GenomeNet

Database: UniProt
Entry: Q5XJ12_DANRE
LinkDB: Q5XJ12_DANRE
Original site: Q5XJ12_DANRE 
ID   Q5XJ12_DANRE            Unreviewed;       682 AA.
AC   Q5XJ12;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=Stress-70 protein, mitochondrial {ECO:0000256|ARBA:ARBA00019355};
DE   AltName: Full=75 kDa glucose-regulated protein {ECO:0000256|ARBA:ARBA00031419};
DE   AltName: Full=Heat shock 70 kDa protein 9 {ECO:0000256|ARBA:ARBA00030055};
GN   Name=hspa9 {ECO:0000313|EMBL:AAH83504.1,
GN   ECO:0000313|RefSeq:NP_958483.2, ECO:0000313|ZFIN:ZDB-GENE-030828-12};
GN   Synonyms=cb740 {ECO:0000313|RefSeq:NP_958483.2}, crs
GN   {ECO:0000313|RefSeq:NP_958483.2}, hspa9b
GN   {ECO:0000313|RefSeq:NP_958483.2}, wu:fc14d08
GN   {ECO:0000313|RefSeq:NP_958483.2}, wu:fc38a06
GN   {ECO:0000313|RefSeq:NP_958483.2};
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 {ECO:0000313|EMBL:AAH83504.1};
RN   [1] {ECO:0000313|EMBL:AAH83504.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo {ECO:0000313|EMBL:AAH83504.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|RefSeq:NP_958483.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15650063;
RA   Craven S.E., French D., Ye W., de Sauvage F., Rosenthal A.;
RT   "Loss of Hspa9b in zebrafish recapitulates the ineffective hematopoiesis of
RT   the myelodysplastic syndrome.";
RL   Blood 105:3528-3534(2005).
RN   [3] {ECO:0000313|RefSeq:NP_958483.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18256191; DOI=10.1242/dev.018150;
RA   Hawkins T.A., Haramis A.P., Etard C., Prodromou C., Vaughan C.K.,
RA   Ashworth R., Ray S., Behra M., Holder N., Talbot W.S., Pearl L.H.,
RA   Strahle U., Wilson S.W.;
RT   "The ATPase-dependent chaperoning activity of Hsp90a regulates thick
RT   filament formation and integration during skeletal muscle
RT   myofibrillogenesis.";
RL   Development 135:1147-1156(2008).
RN   [4] {ECO:0000313|RefSeq:NP_958483.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18846223;
RA   Imamura S., Uchiyama J., Koshimizu E., Hanai J., Raftopoulou C.,
RA   Murphey R.D., Bayliss P.E., Imai Y., Burns C.E., Masutomi K., Gagos S.,
RA   Zon L.I., Roberts T.M., Kishi S.;
RT   "A non-canonical function of zebrafish telomerase reverse transcriptase is
RT   required for developmental hematopoiesis.";
RL   PLoS ONE 3:e3364-e3364(2008).
RN   [5] {ECO:0000313|RefSeq:NP_958483.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18950614;
RA   Yoshinari N., Ishida T., Kudo A., Kawakami A.;
RT   "Gene expression and functional analysis of zebrafish larval fin fold
RT   regeneration.";
RL   Dev. Biol. 325:71-81(2009).
RN   [6] {ECO:0000313|RefSeq:NP_958483.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20339547;
RA   Tiefenbach J., Moll P.R., Nelson M.R., Hu C., Baev L., Kislinger T.,
RA   Krause H.M.;
RT   "A live zebrafish-based screening system for human nuclear receptor ligand
RT   and cofactor discovery.";
RL   PLoS ONE 5:e9797-e9797(2010).
RN   [7] {ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
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., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   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   [8] {ECO:0000313|RefSeq:NP_958483.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=27189481;
RA   Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA   Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA   Bobe J.;
RT   "Gene evolution and gene expression after whole genome duplication in fish:
RT   the PhyloFish database.";
RL   BMC Genomics 17:368-368(2016).
RN   [9] {ECO:0000313|RefSeq:NP_958483.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28138518;
RA   Chen W.C., Wang Z., Missinato M.A., Park D.W., Long D.W., Liu H.J.,
RA   Zeng X., Yates N.A., Kim K., Wang Y.;
RT   "Decellularized zebrafish cardiac extracellular matrix induces mammalian
RT   heart regeneration.";
RL   Sci. Adv. 2:e1600844-e1600844(2016).
