DJB14_BOVIN
ID DJB14_BOVIN Reviewed; 379 AA.
AC Q0IIE8;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=DnaJ homolog subfamily B member 14;
GN Name=DNAJB14;
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=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a co-chaperone with HSPA8/Hsc70; required to promote
CC protein folding and trafficking, prevent aggregation of client
CC proteins, and promote unfolded proteins to endoplasmic reticulum-
CC associated degradation (ERAD) pathway. Acts by determining
CC HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act
CC independently of HSPA8/Hsc70: together with DNAJB12, acts as a
CC chaperone that promotes maturation of potassium channels KCND2 and
CC KCNH2 by stabilizing nascent channel subunits and assembling them into
CC tetramers. While stabilization of nascent channel proteins is dependent
CC on HSPA8/Hsc70, the process of oligomerization of channel subunits is
CC independent of HSPA8/Hsc70. When overexpressed, forms membranous
CC structures together with DNAJB12 and HSPA8/Hsc70 within the nucleus;
CC the role of these structures, named DJANGOs, is still unclear.
CC {ECO:0000250|UniProtKB:Q8TBM8}.
CC -!- SUBUNIT: Interacts (via J domain) with HSPA8/Hsc70. Forms a
CC multiprotein complex, at least composed of DNAJB12, DNAJB14,
CC HSPA8/Hsc70 and SGTA; interaction with DNAJB14 and HSPA8/Hsc70 is
CC direct. {ECO:0000250|UniProtKB:Q8TBM8}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8TBM8}; Single-pass membrane protein
CC {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:Q8TBM8}; Single-
CC pass membrane protein {ECO:0000255}. Note=Localizes to the endoplasmic
CC reticulum membrane. When overexpressed, forms membranous structures in
CC the nucleus. {ECO:0000250|UniProtKB:Q8TBM8}.
CC -!- SIMILARITY: Belongs to the DnaJ family. DNAJB12/DNAJB14 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC122680; AAI22681.1; -; mRNA.
DR RefSeq; NP_001069599.1; NM_001076131.1.
DR RefSeq; XP_010804251.1; XM_010805949.2.
DR AlphaFoldDB; Q0IIE8; -.
DR SMR; Q0IIE8; -.
DR STRING; 9913.ENSBTAP00000005799; -.
DR PaxDb; Q0IIE8; -.
DR PRIDE; Q0IIE8; -.
DR Ensembl; ENSBTAT00000005799; ENSBTAP00000005799; ENSBTAG00000004426.
DR Ensembl; ENSBTAT00000083490; ENSBTAP00000058072; ENSBTAG00000004426.
DR GeneID; 538849; -.
DR KEGG; bta:538849; -.
DR CTD; 79982; -.
DR VEuPathDB; HostDB:ENSBTAG00000004426; -.
DR VGNC; VGNC:53699; DNAJB14.
DR eggNOG; KOG0714; Eukaryota.
DR GeneTree; ENSGT00940000157887; -.
DR HOGENOM; CLU_043579_3_0_1; -.
DR InParanoid; Q0IIE8; -.
DR OMA; AYCRKPA; -.
DR OrthoDB; 1173544at2759; -.
DR TreeFam; TF105145; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000004426; Expressed in conceptus and 109 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030544; F:Hsp70 protein binding; IBA:GO_Central.
DR GO; GO:0071218; P:cellular response to misfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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; IPR015399; DUF1977_DnaJ-like.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF09320; DUF1977; 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; Membrane; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..379
FT /note="DnaJ homolog subfamily B member 14"
FT /id="PRO_0000281477"
FT TOPO_DOM 1..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..379
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 108..172
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 55..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 379 AA; 42488 MW; 1B7AB604AF45C1DE CRC64;
MEGNRDEAEK CVEIAREALN AGNREKAQRF LQKAEKLYPL PSARALLEII MKNGSTAGNS
PHCRKPSGGG DQSKPNCTKD SSSGSGESGK GYTKDQVDGV LSINKCKNYY EVLGVTKDAG
DEDLKKAYRK LALKFHPDKN HAPGATDAFK KIGNAYAVLS NPEKRKQYDL TGNEEQACNQ
QNNGRFNFHR GCEADITPED LFNIFFGGGF PSGSVHSFSN GRAGYSNQHQ HRHSGHEREE
ERGDGGFSVF IQLMPIIVLI LVSLLSQLMV SNPPYSLYPR SGSGQTIKMQ TENLGVIYYV
NKDFKNEYKG MLLQKVEKSV EEDYVTNIRN NCWKERQQKT DMQYAAKVYH DERLRRKAEA
LSMDNCKELE RLTSIYKGG
