DNJC7_PONAB
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