also plays a role in energy metabolism and storage. Inhibits adrenocortical cell proliferation with minor stimulation on corticosteroid release (By similarity). {ECO:0000250}.; FUNCTION: [Spexin-1]: Acts as a ligand for galanin receptors GALR2 and GALR3. Intracerebroventricular administration of the peptide induces an increase in arterial blood pressure, a decrease in both heart rate and renal excretion and delayed natriuresis. Intraventricular administration of the peptide induces antinociceptive activity. Also induces contraction of muscarinic-like stomach smooth muscles (By similarity). Intraperitoneal administration of the peptide induces a reduction in food consumption and body weight. Inhibits long chain fatty acid uptake into adipocytes (PubMed:24550067). {ECO:0000250, ECO:0000269|PubMed:24550067}.; FUNCTION: [Spexin-2]: Intracerebroventricular administration of the peptide induces a decrease in heart rate, but no change in arterial pressure, and an increase in urine flow rate. Intraventricular administration of the peptide induces antinociceptive activity (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
D3Z7A5 | DAW1_MOUSE | MKLKSLLLRYYPPGIMLEYEKGGELKTKSIDLLELSPSTDVNTLVGEIQQAEPLITASRTKQVRLLVQRLQEKLRQHSDHNFYLFKVLRAHILPLTNVALNKAGSCFITGSYDRTCKVWDTASGEELHTLEGHKNVVYAIAFNNPYGDKIATGSFDKTCKLWSAETGKCYHTFRGHTAEIVCLSFNPQSTVVATGSMDTTAKLWDIQNGEEVVTLTGHLAEIISLSFDTSGDRIITGSFDHTVVVWDASTGRKVHTLIGHCAEISSALFNWDCSLILTGSMDKTCMLWDATSGKYVATLTGHDDEILDSCFDYTGKLIATASADGTARVYNATTRKCVTKLEGHEGEISKISFNPQGNRLLTGSSDKTARIWDVQTGQCLQVLEGHTDEIFSCAFNYKGNIVITGSKDNSCRIWR | null | null | cerebrospinal fluid circulation [GO:0090660]; determination of left/right symmetry [GO:0007368]; epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; establishment of localization in cell [GO:0051649]; heart development [GO:0007507]; intraciliary transport [GO:0042073]; outer dynein arm assembly [GO:0036158]; protein polyubiquitination [GO:0000209] | ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; motile cilium [GO:0031514]; SCF ubiquitin ligase complex [GO:0019005]; Set1C/COMPASS complex [GO:0048188] | histone binding [GO:0042393]; ubiquitin ligase-substrate adaptor activity [GO:1990756] | PF00400; | 2.130.10.10; | WD repeat WDR69 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, flagellum basal body {ECO:0000250|UniProtKB:Q3Y8L7}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q3Y8L7}. Note=Expression is concentrated at the flagellum basal body but is also detected along the length of the flagellum. {ECO:0000250|UniProtKB:Q3Y8L7}. | null | null | null | null | null | FUNCTION: Required for axonemal dynein assembly and ciliary motility in ciliated organs, including Kupffer's vesicle, during embryogenesis (By similarity). Facilitates the onset of robust cilia motility during development (By similarity). {ECO:0000250|UniProtKB:Q8N136}. | Mus musculus (Mouse) |
D3Z7P3 | GLSK_MOUSE | MMRLRGSAMLRELLLRPPAAVGAVLRRAQPLGTLCRRPRGGSRPTAGLVAAARLHPWWGGGGRAKGPGAGGLSSSPSEILQELGKGGTPPQQQQQQQQQPGASPPAAPGPKDSPGETDAFGNSEGKEMVAAGDNKIKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSGLRFNKLFLNEDDKPHNPMVNAGAIVVTSLIKQGVNNAEKFDYVMQFLNKMAGNEYVGFSNATFQSERESGDRNFAIGYYLKEKKCFPEGTDMVGILDFYFQLCSIEVTCESASVMAATLANGGFCPITGERVLSPEAVRNTLSLMHSCGMYDFSGQFAFHVGLPAKSGVAGGILLVVPNVMGMMCWSPPLDKMGNSVKGIHFCHDLVSLCNFHNYDNLRHFAKKLDPRREGGDQRVKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVVKFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDDGKGNQTVHKNLDGLL | 3.5.1.2 | null | chemical synaptic transmission [GO:0007268]; glutamate biosynthetic process [GO:0006537]; glutamine catabolic process [GO:0006543]; intracellular glutamate homeostasis [GO:0090461]; protein homotetramerization [GO:0051289]; regulation of respiratory gaseous exchange by nervous system process [GO:0002087]; suckling behavior [GO:0001967] | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; synapse [GO:0045202] | glutaminase activity [GO:0004359]; identical protein binding [GO:0042802] | PF12796;PF17959;PF04960; | 1.10.238.210;1.25.40.20;3.40.710.10; | Glutaminase family | PTM: Synthesized as a 74-kDa cytosolic precursor which is proteolytically processed by the mitochondrial-processing peptidase (MPP) via a 72-kDa intermediate to yield the mature mitochondrial 68- and 65-kDa