ID   HSP7E_DANRE             Reviewed;         504 AA.
AC   Q5RGE6; A2VD43;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Heat shock 70 kDa protein 14;
GN   Name=hspa14; ORFNames=si:dkey-153k10.2;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (DEC-2006) 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. {ECO:0000250}.
CC   -!- SUBUNIT: Component of ribosome-associated complex (RAC). {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; BX901962; CAI20676.1; -; Genomic_DNA.
DR   EMBL; BC129343; AAI29344.1; -; mRNA.
DR   RefSeq; NP_001038541.1; NM_001045076.1.
DR   AlphaFoldDB; Q5RGE6; -.
DR   SMR; Q5RGE6; -.
DR   STRING; 7955.ENSDARP00000075275; -.
DR   PaxDb; Q5RGE6; -.
DR   PRIDE; Q5RGE6; -.
DR   Ensembl; ENSDART00000080829; ENSDARP00000075275; ENSDARG00000058030.
DR   Ensembl; ENSDART00000184048; ENSDARP00000146414; ENSDARG00000112257.
DR   GeneID; 565232; -.
DR   KEGG; dre:565232; -.
DR   CTD; 51182; -.
DR   ZFIN; ZDB-GENE-041210-73; hspa14.
DR   eggNOG; KOG0101; Eukaryota.
DR   GeneTree; ENSGT00940000156380; -.
DR   HOGENOM; CLU_005965_0_3_1; -.
DR   InParanoid; Q5RGE6; -.
DR   OMA; TSVFHYR; -.
DR   OrthoDB; 646813at2759; -.
DR   PhylomeDB; Q5RGE6; -.
DR   TreeFam; TF105045; -.
DR   Reactome; R-DRE-3371453; Regulation of HSF1-mediated heat shock response.
DR   PRO; PR:Q5RGE6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 4.
DR   Bgee; ENSDARG00000058030; Expressed in presomitic mesoderm and 29 other tissues.
DR   ExpressionAtlas; Q5RGE6; baseline.
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; 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.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..504
FT                   /note="Heat shock 70 kDa protein 14"
FT                   /id="PRO_0000405827"
FT   CONFLICT        106
FT                   /note="E -> A (in Ref. 2; AAI29344)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   504 AA;  54270 MW;  6FC95099788CB780 CRC64;
     MAAIGVHFGY TCACVAVFKD GRADVVANDA GDRVTPAVVA YRDTEQIVGI AAKQGRIRNA
     ANTVVKVKQI LGRRYDDPDA QAHKEESKCI VVNKSGLPRY EIDTGETTKY VSPEDVAKLI
     FHKMKETAQS ALGSDVKDAV ITVPFEFDEM QKNALRQAAE SAGFNVLRLI HEPSAALLAY
     DIGQDSPLGK SHVLVYKLGG TSLSVTVLEV NSGVYRVLAT QTDHQTGGES FTQELAQHLA
     AEFKKTFKQD VSGNARAMMK LMNSADVAKH TLSTLGSANC FVDSLYDGMD FECNVSRARF
     ELICSSLFNK CIQPIKSLLE QVNLSTSDVN KVVLSGGSAR IPKLQQMIRD LFPDVELLNS
     IPPDEVIPVG AAMQAGILVG KDSLALGEDS ITVDCCASDI TLKEVDDSGL EVFTVLFPSG
     TPLPARRQHT LQGPGSLSSV RLQLFQAQQP IAQIVLGDLE PKEELHDVVT VLTMKRDGSL
     HVTCTEQSSG RSEAITIETA AAAS