ID A0A1L8EU80_XENLA Unreviewed; 852 AA.
AC A0A1L8EU80;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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=itch.L {ECO:0000313|Xenbase:XB-GENE-6486380};
GN Synonyms=LOC108701064 {ECO:0000313|RefSeq:XP_018090698.1,
GN ECO:0000313|RefSeq:XP_018090700.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|RefSeq:XP_018090698.1};
RN [1] {ECO:0000313|RefSeq:XP_018090698.1, ECO:0000313|RefSeq:XP_018090700.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018090698.1,
RC ECO:0000313|RefSeq:XP_018090700.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018090698.1,
RC ECO:0000313|RefSeq:XP_018090700.1};
RG RefSeq;
RL Submitted (APR-2022) 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_018090698.1; XM_018235209.2.
DR RefSeq; XP_018090700.1; XM_018235211.2.
DR RefSeq; XP_018090701.1; XM_018235212.1.
DR STRING; 8355.A0A1L8EU80; -.
DR PaxDb; 8355-A0A1L8EU80; -.
DR GeneID; 108701064; -.
DR KEGG; xla:108701064; -.
DR CTD; 108701064; -.
DR Xenbase; XB-GENE-6486380; itch.L.
DR OMA; KXASQND; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 108701064; Expressed in intestine and 19 other cell types or tissues.
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:UP000186698};
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 277..310
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 309..342
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 387..420
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 427..460
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 518..852
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 168..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..218
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 820
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 852 AA; 97873 MW; 40D65633132D12B5 CRC64;
MDGSGSRSGA VNGFTMKSQL QVIVISAKLK DNRKNWFGPS PYVELSVDGQ SKKTETKNKT
HSPKWKQPLT VIVTPFSVLN FRVWSHQTLK SDALIGSASL NMHETLLSNH MKLEEVIVNM
QLLSERETVG DLSVCLDGMQ VDPELLANGD PAISSGSTDN SAMQIETQPA SADTANGTNS
TDSRTTNGTS SPSLANGGFK SSRPPRPSRP PPPTPRRLSS IAPAINETCS QPEAELLPTP
SVASIPEAEA PSSTPPVSRQ IAPINIDGQR MGLVGQGPLP TGWEQRVDQQ GRVYYVDHVA
KRTTWDRPEP LPPGWERRVD NMSRIYYVDH ITRTTTWQRP TLESVRNYEQ WQLQRNQLEG
AMQQFNQRFI YATQEPGAQN KEYDPLGPLP VGWEKRMDGN GRVYFVNHTT RATQWEDPRN
QGQMNEKPLP EGWEMRFTVD GIPYFVDHNR KTTTYIDPRT GKSALDNGPH IAYVRDFKAK
VQYFKFWCQQ LYMPQHVKIT VNRKTLFEDS FQQIMSFNPQ DLRRRLWIII PGEEGLDYGG
VAREWFFLLS HEVMNPMYCL FEYAGKDNYC LQINPASYIN PDHLRYFRFI GRFIAMALFH
GKFIDTGFSL PFYKRILNKL VGLKDLESVD PEFYNSLMWI KDNNIEECGL EMFFSVDKEI
LGEVQSHDLK PEGSNIQVTE ENKEEYIRLV AEWRLSRGVE EQTQAFFEGF NEILPQQYLQ
YFDAKELEVL LCGMQEIDLN DWQRNTIYRH YTKTSKLIIW FWQFVKEIDN EKRMRLLQFV
TGTCRLPVGG FADLMGSNGP QKFCIEKVGK ENWLPRSHTC FNRLDLPPYK SYEQLKEKLL
FAIEETEGFG QE
//
