ID A0A3Q7S987_VULVU Unreviewed; 1251 AA.
AC A0A3Q7S987;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=NEDD4 {ECO:0000313|RefSeq:XP_025852518.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025852518.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025852518.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025852518.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025852518.1};
RG RefSeq;
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_025852518.1; XM_025996733.1.
DR AlphaFoldDB; A0A3Q7S987; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 4.
DR Gene3D; 2.20.70.10; -; 3.
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; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF282; E3 UBIQUITIN-PROTEIN LIGASE NEDD4; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 4.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 4.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 4.
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:UP000286640};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 542..575
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 699..732
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 772..805
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 824..857
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 916..1250
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 206..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1218
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1251 AA; 141243 MW; 8B3B758AA0E41CDE CRC64;
MAQSLRLHFA ARRSNTYPLS ETSGDDLDSN VHMCFKRPTR ISTSNVVQMK LTPRQTALAP
LIQENVNSQE RSSVPSPENV NKKSSCLQIS LQPTRYSGCL QSGNVLADGD DASFTSVFKD
GIYNNAVADN ELNAVNDGNL VSSSAIHSGS LSNFSTSENG SYSSNGSDYG SCTSITSGGS
YTNSIISDSS GYTFPPTDDT FFGGNLSSDS TSNRSVPNRN TTPCDIFSRS PSTVPFVQDD
LEHGLEIMKL PVTRNSKIPL KRCSSLVIFP RSPLNTPPTS PTSTDVLPSK GSYQTSHQFI
ISPSEIAHSE DGSSTKGFLS TAVNGLRLSK TICTPGEVRD IRPLHRKGSL QKKIVIANDS
LNQTVREKSS EGYSCVSVHF TQQKATTLDC ETASGDCKPE MSEIKLNSHS ECIKLMQRTS
ACLPSSQHLD YQININGQLE RPNLQINKNH AILQRSVSLG GTYPNVSCLS SLKHNCSKGG
PSQLLIKFAP GNEDKVDNLS RDNDRDFTNE LSNSLKHSCK PGWVVLDQPD AACHLQQQQE
PSPLPPGWEE RQDILGRTYY VNHESRRTQW KRPTAQDNLT DAENGNMQLQ AQRAFTTRRQ
ISEETESVDN RESSESWEII REDEATMYSN QAFPSPPASN NLDVQTHLAE ELNARLTICR
NSATSQPVSS SNHSSRRGSL QAYTFEEQPT LPVLLPTSSG LPPGWEEKQD ERGRSYYVDH
NSRTTTWTKP VVQATVETSQ LQPSQSAACP QPQVPVSESA QQGTQAAEME QGFLPKGWEV
RHAPNGRPFF IDHNTKTTTW EDPRLKIPAH LRGKMSLDSS NDLGPLPPGW EERTHTDGRI
FYINHNIKRT QWEDPRLQNV AITGPAVPYS RDYKRKYEFF RRKLKKQNDI PNKFEMKLRR
ATVLEDSYRR IMGVKRADFL KARLWIEFDG EKGLDYGGVA REWFFLISKE MFNPYYGLFE
YSATDNYTLQ INPNSGLCNE DHLSYFKFIG RVAGMAVYHG KLLDGFFIRP FYKMMLHKPI
TLHDMESVDG EYYNSLRWIL ENDPTELDLR FVIDEELFGQ THQHELKIGG SEIVVTNKNK
KEYIYLVIQW RFVNRIQKQM AAFKEGFFEL IPQDLIKIFD ENELELLMCG LGDVDVNDWR
EHTKYKNGYS VNHQVIQWFW KAVLMMDSEK RIRLLQFVTG TSRVPMNGFA ELYGSNGPQS
FTVEQWGTPE KLPRAHTCFN RLDLPPYESF EELWDKLQMA IENTQGFDGV D
//
