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HSP73_DROME
ID   HSP73_DROME             Reviewed;         641 AA.
AC   Q9BIS2; B0BNN7; P02824; Q53XF0; Q5I7H2; Q5I7H4; Q5I7H6; Q5I7H8; Q5I7I3;
AC   Q5I7I6; Q5I7I8; Q9BIS1; Q9I7J6;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=Major heat shock 70 kDa protein Bb;
DE            Short=Heat shock protein 70Bb;
DE   AltName: Full=HSP70-87C1;
GN   Name=Hsp70Bb; ORFNames=CG31359;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6777045; DOI=10.1016/0092-8674(80)90430-4;
RA   Ingolia T.D., Craig E.A., McCarthy B.J.;
RT   "Sequence of three copies of the gene for the major Drosophila heat shock
RT   induced protein and their flanking regions.";
RL   Cell 21:669-679(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=3CPA126, 3CPA2, 3CPA35, 3CPA43, 3CPA47, 3CPA61, 3CPA81, 3CPA86, AUS,
RC   B25, B28, FrV3-1, QD18, Z(H)1, and ZZ30;
RX   PubMed=11965431; DOI=10.1007/s00239-001-0044-7;
RA   Bettencourt B.R., Feder M.E.;
RT   "Rapid concerted evolution via gene conversion at the Drosophila hsp70
RT   genes.";
RL   J. Mol. Evol. 54:569-586(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kapadia B., Kronmiller B., Li P.W., Liao G.,
RA   Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA   Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA   Celniker S.E.;
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-609.
RC   STRAIN=IS2, IS25, IS3, IS4, IS5, IS9, Z(S)10, Z(S)11, Z(S)15, Z(S)2,
RC   Z(S)24, Z(S)29, Z(S)30, Z(S)30A, Z(S)49, Z(S)53, Z(S)56, and Z(S)6;
RX   PubMed=12361573; DOI=10.1016/s0960-9822(02)01181-8;
RA   Maside X., Bartolome C., Charlesworth B.;
RT   "S-element insertions are associated with the evolution of the Hsp70 genes
RT   in Drosophila melanogaster.";
RL   Curr. Biol. 12:1686-1691(2002).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55.
RC   STRAIN=Evolution Canyon 2000;
RX   PubMed=15574805; DOI=10.1093/molbev/msi063;
RA   Lerman D.N., Feder M.E.;
RT   "Naturally occurring transposable elements disrupt hsp70 promoter function
RT   in Drosophila melanogaster.";
RL   Mol. Biol. Evol. 22:776-783(2005).
CC   -!- INDUCTION: Heat shock induces the synthesis of seven proteins at five
CC       otherwise inactive sites in the polytene chromosomes of fruit fly
CC       larvae. Two separate sites, producing two and three copies,
CC       respectively, code for the 70 kDa protein.
CC   -!- MISCELLANEOUS: Most strains have three copies of the gene coding for
CC       this protein at chromosome locus 87C1; two tandemly repeated Hsp70
CC       genes (Hsp70Bb and Hsp70Bc) and one in reverse orientation (Hsp70Ba).
CC       Some strains, including that sequenced in the Drosophila genome project
CC       have three tandemly repeated Hsp70 genes (Hsp70Bb, Hsp70Bbb and
CC       Hsp70Bc).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; J01104; AAD15226.1; -; Genomic_DNA.
DR   EMBL; AF295951; AAG26905.1; -; Genomic_DNA.
DR   EMBL; AF295952; AAG26906.1; -; Genomic_DNA.
DR   EMBL; AF295953; AAG26907.1; -; Genomic_DNA.
DR   EMBL; AF295954; AAG26908.1; -; Genomic_DNA.
DR   EMBL; AF295955; AAG26909.1; -; Genomic_DNA.
DR   EMBL; AF295956; AAG26910.1; -; Genomic_DNA.
DR   EMBL; AF295957; AAG26911.1; -; Genomic_DNA.
DR   EMBL; AF350476; AAK30233.1; -; Genomic_DNA.
DR   EMBL; AF350477; AAK30234.1; -; Genomic_DNA.
