ID   A0A2I3THH9_PANTR        Unreviewed;       556 AA.
AC   A0A2I3THH9;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=LOC471113 {ECO:0000313|Ensembl:ENSPTRP00000088726.1};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000088726.1, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000088726.1, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000088726.1}
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   EMBL; AACZ04038570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2I3THH9; -.
DR   Ensembl; ENSPTRT00000089302.1; ENSPTRP00000088726.1; ENSPTRG00000043691.1.
DR   GeneTree; ENSGT00940000154635; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000002277; Chromosome 3.
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; 2.
DR   Gene3D; 2.20.70.10; -; 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; 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; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          98..131
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          138..171
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          222..556
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        524
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   556 AA;  63574 MW;  5FDD6A7DAE4CDB5E CRC64;
     ESSSFAPTDN ASVMGIPVVS EENALSPNCT STTVEDPPVQ EILTSSENNE CIPSTSAELG
     SESRSILDPD TSNSGSSSAF ETAKSRQPDG SAENDPHGPL PPGREKRVDS TDRVYFANHN
     TKTTQWEDPR TQGLQNEEPL PEGWEIRYTR EGVRYFVYHN ARTTTFKDPC NGKSSITKGG
     PQIDYEHSFR QKLSNALPSH VKINVSRQTL FEDSFQQIMA LKPYDLRRCL YVIFRGEEGL
     DYGGLAREWL FLLSHEVLNP MYCLFEYVGK NNYSLQINPA STINPDHLSY FCFIGRFIAM
     ALFHGKLIDT GFSLPFYKHM LSKKLTIKDL ESIDTEFYNS LIWIRDNNIE ECGLELYFSV
     DMESWGKVTS HDLKLGVSNI LVTEENKDEY IGLMTEWHFS RGVQEQTKAF LDGFNGVVPH
     QWLQYFNEKE LEVTLCGTQQ VDLADWQRNT VYQHYTRNSK QIIRFWQFVK ETDNEVRMLL
     LQFVTGTCRL SLGGFAELMG SNGPQKFCIE KVDKDTWLPR SHTCFNLLDL PPYKSYEQLK
     EKLLFAIEET EGCGQE
//