DNJB4_BOVIN
ID DNJB4_BOVIN Reviewed; 337 AA.
AC Q2KIT4;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=DnaJ homolog subfamily B member 4;
GN Name=DNAJB4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) 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}.
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DR EMBL; BC112518; AAI12519.1; -; mRNA.
DR RefSeq; NP_001039968.1; NM_001046503.1.
DR AlphaFoldDB; Q2KIT4; -.
DR SMR; Q2KIT4; -.
DR STRING; 9913.ENSBTAP00000028994; -.
DR PaxDb; Q2KIT4; -.
DR PRIDE; Q2KIT4; -.
DR Ensembl; ENSBTAT00000028994; ENSBTAP00000028994; ENSBTAG00000021752.
DR GeneID; 541274; -.
DR KEGG; bta:541274; -.
DR CTD; 11080; -.
DR VEuPathDB; HostDB:ENSBTAG00000021752; -.
DR VGNC; VGNC:55166; DNAJB4.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000156826; -.
DR HOGENOM; CLU_017633_0_0_1; -.
DR InParanoid; Q2KIT4; -.
DR OMA; DVNFPET; -.
DR OrthoDB; 1393097at2759; -.
DR TreeFam; TF105141; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000021752; Expressed in gluteal muscle and 105 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
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_0000286174"
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; 37851 MW; B782AEA625092421 CRC64;
MGKDYYCILG IEKGASDEDI KKAYRKQALR FHPDKNKSPQ AEERFKEVAE AYEVLSDPKK
REIYDQFGEE GLKGGAGGTD GQGGTFRYTF HGDPHATFAA FFGGSNPFEI FFGRRMGGGR
DSDEMEVDGD PFGAFGFSMN GYPRDRNSVG PSRLKQDPPV IHELRVSLEE IYSGCTKRMK
ISRKRLNPDG RSYRTEDKIL TIEIKKGWKE GTKITFPREG DETPTSIPAD IVFVIKDKDH
PKFKRDGSNI IYTAKISLRE ALCGCSINVP TMDGRTIPMT INDIVKPGMR RRIIGYGLPF
PKNPDQRGDL LIEFEVSFPD TISSSSKEVL RKHLPAS