DR   EMBL; AF350478; AAK30235.1; -; Genomic_DNA.
DR   EMBL; AF350479; AAK30236.1; -; Genomic_DNA.
DR   EMBL; AF350480; AAK30237.1; -; Genomic_DNA.
DR   EMBL; AF350481; AAK30238.1; -; Genomic_DNA.
DR   EMBL; AF350482; AAK30239.1; -; Genomic_DNA.
DR   EMBL; AF350483; AAK30240.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13546.1; -; Genomic_DNA.
DR   EMBL; BT011058; AAR31129.1; -; mRNA.
DR   EMBL; BT011379; AAR96171.1; -; mRNA.
DR   EMBL; BT031349; ABY76186.1; -; mRNA.
DR   EMBL; AY846848; AAW34339.1; -; Genomic_DNA.
DR   EMBL; AY846849; AAW34340.1; -; Genomic_DNA.
DR   EMBL; AY846850; AAW34341.1; -; Genomic_DNA.
DR   EMBL; AY846851; AAW34342.1; -; Genomic_DNA.
DR   EMBL; AY846852; AAW34343.1; -; Genomic_DNA.
DR   EMBL; AY846853; AAW34344.1; -; Genomic_DNA.
DR   EMBL; AY846854; AAW34345.1; -; Genomic_DNA.
DR   EMBL; AY846855; AAW34346.1; -; Genomic_DNA.
DR   EMBL; AY846856; AAW34347.1; -; Genomic_DNA.
DR   EMBL; AY846857; AAW34348.1; -; Genomic_DNA.
DR   EMBL; AY846858; AAW34349.1; -; Genomic_DNA.
DR   EMBL; AY846859; AAW34350.1; -; Genomic_DNA.
DR   EMBL; AY846860; AAW34351.1; -; Genomic_DNA.
DR   EMBL; AY846861; AAW34352.1; -; Genomic_DNA.
DR   EMBL; AY846862; AAW34353.1; -; Genomic_DNA.
DR   EMBL; AY846863; AAW34354.1; -; Genomic_DNA.
DR   EMBL; AY846864; AAW34355.1; -; Genomic_DNA.
DR   EMBL; AY846865; AAW34356.1; -; Genomic_DNA.
DR   EMBL; AY370940; AAQ75092.1; -; Genomic_DNA.
DR   RefSeq; NP_524927.2; NM_080188.3.
DR   RefSeq; NP_650209.1; NM_141952.2.
DR   AlphaFoldDB; Q9BIS2; -.
DR   SMR; Q9BIS2; -.
DR   BioGRID; 71512; 47.
DR   BioGRID; 71513; 47.
DR   IntAct; Q9BIS2; 18.
DR   PRIDE; Q9BIS2; -.
DR   DNASU; 48583; -.
DR   EnsemblMetazoa; FBtr0082637; FBpp0082106; FBgn0013278.
DR   EnsemblMetazoa; FBtr0082638; FBpp0082107; FBgn0013279.
DR   GeneID; 48582; -.
DR   GeneID; 48583; -.
DR   KEGG; dme:Dmel_CG31359; -.
DR   KEGG; dme:Dmel_CG6489; -.
DR   CTD; 48582; -.
DR   CTD; 48583; -.
DR   FlyBase; FBgn0013278; Hsp70Bb.
DR   VEuPathDB; VectorBase:FBgn0013278; -.
DR   VEuPathDB; VectorBase:FBgn0013279; -.
DR   GeneTree; ENSGT00940000154813; -.
DR   HOGENOM; CLU_005965_3_0_1; -.
DR   InParanoid; Q9BIS2; -.
DR   OMA; ECEACIK; -.
DR   OrthoDB; 288077at2759; -.
DR   PhylomeDB; Q9BIS2; -.
DR   Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR   Reactome; R-DME-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   Reactome; R-DME-3371571; HSF1-dependent transactivation.
DR   Reactome; R-DME-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   SignaLink; Q9BIS2; -.
DR   BioGRID-ORCS; 48582; 0 hits in 3 CRISPR screens.
DR   BioGRID-ORCS; 48583; 0 hits in 3 CRISPR screens.
