Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9QYI3 (DNJC7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DnaJ homolog subfamily C member 7
Alternative name(s):
Cytoplasmic CAR retention protein
Short name=CCRP
MDj11
Tetratricopeptide repeat protein 2
Short name=TPR repeat protein 2
Gene names
Name:Dnajc7
Synonyms:Ttc2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes By similarity. Recruits NR1I3 to the cytoplasm.

Subunit structure

Associates with complexes containing chaperones HSP70 and HSP90. Interacts with the GAP domain of NF1. Interacts with HSP90AA1. Interacts with HSPA1A/B; the interaction is enhanced by ATP. Interacts with HSP90AB1. Interacts with PGR. Interacts with RAD9A; the interaction is interrupted by UV and heat shock treatments. Interacts with HUS1 and RAD1 By similarity. Interacts with NR1I3; this complex may also include HSP90 Interacts with HSPA8 By similarity. Ref.3

Subcellular location

Cytoplasm. Nucleus By similarity. Cytoplasmcytoskeleton By similarity. Note: Colocalizes with NR1I3 at microtubules By similarity. Ref.3

Tissue specificity

Widely expressed with high levels in liver, skeletal muscle, kidney and testis. Ref.3

Sequence similarities

Contains 1 J domain.

Contains 8 TPR repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   DomainRepeat
TPR repeat
   Molecular functionChaperone
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchaperone cofactor-dependent protein refolding

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 494493DnaJ homolog subfamily C member 7
PRO_0000071059

Regions

Repeat28 – 6134TPR 1
Repeat62 – 9534TPR 2
Repeat96 – 12934TPR 3
Repeat142 – 17534TPR 4
Repeat210 – 24334TPR 5
Repeat256 – 28934TPR 6
Repeat294 – 32734TPR 7
Repeat328 – 36134TPR 8
Domain381 – 45171J

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict86 – 872QQ → HE in BAB27893. Ref.2
Sequence conflict1181S → I in BAA88309. Ref.1
Sequence conflict1361F → L in AAQ91291. Ref.3
Sequence conflict1921Y → F in BAC36133. Ref.2
Sequence conflict2851I → V in BAB27893. Ref.2
Sequence conflict4891F → L in BAA88309. Ref.1
Sequence conflict4891F → L in AAQ91291. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9QYI3 [UniParc].

Last modified April 13, 2004. Version 2.
Checksum: 8D82EBFA19C556B9

FASTA49456,476
        10         20         30         40         50         60 
MAATAECDVV MAATEPELLE DEDAKREAES FKEQGNAYYA KKDYNEAYNY YTKAIDMCPN 

        70         80         90        100        110        120 
NASYYGNRAA TLMMLGRFRE ALGDAQQSVR LDDSFVRGHL REGKCHLSLG NAMAACRSFQ 

       130        140        150        160        170        180 
RALELDHKNA QAQQEFKNAN AVMEYEKIAE VDFEKRDFRK VVFCMDRALE FAPACHRFKI 

       190        200        210        220        230        240 
LKAECLAMLG RYPEAQFVAS DILRMDSTNA DALYVRGLCL YYEDCIEKAV QFFVQALRMA 

       250        260        270        280        290        300 
PDHEKACVAC RNAKALKAKK EDGNKAFKEG NYKLAYELYT EALGIDPNNI KTNAKLYCNR 

       310        320        330        340        350        360 
GTVNSKLRQL EDAIEDCTNA VKLDDTYIKA YLRRAQCYMD TEQFEEAVRD YEKVYQTEKT 

       370        380        390        400        410        420 
KEHKQLLKNA QLELKKSKRK DYYKILGVDK NASEDEIKKA YRKRALMHHP DRHSGASAEV 

       430        440        450        460        470        480 
QKEEEKKFKE VGEAFTILSD PKKKTRYDSG QDLDEEGMNM GDFDANNIFK AFFGGPGGFS 

       490 
FEASGPGNFY FQFG 

« Hide

References

« Hide 'large scale' references
[1]"Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal for their classification and nomenclature."
Ohtsuka K., Hata M.
Cell Stress Chaperones 5:98-112(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[3]"Cytoplasmic accumulation of the nuclear receptor CAR by a tetratricopeptide repeat protein in HepG2 cells."
Kobayashi K., Sueyoshi T., Inoue K., Moore R., Negishi M.
Mol. Pharmacol. 64:1069-1075(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH NR1I3 AND HSP90, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6 and FVB/N.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB028861 mRNA. Translation: BAA88309.1.
AK011384 mRNA. Translation: BAB27584.1.
AK011875 mRNA. Translation: BAB27893.1.
AK076032 mRNA. Translation: BAC36133.1.
AK145506 mRNA. Translation: BAE26476.1.
AK166872 mRNA. Translation: BAE39083.1.
AY323828 mRNA. Translation: AAQ91291.1.
BC023681 mRNA. Translation: AAH23681.1.
BC055729 mRNA. Translation: AAH55729.1.
CCDSCCDS25428.1.
RefSeqNP_062769.2. NM_019795.4.
UniGeneMm.402409.

3D structure databases

ProteinModelPortalQ9QYI3.
SMRQ9QYI3. Positions 22-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207919. 3 interactions.
STRING10090.ENSMUSP00000014339.

PTM databases

PhosphoSiteQ9QYI3.

2D gel databases

REPRODUCTION-2DPAGEQ9QYI3.

Proteomic databases

MaxQBQ9QYI3.
PaxDbQ9QYI3.
PRIDEQ9QYI3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000014339; ENSMUSP00000014339; ENSMUSG00000014195.
GeneID56354.
KEGGmmu:56354.
UCSCuc007lls.1. mouse.

Organism-specific databases

CTD7266.
MGIMGI:1928373. Dnajc7.

Phylogenomic databases

eggNOGCOG0484.
GeneTreeENSGT00720000108760.
HOVERGENHBG051376.
InParanoidQ6VVW6.
KOK09527.
OMACFQRVLE.
OrthoDBEOG7KDF9K.
PhylomeDBQ9QYI3.
TreeFamTF105166.

Gene expression databases

ArrayExpressQ9QYI3.
BgeeQ9QYI3.
CleanExMM_DNAJC7.
GenevestigatorQ9QYI3.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
1.25.40.10. 3 hits.
InterProIPR001623. DnaJ_domain.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF00226. DnaJ. 1 hit.
PF00515. TPR_1. 2 hits.
[Graphical view]
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
SM00028. TPR. 7 hits.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
PROSITEPS50076. DNAJ_2. 1 hit.
PS50005. TPR. 8 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDNAJC7. mouse.
NextBio312362.
PROQ9QYI3.
SOURCESearch...

Entry information

Entry nameDNJC7_MOUSE
AccessionPrimary (citable) accession number: Q9QYI3
Secondary accession number(s): Q3TKR1 expand/collapse secondary AC list , Q6VVW6, Q8BPG3, Q8CIL2, Q9CT29, Q9D026
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: July 9, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot