ID A0A2Y9IM64_ENHLU Unreviewed; 862 AA.
AC A0A2Y9IM64;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN Name=LOC111141415 {ECO:0000313|RefSeq:XP_022349653.1,
GN ECO:0000313|RefSeq:XP_022349654.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022349653.1};
RN [1] {ECO:0000313|RefSeq:XP_022349653.1, ECO:0000313|RefSeq:XP_022349654.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022349653.1,
RC ECO:0000313|RefSeq:XP_022349654.1};
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 ECO:0000256|PIRNR:PIRNR001569};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.
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DR RefSeq; XP_022349653.1; XM_022493945.1.
DR RefSeq; XP_022349654.1; XM_022493946.1.
DR KEGG; elk:111141415; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000248482; Unplaced.
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:SF66; E3 UBIQUITIN-PROTEIN LIGASE ITCHY HOMOLOG; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 4.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
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:UP000248482};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 1..115
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 285..318
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 317..350
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 397..430
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 437..470
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 528..862
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 152..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..227
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 830
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 862 AA; 98705 MW; FFE4396EC037894A CRC64;
MSGSGSQLGS MGSLTMKSQL QITVISAKLK ENKKNWFGPS PYVEVTVDGQ SKKTEKCNNT
NSPKWKQPLT VIVTPVSKLH FRVWSHQTLK SDVLLGTAAL DIFETLKSNN MKLEEVVVTL
QLVGDKEPTE TIGDLSVCLD GLQLDSEVVT NGETTCSESA SQSDDGSRPK DETRTNTNGS
DEPEDAGAGE NRKVNGNNSP SLSNGGFKPS RPPRPSRPPP PTPRRPASVN GSPSATSESD
GSSTGSLPPT NINSNTSEGA TSGLIIPLTI SGGSGPRPLN PVPQAPLPPG WEQRVDQHGR
VYYVDHIEKR TTWDRPEPLP PGWERRVDNM GRIYYVDHFT RTTTWQRPTL ESVRNYEQWQ
LQRSQLQGAM QQFNQRFIYG NQDLFTTSQN KEFDPLGPLP PGWEKRTDSN GRVYFVNHNT
RITQWEDPRS QGQLNEKPLP EGWEMRFTVD GIPYFVDHNR RTTTYIDPRT GKSALDNGPQ
IAYVRDFKAK VQYFRFWCQQ LAMPQHIKIT VTRKTLFEDS FQQIMSFNPQ DLRRRLWVIF
PGEEGLDYGG VAREWFFLLS HEVLNPMYCL FEYAGKDNYC LQINPASYIN PDHLKYFRFI
GRFIAMALFH GKFIDTGFSL PFYKRILNKP VGLKDLESID PEFYNSLIWV KENNIEECGL
EMYFSVDKEI LGEIKSHDLK PNGGNILVTE ENKEEYIRMV AEWRLSRGVE EQTQAFFEGF
NEILPQQYLQ YFDAKELEVL LCGMQEIDLN DWQRHAIYRH YTRTSKQIMW FWQFVKEIDN
EKRMRLLQFV TGTCRLPVGG FADLMGSNGP QKFCIEKVGK ENWLPRSHTC FNRLDLPPYK
SYEQLKEKLL FAIEETEGFG QE
//
