UFD1_RAT
ID UFD1_RAT Reviewed; 307 AA.
AC Q9ES53;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Ubiquitin recognition factor in ER-associated degradation protein 1;
DE AltName: Full=Ubiquitin fusion degradation protein 1 homolog;
DE Short=UB fusion protein 1;
GN Name=Ufd1 {ECO:0000312|RGD:619822};
GN Synonyms=Ufd1l {ECO:0000312|RGD:619822};
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], FUNCTION, INTERACTION WITH NPLOC4 AND VCP, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10811609; DOI=10.1093/emboj/19.10.2181;
RA Meyer H.H., Shorter J.G., Seemann J., Pappin D., Warren G.;
RT "A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to
RT ubiquitin and nuclear transport pathways.";
RL EMBO J. 19:2181-2192(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway/Mcwi {ECO:0000269|PubMed:15489334};
RC TISSUE=Spleen {ECO:0000312|EMBL:AAI61818.1};
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Maurya D.K., Bhargava P.;
RL Submitted (MAR-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Essential component of the ubiquitin-dependent proteolytic
CC pathway which degrades ubiquitin fusion proteins. The ternary complex
CC containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is
CC necessary for the export of misfolded proteins from the ER to the
CC cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-
CC VCP complex regulates spindle disassembly at the end of mitosis and is
CC necessary for the formation of a closed nuclear envelope. It may be
CC involved in the development of some ectoderm-derived structures
CC (PubMed:10811609). Acts as a negative regulator of type I interferon
CC production via the complex formed with VCP and NPLOC4, which binds to
CC DDX58/RIG-I and recruits RNF125 to promote ubiquitination and
CC degradation of DDX58/RIG-I (By similarity).
CC {ECO:0000250|UniProtKB:Q92890, ECO:0000269|PubMed:10811609}.
CC -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent pathway.
CC {ECO:0000269|PubMed:10811609}.
CC -!- SUBUNIT: Interacts with USP13 (By similarity). Heterodimer with NPLOC4,
CC this heterodimer binds VCP and inhibits Golgi membrane fusion
CC (PubMed:10811609). Interacts with ZFAND2B; probably through VCP (By
CC similarity). {ECO:0000250|UniProtKB:Q92890,
CC ECO:0000269|PubMed:10811609}.
CC -!- INTERACTION:
CC Q9ES53; Q9ES54: Nploc4; NbExp=6; IntAct=EBI-399031, EBI-1993990;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10811609}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:10811609}.
CC -!- SIMILARITY: Belongs to the UFD1 family. {ECO:0000255}.
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DR EMBL; AF234601; AAG27535.1; -; mRNA.
DR EMBL; CH473999; EDL77960.1; -; Genomic_DNA.
DR EMBL; BC161818; AAI61818.1; -; mRNA.
DR RefSeq; NP_445870.1; NM_053418.2.
DR AlphaFoldDB; Q9ES53; -.
DR SMR; Q9ES53; -.
DR BioGRID; 249978; 4.
DR ComplexPortal; CPX-138; Vcp-Npl4-Ufd1 AAA ATPase complex.
DR CORUM; Q9ES53; -.
DR IntAct; Q9ES53; 6.
DR MINT; Q9ES53; -.
DR STRING; 10116.ENSRNOP00000067081; -.
DR iPTMnet; Q9ES53; -.
DR PhosphoSitePlus; Q9ES53; -.
DR jPOST; Q9ES53; -.
DR PaxDb; Q9ES53; -.
DR PRIDE; Q9ES53; -.
DR Ensembl; ENSRNOT00000100452; ENSRNOP00000084640; ENSRNOG00000047394.
DR GeneID; 84478; -.
DR KEGG; rno:84478; -.
DR CTD; 7353; -.
DR RGD; 619822; Ufd1.
DR eggNOG; KOG1816; Eukaryota.
DR GeneTree; ENSGT00390000002408; -.
DR HOGENOM; CLU_037790_2_0_1; -.
DR InParanoid; Q9ES53; -.
DR OMA; NIEYPMI; -.
DR OrthoDB; 1134444at2759; -.
DR PhylomeDB; Q9ES53; -.
DR Reactome; R-RNO-110320; Translesion Synthesis by POLH.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-9755511; KEAP1-NFE2L2 pathway.
DR UniPathway; UPA00144; -.
DR PRO; PR:Q9ES53; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Proteomes; UP000234681; Chromosome 11.
DR Bgee; ENSRNOG00000047394; Expressed in heart and 20 other tissues.
DR Genevisible; Q9ES53; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0036501; C:UFD1-NPL4 complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:0051117; F:ATPase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; ISO:RGD.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISO:RGD.
DR GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; ISS:UniProtKB.
DR GO; GO:0032480; P:negative regulation of type I interferon production; ISS:UniProtKB.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:RGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 2.40.40.50; -; 1.
DR InterPro; IPR004854; Ufd1-like.
DR InterPro; IPR042299; Ufd1-like_Nn.
DR PANTHER; PTHR12555; PTHR12555; 1.
DR Pfam; PF03152; UFD1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..307
FT /note="Ubiquitin recognition factor in ER-associated
FT degradation protein 1"
FT /id="PRO_0000371229"
FT REGION 230..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q92890"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92890"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92890"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92890"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92890"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ 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