subunits. {ECO:0000250|UniProtKB:P13264}. | SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000250|UniProtKB:P13264}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P13264}. Note=The 74-kDa cytosolic precursor is translocated into the mitochondria and processed via a 72-kDa intermediate to yield the mature 68- and 65-kDa subunits. {ECO:0000250|UniProtKB:P13264}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion {ECO:0000269|PubMed:16641247, ECO:0000269|PubMed:27542409}.; SUBCELLULAR LOCATION: [Glutaminase kidney isoform, mitochondrial 68 kDa chain]: Mitochondrion matrix {ECO:0000250|UniProtKB:P13264}. Note=Produced by the proteolytic processing of the 74-kDa cytosolic precursor. {ECO:0000250|UniProtKB:P13264}.; SUBCELLULAR LOCATION: [Glutaminase kidney isoform, mitochondrial 65 kDa chain]: Mitochondrion matrix {ECO:0000250|UniProtKB:P13264}. Note=Produced by the proteolytic processing of the 74-kDa cytosolic precursor. {ECO:0000250|UniProtKB:P13264}. | CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; Evidence={ECO:0000269|PubMed:22228304, ECO:0000269|PubMed:23935106, ECO:0000269|PubMed:27542409}; | null | null | null | null | FUNCTION: Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate, the main excitatory neurotransmitter in the brain. {ECO:0000269|PubMed:16641247, ECO:0000269|PubMed:22228304, ECO:0000269|PubMed:22373647}. | Mus musculus (Mouse) |
D3Z8D9 | MD2L2_RAT | MTTLTRQDLNFGQVVADVLSEFLEVAVHLILYVREVYPVGIFQKRKKYNVPVQMSCHPELNQYIQDTLHCVKPLLEKNDVEKVVVVILDKEHRPVEKFVFEITQPPLLSINSDSLLSHVEQLLRAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQVIKDFPWILADEQDVHMHDPRLIPLKTMTSDILKMQLYVEERAHKNS | null | null | actin filament organization [GO:0007015]; cell cycle [GO:0007049]; cell division [GO:0051301]; DNA damage response, signal transduction resulting in transcription [GO:0042772]; double-strand break repair [GO:0006302]; error-prone translesion synthesis [GO:0042276]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell-cell adhesion mediated by cadherin [GO:2000048]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of protein catabolic process [GO:0042177]; negative regulation of transcription by competitive promoter binding [GO:0010944]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of ubiquitin protein ligase activity [GO:1904667]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of double-strand break repair via nonhomologous end joining [GO:2001034]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of extracellular matrix assembly [GO:1901203]; positive regulation of gene expression [GO:0010628]; positive regulation of isotype switching [GO:0045830]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; regulation of cell growth [GO:0001558] | anaphase-promoting complex [GO:0005680]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]; zeta DNA polymerase complex [GO:0016035] | JUN kinase binding [GO:0008432]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629] | PF02301; | 3.30.900.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Adapter protein able to interact with different proteins and involved in different biological processes. Mediates the interaction between the error-prone DNA polymerase zeta catalytic subunit REV3L and the inserter polymerase REV1, thereby mediating the second polymerase switching in translesion DNA synthesis. Translesion DNA synthesis releases the replication blockade of replicative polymerases, stalled in presence of DNA lesions. Component of the shieldin complex, which plays an important role in repair of DNA double-stranded breaks (DSBs). During G1 and S phase of the cell cycle, the complex functions downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and suppress DNA end resection. Mediates various NHEJ-dependent processes including immunoglobulin class-switch recombination, and fusion of unprotected telomeres. May also regulate another aspect of cellular response to DNA damage through regulation of the JNK-mediated phosphorylation and activation of the transcriptional activator ELK1. Inhibits the FZR1- and probably CDC20-mediated activation of the anaphase promoting complex APC thereby regulating progression through the cell cycle. Regulates TCF7L2-mediated gene transcription and may play a role in epithelial-mesenchymal transdifferentiation. {ECO:0000250|UniProtKB:Q9UI95}. | Rattus norvegicus (Rat) |
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