ID   DNJC7_PONAB             Reviewed;         494 AA.
AC   Q5R8D8;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=DnaJ homolog subfamily C member 7;
GN   Name=DNAJC7;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. Recruits NR1I3 to
CC       the cytoplasm (By similarity). {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. Interacts with NR1I3; this complex may also include
CC       HSP90. Interacts with HSPA8 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99615}. Nucleus
CC       {ECO:0000250|UniProtKB:Q99615}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q9QYI3}.
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DR   EMBL; CR859815; CAH91972.1; -; mRNA.
DR   RefSeq; NP_001126143.1; NM_001132671.1.
DR   AlphaFoldDB; Q5R8D8; -.
DR   SMR; Q5R8D8; -.
DR   STRING; 9601.ENSPPYP00000009447; -.
DR   GeneID; 100173101; -.
DR   KEGG; pon:100173101; -.
DR   CTD; 7266; -.
DR   eggNOG; KOG0550; Eukaryota.
DR   InParanoid; Q5R8D8; -.
DR   OrthoDB; 506649at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 3.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS50005; TPR; 8.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   2: Evidence at transcript 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_0000290024"
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          177..209
FT                   /note="TPR 5"
FT   REPEAT          210..243
FT                   /note="TPR 6"
FT   REPEAT          256..289
FT                   /note="TPR 7"
FT   REPEAT          294..327
FT                   /note="TPR 8"
FT   REPEAT          328..361
FT                   /note="TPR 9"
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"
SQ   SEQUENCE   494 AA;  56431 MW;  BDE2F89A00407F8C CRC64;
     MAAAAECDVV MAATEPELLD DQEAKREAET FKEQGNAYYA KKDYNEAYNY YTKAIDMCPK
     NASYYGNRAA TLMMLGRFRE ALGDAQQSVR LDDSFVRGRL 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
     KEHKQLLKSA QLELKKSKRR DYYKILGVDK NASEDEIKKA YRKRALMHHP DRHSGASAEV
     QKEEEKKFKE VGEAFTILSD PKKKTRYDSG QDLDEEGTNM GDFDPNNIFK AFFGGPGGFS
     FEASGPGNFF FQFG