ID   DNJB6_XENTR             Reviewed;         242 AA.
AC   Q6P642;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=DnaJ homolog subfamily B member 6;
GN   Name=dnajb6 {ECO:0000250|UniProtKB:O75190};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:AAH62492.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH62492.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an indispensable role in the organization of krt8/krt18
CC       filaments. Acts as an endogenous molecular chaperone for neuronal
CC       proteins including huntingtin. Has a stimulatory effect on the ATPase
CC       activity of HSP70 in a dose-dependent and time-dependent manner and
CC       hence acts as a co-chaperone of HSP70 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}.
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DR   EMBL; BC062492; AAH62492.1; -; mRNA.
DR   RefSeq; NP_989107.1; NM_203776.1.
DR   AlphaFoldDB; Q6P642; -.
DR   SMR; Q6P642; -.
DR   STRING; 8364.ENSXETP00000046731; -.
DR   PaxDb; Q6P642; -.
DR   DNASU; 394712; -.
DR   GeneID; 394712; -.
DR   KEGG; xtr:394712; -.
DR   CTD; 10049; -.
DR   Xenbase; XB-GENE-972413; dnajb6.
DR   eggNOG; KOG0714; Eukaryota.
DR   InParanoid; Q6P642; -.
DR   OrthoDB; 1152652at2759; -.
DR   Reactome; R-XTR-3371453; Regulation of HSF1-mediated heat shock response.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR036869; J_dom_sf.
DR   Pfam; PF00226; DnaJ; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Cytoplasm; Nucleus; Reference proteome.
FT   CHAIN           1..242
FT                   /note="DnaJ homolog subfamily B member 6"
FT                   /id="PRO_0000292344"
FT   DOMAIN          3..69
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
SQ   SEQUENCE   242 AA;  26978 MW;  296E559AEB3453C4 CRC64;
     MVEYYDVLGV QRNASPEDIK KAYRKLALKW HPDKNPDNKD EAERRFKEVA EAYEVLSDSK
     KRDIYDKYGK EGLTGGGGGS HFDNPYEFGF TFRSPDDVFR DFFGGRDPFS FDLFADDPFD
     DFFGRRGHRA NRSRPGGSFL STFGGFPAFG PTFSPFDSGF SSSFGSFGGH GGFSSFSSSS
     FGGSGMGNFR SVSTSTKVVN GRRVTTKRIV ENGQERIEVE EDGQLKSLTI NGKEQLLRLD
     NK