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DescriptionSubName: Full=Heat shock cognate 70-kd protein, tandem duplicate 1 {ECO:0000313|Ensembl:ENSDARP00000109199}; SubName: Full=Zgc:174006 protein {ECO:0000313|EMBL:AAI60648.1};
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MyHits synonymsB0UXS6_DANRE , B0UXS6 , C3418906DFCB6962
match map segment
ipat:HSP70_3 ipat:HSP70_1 ipat:HSP70_2 ipfam:HSP70  
Legends: 1, ipat:HSP70_3 [T]; 2, ipat:HSP70_1 [T]; 3, ipat:HSP70_2 [T].
ID   B0UXS6_DANRE            Unreviewed;       643 AA.
AC   B0UXS6;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   10-MAY-2017, entry version 88.
DE   SubName: Full=Heat shock cognate 70-kd protein, tandem duplicate 1 {ECO:0000313|Ensembl:ENSDARP00000109199};
DE   SubName: Full=Zgc:174006 protein {ECO:0000313|EMBL:AAI60648.1};
GN   Name=mcm5 {ECO:0000313|ZFIN:ZDB-GENE-021209-1};
GN   Synonyms=hsp70.1 {ECO:0000313|Ensembl:ENSDARP00000109199,
GN   ECO:0000313|ZFIN:ZDB-GENE-990415-91},
GN   zgc:174006 {ECO:0000313|EMBL:AAI60648.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000109199, ECO:0000313|Proteomes:UP000000437};
RN   [1] {ECO:0000313|EMBL:AAI60648.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testes {ECO:0000313|EMBL:AAI60648.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000109199, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000109199,
RC   ECO:0000313|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   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.,
RA   Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P.,
RA   Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G.,
RA   Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D.,
RA   Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K.,
RA   Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C.,
RA   Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J.,
RA   Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S.,
RA   Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A.,
RA   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.,
RA   Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z.,
RA   Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J.,
RA   Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C.,
RA   Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C.,
RA   Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000109199}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000109199};
RG   Ensembl;
RL   Submitted (MAY-2013) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; FP016243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC160648; AAI60648.1; -; mRNA.
DR   RefSeq; XP_005163979.1; XM_005163922.3.
DR   UniGene; Dr.75519; -.
DR   STRING; 7955.ENSDARP00000109199; -.
DR   Ensembl; ENSDART00000124762; ENSDARP00000109199; ENSDARG00000029688.
DR   GeneID; 100126123; -.
DR   KEGG; dre:100126123; -.
DR   CTD; 100126123; -.
DR   ZFIN; ZDB-GENE-990415-91; hsp70.1.
DR   ZFIN; ZDB-GENE-021209-1; mcm5.
DR   eggNOG; KOG0101; Eukaryota.
DR   eggNOG; COG0443; LUCA.
DR   GeneTree; ENSGT00870000136409; -.
DR   HOGENOM; HOG000228135; -.
DR   HOVERGEN; HBG051845; -.
DR   KO; K03283; -.
DR   OrthoDB; EOG091G03SF; -.
DR   TreeFam; TF105042; -.
DR   Proteomes; UP000000437; Chromosome 3.
DR   Bgee; ENSDARG00000029688; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0005634; C:nucleus; ISS:AgBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0048593; P:camera-type eye morphogenesis; IMP:ZFIN.
DR   GO; GO:0043009; P:chordate embryonic development; IMP:ZFIN.
DR   GO; GO:0000278; P:mitotic cell cycle; IMP:ZFIN.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:ZFIN.
DR   GO; GO:0046686; P:response to cadmium ion; IEP:ZFIN.
DR   GO; GO:0009408; P:response to heat; IDA:ZFIN.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IDA:ZFIN.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C.
DR   InterPro; IPR029047; HSP70_peptide-bd.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|RuleBase:RU003322};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000437};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003322};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437}.
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CC   The following FT lines are automated annotations from the MyHits database.
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FT   MYHIT       336    350       ipat:HSP70_3 [T]
FT   MYHIT        11     18       ipat:HSP70_1 [T]
FT   MYHIT       199    212       ipat:HSP70_2 [T]
FT   MYHIT         8    614       ipfam:HSP70 [T]
SQ   SEQUENCE   643 AA;  70442 MW;  C3418906DFCB6962 CRC64;
     MSSPKGIAIG IDLGTTYSCV GVFQHGKVEI IANDQGNRTT PSYVAFTDTE RLIGDAAKNQ
     VAMNPNNTVF DAKRLIGRRF DDPVVQSDMK HWSFKVVSDG GKPKVAVEHK GENKTFNPEE
     ISSMVLVKMK EIAEAYLGQK VTNAVITVPA YFNDSQRQAT KDAGVIAGLN VLRIINEPTA
     AAIAYGLDKG KSSERNVLIF DLGGGTFDVS ILTIEDGIFE VKATAGDTHL GGEDFDNRMV
     NHFVEEFKRK HKKDISQNKR ALRRLRTACE RAKRTLSSSS QASIEIDSLY EGIDFYTSIT
     RARFEELCSD LFRGTLDPVE KALKDAKMDK AQIHDIVLVG GSTRIPKIQK LLQDFFNGRE
     LNKSINPDEA VAYGAAVQAA ILMGDTSGNV QDLLLLDVAP LSLGIETAGG VMTALIKRNT
     TIPTKQTQTF TTYSDNQPGV LIQVFEGERA MTKDNNLLGK FELTGIPPAP RGVPQIEVTF
     DIDANGILNV SAADKSTGKQ NKITITNDKG RLSKEEIERM VQEADKYKAE DDLQREKISA
     KNSLESYAFN MKNSVEDDNL KGKISEEDKK RVIEKCNEAV SWLENNQLAD KEEYEHQLKE
     LEKVCNPVIS KLYQGGMPAG GCGAQARGAS GASAQGPTIE EVD
//