ID   DNJC7_HUMAN             Reviewed;         494 AA.
AC   Q99615;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   25-JAN-2012, entry version 114.
DE   RecName: Full=DnaJ homolog subfamily C member 7;
DE   AltName: Full=Tetratricopeptide repeat protein 2;
DE            Short=TPR repeat protein 2;
GN   Name=DNAJC7; Synonyms=TPR2, TTC2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, and Skin;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-26; 69-77; 80-90; 138-156; 192-238; 274-291 AND
RP   430-442, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RA   Bienvenut W.V., Waridel P., Quadroni M.;
RL   Submitted (MAR-2009) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-494.
RX   MEDLINE=96433003; PubMed=8836031; DOI=10.1089/dna.1996.15.727;
RA   Murthy A.E., Bernards A., Church D., Wasmuth J., Gusella J.F.;
RT   "Identification and characterization of two novel tetratricopeptide
RT   repeat-containing genes.";
RL   DNA Cell Biol. 15:727-735(1996).
RN   [5]
RP   INTERACTION WITH HSPA8.
RX   MEDLINE=20036592; PubMed=10567422; DOI=10.1074/jbc.274.48.34425;
RA   Liu F.H., Wu S.J., Hu S.M., Hsiao C.D., Wang C.;
RT   "Specific interaction of the 70-kDa heat shock cognate protein with
RT   the tetratricopeptide repeats.";
RL   J. Biol. Chem. 274:34425-34432(1999).
RN   [6]
RP   INTERACTION WITH RAD9A; HUS1 AND RAD1, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF HIS-409.
RX   PubMed=11573955; DOI=10.1006/bbrc.2001.5685;
RA   Xiang S.L., Kumano T., Iwasaki S.I., Sun X., Yoshioka K.,
RA   Yamamoto K.C.;
RT   "The J domain of Tpr2 regulates its interaction with the proapoptotic
RT   and cell-cycle checkpoint protein, Rad9.";
RL   Biochem. Biophys. Res. Commun. 287:932-940(2001).
RN   [7]
RP   FUNCTION, INTERACTION WITH HSP90AA1 AND HSPA1A/B, SUBCELLULAR
RP   LOCATION, AND MUTAGENESIS OF ARG-101; ARG-333 AND HIS-409.
RX   PubMed=12853476; DOI=10.1093/emboj/cdg362;
RA   Brychzy A., Rein T., Winklhofer K.F., Hartl F.U., Young J.C.,
RA   Obermann W.M.;
RT   "Cofactor Tpr2 combines two TPR domains and a J domain to regulate the
RT   Hsp70/Hsp90 chaperone system.";
RL   EMBO J. 22:3613-3623(2003).
RN   [8]
RP   INTERACTION WITH NR1I3.
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-50, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH HSP90AB1; HSPA1A/B AND PGR.
RX   PubMed=18620420; DOI=10.1021/bi800770g;
RA   Moffatt N.S., Bruinsma E., Uhl C., Obermann W.M., Toft D.;
RT   "Role of the cochaperone Tpr2 in Hsp90 chaperoning.";
RL   Biochemistry 47:8203-8213(2008).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
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
CC       act as a recycling chaperone by facilitating the return of
CC       chaperone substrates to early stages of chaperoning if further
CC       folding is required. In vitro, induces ATP-independent
CC       dissociation of HSP90 but not of HSP70 from the chaperone-
CC       substrate complexes. Recruits NR1I3 to the cytoplasm (By
CC       similarity).
CC   -!- SUBUNIT: Associates with complexes containing chaperones HSP70 and
CC       HSP90. Interacts with the GAP domain of NF1. Interacts with
CC       HSP90AA1. Interacts with HSPA1A/B; the interaction is enhanced by
CC       ATP. Interacts with HSP90AB1. Interacts with PGR. Interacts with
CC       RAD9A; the interaction is interrupted by UV and heat shock
CC       treatments. Interacts with HUS1 and RAD1. Interacts with NR1I3.
CC       The DNAJC7-NR1I3 complex may also include HSP90 (By similarity).
CC       Interacts with HSPA8.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton.
CC       Note=Colocalizes with NR1I3 to microtubules (By similarity).
CC   -!- SIMILARITY: Contains 1 J domain.
CC   -!- SIMILARITY: Contains 9 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB36872.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAH33772.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; BX647209; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC011837; AAH11837.2; -; mRNA.
DR   EMBL; BC033772; AAH33772.1; ALT_INIT; mRNA.
DR   EMBL; U46571; AAB36872.1; ALT_INIT; mRNA.
DR   IPI; IPI00329629; -.
DR   RefSeq; NP_003306.3; NM_003315.3.
DR   UniGene; Hs.500156; -.
DR   ProteinModelPortal; Q99615; -.
