DNJC8_RAT
ID DNJC8_RAT Reviewed; 253 AA.
AC Q642C0;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DnaJ homolog subfamily C member 8;
GN Name=Dnajc8;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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).
CC -!- FUNCTION: Suppresses polyglutamine (polyQ) aggregation of ATXN3 in
CC neuronal cells. {ECO:0000250|UniProtKB:O75937}.
CC -!- SUBUNIT: Interacts with SRPK1. Interacts with HSP70 (HSPA1A or HSPA1B).
CC {ECO:0000250|UniProtKB:O75937}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75937}.
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DR EMBL; BC081863; AAH81863.1; -; mRNA.
DR RefSeq; NP_001013186.1; NM_001013168.1.
DR AlphaFoldDB; Q642C0; -.
DR SMR; Q642C0; -.
DR STRING; 10116.ENSRNOP00000017740; -.
DR iPTMnet; Q642C0; -.
DR PhosphoSitePlus; Q642C0; -.
DR jPOST; Q642C0; -.
DR PaxDb; Q642C0; -.
DR PRIDE; Q642C0; -.
DR Ensembl; ENSRNOT00000017740; ENSRNOP00000017740; ENSRNOG00000013255.
DR GeneID; 313035; -.
DR KEGG; rno:313035; -.
DR UCSC; RGD:1306024; rat.
DR CTD; 22826; -.
DR RGD; 1306024; Dnajc8.
DR eggNOG; KOG1150; Eukaryota.
DR GeneTree; ENSGT00390000012569; -.
DR HOGENOM; CLU_070940_2_0_1; -.
DR InParanoid; Q642C0; -.
DR OrthoDB; 1434217at2759; -.
DR PhylomeDB; Q642C0; -.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q642C0; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000013255; Expressed in thymus and 20 other tissues.
DR ExpressionAtlas; Q642C0; baseline and differential.
DR Genevisible; Q642C0; RN.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:RGD.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR042858; DNAJC8.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR15606; PTHR15606; 1.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chaperone; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O75937"
FT CHAIN 2..253
FT /note="DnaJ homolog subfamily C member 8"
FT /id="PRO_0000071062"
FT DOMAIN 68..135
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 181..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..253
FT /note="Essential for polyglutamine aggregation suppression"
FT /evidence="ECO:0000250|UniProtKB:O75937"
FT MOTIF 189..192
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O75937"
FT MOTIF 203..206
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:O75937"
FT COMPBIAS 181..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O75937"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75937"
FT MOD_RES 146
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75937"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75937"
SQ SEQUENCE 253 AA; 29813 MW; 295D0C3F0B2A0F49 CRC64;
MAASGESGAS GGGGSTEEAF MTFYSEVKQI EKRDSVLTSK NQIERLTRPG SSYFNLNPFE
VLQIDPEVTD EEIKKRFRQL SILVHPDKNQ DDADRAQKAF EAVDKAYKLL LDQEQKKRAL
DVIQAGKEYV EHTVKERKKQ LKKEGKPTNV EEDDPELFKQ AVYKQTMKLF AELEIKRKER
EAKEMHERKR QREEEIEAQE KAKREREWQK NFEESRDGRV DSWRNFQANT KGKKEKKNRT
FLRPPKVKME QRE