DR   PRO; PR:Q9BIS2; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0013278; Expressed in imaginal disc and 11 other tissues.
DR   ExpressionAtlas; Q9BIS2; baseline and differential.
DR   Genevisible; Q9BIS2; DM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0035080; P:heat shock-mediated polytene chromosome puffing; IMP:FlyBase.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0009408; P:response to heat; IMP:FlyBase.
DR   GO; GO:0001666; P:response to hypoxia; IMP:FlyBase.
DR   GO; GO:0006986; P:response to unfolded protein; NAS:UniProtKB.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
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   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
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; Nucleotide-binding; Reference proteome; Stress response.
FT   CHAIN           1..641
FT                   /note="Major heat shock 70 kDa protein Bb"
FT                   /id="PRO_0000078333"
FT   REGION          609..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         43
FT                   /note="D -> E (in strain: 3CPA86)"
FT   VARIANT         60
FT                   /note="P -> S (in strain: FrV3-1)"
FT   VARIANT         67
FT                   /note="A -> P (in Z(S)29)"
FT   VARIANT         71
FT                   /note="I -> T (in Z(S)2)"
FT   VARIANT         187
FT                   /note="K -> N (in strain: IS2, IS3, IS4, IS5, IS25 and
FT                   QD18)"
FT   VARIANT         195
FT                   /note="F -> L (in strain: ZZ30)"
FT   VARIANT         241
FT                   /note="E -> D (in strain: Z(H)1)"
FT   VARIANT         350
FT                   /note="E -> D (in strain: Z(H)1)"
FT   VARIANT         430
FT                   /note="S -> A (in strain: Z(H)1)"
FT   VARIANT         437
FT                   /note="S -> P (in strain: IS4 and IS5)"
FT   VARIANT         516
FT                   /note="M -> I (in strain: B28)"
FT   VARIANT         524
FT                   /note="A -> V (in strain: B28)"
FT   VARIANT         544
FT                   /note="V -> I (in strain: Z(S)24 and Z(S)49)"
FT   VARIANT         606
FT                   /note="K -> T (in strain: 3CPA126)"
FT   VARIANT         607
FT                   /note="M -> V (in strain: Z(S)30A)"
FT   CONFLICT        26..28
FT                   /note="IAN -> NAY (in Ref. 1; AAD15226)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        48..50
FT                   /note="IGD -> NGE (in Ref. 1; AAD15226)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306
FT                   /note="D -> N (in Ref. 1; AAD15226)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   641 AA;  70195 MW;  F2C9C204F67EBB59 CRC64;
     MPAIGIDLGT TYSCVGVYQH GKVEIIANDQ GNRTTPSYVA FTDSERLIGD PAKNQVAMNP
     RNTVFDAKRL IGRKYDDPKI AEDMKHWPFK VVSDGGKPKI GVEYKGESKR FAPEEISSMV
     LTKMKETAEA YLGESITDAV ITVPAYFNDS QRQATKDAGH IAGLNVLRII NEPTAAALAY
     GLDKNLKGER NVLIFDLGGG TFDVSILTID EGSLFEVRST AGDTHLGGED FDNRLVTHLA
     EEFKRKYKKD LRSNPRALRR LRTAAERAKR TLSSSTEATI EIDALFEGQD FYTKVSRARF
     EELCADLFRN TLQPVEKALN DAKMDKGQIH DIVLVGGSTR IPKVQSLLQE FFHGKNLNLS
     INPDEAVAYG AAVQAAILSG DQSGKIQDVL LVDVAPLSLG IETAGGVMTK LIERNCRIPC
     KQTKTFSTYS DNQPGVSIQV YEGERAMTKD NNALGTFDLS GIPPAPRGVP QIEVTFDLDA
     NGILNVSAKE MSTGKAKNIT IKNDKGRLSQ AEIDRMVNEA EKYADEDEKH RQRITSRNAL
     ESYVFNVKQS VEQAPAGKLD EADKNSVLDK CNETIRWLDS NTTAEKEEFD HKMEELTRHC
     SPIMTKMHQQ GAGAAGGPGA NCGQQAGGFG GYSGPTVEEV D
 
 
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