DNJC7_MOUSE
ID DNJC7_MOUSE Reviewed; 494 AA.
AC Q9QYI3; Q3TKR1; Q6VVW6; Q8BPG3; Q8CIL2; Q9CT29; Q9D026;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=DnaJ homolog subfamily C member 7;
DE AltName: Full=Cytoplasmic CAR retention protein;
DE Short=CCRP;
DE AltName: Full=MDj11;
DE AltName: Full=Tetratricopeptide repeat protein 2;
DE Short=TPR repeat protein 2;
GN Name=Dnajc7; Synonyms=Ttc2;
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=C3H/HeJ;
RX PubMed=11147971; DOI=10.1379/1466-1268(2000)005<0098:mhdhco>2.0.co;2;
RA Ohtsuka K., Hata M.;
RT "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for
RT their classification and nomenclature.";
RL Cell Stress Chaperones 5:98-112(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [MRNA], INTERACTION WITH NR1I3 AND HSP90, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=14573755; DOI=10.1124/mol.64.5.1069;
RA Kobayashi K., Sueyoshi T., Inoue K., Moore R., Negishi M.;
RT "Cytoplasmic accumulation of the nuclear receptor CAR by a
RT tetratricopeptide repeat protein in HepG2 cells.";
RL Mol. Pharmacol. 64:1069-1075(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; 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 [5]
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).
CC -!- FUNCTION: Acts as co-chaperone regulating the molecular chaperones
CC HSP70 and HSP90 in folding of steroid receptors, such as the
CC glucocorticoid receptor and the progesterone receptor. Proposed to act
CC as a recycling chaperone by facilitating the return of chaperone
CC substrates to early stages of chaperoning if further folding is
CC required. In vitro, induces ATP-independent dissociation of HSP90 but
CC not of HSP70 from the chaperone-substrate complexes (By similarity).
CC Recruits NR1I3 to the cytoplasm. {ECO:0000250}.
CC -!- SUBUNIT: Associates with complexes containing chaperones HSP70 and
CC HSP90. Interacts with the GAP domain of NF1. Interacts with HSP90AA1.
CC Interacts with HSPA1A/B; the interaction is enhanced by ATP. Interacts
CC with HSP90AB1. Interacts with PGR. Interacts with RAD9A; the
CC interaction is interrupted by UV and heat shock treatments. Interacts
CC with HUS1 and RAD1 (By similarity). Interacts with NR1I3; this complex
CC may also include HSP90 Interacts with HSPA8 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14573755}. Nucleus
CC {ECO:0000250|UniProtKB:Q99615}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14573755}. Note=Colocalizes with NR1I3 at
CC microtubules. {ECO:0000269|PubMed:14573755}.
CC -!- TISSUE SPECIFICITY: Widely expressed with high levels in liver,
CC skeletal muscle, kidney and testis. {ECO:0000269|PubMed:14573755}.
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DR EMBL; AB028861; BAA88309.1; -; mRNA.
DR EMBL; AK011384; BAB27584.1; -; mRNA.
DR EMBL; AK011875; BAB27893.1; -; mRNA.
DR EMBL; AK076032; BAC36133.1; -; mRNA.
DR EMBL; AK145506; BAE26476.1; -; mRNA.
DR EMBL; AK166872; BAE39083.1; -; mRNA.
DR EMBL; AY323828; AAQ91291.1; -; mRNA.
DR EMBL; BC023681; AAH23681.1; -; mRNA.
DR EMBL; BC055729; AAH55729.1; -; mRNA.
DR CCDS; CCDS25428.1; -.
DR RefSeq; NP_062769.2; NM_019795.4.
DR AlphaFoldDB; Q9QYI3; -.
DR SMR; Q9QYI3; -.
DR BioGRID; 207919; 15.
DR IntAct; Q9QYI3; 2.
DR MINT; Q9QYI3; -.
DR STRING; 10090.ENSMUSP00000014339; -.
DR iPTMnet; Q9QYI3; -.
DR PhosphoSitePlus; Q9QYI3; -.
