ID   UBE4A_PONAB             Reviewed;        1066 AA.
AC   Q5R9G3; Q5RCL3;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 2.
DT   25-MAY-2022, entry version 71.
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:0000305};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR858257; CAH90494.1; -; mRNA.
DR   EMBL; CR859425; CAH91597.1; -; mRNA.
DR   RefSeq; NP_001127294.1; NM_001133822.1.
DR   RefSeq; NP_001128821.1; NM_001135349.1.
DR   AlphaFoldDB; Q5R9G3; -.
DR   SMR; Q5R9G3; -.
DR   STRING; 9601.ENSPPYP00000004503; -.
DR   GeneID; 100174352; -.
DR   GeneID; 100189732; -.
DR   KEGG; pon:100189732; -.
DR   CTD; 9354; -.
DR   eggNOG; KOG2042; Eukaryota.
DR   InParanoid; Q5R9G3; -.
DR   OrthoDB; 194967at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:InterPro.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:InterPro.
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_0000194991"
FT   DOMAIN          987..1061
FT                   /note="U-box"
FT   REGION          33..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..52
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"
FT   CONFLICT        460
FT                   /note="F -> S (in Ref. 1; CAH91597)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        594
FT                   /note="L -> P (in Ref. 1; CAH90494)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        771
FT                   /note="Y -> C (in Ref. 1; CAH91597)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1066 AA;  122488 MW;  1DE3707090CE6593 CRC64;
     MTDQENNNNI SSNPFAALFG SLADAKQFAA IQKEQLKQQS DELPASPDDS DNSVSESLDE
     FDYSVAEISR SFRSQQEICE QLNINHMIQR IFLITLDNSD PSLKSGNGIP SRCVYLEEMA
     VELEDQDWLD MGNVEQALFA RLLLQDPGNH LINMTSSTTL NLSADRDAGE RHIFCYLYSC
     FQRAKEEITK VPENLLPFAV QCRNLTVSNT RTVLLTPEIY VDQNIHEQLV DLMLEAIQGA
     HFEDVTEFLE EVIEALILDE EVRTFSEVMI PVFDILLGRI KDLELCQILL YAYLDILLYF
     TRQKDMAKVF VEYIQPKDPT NGQMYQKTLL GVILNISCLL KTPGVVENHG YFLNPSRSSP
     QEIKVQEANI HQFMAQFHEK IYQMLKNLLQ LSPETKHCIL SWLGNCLHAN AGRTKIWANQ
     MPEIFFQMYA SDAFFLNLGA ALLKLCQPFC KPRSSRLLTF NPTYCALKEL NDEERKIKNV
     HMRGLDKETC LIPAVQEPKF PQNYNLVTEN LALTEYTLYL GFHRLHDQMV KINQNLHRLQ
     VAWRDAQQSS SPAADSLREQ FERLMTIYLS TKTAMTEPQM LQNCLNLQVS MAVLLVQLAI
     GNEGSQPIEL TFPLPDGYSS LAYVPEFFAD NLGDFLIFLR RFADDILETS ADSLEHVLHF
     ITIFTGSIER MKNPHLRAKL AEVLEAVMPH LDQTPNPLVS SVFHRKRVFC NFQYAPQLAE
     ALIKVFVDIE FTGDPHQFEQ KFNYRRPMYP ILRYMWGTDT YRESIKDLAD YASKNLEAMN
     PPLFLRFLNL LMNDAIFLLD EAIQYLSKIK IQQIEKDRGE WDSLTPEARR EKEAGLQMFG
     QLARFHNIMS NETIGTLAFL TSEIKSLFVH PFLAERIISM LNYFLQHLVG PKMGALKVKD
     FSEFDFKPQQ LVSDICTIYL NLGDEENFCA TVPKDGRSYS PTLFAQTVRV LKKINKPGNM
     IVAFSNLAER IKSLADLQQQ EEETYADACD EFLDPIMSTL MCDPVVLPSS RVTVDRSTIA
     RHLLSDQTDP FNRSPLTMDQ IRPNTELKEK IQRWLAERKQ QKEQLE