ID A0A1S3EVI1_DIPOR Unreviewed; 920 AA.
AC A0A1S3EVI1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN Name=Wwp1 {ECO:0000313|RefSeq:XP_012867959.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012867959.1};
RN [1] {ECO:0000313|RefSeq:XP_012867959.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012867959.1};
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_012867959.1; XM_013012505.1.
DR AlphaFoldDB; A0A1S3EVI1; -.
DR STRING; 10020.ENSDORP00000014686; -.
DR GeneID; 105982819; -.
DR KEGG; dord:105982819; -.
DR CTD; 11059; -.
DR InParanoid; A0A1S3EVI1; -.
DR OMA; YNGRCEY; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000081671; 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; 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; 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:UP000081671};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 1..116
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 347..380
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 379..412
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 454..487
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 494..527
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 586..920
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 213..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 888
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 920 AA; 104734 MW; CF4BF42BA661C143 CRC64;
MATASPRSDS SDNHSGRLQL QVTVSSAKLK RKKNWFGTAI YTEVTVDGEI KKTAKSSSSS
NPKWDEQLTV NVTPQTTLEF RVCSHHTLKA DALLGRAMVD LKQVLLTHNR KLEKVKEQLK
LSLENKNGIV QTGELTVVLD GLVIEPENLA NCSSSPTIEI QQNGDALHED GDPSARTTTR
LALEGTNGID NHVPTNTVIS NSCCSYVVNG DNTPSSPSQV AARPKNTPAP KPLTSEPAND
TVNGESSSSA LTANASAMGT PVPSEEPTLT SECISTTIEG SSVQELLASS EHNECIPSVS
TELGSETQNV LDLNSSNSGS SSAFDKLRQS DGCVEPLRQQ SGNANTESLP SGWEQRKDPH
GRTYYVDHNT RTTTWERPQP LPPGWERRVD DRGRVYYVDH NTRTTTWQRP TMESVRNFEQ
WQSQRNQLQG AMQQFNQRYL YSASMLAAEN DPYGPLPPGW EKRVDSTDRV YFVNHNTKTT
QWEDPRTQGL QNEEPLPEGW EIRYTREGVR YFVDHNTRTT TFKDPRNGKS SVTKGGPQIA
YERSFRWKLA HFRYLCQSNA LPSHVKINVS RQTLFEDSFQ QIMALKPYDL RRRLYVIFRG
EEGLDYGGLA REWFFLLSHE VLNPMYCLFE YAGKNNYCLQ INPASTINPD HLSYFCFIGR
FIAMALFHGK FIDTGFSLPF YKRMLSKKLT IKDLESIDTE FYNSLIWIRD NNIEECGLEM
YFSVDMEILG KVTSHDLKLG GSNILVTEEN KDEYIGLMTE WRFSRGVQEQ TKAFLDGFNE
VVPLQWLQYF DEKELEVMLC GMQEVDLTDW QRNTVYRHYT RNSKQIIWFW QFVKETDNEV
RMRLLQFVTG TCRLPLGGFA ELMGSNGPQK FCIEKVGKDT WLPRSHTCFN RLDLPPYKSY
EQLKEKLLFA IEETEGFGQE
//
