ID   HSP7E_BOVIN             Reviewed;         509 AA.
AC   Q2YDD0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Heat shock 70 kDa protein 14;
GN   Name=HSPA14;
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=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the ribosome-associated complex (RAC), a complex
CC       involved in folding or maintaining nascent polypeptides in a folding-
CC       competent state. In the RAC complex, binds to the nascent polypeptide
CC       chain, while DNAJC2 stimulates its ATPase activity (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of ribosome-associated complex (RAC), a heterodimer
CC       composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type
CC       chaperone DNAJC2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; BC110281; AAI10282.1; -; mRNA.
DR   RefSeq; NP_001039853.1; NM_001046388.2.
DR   AlphaFoldDB; Q2YDD0; -.
DR   SMR; Q2YDD0; -.
DR   STRING; 9913.ENSBTAP00000021872; -.
DR   PaxDb; Q2YDD0; -.
DR   PRIDE; Q2YDD0; -.
DR   Ensembl; ENSBTAT00000021872; ENSBTAP00000021872; ENSBTAG00000016451.
DR   GeneID; 534751; -.
DR   KEGG; bta:534751; -.
DR   CTD; 51182; -.
DR   VEuPathDB; HostDB:ENSBTAG00000016451; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   GeneTree; ENSGT00940000156380; -.
DR   HOGENOM; CLU_005965_0_3_1; -.
DR   InParanoid; Q2YDD0; -.
DR   OMA; TSVFHYR; -.
DR   OrthoDB; 1318335at2759; -.
DR   TreeFam; TF105045; -.
DR   Reactome; R-BTA-3371453; Regulation of HSF1-mediated heat shock response.
DR   PRO; PR:Q2YDD0; -.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000016451; Expressed in oocyte and 107 other tissues.
DR   ExpressionAtlas; Q2YDD0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR   GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   CDD; cd10238; HSPA14-like_NBD; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   InterPro; IPR042049; HSPA14_NBD.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..509
FT                   /note="Heat shock 70 kDa protein 14"
FT                   /id="PRO_0000289945"
SQ   SEQUENCE   509 AA;  54930 MW;  A43C0A8F9A9BA379 CRC64;
     MAAIGVHLGC TSACVAVYKD GRADVVANDA GDRVTPAIVA YSKNEEVVGL AAKQSRIRNI
     SNTVMKVKQI LGRSSDDPQS RKYITESKCL VIEKNGKLLY EIDTGEEKKF VSPEDVARLI
     FSKMKETAHS VLGSDANDVV ITVPFDFGEK QKSALGEAAR AAGFNVLRLI HEPSAALLAY
     GIGQDSPTGK SNILVFKLGG TSLSISVMEV NSGIYRVLST NTDNNIGGTH FTETLAQYLA
     SEFQRSFRHD VRGNARAMMK LMNGADTAKH SLSTLGSANC FLDSLYEGQD FDCNVSRARF
     ELLCSPLFNK CIEAIREVLE QSGFTADDIN KVVLCGGSSR IPRLQQMIRD LFPAVELLNS
     IPPDEVIPIG AAIEAGILIG KESLSVEDAL QIECSAKDIL VKGVDESGAN SFKVLFPSGT
     PLPARRQHTL QAPGSISSVC LELYESEGKN SAKVENKFAQ VVLQDLDKKE NGLRDILAVL
     TMKRDGSLHV TCTDQETGKC EAITIEVAS