ID   HSP7E_MACFA             Reviewed;         509 AA.
AC   Q4R6J2;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Heat shock 70 kDa protein 14;
GN   Name=HSPA14; ORFNames=QtsA-17902;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-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; AB169191; BAE01283.1; -; mRNA.
DR   RefSeq; NP_001271024.1; NM_001284095.1.
DR   AlphaFoldDB; Q4R6J2; -.
DR   SMR; Q4R6J2; -.
DR   STRING; 9541.XP_005564742.1; -.
DR   Ensembl; ENSMFAT00000083635; ENSMFAP00000050740; ENSMFAG00000044126.
DR   GeneID; 101865350; -.
DR   CTD; 51182; -.
DR   VEuPathDB; HostDB:ENSMFAG00000044126; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   GeneTree; ENSGT00940000156380; -.
DR   OMA; YIKESKC; -.
DR   OrthoDB; 646813at2759; -.
DR   Proteomes; UP000233100; Chromosome 9.
DR   Bgee; ENSMFAG00000044126; Expressed in thymus and 13 other tissues.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005840; C:ribosome; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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_0000405824"
SQ   SEQUENCE   509 AA;  54882 MW;  C0ECE7A36859AEC7 CRC64;
     MAAIGVHLGC TSACVAVYKD GRAGVVANDA GDRVTPAVVA YSENEEIVGL AAKQSRIRNI
     SNTVMKVKQI LGRSSNDPQA QKYITESKCL VIEKNGKLRY EIDTGEETRF VNPEDVVRLI
     FSKMKETAHS VLGSDANDVV ITVPFDFGEK QKNALGEAAR AAGFNVLRLI HEPSAALLAY
     GIGQDSPNGK SNILVFKLGG TSLSLSVMEV NSGIYRVLST NTDDNIGGAH FTETLAQYLA
     SEFQRSFKHD VKGNARAMMK LMNSAEVAKH SLSTLGSANC FLDSLYEGQD FDCNVSRARF
     ELLCSPLFNK CIEAIRGLLD QSGFTADDIN KVVLCGGSSR IPKLQQLIKD LFPAVELLNS
     IPPDEVIPIG AAIEAGILIG KENLLVEDSL MIECSARDIL VKGVDESGAS RFTVLFPSGT
     PLPARRQHTL QAPGSISSVC LELYESDGKN SAKEETKFAQ VVLQDLDKKE NGLRDILAVL
     TMKRDGSLHV TCTDQETGKC EAISIEVAS