ID   DNJB6_MACFA             Reviewed;         241 AA.
AC   Q4R7Y5;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=DnaJ homolog subfamily B member 6;
GN   Name=DNAJB6 {ECO:0000250|UniProtKB:O75190}; ORFNames=QtsA-14076;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1] {ECO:0000312|EMBL:BAE00787.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis {ECO:0000269|Ref.1};
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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. 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: Homooligomer. Interacts with BAG3, HSPB8 and STUB1. Interacts
CC       with HSP70, KRT18 and PTTG. Interacts with ALKBH1. Interacts with
CC       histone deacetylases HDAC4, HDAC6, and SIRT2, HDAC activity is required
CC       for antiaggregation. {ECO:0000250}.
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}.
CC   -!- DOMAIN: The antiaggregation activity of resides in the serine-rich
CC       region and the C-terminus. {ECO:0000250}.
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DR   EMBL; AB168676; BAE00787.1; -; mRNA.
DR   AlphaFoldDB; Q4R7Y5; -.
DR   SMR; Q4R7Y5; -.
DR   STRING; 9541.XP_005551338.1; -.
DR   Ensembl; ENSMFAT00000101818; ENSMFAP00000047153; ENSMFAG00000036682.
DR   eggNOG; KOG0714; Eukaryota.
DR   GeneTree; ENSGT00940000154205; -.
DR   Proteomes; UP000233100; Chromosome 3.
DR   Bgee; ENSMFAG00000036682; Expressed in skeletal muscle tissue and 13 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030018; C:Z disc; ISS:UniProtKB.
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; Methylation; Nucleus; Reference proteome.
FT   CHAIN           1..241
FT                   /note="DnaJ homolog subfamily B member 6"
FT                   /id="PRO_0000292339"
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"
FT   REGION          119..241
FT                   /note="Interaction with KRT18"
FT                   /evidence="ECO:0000250|UniProtKB:O75190"
FT   MOD_RES         135
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O54946"
SQ   SEQUENCE   241 AA;  26884 MW;  CDAF5C6EB6783BA6 CRC64;
     MVDYYEVLGV QRHASPEDIK KAYRKLALKW HPDKNPENKE EAERKFKQVA EAYEVLSDAK
     KRDIYDKYGK EGLNGGGGGG SHFDSPFEFG FTFRNPDDVF REFFGGRDPF SFEFFEDPFE
     DFFGNRRGPR GSRSRGTGSF FSAFSGFPSF GSGFSSFDTG FTSFGSLGHG GLTSFSSTSF
     GGGGMGNFKS ISTSTKMVNG RKITTKRIVE NGQERVEVEE DGQLKSLTIN GKEQLLRLDN
     K