DNJB6_RAT
ID DNJB6_RAT Reviewed; 357 AA.
AC Q6AYU3;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DnaJ homolog subfamily B member 6;
DE AltName: Full=Heat shock protein J2;
DE Short=HSJ-2;
DE AltName: Full=Hsp40 homolog;
DE AltName: Full=MRJ;
DE AltName: Full=MSJ-1;
GN Name=Dnajb6 {ECO:0000312|EMBL:AAH78908.1, ECO:0000312|RGD:1308207};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAH78908.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAH78908.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PROTEIN SEQUENCE OF 48-60 AND 71-95, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3] {ECO:0000305}
RP DEVELOPMENTAL STAGE.
RX PubMed=9915854; DOI=10.1074/jbc.274.5.3151;
RA Pei L.;
RT "Pituitary tumor-transforming gene protein associates with ribosomal
RT protein S10 and a novel human homologue of DnaJ in testicular cells.";
RL J. Biol. Chem. 274:3151-3158(1999).
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY.
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).
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. {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: Highest levels of expression found in brain and
CC retina, and lower levels in heart, kidney, liver and placenta.
CC {ECO:0000269|PubMed:11896048}.
CC -!- DEVELOPMENTAL STAGE: Low levels detected in testes at day 7
CC postnatally, with 10-fold increased levels detected by day 28,
CC remaining into adulthood. {ECO:0000269|PubMed:9915854}.
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DR EMBL; BC078908; AAH78908.1; -; mRNA.
DR RefSeq; NP_001013227.1; NM_001013209.1.
DR AlphaFoldDB; Q6AYU3; -.
DR SMR; Q6AYU3; -.
DR BioGRID; 263341; 1.
DR IntAct; Q6AYU3; 4.
DR STRING; 10116.ENSRNOP00000041883; -.
DR iPTMnet; Q6AYU3; -.
DR PhosphoSitePlus; Q6AYU3; -.
DR jPOST; Q6AYU3; -.
DR PaxDb; Q6AYU3; -.
DR PRIDE; Q6AYU3; -.
DR Ensembl; ENSRNOT00000035996; ENSRNOP00000041883; ENSRNOG00000010353.
DR GeneID; 362293; -.
DR KEGG; rno:362293; -.
DR UCSC; RGD:1308207; rat.
DR CTD; 10049; -.
DR RGD; 1308207; Dnajb6.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000154205; -.
DR HOGENOM; CLU_017633_12_0_1; -.
DR InParanoid; Q6AYU3; -.
DR OMA; MFFGDST; -.
DR OrthoDB; 1152652at2759; -.
DR PhylomeDB; Q6AYU3; -.
DR TreeFam; TF105142; -.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR PRO; PR:Q6AYU3; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000010353; Expressed in testis and 18 other tissues.
DR Genevisible; Q6AYU3; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0001671; F:ATPase activator activity; ISO:RGD.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0060710; P:chorio-allantoic fusion; ISO:RGD.
DR GO; GO:0060717; P:chorion development; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0045109; P:intermediate filament organization; ISO:RGD.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006457; P:protein folding; ISO:RGD.
DR GO; GO:0034504; P:protein localization to nucleus; ISO:RGD.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0060715; P:syncytiotrophoblast cell differentiation involved in labyrinthine layer development; ISO:RGD.
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 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Direct protein sequencing; Methylation; Nucleus;
KW Reference proteome.
FT CHAIN 1..357
FT /note="DnaJ homolog subfamily B member 6"
FT /id="PRO_0000292340"
FT DOMAIN 3..69
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 1..147
FT /note="Interaction with HSP70"
FT /evidence="ECO:0000250"
FT REGION 120..243
FT /note="Interaction with KRT18"
FT /evidence="ECO:0000250|UniProtKB:O75190"
FT REGION 243..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 136
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O54946"
SQ SEQUENCE 357 AA; 38922 MW; 55899E4DE4DF9E76 CRC64;
MVDYYEVLGV QRHASPEDIK KAYRKQALKW HPDKNPENKE EAERKFKQVA EAYEVLSDAK
KRDIYDKYGK EGLNGGGGGG GSHFDSPFEF GFTFRNPDDV FREFFGGRDP FSFDFFEDPF
DDFFGNRRGP RGSRSRGAGS FFSAFSGFPS FGSGFPAFDT GFTPFGSLGH GGLTSFSSAS
FGGSGMGNFK SISTSTKIVN GKKITTKRIV ENGQERVEVE EDGQLKSLTI NGVADENALA
EECRRRGQPT PALAPGPAPA PARVPSQARP PTPAPTPAPA QTPAPSVSTR PQKPPRPAPT
AKLVSKSNWE DEEQDRQRVP GNCDAPMTSA GLKEGGKRKK QKQKEDSKKK KSTKGNH
