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Database: UniProt
Entry: M3ZQ86_XIPMA
LinkDB: M3ZQ86_XIPMA
Original site: M3ZQ86_XIPMA 
ID   M3ZQ86_XIPMA            Unreviewed;       959 AA.
AC   M3ZQ86;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=WWP1 {ECO:0000313|Ensembl:ENSXMAP00000004379.1};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000004379.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000004379.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000004379.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   RefSeq; XP_005808421.1; XM_005808364.2.
DR   AlphaFoldDB; M3ZQ86; -.
DR   STRING; 8083.ENSXMAP00000004379; -.
DR   Ensembl; ENSXMAT00000004384.2; ENSXMAP00000004379.1; ENSXMAG00000004345.2.
DR   GeneID; 102223052; -.
DR   KEGG; xma:102223052; -.
DR   CTD; 11059; -.
DR   eggNOG; KOG0940; Eukaryota.
DR   GeneTree; ENSGT00940000154635; -.
DR   HOGENOM; CLU_002173_0_1_1; -.
DR   InParanoid; M3ZQ86; -.
DR   OMA; YNGRCEY; -.
DR   OrthoDB; 5480520at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd04021; C2_E3_ubiquitin_ligase; 1.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 4.
DR   Gene3D; 2.20.70.10; -; 3.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   PANTHER; PTHR11254:SF299; NEDD4-LIKE E3 UBIQUITIN-PROTEIN LIGASE WWP1; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 4.
DR   PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 4.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF51045; WW domain; 4.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 4.
DR   PROSITE; PS50020; WW_DOMAIN_2; 4.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1..114
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          387..420
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          419..452
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          494..527
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          534..567
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          625..959
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          153..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..268
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..305
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..378
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        927
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   959 AA;  107190 MW;  0BBC64786D714BBB CRC64;
     MATASSRAET SHNHRRTSQL HAIVSCAKLK RKKSVFGAAI YVEVTAEGET RRTAKSHSSS
     NPKWDERLTL TVAPHTQVDF KVWSHHTLKA DALLGKATLD LLQALERHDR KLENVKEVLK
     LSVEQKGLSV PVGELTVYLD GLTVTDQEEL APLTNGNAAN GTKVQQNGDA IHENGDSSSS
     SSRAANSTVN GTDLGQRSGS CSASSGADGP VPSSPALDHT TGMINGDPTP NSTPVHQPPD
     SSPDTRMVNG ESSETVPRQS SASRRETQPS AGETEESSHD AAPPNAETSP ASTSRPPPAP
     TPSSASSPAA KPANGAASSS SSAAAASTTS ASATQGEPTV TTSSSLSSSP APGEAGASGA
     GSSSSSTTTT TDGVKPRQQV SNAPAGDPLP PGWEQRKDPH GRTYYVDHNT RTTTWERPQP
     LPPGWERRVD DRGRIYYVDH NTRTTTWQRP TMESVRNFEQ WQSQRSQLQG AMHQFNQRYL
     YSASMMSAEN DPLGPLPPGW ERRVDSNDRV YFVNHNTKTT QWEDPRTQGL QNEDPLPEGW
     EIRYTREGVR YFVDHNTRTT TFSDPRTGKS SVTKGPQIAY ERSFRWKLAH FRYLCQSNAL
     PSHVKITVSR QTLFEDSFQQ IMALKPYDLR RRLYVIFRGE EGLDYGGLAR EWFFLLSHEV
     LNPMYCLFEY AGKSNYCLQI NPASAINPDH LSYFCFIGRF IAMALFHGKF IDTGFSLPFY
     KRMLNKKLIL KDLESIDPEF YNSLIWIRDN NIEECGLEMY FSVDMEILGK ISSHDLKPDG
     ANILVTEENK EEYISLMAEW RFSRGVEGQT KAFLDGFNEV VPLQWLQYFD EKELEVMLCG
     MQEVDLQDWQ RNTVYRHYTR NSKQIIWFWQ LVKEVDNEVR LRLMQFVTGT CRLPLGGFAE
     LMGSNGPQKF CIEKVGKDTW LPRSHTCFNR LDLPPYKSYE QLKEKLLFAI EETEGFGQE
//
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