UBD_RAT
ID UBD_RAT Reviewed; 161 AA.
AC Q921A3; Q6MFX3;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Ubiquitin D;
DE AltName: Full=Diubiquitin;
DE AltName: Full=Ubiquitin-like protein FAT10;
GN Name=Ubd; Synonyms=Fat10;
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 [MRNA].
RA Walter L.;
RT "Characterization of the rat Ubd gene.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
CC -!- FUNCTION: Ubiquitin-like protein modifier which can be covalently
CC attached to target protein and subsequently leads to their degradation
CC by the 26S proteasome, in a NUB1-dependent manner. Probably functions
CC as a survival factor. Promotes the expression of the proteasome subunit
CC beta type-9 (PSMB9/LMP2). Regulates TNF-alpha-induced and LPS-mediated
CC activation of the central mediator of innate immunity NF-kappa-B by
CC promoting TNF-alpha-mediated proteasomal degradation of ubiquitinated-
CC I-kappa-B-alpha. Required for TNF-alpha-induced p65 nuclear
CC translocation in renal tubular epithelial cells (RTECs). May be
CC involved in dendritic cell (DC) maturation, the process by which
CC immature dendritic cells differentiate into fully competent antigen-
CC presenting cells that initiate T-cell responses. Mediates mitotic non-
CC disjunction and chromosome instability, in long-term in vitro culture
CC and cancers, by abbreviating mitotic phase and impairing the
CC kinetochore localization of MAD2L1 during the prometaphase stage of the
CC cell cycle. May be involved in the formation of aggresomes when
CC proteasome is saturated or impaired. Mediates apoptosis in a caspase-
CC dependent manner, especially in renal epithelium and tubular cells
CC during renal diseases (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts directly with the 26S proteasome. The interaction
CC with NUB1 via the N-terminal ubiquitin domain facilitates the linking
CC of UBD-conjugated target protein to the proteasome complex and
CC accelerates its own degradation and that of its conjugates. Interacts
CC (via ubiquitin-like 1 domain) with the spindle checkpoint protein
CC MAD2L1 during mitosis. Present in aggresomes of proteasome inhibited
CC cells. Interacts with HDAC6 under proteasome impairment conditions.
CC Forms a thioester with UBA6 in cells stimulated with tumor necrosis
CC factor-alpha (TNFa) and interferon-gamma (IFNg). Interacts with SQSTM1
CC and TP53/p53 (By similarity). {ECO:0000250|UniProtKB:O15205}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Accumulates in aggresomes under proteasome inhibition conditions.
CC {ECO:0000250}.
CC -!- INDUCTION: Possible cell-cycle regulation with highest expression
CC during the S-phase (at protein level). Probably rapidly degraded by the
CC proteasome.
CC -!- PTM: Can be acetylated. {ECO:0000250}.
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DR EMBL; AJ312394; CAC42833.1; -; mRNA.
DR EMBL; BX883052; CAE84074.1; -; Genomic_DNA.
DR RefSeq; NP_445751.2; NM_053299.2.
DR AlphaFoldDB; Q921A3; -.
DR SMR; Q921A3; -.
DR STRING; 10116.ENSRNOP00000000995; -.
DR PhosphoSitePlus; Q921A3; -.
DR PaxDb; Q921A3; -.
DR GeneID; 29168; -.
DR KEGG; rno:29168; -.
DR UCSC; RGD:69418; rat.
DR CTD; 10537; -.
DR RGD; 69418; Ubd.
DR eggNOG; KOG0001; Eukaryota.
DR InParanoid; Q921A3; -.
DR OrthoDB; 1377739at2759; -.
DR PhylomeDB; Q921A3; -.
DR Reactome; R-RNO-8951664; Neddylation.
DR PRO; PR:Q921A3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016235; C:aggresome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; ISS:UniProtKB.
DR GO; GO:0070842; P:aggresome assembly; ISS:UniProtKB.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0034341; P:response to interferon-gamma; ISO:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0034612; P:response to tumor necrosis factor; ISO:RGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR042969; Ubiquitin_D.
DR InterPro; IPR019956; Ubiquitin_dom.
DR PANTHER; PTHR47731; PTHR47731; 1.
DR Pfam; PF00240; ubiquitin; 2.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 2.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..161
FT /note="Ubiquitin D"
FT /id="PRO_0000114895"
FT DOMAIN 3..77
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 86..159
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT SITE 160..161
FT /note="Activation by thioester intermediate formation with
FT UBA6"
FT /evidence="ECO:0000250"
FT CONFLICT 9
FT /note="R -> H (in Ref. 2; CAE84074)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="I -> F (in Ref. 2; CAE84074)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 17983 MW; 5BAB9D199885A0D8 CRC64;
MASCVCVVRS EQWPLMTFDT TMSDKVKKIN EHIRSQTKVS VQDQILLLDS KILKPHRALS
SYGIDKENTI HLTLKVVKPS DEELPLSLVE SGDEGQRHLL RVRRSSSVAQ VKEMIENVTA
VPPKKQIVNC NGKRLEDGKI MADYNIKSGS LLFLTAHCIG G