DR REPRODUCTION-2DPAGE; Q9QYI3; -.
DR EPD; Q9QYI3; -.
DR MaxQB; Q9QYI3; -.
DR PaxDb; Q9QYI3; -.
DR PRIDE; Q9QYI3; -.
DR ProteomicsDB; 279746; -.
DR Antibodypedia; 8072; 229 antibodies from 28 providers.
DR DNASU; 56354; -.
DR Ensembl; ENSMUST00000014339; ENSMUSP00000014339; ENSMUSG00000014195.
DR GeneID; 56354; -.
DR KEGG; mmu:56354; -.
DR UCSC; uc007lls.1; mouse.
DR CTD; 7266; -.
DR MGI; MGI:1928373; Dnajc7.
DR VEuPathDB; HostDB:ENSMUSG00000014195; -.
DR eggNOG; KOG0550; Eukaryota.
DR GeneTree; ENSGT00940000155338; -.
DR HOGENOM; CLU_015935_3_1_1; -.
DR InParanoid; Q9QYI3; -.
DR OMA; EILFSMM; -.
DR OrthoDB; 506649at2759; -.
DR PhylomeDB; Q9QYI3; -.
DR TreeFam; TF105166; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR BioGRID-ORCS; 56354; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Dnajc7; mouse.
DR PRO; PR:Q9QYI3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9QYI3; protein.
DR Bgee; ENSMUSG00000014195; Expressed in floor plate of midbrain and 265 other tissues.
DR ExpressionAtlas; Q9QYI3; baseline and differential.
DR Genevisible; Q9QYI3; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISO:MGI.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF13181; TPR_8; 2.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS50005; TPR; 8.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99615"
FT CHAIN 2..494
FT /note="DnaJ homolog subfamily C member 7"
FT /id="PRO_0000071059"
FT REPEAT 28..61
FT /note="TPR 1"
FT REPEAT 62..95
FT /note="TPR 2"
FT REPEAT 96..129
FT /note="TPR 3"
FT REPEAT 142..175
FT /note="TPR 4"
FT REPEAT 210..243
FT /note="TPR 5"
FT REPEAT 256..289
FT /note="TPR 6"
FT REPEAT 294..327
FT /note="TPR 7"
FT REPEAT 328..361
FT /note="TPR 8"
FT DOMAIN 381..451
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q99615"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99615"
FT CONFLICT 86..87
FT /note="QQ -> HE (in Ref. 2; BAB27893)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="S -> I (in Ref. 1; BAA88309)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="F -> L (in Ref. 3; AAQ91291)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="Y -> F (in Ref. 2; BAC36133)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="I -> V (in Ref. 2; BAB27893)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="F -> L (in Ref. 1; BAA88309 and 3; AAQ91291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 56476 MW; 8D82EBFA19C556B9 CRC64;
MAATAECDVV MAATEPELLE DEDAKREAES FKEQGNAYYA KKDYNEAYNY YTKAIDMCPN
NASYYGNRAA TLMMLGRFRE ALGDAQQSVR LDDSFVRGHL REGKCHLSLG NAMAACRSFQ
RALELDHKNA QAQQEFKNAN AVMEYEKIAE VDFEKRDFRK VVFCMDRALE FAPACHRFKI
LKAECLAMLG RYPEAQFVAS DILRMDSTNA DALYVRGLCL YYEDCIEKAV QFFVQALRMA
PDHEKACVAC RNAKALKAKK EDGNKAFKEG NYKLAYELYT EALGIDPNNI KTNAKLYCNR
GTVNSKLRQL EDAIEDCTNA VKLDDTYIKA YLRRAQCYMD TEQFEEAVRD YEKVYQTEKT
KEHKQLLKNA QLELKKSKRK DYYKILGVDK NASEDEIKKA YRKRALMHHP DRHSGASAEV
QKEEEKKFKE VGEAFTILSD PKKKTRYDSG QDLDEEGMNM GDFDANNIFK AFFGGPGGFS
FEASGPGNFY FQFG
