ID   DNJB9_PONAB             Reviewed;         223 AA.
AC   Q5R9A4;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 79.
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   Flags: Precursor;
GN   Name=DNAJB9 {ECO:0000250|UniProtKB:Q9QYI6};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CR859486; CAH91656.1; -; mRNA.
DR   RefSeq; NP_001125972.1; NM_001132500.1.
DR   AlphaFoldDB; Q5R9A4; -.
DR   SMR; Q5R9A4; -.
DR   STRING; 9601.ENSPPYP00000020080; -.
DR   GeneID; 100172910; -.
DR   KEGG; pon:100172910; -.
DR   CTD; 4189; -.
DR   eggNOG; KOG0714; Eukaryota.
DR   InParanoid; Q5R9A4; -.
DR   OrthoDB; 1173544at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR   GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
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..223
FT                   /note="DnaJ homolog subfamily B member 9"
FT                   /id="PRO_0000071033"
FT   DOMAIN          26..90
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          91..223
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   223 AA;  25605 MW;  06FC217AD4E1197D CRC64;
     MATPQSIFIF AICILMITEL ILASKSYYDI LGVPKSASER QIKKAFHKLA MKYHPDKNKS
     PDAEAKFREI AEAYETLSDA NRRKEYDTLG HSAFTNGKGQ RGSGSSFEQS FNFNFDDLFK
     DFGFFGQNQN TRSKKHFENH FQTRPDGGSS RQRHHFQEFS FGGGLFDDMF EDMEKMFSFS
     GFDPTSRHTV QTENRFHGSS KHCRTVTQRR GNMVTTYTDC SGQ