DNJ1_CAEEL
ID DNJ1_CAEEL Reviewed; 401 AA.
AC Q17438; K8ESE7;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=DnaJ homolog subfamily B member 1 {ECO:0000305};
GN Name=dnj-1 {ECO:0000312|WormBase:B0035.14a};
GN ORFNames=B0035.14 {ECO:0000312|WormBase:B0035.14a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND TISSUE SPECIFICITY.
RX PubMed=27916661; DOI=10.1016/j.molcel.2016.10.027;
RA Li K., Jiang Q., Bai X., Yang Y.F., Ruan M.Y., Cai S.Q.;
RT "Tetrameric assembly of K(+) channels requires ER-located chaperone
RT proteins.";
RL Mol. Cell 65:52-65(2017).
CC -!- FUNCTION: Acts as a co-chaperone with Hsp70 required to promote protein
CC folding and trafficking, prevent aggregation of client proteins, and
CC promote unfolded proteins to endoplasmic reticulum-associated
CC degradation (ERAD) pathway (By similarity). Acts by determining Hsp70's
CC ATPase and polypeptide-binding activities (By similarity). Can also act
CC as a chaperone that promotes maturation of potassium channel unc-103 by
CC stabilizing nascent channel subunits and assembling them into tetramers
CC (PubMed:27916661). {ECO:0000250|UniProtKB:Q9NXW2,
CC ECO:0000269|PubMed:27916661}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:27916661}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q17438-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q17438-2; Sequence=VSP_058895;
CC -!- TISSUE SPECIFICITY: Expressed in many head neurons, vulva muscles and
CC some tail neurons. {ECO:0000269|PubMed:27916661}.
CC -!- SIMILARITY: Belongs to the DnaJ family. DNAJB12/DNAJB14 subfamily.
CC {ECO:0000305}.
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DR EMBL; BX284604; CAA97416.1; -; Genomic_DNA.
DR EMBL; BX284604; CCO25610.1; -; Genomic_DNA.
DR PIR; T18661; T18661.
DR RefSeq; NP_001263785.1; NM_001276856.1. [Q17438-2]
DR RefSeq; NP_502122.1; NM_069721.6. [Q17438-1]
DR AlphaFoldDB; Q17438; -.
DR SMR; Q17438; -.
DR STRING; 6239.B0035.14a.2; -.
DR EPD; Q17438; -.
DR PaxDb; Q17438; -.
DR PeptideAtlas; Q17438; -.
DR EnsemblMetazoa; B0035.14a.1; B0035.14a.1; WBGene00001019. [Q17438-1]
DR EnsemblMetazoa; B0035.14b.1; B0035.14b.1; WBGene00001019. [Q17438-2]
DR GeneID; 178040; -.
DR KEGG; cel:CELE_B0035.14; -.
DR UCSC; B0035.14.1; c. elegans. [Q17438-1]
DR CTD; 178040; -.
DR WormBase; B0035.14a; CE05169; WBGene00001019; dnj-1. [Q17438-1]
DR WormBase; B0035.14b; CE47882; WBGene00001019; dnj-1. [Q17438-2]
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000168650; -.
DR HOGENOM; CLU_043579_3_0_1; -.
DR InParanoid; Q17438; -.
DR OMA; VRVHQFG; -.
DR OrthoDB; 1173544at2759; -.
DR PhylomeDB; Q17438; -.
DR PRO; PR:Q17438; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001019; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030544; F:Hsp70 protein binding; IBA:GO_Central.
DR GO; GO:0071218; P:cellular response to misfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; 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; IPR015399; DUF1977_DnaJ-like.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF09320; DUF1977; 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 Alternative splicing; Chaperone; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..401
FT /note="DnaJ homolog subfamily B member 1"
FT /id="PRO_0000439644"
FT TOPO_DOM 1..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27916661"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..401
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:27916661"
FT DOMAIN 137..201
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 50..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..355
FT /note="Missing (in isoform b)"
FT /id="VSP_058895"
SQ SEQUENCE 401 AA; 46582 MW; 74E2170B3BADBD5A CRC64;
MTADANKSES LLCMDKAREA IKSGDTDKAR RMLLKAKKLD PGQNIEFLTK KIDDMTNNTS
SSSQTSSSRA SEERSYAHDD HYDDPNLRNR KARSPVKKNG KTEPEPKQRS ASRTPKLGVD
YTSEQKELVE RIRHCKDYYE ILKIDKKASD DDIRKEYRKL ALKLHPDKCR APHATEAFKA
LGNAYAVLSD TDKRRQYDQY GAEAANSHTP TTRRRGGGHG AFFEHDYAHG FEAEFTPEEI
FNMFFGGGFP TEQVRRRARY AQQQQYHHYE QQQSPYGPLL QLLPLIAIMV IGLLAQLMVG
EPAYSLHQTS KFTIKRLTAD LRVPYFVRTD FETSYRGRIR QVEQQVEDDY IQNLRMNCYK
EQNLKETKLY RARWMRDEAM MRDAERTPLP SCIRLNEIYS H
