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Ubiquitin recognition factor in ER-associated degradation protein 1 (Ubiquitin fusion degradation protein 1 homolog) (UB fusion protein 1)

 UFD1_RAT                Reviewed;         307 AA.
Q9ES53;
05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-MAY-2022, entry version 106.
RecName: Full=Ubiquitin recognition factor in ER-associated degradation protein 1;
AltName: Full=Ubiquitin fusion degradation protein 1 homolog;
Short=UB fusion protein 1;
Name=Ufd1 {ECO:0000312|RGD:619822};
Synonyms=Ufd1l {ECO:0000312|RGD:619822};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH NPLOC4 AND VCP, AND
SUBCELLULAR LOCATION.
PubMed=10811609; DOI=10.1093/emboj/19.10.2181;
Meyer H.H., Shorter J.G., Seemann J., Pappin D., Warren G.;
"A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to
ubiquitin and nuclear transport pathways.";
EMBO J. 19:2181-2192(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Brown Norway/Mcwi {ECO:0000269|PubMed:15489334};
TISSUE=Spleen {ECO:0000312|EMBL:AAI61818.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY.
Maurya D.K., Bhargava P.;
Submitted (MAR-2009) to UniProtKB.
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14 different rat
organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Essential component of the ubiquitin-dependent proteolytic
pathway which degrades ubiquitin fusion proteins. The ternary complex
containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is
necessary for the export of misfolded proteins from the ER to the
cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-
VCP complex regulates spindle disassembly at the end of mitosis and is
necessary for the formation of a closed nuclear envelope. It may be
involved in the development of some ectoderm-derived structures
(PubMed:10811609). Acts as a negative regulator of type I interferon
production via the complex formed with VCP and NPLOC4, which binds to
DDX58/RIG-I and recruits RNF125 to promote ubiquitination and
degradation of DDX58/RIG-I (By similarity).
{ECO:0000250|UniProtKB:Q92890, ECO:0000269|PubMed:10811609}.
-!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent pathway.
{ECO:0000269|PubMed:10811609}.
-!- SUBUNIT: Interacts with USP13 (By similarity). Heterodimer with NPLOC4,
this heterodimer binds VCP and inhibits Golgi membrane fusion
(PubMed:10811609). Interacts with ZFAND2B; probably through VCP (By
similarity). {ECO:0000250|UniProtKB:Q92890,
ECO:0000269|PubMed:10811609}.
-!- INTERACTION:
Q9ES53; Q9ES54: Nploc4; NbExp=6; IntAct=EBI-399031, EBI-1993990;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10811609}. Cytoplasm,
cytosol {ECO:0000269|PubMed:10811609}.
-!- SIMILARITY: Belongs to the UFD1 family. {ECO:0000255}.
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EMBL; AF234601; AAG27535.1; -; mRNA.
EMBL; CH473999; EDL77960.1; -; Genomic_DNA.
EMBL; BC161818; AAI61818.1; -; mRNA.
RefSeq; NP_445870.1; NM_053418.2.
AlphaFoldDB; Q9ES53; -.
SMR; Q9ES53; -.
BioGRID; 249978; 4.
ComplexPortal; CPX-138; Vcp-Npl4-Ufd1 AAA ATPase complex.
CORUM; Q9ES53; -.
IntAct; Q9ES53; 6.
MINT; Q9ES53; -.
STRING; 10116.ENSRNOP00000067081; -.
iPTMnet; Q9ES53; -.
PhosphoSitePlus; Q9ES53; -.
jPOST; Q9ES53; -.
PaxDb; Q9ES53; -.
Ensembl; ENSRNOT00000100452; ENSRNOP00000084640; ENSRNOG00000047394.
GeneID; 84478; -.
KEGG; rno:84478; -.
CTD; 7353; -.
RGD; 619822; Ufd1.
eggNOG; KOG1816; Eukaryota.
GeneTree; ENSGT00390000002408; -.
HOGENOM; CLU_037790_2_0_1; -.
InParanoid; Q9ES53; -.
OMA; NIEYPMI; -.
OrthoDB; 1134444at2759; -.
PhylomeDB; Q9ES53; -.
Reactome; R-RNO-110320; Translesion Synthesis by POLH.
Reactome; R-RNO-5689880; Ub-specific processing proteases.
UniPathway; UPA00144; -.
PRO; PR:Q9ES53; -.
Proteomes; UP000002494; Chromosome 11.
Proteomes; UP000234681; Chromosome 11.
Bgee; ENSRNOG00000047394; Expressed in heart and 22 other tissues.
Genevisible; Q9ES53; RN.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0036501; C:UFD1-NPL4 complex; IDA:ParkinsonsUK-UCL.
GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:ParkinsonsUK-UCL.
GO; GO:0051117; F:ATPase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; ISO:RGD.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISO:RGD.
GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; ISS:UniProtKB.
GO; GO:0032480; P:negative regulation of type I interferon production; ISS:UniProtKB.
GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:RGD.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
Gene3D; 2.40.40.50; -; 1.
InterPro; IPR004854; Ufd1-like.
InterPro; IPR042299; Ufd1-like_Nn.
PANTHER; PTHR12555; PTHR12555; 1.
Pfam; PF03152; UFD1; 1.
1: Evidence at protein level;
Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
Ubl conjugation pathway.
CHAIN 1..307
/note="Ubiquitin recognition factor in ER-associated
degradation protein 1"
/id="PRO_0000371229"
REGION 230..255
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 282..307
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0000250|UniProtKB:Q92890"
MOD_RES 129
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92890"
MOD_RES 231
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92890"
MOD_RES 245
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92890"
MOD_RES 247
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q92890"
MOD_RES 299
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:22673903"
SEQUENCE 307 AA; 34485 MW; C482D6B1B910494D CRC64;
MFSFNMFDHP IPRVFQNRFS TQYRCFSVSM LAGPNDRSDV EKGGKIIMPP SALDQLSRLN
ITYPMLFKLT NKNSDRMTHC GVLEFVADEG ICYLPHWMMQ NLLLEEGGLV QVESVNLQVA
TYSKFQPQSP DFLDITNPKA VLENALRNFA CLTTGDVIAI NYNEKIYELR VMETKPDKAV
SIIECDMNVD FDAPLGYKEP ERPVQHEESI EGEADHSGYA GEVGFRAFSG SGNRLDGKKK
GVEPSPSPIK PGDIKRGIPN YEFKLGKITF IRNSRPMVKK VEEDEAGGRF VAFSGEGQSL
RKKGRKP


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