ID I3L6R7_PIG Unreviewed; 1283 AA.
AC I3L6R7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 4.
DT 27-MAR-2024, entry version 74.
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|Ensembl:ENSSSCP00000019719.4,
GN ECO:0000313|VGNC:VGNC:90666};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000019719.4, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000019719.4, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000019719.4,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000019719.4}
RP IDENTIFICATION.
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 PaxDb; 9823-ENSSSCP00000019719; -.
DR PeptideAtlas; I3L6R7; -.
DR Ensembl; ENSSSCT00000024384.4; ENSSSCP00000019719.4; ENSSSCG00000037499.3.
DR VGNC; VGNC:90666; NEDD4.
DR GeneTree; ENSGT00940000158905; -.
DR HOGENOM; CLU_002173_9_2_1; -.
DR TreeFam; TF323658; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008227; Chromosome 1.
DR Bgee; ENSSSCG00000037499; Expressed in skeletal muscle tissue and 45 other cell types or tissues.
DR ExpressionAtlas; I3L6R7; baseline and differential.
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; 3.
DR Gene3D; 2.20.70.10; -; 2.
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; IPR035892; C2_domain_sf.
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; 3.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 3.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 3.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 3.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 611..644
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 804..837
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 856..889
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 948..1282
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 755..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1250
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1283 AA; 144432 MW; A760E86097AB1164 CRC64;
MAQSLRLHFA ARRSNTYPLS ETSGDDLDSS IHMCFTRPTR ISTSNVVQMK LTPRQTALAP
LIKENVKSQE RSSVPSPENV NKKSSCLQIS LQPTRYSGCL QSSHVLAGSD DASFTCVLKD
GSAVVDNDLS AVDDGTFLSS SVICSGSLSN FSASENGSYS SNSSDYGSCT SITSGGSYTN
SITSDSSGCG FPPTDDTFFG GNLSSDSTSN RSVPNRNTAP CEILSRSTST VPFVQDDLDH
GLEIMKLPMI RNSKIPLKRC SSLVIFPRSP SNTPPTSPTS TGTFLSKGSY QTSHQFVISP
SEVAHNEDGT NAKGFLSTAV NGLRLSKTTS TPGEVRDIRP LHRKGSLQKK TVIANNSPNQ
TACEKSSEGY SCVSVHFTQQ KATTLNCETA NGDCKPGMSE IKLNSDSEYI KRMHRTSAYL
PSSQNIDCQI NISRQLERPN LQINKNHAIL RRSISLGGTY PNISCLSSLK HNCSKGGPSQ
LLIKFASGNE GKVDNLTRDS NRDFTNDPSN SLKHSCKTRD DFLGQVDVPL YPLPTENPRM
ERPYTFKDFV LHPRSHKSRV KGYLRLKMTY LPKTSGSEED NTEQAEELEP GWVVLDQPDA
ACNLQQQQEP SPLPPGWEER QDILGRTYYV NHESRRTQWK RPSLQDTLTD AENGNIQLQA
QRAFTTRRQI SEETESVDSR ESSENWEIIR EDEATMYSNQ AFPSSPPSNN LDVQTHLAEE
LNARLTVCGN SATGQPVSSS NHSSRRSSLQ AYTFEEQPTL PVASVTTETS QLPSSQSSST
GPQAQAPTSD AAQQVTQPSE MEQGSLPKGW EVRHAPNGRP FFIDHNTKTT TWEDPRLKIP
AHLRGKTSLD PSSDLGPLPP GWEERTHTDG RIFYINHNIK KTQWEDPRLQ NVAITGPAVP
YSRDYKRKYE FFRRKLKKQN DIPNKFEMKL RRATVLEDSY RRIMGVKRAD FLKARLWIEF
DGEKGLDYGG VAREWFFLIS KEMFNPYYGL FEYSATDNYT LQINPNSGLC NEDHLSYFKF
IGRVAGMAVY HGKLLDGFFI RPFYKMMLHK TITLHDMESV DGEYYNSLRW ILENDPTELD
LRFVIDEELF GQTHQHELKN GGSEIVVTNK NKKEYIYLVI QWRFVNRIQK QMAAFKEGFF
ELIPQDLIKI FDENELELLM CGLGDVDVND WREHTKYKNG YSVNHQVIQW FWKAVLMMDS
EKRIRLLQFV TGTSRVPMNG FAELYGSNGP QSFTVEQWGT PEKLPRAHTC FNRLDLPPYE
SFEELWDKLQ MAIENTQGFD GVD
//