DR   SMR; Q99615; 24-449.
DR   IntAct; Q99615; 4.
DR   MINT; MINT-1143801; -.
DR   STRING; Q99615; -.
DR   PhosphoSite; Q99615; -.
DR   DMDM; 46397879; -.
DR   PeptideAtlas; Q99615; -.
DR   PRIDE; Q99615; -.
DR   Ensembl; ENST00000457167; ENSP00000406463; ENSG00000168259.
DR   GeneID; 7266; -.
DR   KEGG; hsa:7266; -.
DR   CTD; 7266; -.
DR   GeneCards; GC17M040128; -.
DR   H-InvDB; HIX0013829; -.
DR   HGNC; HGNC:12392; DNAJC7.
DR   HPA; HPA023015; -.
DR   MIM; 601964; gene.
DR   neXtProt; NX_Q99615; -.
DR   GeneTree; ENSGT00590000083090; -.
DR   HOGENOM; HBG717809; -.
DR   HOVERGEN; HBG051376; -.
DR   InParanoid; Q99615; -.
DR   OMA; REAESFK; -.
DR   OrthoDB; EOG4W3SMS; -.
DR   PhylomeDB; Q99615; -.
DR   NextBio; 28407; -.
DR   PMAP-CutDB; Q99615; -.
DR   ArrayExpress; Q99615; -.
DR   Bgee; Q99615; -.
DR   CleanEx; HS_DNAJC7; -.
DR   Genevestigator; Q99615; -.
DR   GermOnline; ENSG00000168259; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0070389; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR023114; Elongated_TPR_rpt_dom.
DR   InterPro; IPR003095; Hsp_DnaJ.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Gene3D; G3DSA:1.10.150.160; Elongated_TPR_rpt_dom; 1.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 3.
DR   KO; K09527; -.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF00515; TPR_1; 4.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM00028; TPR; 7.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   PROSITE; PS00636; DNAJ_1; FALSE_NEG.
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; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; TPR repeat.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    494       DnaJ homolog subfamily C member 7.
FT                                /FTId=PRO_0000071058.
FT   REPEAT       28     61       TPR 1.
FT   REPEAT       62     95       TPR 2.
FT   REPEAT       96    129       TPR 3.
FT   REPEAT      142    175       TPR 4.
FT   REPEAT      177    209       TPR 5.
FT   REPEAT      210    243       TPR 6.
FT   REPEAT      256    289       TPR 7.
FT   REPEAT      294    327       TPR 8.
FT   REPEAT      328    361       TPR 9.
FT   DOMAIN      381    451       J.
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES      50     50       Phosphotyrosine.
FT   MUTAGEN     101    101       R->A: Impairs interaction with HSP90AA1
FT                                and HSPA1A/B. Abolishes interaction with
FT                                HSP90AA1 and HSPA1A/B; when associated
FT                                with A-333 and A-409.
FT   MUTAGEN     333    333       R->A: Impairs interaction with HSP90AA1
FT                                and HSPA1A/B. Abolishes interaction with
FT                                HSP90AA1 and HSPA1A/B; when associated
FT                                with A-101 and A-409.
FT   MUTAGEN     409    409       H->A: Predominantly nuclear localization.
FT                                Abolishes interaction with HSP90AA1 and
FT                                HSPA1A/B; when associated with A-101 and
FT                                A-333.
FT   CONFLICT    375    375       K -> R (in Ref. 1; BX647209).
SQ   SEQUENCE   494 AA;  56441 MW;  81C60CF71BFE951D CRC64;
     MAAAAECDVV MAATEPELLD DQEAKREAET FKEQGNAYYA KKDYNEAYNY YTKAIDMCPK
     NASYYGNRAA TLMMLGRFRE ALGDAQQSVR LDDSFVRGHL REGKCHLSLG NAMAACRSFQ
     RALELDHKNA QAQQEFKNAN AVMEYEKIAE TDFEKRDFRK VVFCMDRALE FAPACHRFKI
     LKAECLAMLG RYPEAQSVAS DILRMDSTNA DALYVRGLCL YYEDCIEKAV QFFVQALRMA
     PDHEKACIAC RNAKALKAKK EDGNKAFKEG NYKLAYELYT EALGIDPNNI KTNAKLYCNR
     GTVNSKLRKL DDAIEDCTNA VKLDDTYIKA YLRRAQCYMD TEQYEEAVRD YEKVYQTEKT
     KEHKQLLKNA QLELKKSKRK DYYKILGVDK NASEDEIKKA YRKRALMHHP DRHSGASAEV
     QKEEEKKFKE VGEAFTILSD PKKKTRYDSG QDLDEEGMNM GDFDPNNIFK AFFGGPGGFS
     FEASGPGNFF FQFG
//