ID   UBE3D_RAT               Reviewed;         370 AA.
AC   Q3T1H6;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, 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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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 167-370) 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; BC101916; AAI01917.1; -; mRNA.
DR   RefSeq; NP_001034699.1; NM_001039610.1.
DR   AlphaFoldDB; Q3T1H6; -.
DR   STRING; 10116.ENSRNOP00000014600; -.
DR   PhosphoSitePlus; Q3T1H6; -.
DR   PaxDb; Q3T1H6; -.
DR   Ensembl; ENSRNOT00000014600; ENSRNOP00000014600; ENSRNOG00000010802.
DR   GeneID; 315863; -.
DR   KEGG; rno:315863; -.
DR   UCSC; RGD:1306773; rat.
DR   CTD; 90025; -.
DR   RGD; 1306773; Ube3d.
DR   eggNOG; KOG4784; Eukaryota.
DR   GeneTree; ENSGT00390000003986; -.
DR   InParanoid; Q3T1H6; -.
DR   OMA; DPFANRK; -.
DR   OrthoDB; 1587082at2759; -.
DR   PhylomeDB; Q3T1H6; -.
DR   TreeFam; TF324684; -.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q3T1H6; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000010802; Expressed in quadriceps femoris and 18 other tissues.
DR   ExpressionAtlas; Q3T1H6; baseline and differential.
DR   Genevisible; Q3T1H6; RN.
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; ISO:RGD.
DR   GO; GO:0030332; F:cyclin binding; ISO:RGD.
DR   GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR   GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; ISO:RGD.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0051865; P:protein autoubiquitination; ISO:RGD.
DR   GO; GO:0006513; P:protein monoubiquitination; ISO:RGD.
DR   GO; GO:0000209; P:protein polyubiquitination; ISO:RGD.
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..370
FT                   /note="E3 ubiquitin-protein ligase E3D"
FT                   /id="PRO_0000311193"
FT   REGION          214..236
FT                   /note="Interaction with UBE2C"
FT                   /evidence="ECO:0000250"
FT   REGION          332..368
FT                   /note="HECT-like"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7Z6J8"
SQ   SEQUENCE   370 AA;  41056 MW;  FF97D69330D51B83 CRC64;
     MAVVEAETRV FLEVRRRLQS ALLILGEPDE GGMNLDISVT PTSLLMRSPD GCTEIRLPAG
     VRLAPSSCGG LQYISGDGLH LRLRAQAESS PQPISGFNQS LQAQECCSFY CQSCGEVTIK
     DRKLLRVLPL PSENWSALVG EWCCHPDPFA NKPLHPREND CFVGDSFFLV NSRSDLEQEP
     KANTKVICKR CKVMLGETVS SETTKFYMTE VIVQPSEGSF PNIPRSQFVQ SVIARCLVEL
     CTARSTFRFT IQGQDGKVYI LLWVLNSDSL VMEPLSSSGC IRKFPLLEDS LEADSGSAWN
     AIKVLYQPCI KSRNKELASS WEGDISVHPL TLPSTTCLEL LLILSRNNAS LPLSLRQMNS
     FQLWCSHCKT