UFD1_MOUSE
ID UFD1_MOUSE Reviewed; 307 AA.
AC P70362; Q923C4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 148.
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|MGI:MGI:109353}; Synonyms=Ufd1l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9063746; DOI=10.1093/hmg/6.2.259;
RA Pizzuti A., Novelli G., Ratti A., Amati F., Mari A., Calabrese G.,
RA Nicolis S., Silani V., Marino B., Scarlato G., Ottolenghi S.,
RA Dallapiccola B.;
RT "UFD1L, a developmentally expressed ubiquitination gene, is deleted in
RT CATCH 22 syndrome.";
RL Hum. Mol. Genet. 6:259-265(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND SER-299, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH ZFAND2B.
RX PubMed=24160817; DOI=10.1042/bj20130710;
RA Glinka T., Alter J., Braunstein I., Tzach L., Wei Sheng C., Geifman S.,
RA Edelmann M.J., Kessler B.M., Stanhill A.;
RT "Signal-peptide-mediated translocation is regulated by a p97-AIRAPL
RT complex.";
RL Biochem. J. 457:253-261(2014).
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 (By
CC similarity). 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:0000250|UniProtKB:Q9ES53}.
CC -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent pathway.
CC {ECO:0000250|UniProtKB:Q9ES53}.
CC -!- SUBUNIT: Heterodimer with NPLOC4, this heterodimer binds VCP and
CC inhibits Golgi membrane fusion. Interacts with USP13 (By similarity).
CC Interacts with ZFAND2B; probably through VCP (PubMed:24160817).
CC {ECO:0000250|UniProtKB:Q92890, ECO:0000269|PubMed:24160817}.
CC -!- INTERACTION:
CC P70362; Q01853: Vcp; NbExp=9; IntAct=EBI-7961331, EBI-80597;
CC P70362; Q9ES54: Nploc4; Xeno; NbExp=18; IntAct=EBI-7961331, EBI-1993990;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ES53}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9ES53}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels in the otocyst (between
CC 9.5 dpc and 11.5 dpc embryos fading away after 12 dpc) and in the
CC developing eye. Lower expression is found in different sites of the
CC embryos such as developing brain, the lungs and the cardiac outflow
CC tract.
CC -!- SIMILARITY: Belongs to the UFD1 family. {ECO:0000305}.
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DR EMBL; U64445; AAD08719.1; -; mRNA.
DR EMBL; AK147138; BAE27708.1; -; mRNA.
DR EMBL; AK169062; BAE40849.1; -; mRNA.
DR EMBL; CH466521; EDK97535.1; -; Genomic_DNA.
DR EMBL; BC006630; AAH06630.1; -; mRNA.
DR CCDS; CCDS28028.1; -.
DR RefSeq; NP_035802.3; NM_011672.4.
DR RefSeq; XP_006522068.1; XM_006522005.3.
DR AlphaFoldDB; P70362; -.
DR SMR; P70362; -.
DR BioGRID; 204430; 35.
DR ComplexPortal; CPX-136; Vcp-Npl4-Ufd1 AAA ATPase complex.
DR CORUM; P70362; -.
DR DIP; DIP-60008N; -.
DR IntAct; P70362; 4.
DR MINT; P70362; -.
DR STRING; 10090.ENSMUSP00000111241; -.
DR iPTMnet; P70362; -.
DR PhosphoSitePlus; P70362; -.
DR SwissPalm; P70362; -.
DR REPRODUCTION-2DPAGE; P70362; -.
DR CPTAC; non-CPTAC-3293; -.
DR EPD; P70362; -.
DR jPOST; P70362; -.
DR MaxQB; P70362; -.
DR PaxDb; P70362; -.
DR PeptideAtlas; P70362; -.
DR PRIDE; P70362; -.
DR ProteomicsDB; 298469; -.
DR Antibodypedia; 22930; 377 antibodies from 32 providers.
DR DNASU; 22230; -.
DR Ensembl; ENSMUST00000005394; ENSMUSP00000005394; ENSMUSG00000005262.
DR Ensembl; ENSMUST00000115578; ENSMUSP00000111241; ENSMUSG00000005262.
DR GeneID; 22230; -.
DR KEGG; mmu:22230; -.
DR UCSC; uc007yon.2; mouse.
DR CTD; 7353; -.
DR MGI; MGI:109353; Ufd1.
DR VEuPathDB; HostDB:ENSMUSG00000005262; -.
DR eggNOG; KOG1816; Eukaryota.
DR GeneTree; ENSGT00390000002408; -.
DR HOGENOM; CLU_037790_2_0_1; -.
DR InParanoid; P70362; -.
DR OMA; NIEYPMI; -.
DR OrthoDB; 1134444at2759; -.
DR PhylomeDB; P70362; -.
DR TreeFam; TF314581; -.
DR Reactome; R-MMU-110320; Translesion Synthesis by POLH.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR UniPathway; UPA00144; -.
DR BioGRID-ORCS; 22230; 25 hits in 71 CRISPR screens.
DR PRO; PR:P70362; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P70362; protein.
DR Bgee; ENSMUSG00000005262; Expressed in dorsomedial nucleus of hypothalamus and 263 other tissues.
DR ExpressionAtlas; P70362; baseline and differential.
DR Genevisible; P70362; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISO:MGI.
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:MGI.
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_0000194985"
FT REGION 230..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..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:0007744|PubMed:21183079"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 152
FT /note="L -> M (in Ref. 1; AAD08719)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="E -> K (in Ref. 1; AAD08719)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="I -> V (in Ref. 1; AAD08719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 34481 MW; C85E06B1B910485D 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 IRNSRPLVKK VEEDEAGGRF IAFSGEGQSL
RKKGRKP
