ID   DNJB6_CHICK             Reviewed;         326 AA.
AC   Q5F3Z5;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=DnaJ homolog subfamily B member 6;
GN   Name=DNAJB6 {ECO:0000250|UniProtKB:O75190}; ORFNames=RCJMB04_4b8;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1] {ECO:0000312|EMBL:CAH65139.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB {ECO:0000312|EMBL:CAH65139.1};
RC   TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAH65139.1};
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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. Suppresses aggregation and toxicity of
CC       polyglutamine-containing, aggregation-prone proteins (By similarity).
CC       Has a stimulatory effect on the ATPase activity of HSP70 in a dose-
CC       dependent and time-dependent manner and hence acts as a co-chaperone of
CC       HSP70. Also reduces cellular toxicity and caspase-3 activity (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with HSP70, KRT18 and PTTG.
CC       {ECO:0000250|UniProtKB:O75190}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}.
CC       Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}.
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DR   EMBL; AJ851505; CAH65139.1; -; mRNA.
DR   RefSeq; NP_001012574.1; NM_001012556.1.
DR   RefSeq; XP_015136821.1; XM_015281335.1.
DR   AlphaFoldDB; Q5F3Z5; -.
DR   SMR; Q5F3Z5; -.
DR   STRING; 9031.ENSGALP00000010453; -.
DR   PaxDb; Q5F3Z5; -.
DR   PRIDE; Q5F3Z5; -.
DR   Ensembl; ENSGALT00000010467; ENSGALP00000010453; ENSGALG00000006477.
DR   GeneID; 420448; -.
DR   KEGG; gga:420448; -.
DR   CTD; 10049; -.
DR   VEuPathDB; HostDB:geneid_420448; -.
DR   eggNOG; KOG0714; Eukaryota.
DR   GeneTree; ENSGT00940000154205; -.
DR   HOGENOM; CLU_017633_12_0_1; -.
DR   InParanoid; Q5F3Z5; -.
DR   OMA; MFFGDST; -.
DR   OrthoDB; 1152652at2759; -.
DR   PhylomeDB; Q5F3Z5; -.
DR   TreeFam; TF105142; -.
DR   PRO; PR:Q5F3Z5; -.
DR   Proteomes; UP000000539; Chromosome 2.
DR   Bgee; ENSGALG00000006477; Expressed in heart and 14 other tissues.
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:0030018; C:Z disc; 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; Phosphoprotein; Reference proteome.
FT   CHAIN           1..326
FT                   /note="DnaJ homolog subfamily B member 6"
FT                   /id="PRO_0000292341"
FT   DOMAIN          3..69
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          1..146
FT                   /note="Interaction with HSP70"
FT                   /evidence="ECO:0000250|UniProtKB:O75190"
FT   REGION          119..242
FT                   /note="Interaction with KRT18"
FT                   /evidence="ECO:0000250|UniProtKB:O75190"
FT   REGION          249..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         277
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75190"
SQ   SEQUENCE   326 AA;  36675 MW;  E364E48D0EAFFD08 CRC64;
     MVDYYEVLGV QKHASAEDIK KAYRKLALKW HPDKNPENKE EAEQQFKQVA EAYEVLSDAK
     KRDIYDRFGK EGLINGGGGG SHHDNPFEFG FTFRNPDDVF REFFGGRDPF SFDFFEDPFE
     DFFGGRRGPR GSRSRAGGSF LSAFGGFPAF GNAFPSFDTG FTSFGSLGHG GLTSFSSTSF
     GGSGMGNFKS VSTSTKIVNG RKITTKRIVE NGQERVEVEE DGQLRSLTIN GEANEEAFAE
     ECRRRGQHAL PFQPTNTRLL KPHKPASSPR YAYHYNSDEV EEQEKSRVAS SLETPFYLSG
     YKEGSKRRKQ KQREEQKKKK STKGSY