DNJB9_CRIGR
ID DNJB9_CRIGR Reviewed; 222 AA.
AC G3H0N9;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=DnaJ homolog subfamily B member 9 {ECO:0000250|UniProtKB:Q9UBS3};
DE AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 4 {ECO:0000303|PubMed:29198525};
DE Short=ER-resident protein ERdj4 {ECO:0000303|PubMed:29198525};
DE Short=ERdj4 {ECO:0000303|PubMed:29198525};
DE Flags: Precursor;
GN Name=DNAJB9 {ECO:0000250|UniProtKB:Q9UBS3};
GN ORFNames=I79_003703 {ECO:0000312|EMBL:EGV93680.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
RN [2]
RP FUNCTION, INTERACTION WITH HSPA5 AND ERN1, AND MUTAGENESIS OF HIS-54.
RX PubMed=29198525; DOI=10.1016/j.cell.2017.10.040;
RA Amin-Wetzel N., Saunders R.A., Kamphuis M.J., Rato C., Preissler S.,
RA Harding H.P., Ron D.;
RT "A J-Protein co-chaperone recruits bip to monomerize IRE1 and repress the
RT unfolded protein response.";
RL Cell 171:1625-1637(2017).
CC -!- FUNCTION: Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key
CC repressor of the ERN1/IRE1-mediated unfolded protein response (UPR)
CC (PubMed:29198525). J domain-containing co-chaperones stimulate the
CC ATPase activity of Hsp70 proteins and are required for efficient
CC substrate recognition by Hsp70 proteins (PubMed:29198525). In the
CC unstressed endoplasmic reticulum, interacts with the luminal region of
CC ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the
CC dimerization of the active ERN1/IRE1 luminal region, thereby
CC inactivating ERN1/IRE1 (PubMed:29198525). Also involved in endoplasmic
CC reticulum-associated degradation (ERAD) of misfolded proteins (By
CC similarity). Required for survival of B-cell progenitors and normal
CC antibody production (By similarity). {ECO:0000250|UniProtKB:Q9QYI6,
CC ECO:0000269|PubMed:29198525}.
CC -!- SUBUNIT: Interacts with HSPA5/BiP; interaction is direct
CC (PubMed:29198525). Interacts with ERN1/IRE1 (via the luminal region)
CC (PubMed:29198525). Interacts with DERL1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9QYI6, ECO:0000269|PubMed:29198525}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q9QYI6}.
CC -!- DOMAIN: The J domain stimulates the ATPase activity of HSPA5/BiP, while
CC the divergent targeting domain is required for efficient substrate
CC recognition by HSPA5/BiP. The divergent targeting domain specifically
CC recognizes and binds to aggregation-prone sequences.
CC {ECO:0000250|UniProtKB:Q9QYI6}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH000095; EGV93680.1; -; Genomic_DNA.
DR AlphaFoldDB; G3H0N9; -.
DR SMR; G3H0N9; -.
DR STRING; 10029.XP_007609132.1; -.
DR Ensembl; ENSCGRT00001007751; ENSCGRP00001005077; ENSCGRG00001006614.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000156246; -.
DR InParanoid; G3H0N9; -.
DR OMA; HFDSHFQ; -.
DR OrthoDB; 1173544at2759; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0051087; F:chaperone binding; IDA:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
DR GO; GO:0051787; F:misfolded protein binding; IEA:Ensembl.
DR GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
DR GO; GO:1903895; P:negative regulation of IRE1-mediated unfolded protein response; IDA:UniProtKB.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISS:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:Ensembl.
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; Endoplasmic reticulum; Phosphoprotein; Reference proteome;
KW Signal; Unfolded protein response.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..222
FT /note="DnaJ homolog subfamily B member 9"
FT /evidence="ECO:0000255"
FT /id="PRO_5003444047"
FT DOMAIN 26..90
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 91..222
FT /note="Divergent targeting domain"
FT /evidence="ECO:0000250|UniProtKB:Q9QYI6"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS3"
FT MUTAGEN 54
FT /note="H->Q: Abolishes ability to stimulate ATPase activity
FT of HSPA5/BiP."
FT /evidence="ECO:0000269|PubMed:29198525"
SQ SEQUENCE 222 AA; 25646 MW; 0CD8CE0D73B62210 CRC64;
MATPQSVFVF AICILMITEL ILASKSYYDI LGVPKSASER QIKKAFHKLA MKYHPDKNKS
PDAEAKFREI AEAYETLSDA HRRKEYDTVG HTAFTNGKGQ RGSGSPFEQS FNFNFDDLFK
DFNLFGQNQN TRSKKHFENH FQTHQDGSNR QRHHFQEFSF GGGLFDDMFE DMEKMFSFSG
FDTTNRHTVQ TENRFHGSSK HCRTVTQRRG NMVTTYTDCS GQ
