ID   UBE3D_BOVIN             Reviewed;         389 AA.
AC   Q1JQA1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=E3 ubiquitin-protein ligase E3D;
DE            EC=2.3.2.26;
DE   AltName: Full=HECT-type E3 ubiquitin transferase E3D {ECO:0000305};
DE   AltName: Full=UbcH10-binding protein with a HECT-like domain;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2C-binding protein;
GN   Name=UBE3D; Synonyms=H10BH, UBE2CBP;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
CC       specific E2 ubiquitin-conjugating enzymes, and transfers it to
CC       substrates, generally promoting their degradation by the proteasome.
CC       {ECO:0000250|UniProtKB:Q7Z6J8}.
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;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with UBE2C/UbcH10 (E2 ubiquitin-conjugating enzyme).
CC       {ECO:0000250|UniProtKB:Q7Z6J8}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The C-terminal half (AA 188-389) is able to bind cyclin-B and
CC       shows a self-ubiquitination activity (mono-, poly, or multi-
CC       ubiquitination) in a HECT-like sequence dependent manner.
CC       {ECO:0000250|UniProtKB:Q7Z6J8}.
CC   -!- PTM: Ubiquitinated by UBCH10 (E2 ubiquitin-conjugating enzyme).
CC       {ECO:0000250|UniProtKB:Q7Z6J8}.
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DR   EMBL; BC116118; AAI16119.1; -; mRNA.
DR   RefSeq; NP_001069179.1; NM_001075711.1.
DR   AlphaFoldDB; Q1JQA1; -.
DR   STRING; 9913.ENSBTAP00000037931; -.
DR   PaxDb; Q1JQA1; -.
DR   PRIDE; Q1JQA1; -.
DR   Ensembl; ENSBTAT00000038115; ENSBTAP00000037931; ENSBTAG00000019418.
DR   GeneID; 515386; -.
DR   KEGG; bta:515386; -.
DR   CTD; 90025; -.
DR   VEuPathDB; HostDB:ENSBTAG00000019418; -.
DR   VGNC; VGNC:36602; UBE3D.
DR   eggNOG; KOG4784; Eukaryota.
DR   GeneTree; ENSGT00390000003986; -.
DR   HOGENOM; CLU_060972_0_0_1; -.
DR   InParanoid; Q1JQA1; -.
DR   OMA; DPFANRK; -.
DR   OrthoDB; 1587082at2759; -.
DR   TreeFam; TF324684; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Chromosome 9.
DR   Bgee; ENSBTAG00000019418; Expressed in choroid plexus and 108 other tissues.
DR   ExpressionAtlas; Q1JQA1; baseline.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR   GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0051865; P:protein autoubiquitination; IBA:GO_Central.
DR   GO; GO:0006513; P:protein monoubiquitination; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   InterPro; IPR019193; UBQ-conj_enz_E2-bd_prot.
DR   PANTHER; PTHR31531; PTHR31531; 1.
DR   Pfam; PF09814; HECT_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Reference proteome; Transferase; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6J8"
FT   CHAIN           2..389
FT                   /note="E3 ubiquitin-protein ligase E3D"
FT                   /id="PRO_0000311189"
FT   REGION          235..257
FT                   /note="Interaction with UBE2C"
FT                   /evidence="ECO:0000250"
FT   REGION          353..389
FT                   /note="HECT-like"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6J8"
SQ   SEQUENCE   389 AA;  43392 MW;  D48C18F37693922C CRC64;
     MAAVAAEARV FLEVRRRLQS ALLILGDSKE GGLPMAVSVT PSSLRMQSPG GCTELRLPAG
     VRLAPSTCRG LQHVPGDGLH LRLHARAESR PELISVFNQS SQDQECCTFY CQSCGEVIIR
     DRMLLRVLPL PGDNWGALVD EWCCHPDPFA NKPLHPREND CFTGDCFYLV NLKSDLWQPR
     PEGAPVETHH LSSENHLKLK PKANTKVICK RCKVMLGETV SSETTKFYMT EIIILPSERN
     FPIIPRSQFV QSVLAQCVVE LSSARSTFRF TIQGHDDKVY ILLWLLNSDS LVIESLGQYT
     NIKKFPVLED VLKPDSNSAC NAVKVLYQPC IKSRNAELSS LWENDLSVHS LTLPSTTCLE
     LLLILSKSNA TLPPSLRCMN SFQVAFLKM