ID   HSP7E_PONAB             Reviewed;         509 AA.
AC   Q5RE21;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Heat shock 70 kDa protein 14;
GN   Name=HSPA14;
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: 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; CR857718; CAH89986.1; -; mRNA.
DR   AlphaFoldDB; Q5RE21; -.
DR   SMR; Q5RE21; -.
DR   STRING; 9601.ENSPPYP00000002443; -.
DR   eggNOG; KOG0101; Eukaryota.
DR   InParanoid; Q5RE21; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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_0000405825"
SQ   SEQUENCE   509 AA;  54845 MW;  955F263F96BBFF6C CRC64;
     MAAIGVHLGC TSACVAVYKD GRAGVVANDA GDRVTPAVVA YSENEEIVGL AAKQSRIRNI
     SNTVMKVKQI LGRSSNDPQA QKYIVESKCL VIEKNGKLRY EIDTGEETKL VNPEDVARLI
     FSKMKETAHS VLGSDANDVV ITVPFDFGEK QKNALGEAAR AAGFNVLRLI HEPSAALLAY
     GIGQDSPTGK SNILVFKLGG TSLSLSIMEV NSGIYRVLST NTDDNIGGAH FTETLAQYLA
     SEFQRSFKYD VRGNARAMMK LMNSAEVAKH SLSTLGSANC FLDSLYEGQD FDCNVSRARF
     ELLCSPLFNK CIEAIRGLLD QSGFTADDIN KVVLCGGSSR IPKLQQLIKD IFPAVELLNS
     IPPDEVIPIG AAIEAGILIG KENLLVEDSL MIECSARDIL VKGVDESGAS RFTVLFPSGT
     PLPARRQHTL QAPGSISSVC LELYESDGKN SAKEETKFAQ VVLQDLDKKE NGLRDILAVL
     TMKRDGSLHV TCTDQETGKC EAISIEVAS