ID   DNJB9_RAT               Reviewed;         222 AA.
AC   P97554;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=DnaJ homolog subfamily B member 9 {ECO:0000305};
DE   AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 4 {ECO:0000250|UniProtKB:Q9QYI6};
DE            Short=ER-resident protein ERdj4 {ECO:0000250|UniProtKB:Q9QYI6};
DE            Short=ERdj4 {ECO:0000250|UniProtKB:Q9QYI6};
DE   AltName: Full=Microvascular endothelial differentiation gene 1 protein {ECO:0000303|PubMed:11525638};
DE            Short=Mdg-1 {ECO:0000303|PubMed:11525638};
DE   Flags: Precursor;
GN   Name=Dnajb9 {ECO:0000312|RGD:3070};
GN   Synonyms=Mdg1 {ECO:0000303|PubMed:11525638};
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 [MRNA].
RC   TISSUE=Epididymis;
RX   PubMed=11525638; DOI=10.1006/excr.2001.5294;
RA   Proels F., Mayer M.P., Renner O., Czarnecki P.G., Ast M., Gaessler C.,
RA   Wilting J., Kurz H., Christ B.;
RT   "Upregulation of the cochaperone mdg1 in endothelial cells is induced by
RT   stress and during in vitro angiogenesis.";
RL   Exp. Cell Res. 269:42-53(2001).
RN   [2]
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: Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key
CC       repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By
CC       similarity). J domain-containing co-chaperones stimulate the ATPase
CC       activity of Hsp70 proteins and are required for efficient substrate
CC       recognition by Hsp70 proteins (By similarity). In the unstressed
CC       endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1
CC       and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization
CC       of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1
CC       (By similarity). Also involved in endoplasmic reticulum-associated
CC       degradation (ERAD) of misfolded proteins. Required for survival of B-
CC       cell progenitors and normal antibody production (By similarity).
CC       {ECO:0000250|UniProtKB:G3H0N9, ECO:0000250|UniProtKB:Q9QYI6}.
CC   -!- SUBUNIT: Interacts with HSPA5/BiP; interaction is direct (By
CC       similarity). Interacts with ERN1/IRE1 (via the luminal region) (By
CC       similarity). Interacts with DERL1 (By similarity).
CC       {ECO:0000250|UniProtKB:G3H0N9, ECO:0000250|UniProtKB:Q9QYI6}.
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   -!- CAUTION: Was initially reported to localize in the nucleus
CC       (PubMed:11525638). However, it was later shown to localize in the
CC       endoplasmic reticulum lumen. {ECO:0000305|PubMed:11525638}.
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DR   EMBL; X98993; CAA67434.2; -; mRNA.
DR   EMBL; BC070915; AAH70915.1; -; mRNA.
DR   RefSeq; NP_036831.2; NM_012699.2.
DR   RefSeq; XP_006240127.1; XM_006240065.3.
DR   AlphaFoldDB; P97554; -.
DR   SMR; P97554; -.
DR   IntAct; P97554; 6.
DR   STRING; 10116.ENSRNOP00000005363; -.
DR   PaxDb; P97554; -.
DR   PRIDE; P97554; -.
DR   Ensembl; ENSRNOT00000005363; ENSRNOP00000005363; ENSRNOG00000004006.
DR   GeneID; 24908; -.
DR   KEGG; rno:24908; -.
DR   UCSC; RGD:3070; rat.
DR   CTD; 4189; -.
DR   RGD; 3070; Dnajb9.
DR   eggNOG; KOG0714; Eukaryota.
DR   GeneTree; ENSGT00940000156246; -.
DR   HOGENOM; CLU_077239_0_0_1; -.
DR   InParanoid; P97554; -.
DR   OMA; NIYSQNR; -.
DR   OrthoDB; 1173544at2759; -.
DR   PhylomeDB; P97554; -.
DR   TreeFam; TF105143; -.
DR   PRO; PR:P97554; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000004006; Expressed in testis and 20 other tissues.
DR   ExpressionAtlas; P97554; baseline and differential.
DR   Genevisible; P97554; RN.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR   GO; GO:0030544; F:Hsp70 protein binding; ISO:RGD.
DR   GO; GO:0051787; F:misfolded protein binding; ISO:RGD.
DR   GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
DR   GO; GO:1903895; P:negative regulation of IRE1-mediated unfolded protein response; ISS: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; 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; 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                   /id="PRO_0000071034"
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"
SQ   SEQUENCE   222 AA;  25717 MW;  08BF5347F20B65DC CRC64;
     MATPQSVFVF AICILMITEL ILASKNYYDI LGVPKSASER QIKKAFHKLA MKYHPDKNKS
     PDAEAKFREI AEAYETLSDA NRRKEYDIIG HSAFTNGKGQ RSNGSPFEQS FNFNFDDLFK
     DFNLFGQNQN TRSKKHFENH FQTRQDGSSR QRHHFQEFSF GGGLFDDMFE DMEKMFSFSG
     FDSTNRRTVQ TENRFHGSSK HCRTVTQRRG NMVTTYTDCS GQ