ID   UBE4A_RAT               Reviewed;        1066 AA.
AC   Q6P7A2;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Ubiquitin conjugation factor E4 A {ECO:0000305};
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:E9Q735};
DE   AltName: Full=RING-type E3 ubiquitin transferase E4 A;
GN   Name=Ube4a {ECO:0000312|RGD:1303173};
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: Ubiquitin-protein ligase that probably functions as an E3
CC       ligase in conjunction with specific E1 and E2 ligases. May also
CC       function as an E4 ligase mediating the assembly of polyubiquitin chains
CC       on substrates ubiquitinated by another E3 ubiquitin ligase. Mediates
CC       'Lys-48'-linked polyubiquitination of substrates.
CC       {ECO:0000250|UniProtKB:E9Q735, ECO:0000250|UniProtKB:P54860}.
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=2.3.2.27;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000250|UniProtKB:E9Q735}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:E9Q735}.
CC   -!- DOMAIN: The U-box domain is required for the ubiquitin protein ligase
CC       activity. {ECO:0000250|UniProtKB:P54860, ECO:0000250|UniProtKB:Q9ES00}.
CC   -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC       {ECO:0000305}.
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DR   EMBL; BC061761; AAH61761.1; -; mRNA.
DR   RefSeq; NP_997493.1; NM_207610.1.
DR   AlphaFoldDB; Q6P7A2; -.
DR   SMR; Q6P7A2; -.
DR   BioGRID; 261081; 2.
DR   IntAct; Q6P7A2; 1.
DR   STRING; 10116.ENSRNOP00000021321; -.
DR   PhosphoSitePlus; Q6P7A2; -.
DR   PaxDb; Q6P7A2; -.
DR   PeptideAtlas; Q6P7A2; -.
DR   PRIDE; Q6P7A2; -.
DR   GeneID; 315608; -.
DR   KEGG; rno:315608; -.
DR   UCSC; RGD:1303173; rat.
DR   CTD; 9354; -.
DR   RGD; 1303173; Ube4a.
DR   eggNOG; KOG2042; Eukaryota.
DR   InParanoid; Q6P7A2; -.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q6P7A2; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; ISO:RGD.
DR   GO; GO:0000209; P:protein polyubiquitination; ISO:RGD.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR   InterPro; IPR045132; UBE4.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR13931; PTHR13931; 1.
DR   Pfam; PF04564; U-box; 1.
DR   Pfam; PF10408; Ufd2P_core; 1.
DR   SMART; SM00504; Ubox; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..1066
FT                   /note="Ubiquitin conjugation factor E4 A"
FT                   /id="PRO_0000194992"
FT   DOMAIN          987..1061
FT                   /note="U-box"
FT   REGION          35..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         386
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14139"
SQ   SEQUENCE   1066 AA;  122379 MW;  0B54EAA379B4DAF6 CRC64;
     MTDQENNNNI SSNPFAALFG SLADAKQFAA IHKEQLKQQS DELPASPDDS DNSVSESLDE
     FDYSVSEISR SFRTHQEMCE QLNINHMIQR IFLITLDNSD PNLKSGNGIP SRCVYLEEMA
     VELEDQDWLD MSNVEQAIFA RLLLQDPGNH LISMTSSATL NLSADRDAGE RHIFCYLYSC
     FQRAKEEITK VPENLLPFAV QCRNLTVSNT RTVLLTPEIY VDQNIHEQLV DLMLEAIQGA
     HFEDVTEFLE EVIEALLLDE EVRTFPEVMI PVFDILLGRI KDLELCQILL YAYLDILLYF
     TRQKDMAKVF LEYIQPKDPS NGQMYQKTLL GVILNISCLL KTPGVVENHG FFLNPSRSSP
     QEIKVQEANI HQFMAQFHEK IYQMLKNLLQ LSPETKHGIL FWLGNCLHAN AGRTKIWANQ
     MPEIFFQMYA SDAFFLNLGA ALLKLCQPFC KPRSSRLLTF NPTYCVLKDL NDEERKIKSV
     HMRGLDKETC LIPAVQEPVF PQSYNLVTEN LALTEYTLYL GFHRLHDQMV KINQNLHRLQ
     VAWRDAQQSS SPAADNLREQ FERLMTIYLS TKTAMTEPQM LQNCLNLQVS MAVLLVQLAI
     GNEGSQPIEL SFPLPDGYSS LAYVPEFFAD NLGDFLIFLR RFAEDILETS ADSLEHVLHF
     ITIFTGSIER MKNPHLRAKL AEVLEAVMPH LDQTPSPLVS SVFHRKRVFC NFPYAPQLSE
     ALIKVFVDIE FTGDPHQFEQ KFNYRRPMYP ILRYMWGTDS YRESIKDLAD YASKNLEAMN
     PPLFLRFLNL LMNDAIFLLD EAIQYLSKIK IQQIEKDRGE WESLTPEARR EKEAGLQMFG
     QLARFHNIMS NETIGTLSFL TSEIKSLFVH PFLAERIISM LNYFLQHLVG PKMGALKVKD
     FSEFDFKPQQ LVSDICTIYL NLGDEENFCA TVPKDGRSYS PTLFAQTVRV LKKINKPGNM
     IVAFSNLAER IKSLADLQQQ EEETYADACD EFLDPIMSTL MSDPVVLPSS RVTVDGSTIA
     RHLLSDQTDP FNRSPLTMDQ IRPNTELKEK IQRWLAERKQ QKEQLE