DNJC1_MOUSE
ID DNJC1_MOUSE Reviewed; 552 AA.
AC Q61712;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=DnaJ homolog subfamily C member 1;
DE AltName: Full=DnaJ protein homolog MTJ1;
DE Flags: Precursor;
GN Name=Dnajc1; Synonyms=Dnajl1, Mtj1;
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 STRAIN=C57BL/6J; TISSUE=Lung carcinoma;
RX PubMed=7875597; DOI=10.1016/0378-1119(94)00741-a;
RA Brightman S.E., Blatch G.L., Zetter B.R.;
RT "Isolation of a mouse cDNA encoding MTJ1, a new murine member of the DnaJ
RT family of proteins.";
RL Gene 153:249-254(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-478, AND
RP IDENTIFICATION BY 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-478, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, 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).
CC -!- FUNCTION: May modulate protein synthesis. {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via J domain) with HSPA5. Interacts (via cytosolic
CC domain) with ribosomes. Interacts (via SANT 2 domain) with SERPINA3;
CC the interaction delays the formation of the covalent inhibitory complex
CC SERPINA3-chymotrypsin, but does not alter the catalytic activity of
CC SERPINA3. Interacts (via SANT 2 domain) with ITIH4 (via C-terminus);
CC the interaction protects ITIH4 against in vitro cleavage by kallikrein
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC I membrane protein. Nucleus membrane; Single-pass type I membrane
CC protein. Microsome membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Widely expressed.
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DR EMBL; L16953; AAA66349.1; -; mRNA.
DR EMBL; BC080300; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS15709.1; -.
DR PIR; JC4030; JC4030.
DR RefSeq; NP_001177746.1; NM_001190817.1.
DR RefSeq; NP_031895.1; NM_007869.3.
DR AlphaFoldDB; Q61712; -.
DR SMR; Q61712; -.
DR BioGRID; 199250; 4.
DR DIP; DIP-60498N; -.
DR IntAct; Q61712; 1.
DR STRING; 10090.ENSMUSP00000126321; -.
DR iPTMnet; Q61712; -.
DR PhosphoSitePlus; Q61712; -.
DR EPD; Q61712; -.
DR jPOST; Q61712; -.
DR MaxQB; Q61712; -.
DR PaxDb; Q61712; -.
DR PeptideAtlas; Q61712; -.
DR PRIDE; Q61712; -.
DR ProteomicsDB; 279459; -.
DR Antibodypedia; 2466; 92 antibodies from 24 providers.
DR DNASU; 13418; -.
DR Ensembl; ENSMUST00000091418; ENSMUSP00000088980; ENSMUSG00000026740.
DR Ensembl; ENSMUST00000166495; ENSMUSP00000126321; ENSMUSG00000026740.
DR GeneID; 13418; -.
DR KEGG; mmu:13418; -.
DR UCSC; uc008ilt.2; mouse.
DR CTD; 64215; -.
DR MGI; MGI:103268; Dnajc1.
DR VEuPathDB; HostDB:ENSMUSG00000026740; -.
DR eggNOG; KOG0724; Eukaryota.
DR GeneTree; ENSGT00940000156678; -.
DR HOGENOM; CLU_036945_2_0_1; -.
DR InParanoid; Q61712; -.
DR OMA; KEECVAR; -.
DR OrthoDB; 972481at2759; -.
DR PhylomeDB; Q61712; -.
DR TreeFam; TF105161; -.
DR BioGRID-ORCS; 13418; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Dnajc1; mouse.
DR PRO; PR:Q61712; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q61712; protein.
DR Bgee; ENSMUSG00000026740; Expressed in lacrimal gland and 256 other tissues.
DR ExpressionAtlas; Q61712; baseline and differential.
DR Genevisible; Q61712; MM.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; TAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0051087; F:chaperone binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0043022; F:ribosome binding; TAS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IDA:MGI.
DR GO; GO:0050708; P:regulation of protein secretion; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IDA:MGI.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd00167; SANT; 2.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW Chaperone; DNA-binding; Endoplasmic reticulum; Membrane; Microsome;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..43
FT /evidence="ECO:0000255"
FT CHAIN 44..552
FT /note="DnaJ homolog subfamily C member 1"
FT /id="PRO_0000071043"
FT TOPO_DOM 44..149
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..552
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 56..129
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 323..377
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 490..545
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 370..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96KC8"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 552 AA; 63870 MW; 8DFABB217717ECDA CRC64;
MWVPGFGSAR LPQRRRSGLE SSSVRPLWLL LLFLLAAVRP VRAWESGDLE LFDLVEEVQL
NFYEFLGVQQ DASSADIRKA YRKLSLTLHP DKNKDENAET QFRQLVAIYE VLKDDERRQR
YDDVLINGLP DWRQPVFYYR RVRKMSNAEL ALLLFIILTV GHYAVVWSIY LEKQLDELLG
RKKRERKKKT GSKSVDAAKL GASEKNERLL IKPQWHDLLP CKLGIWFCLT LKALPHLIQD
AGQFYAKYKE TKLKEKEDAL ARIEIETLQK QKKVKVKKPK PEFPVYMPLE NTYIQSYDHG
TSIEEIEEQM DDWLENRKRT QKRQAPEWTE EDLSQLTRSM VKFPGGTPGR WDKIAHELGR
SVTDVTTKAK ELKDSVTSSP GMTRLSELKS NGQNSRPIKI ATALPDDIIT QREDSAGAME
DEEHEAAEGE QESATTEARP RRRKSARAAE AVTRVEPEEK LRGKRQKDFD ISEQNDSSDE
EKQRKERTRA AEEAWTQSQQ KLLELALQQY PKGASDRWDK IAKCVPSKSK EDCIARYKLL
VELVQKKKQA KS
