ID   DNJB6_PONAB             Reviewed;         326 AA.
AC   Q5R8H0;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=DnaJ homolog subfamily B member 6;
GN   Name=DNAJB6;
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=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR859782; CAH91940.1; -; mRNA.
DR   RefSeq; NP_001127484.1; NM_001134012.1.
DR   AlphaFoldDB; Q5R8H0; -.
DR   SMR; Q5R8H0; -.
DR   STRING; 9601.ENSPPYP00000020432; -.
DR   GeneID; 100174558; -.
DR   KEGG; pon:100174558; -.
DR   CTD; 10049; -.
DR   eggNOG; KOG0714; Eukaryota.
DR   InParanoid; Q5R8H0; -.
DR   Proteomes; UP000001595; Unplaced.
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; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..326
FT                   /note="DnaJ homolog subfamily B member 6"
FT                   /id="PRO_0000290023"
FT   DOMAIN          2..69
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          1..150
FT                   /note="Interaction with HSP70"
FT                   /evidence="ECO:0000250"
FT   REGION          119..242
FT                   /note="Interaction with KRT18"
FT                   /evidence="ECO:0000250"
FT   REGION          249..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         135
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O54946"
FT   MOD_RES         277
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75190"
SQ   SEQUENCE   326 AA;  36015 MW;  D79F5A69578D8679 CRC64;
     MVDYYEVLGV QRHASPEDIK KAYRKLALKW HPDKNPENKE EAERKFKQVA EAYEVLSDAK
     KRDIYDKYGK EGLNGGGGGG SHFDSPFEFG FTFRNPDDVF REFFGGRDPF SFDFFEDPFE
     DFFGNRRGPR GSRSRGTGSF FSAFSGFPSF GSGFSSFDTG FTSFGSLGHG GLTSFSSTSF
     GGSGMGNFKS ISTSTKMVNG RKITTKRIVE NGQERVEVGE DGQLKSLTIN GVADDDALAE
     ERMRRGQNAL PAQPAGLRPP KPPRPASLLR HAPHCLSEEE GEQDRPRAPG PWDPLASAAG
     LKEGGKRKKQ KQREESKKKK STKGNH