ID   DNJB4_PONAB             Reviewed;         337 AA.
AC   Q5R8J8;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=DnaJ homolog subfamily B member 4;
GN   Name=DNAJB4;
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=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable chaperone. Stimulates ATP hydrolysis and the folding
CC       of unfolded proteins mediated by HSPA1A/B (in vitro).
CC       {ECO:0000250|UniProtKB:Q9UDY4}.
CC   -!- SUBUNIT: Homodimer. The C-terminal section interacts with the C-
CC       terminal tail of OPRM1. Interacts also with SDIM1.
CC       {ECO:0000250|UniProtKB:Q9UDY4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UDY4}. Cell
CC       membrane {ECO:0000250|UniProtKB:Q9UDY4}.
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; CR859754; CAH91912.1; -; mRNA.
DR   RefSeq; NP_001127480.1; NM_001134008.1.
DR   AlphaFoldDB; Q5R8J8; -.
DR   SMR; Q5R8J8; -.
DR   STRING; 9601.ENSPPYP00000001411; -.
DR   GeneID; 100174554; -.
DR   KEGG; pon:100174554; -.
DR   CTD; 11080; -.
DR   eggNOG; KOG0714; Eukaryota.
DR   InParanoid; Q5R8J8; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR036869; J_dom_sf.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; SSF46565; 1.
DR   SUPFAM; SSF49493; SSF49493; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Chaperone; Cytoplasm; Membrane; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..337
FT                   /note="DnaJ homolog subfamily B member 4"
FT                   /id="PRO_0000290021"
FT   DOMAIN          2..70
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   MOD_RES         122
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UDY4"
FT   MOD_RES         148
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UDY4"
SQ   SEQUENCE   337 AA;  37825 MW;  4929857D1DD20AC2 CRC64;
     MGKDYYCILG IEKGASDEDI KKAYRKQALK FHPDKNKSPQ AEEKFKEVAE AYEVLSDPKK
     REIYDQFGEE GLKGGAGGTD GQGGTFRYTF HGDPHATFAA FFGGSNPFEI FFGRRMGGGR
     DSEEMEMDGD PFSAFGFSMN GYPRDRNSVG PSRLKQDPPV IHELRVSLEE IYSGCTKRMK
     ISRKRLNADG RSYRSEDKIL TIEIKKGWKE GTKITFPREG DETPNSIPAD IVFIIKDKDH
     PKFKRDGSNI IYTAKISLRE ALCGCSINVP TLDGRNIPMS VNDIVKPGMR RRIIGYGLPF
     PKNPDQRGDL LIEFEVSFPD TISSSSKEVL RKHLPAS