RN   [10] {ECO:0000313|RefSeq:NP_958483.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28252024;
RA   Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA   Choudhary J.S., Emes R.D., Grant S.G.;
RT   "Evolution of complexity in the zebrafish synapse proteome.";
RL   Nat. Commun. 8:14613-14613(2017).
RN   [11] {ECO:0000313|RefSeq:NP_958483.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30501106;
RA   Xu K., Xu H., Han Z.;
RT   "Genome-Wide Identification of Hsp70 Genes in the Large Yellow Croaker
RT   (Larimichthys crocea) and Their Regulated Expression Under Cold and Heat
RT   Stress.";
RL   Genes (Basel) 9:E590-E590(2018).
RN   [12] {ECO:0000313|RefSeq:NP_958483.2}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30684501;
RA   Umali J., Hawkey-Noble A., French C.R.;
RT   "Loss of foxc1 in zebrafish reduces optic nerve size and cell number in the
RT   retinal ganglion cell layer.";
RL   Vision Res. 156:66-72(2019).
RN   [13] {ECO:0000313|RefSeq:NP_958483.2}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; BC083504; AAH83504.1; -; mRNA.
DR   RefSeq; NP_958483.2; NM_201326.2.
DR   IntAct; Q5XJ12; 1.
DR   GeneID; 373085; -.
DR   KEGG; dre:373085; -.
DR   AGR; ZFIN:ZDB-GENE-030828-12; -.
DR   CTD; 3313; -.
DR   ZFIN; ZDB-GENE-030828-12; hspa9.
DR   OrthoDB; 143at2759; -.
DR   Proteomes; UP000000437; Alternate scaffold 14.
DR   Proteomes; UP000000437; Chromosome 14.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; NAS:ZFIN.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; NAS:ZFIN.
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:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:0031101; P:fin regeneration; IMP:ZFIN.
DR   GO; GO:0030097; P:hemopoiesis; IMP:ZFIN.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   CDD; cd11733; HSPA9-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_00332; DnaK; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR012725; Chaperone_DnaK.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   NCBIfam; TIGR02350; prok_dnaK; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU003322};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q5XJ12};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Stress response {ECO:0000313|EMBL:AAH83504.1}.
FT   REGION          658..682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   682 AA;  73968 MW;  CE17FDC64A5B8FC9 CRC64;
     MLSVSRTARL VRNVSCSQKT SSGVSDLIKK ACLNGWTQKT LQTAARRHYA SEAIRGAVIG
     IDLGTTNSCV AVMDGKNAKV LENAEGARTT PSVVAFTSDG ERLVGMPAKR QAVTNPNNTL
     YATKRLIGRR FDDAEVQKDL KNVPYKIVRA SNGDAWLEVH GKMYSPSQAG AFILIKMKET
     AESYLGQSVK NAVVTVPAYF NDSQRQATKD AGQIAGLNVL RVINEPTAAA LAYGLDKTQD
     KIIAVYDLGG GTFDISVLEI QKGVFEVKST NGDTFLGGED FDQHLLRHIV KEFKKESGVD
     LMKDNMALQR VREAAEKAKC ELSSSLQTDI NLPYLTMDAS GPKHLNMKLT RSQFEGIVAD
     LIRRTVAPCQ KAMQDAEVSK SDIGEVLLVG GMTRMPKVQQ TVQDLFGRAP SKSVNPDEAV
     AIGAAIQGGV LAGDVTDVLL LDVTPLSLGI ETLGGVFTKL INRNTTIPTK KSQVFSTAAD
     GQTQVEIKVC QGEREMATDN KVLGQFTLVG IPPALRGVPQ IEVTFDIDAN GIVHVSAKDK
     GTGREQQIVI QSSGGLSKDD IENMVKNAEK YAEEDRRRKD RVEAVNMAEG IVHDTESKME
     EFKDQLPADE CNKLKEEISK VRELLSRKDT ETGENIKQAA TSLQQASLKL FEMAYKKMAS
     EREGSSGSSS SGEAGEKKEG QQ
//
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