HSP27_DROME
ID HSP27_DROME Reviewed; 213 AA.
AC P02518; Q9VSX6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Heat shock protein 27;
GN Name=Hsp27; ORFNames=CG4466;
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=6302284; DOI=10.1016/s0022-2836(83)80241-1;
RA Southgate R., Ayme A., Voellmy R.;
RT "Nucleotide sequence analysis of the Drosophila small heat shock gene
RT cluster at locus 67B.";
RL J. Mol. Biol. 165:35-57(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6285380; DOI=10.1073/pnas.79.7.2360;
RA Ingolia T.D., Craig E.A.;
RT "Four small Drosophila heat shock proteins are related to each other and to
RT mammalian alpha-crystallin.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:2360-2364(1982).
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=Ovary;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
CC {ECO:0000255|PROSITE-ProRule:PRU00285}.
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DR EMBL; J01101; AAA28638.1; -; Genomic_DNA.
DR EMBL; X03891; CAA27527.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50285.1; -; Genomic_DNA.
DR EMBL; AY118471; AAM49840.1; -; mRNA.
DR PIR; A02921; HHFF27.
DR PIR; D20647; D20647.
DR RefSeq; NP_001287001.1; NM_001300072.1.
DR RefSeq; NP_524000.1; NM_079276.4.
DR AlphaFoldDB; P02518; -.
DR SMR; P02518; -.
DR BioGRID; 64473; 39.
DR DIP; DIP-18749N; -.
DR IntAct; P02518; 4.
DR MINT; P02518; -.
DR STRING; 7227.FBpp0076182; -.
DR iPTMnet; P02518; -.
DR PaxDb; P02518; -.
DR PRIDE; P02518; -.
DR DNASU; 39078; -.
DR EnsemblMetazoa; FBtr0076454; FBpp0076182; FBgn0001226.
DR EnsemblMetazoa; FBtr0346541; FBpp0312159; FBgn0001226.
DR GeneID; 39078; -.
DR KEGG; dme:Dmel_CG4466; -.
DR CTD; 39078; -.
DR FlyBase; FBgn0001226; Hsp27.
DR VEuPathDB; VectorBase:FBgn0001226; -.
DR eggNOG; KOG3591; Eukaryota.
DR HOGENOM; CLU_095001_1_0_1; -.
DR InParanoid; P02518; -.
DR OMA; SPYERSH; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; P02518; -.
DR Reactome; R-DME-3371571; HSF1-dependent transactivation.
DR SignaLink; P02518; -.
DR BioGRID-ORCS; 39078; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Hsp27; fly.
DR GenomeRNAi; 39078; -.
DR PRO; PR:P02518; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0001226; Expressed in imaginal disc and 38 other tissues.
DR ExpressionAtlas; P02518; baseline and differential.
DR Genevisible; P02518; DM.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IPI:FlyBase.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0051082; F:unfolded protein binding; IDA:FlyBase.
DR GO; GO:0042595; P:behavioral response to starvation; IMP:FlyBase.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:FlyBase.
DR GO; GO:0042742; P:defense response to bacterium; IMP:FlyBase.
DR GO; GO:0050832; P:defense response to fungus; IMP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0042026; P:protein refolding; IDA:FlyBase.
DR GO; GO:0009408; P:response to heat; IDA:FlyBase.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR002068; A-crystallin/Hsp20_dom.
DR InterPro; IPR001436; Alpha-crystallin/sHSP_animal.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR PANTHER; PTHR45640; PTHR45640; 1.
DR Pfam; PF00011; HSP20; 1.
DR PRINTS; PR00299; ACRYSTALLIN.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Stress response.
FT CHAIN 1..213
FT /note="Heat shock protein 27"
FT /id="PRO_0000125966"
FT DOMAIN 71..182
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 157..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT CONFLICT 40
FT /note="H -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="H -> P (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="M -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 143..147
FT /note="FDPNE -> LTPTK (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="K -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 167..170
FT /note="SKEQ -> GRER (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="Q -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 213 AA; 23617 MW; E08B39801A181F39 CRC64;
MSIIPLLHLA RELDHDYRTD WGHLLEDDFG FGVHAHDLFH PRRLLLPNTL GLGRRRYSPY
ERSHGHHNQM SRRASGGPNA LLPAVGKDGF QVCMDVSQFK PNELTVKVVD NTVVVEGKHE
EREDGHGMIQ RHFVRKYTLP KGFDPNEVVS TVSSDGVLTL KAPPPPSKEQ AKSERIVQIQ
QTGPAHLSVK APAPEAGDGK AENGSGEKME TSK
