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   24-JAN-2024, entry version 162.
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,
RC   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: Acts as a 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; 19.
DR   IntAct; Q9QYI3; 2.
DR   MINT; Q9QYI3; -.
DR   STRING; 10090.ENSMUSP00000014339; -.
DR   GlyGen; Q9QYI3; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9QYI3; -.
DR   PhosphoSitePlus; Q9QYI3; -.
DR   REPRODUCTION-2DPAGE; Q9QYI3; -.
DR   EPD; Q9QYI3; -.
DR   MaxQB; Q9QYI3; -.
DR   PaxDb; 10090-ENSMUSP00000014339; -.
DR   ProteomicsDB; 279746; -.
DR   Pumba; Q9QYI3; -.
DR   Antibodypedia; 8072; 252 antibodies from 28 providers.
DR   DNASU; 56354; -.
DR   Ensembl; ENSMUST00000014339.15; ENSMUSP00000014339.9; ENSMUSG00000014195.17.
DR   GeneID; 56354; -.
DR   KEGG; mmu:56354; -.
DR   UCSC; uc007lls.1; mouse.
DR   AGR; MGI:1928373; -.
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; KMCLGLD; -.
DR   OrthoDB; 5473367at2759; -.
DR   PhylomeDB; Q9QYI3; -.
DR   TreeFam; TF105166; -.
DR   BioGRID-ORCS; 56354; 5 hits in 78 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 269 other cell types or tissues.
DR   ExpressionAtlas; Q9QYI3; baseline and differential.
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   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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   PANTHER; PTHR44200; DNAJ HOMOLOG SUBFAMILY C MEMBER 7; 1.
DR   PANTHER; PTHR44200:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 7; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF13414; TPR_11; 1.
DR   Pfam; PF13181; TPR_8; 2.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM00028; TPR; 8.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS50005; TPR; 8.
DR   PROSITE; PS50293; TPR_REGION; 1.
DR   Genevisible; Q9QYI3; MM.
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
//