ID   DNJB6_BOVIN             Reviewed;         242 AA.
AC   Q0III6; Q8WN90;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=DnaJ homolog subfamily B member 6;
DE   AltName: Full=MRJ;
GN   Name=DNAJB6; Synonyms=MRJ;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Retina;
RX   PubMed=11896048; DOI=10.1074/jbc.m109613200;
RA   Chuang J.-Z., Zhou H., Zhu M., Li S.-H., Li X.-J., Sung C.-H.;
RT   "Characterization of a brain-enriched chaperone, MRJ, that inhibits
RT   Huntingtin aggregation and toxicity independently.";
RL   J. Biol. Chem. 277:19831-19838(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) 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, ECO:0000269|PubMed:11896048}.
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   -!- TISSUE SPECIFICITY: Expressed in all tissues examined with highest
CC       expression in brain and retina and lower levels observed in testis,
CC       spleen, heart, liver and kidney. {ECO:0000269|PubMed:11896048}.
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; AF426743; AAL73393.1; -; mRNA.
DR   EMBL; BC122622; AAI22623.1; -; mRNA.
DR   RefSeq; NP_776957.2; NM_174532.3.
DR   AlphaFoldDB; Q0III6; -.
DR   SMR; Q0III6; -.
DR   STRING; 9913.ENSBTAP00000033245; -.
DR   PaxDb; Q0III6; -.
DR   PRIDE; Q0III6; -.
DR   GeneID; 282215; -.
DR   KEGG; bta:282215; -.
DR   CTD; 10049; -.
DR   eggNOG; KOG0714; Eukaryota.
DR   HOGENOM; CLU_017633_12_0_1; -.
DR   InParanoid; Q0III6; -.
DR   OrthoDB; 1152652at2759; -.
DR   Proteomes; UP000009136; 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:0030018; C:Z disc; ISS:UniProtKB.
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; Methylation; Nucleus; Reference proteome.
FT   CHAIN           1..242
FT                   /note="DnaJ homolog subfamily B member 6"
FT                   /id="PRO_0000290022"
FT   DOMAIN          2..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..242
FT                   /note="Interaction with KRT18"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         135
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O54946"
FT   CONFLICT        125
FT                   /note="H -> N (in Ref. 1; AAL73393)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152..153
FT                   /note="GA -> SL (in Ref. 1; AAL73393)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        201
FT                   /note="G -> S (in Ref. 1; AAL73393)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   242 AA;  26944 MW;  97A0BF6B48B4A704 CRC64;
     MVDYYEVLGV QRHASAEDIK KAYRKLALKW HPDKNPENKE EAERKFKQVA EAYEVLSDAK
     KRDIYDRYGK EGLNGGGGGG SHFDSPFEFG FTFRNPEDVF REFFGGRDPF SFDFFEDPFE
     DFFGHRRGPR GSRSRGTGSF FSTFSGFPSF GGAFPSFDAG FSSFGSLGHG GLTAFSSSSA
     FGGSGMGNYK SISTSTKVVN GRKITTKRIV ENGQERVEVE EDGQLKSLTI NGKEQLLRLD
     NK