HSP26_DROME
ID HSP26_DROME Reviewed; 208 AA.
AC P02517; Q9VSX3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Heat shock protein 26;
GN Name=Hsp26; ORFNames=CG4183;
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=Embryo;
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., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-52 AND SER-58, AND
RP IDENTIFICATION BY 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J01099; AAA28636.1; -; Genomic_DNA.
DR EMBL; X03890; CAA27526.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50288.1; -; Genomic_DNA.
DR EMBL; AY069419; AAL39564.1; -; mRNA.
DR PIR; A02920; HHFF26.
DR PIR; C20647; C20647.
DR RefSeq; NP_001287000.1; NM_001300071.1.
DR RefSeq; NP_523997.1; NM_079273.3.
DR AlphaFoldDB; P02517; -.
DR SMR; P02517; -.
DR BioGRID; 64470; 63.
DR DIP; DIP-18379N; -.
DR IntAct; P02517; 3.
DR MINT; P02517; -.
DR STRING; 7227.FBpp0076224; -.
DR iPTMnet; P02517; -.
DR PaxDb; P02517; -.
DR PRIDE; P02517; -.
DR DNASU; 39075; -.
DR EnsemblMetazoa; FBtr0076496; FBpp0076224; FBgn0001225.
DR EnsemblMetazoa; FBtr0346539; FBpp0312157; FBgn0001225.
DR GeneID; 39075; -.
DR KEGG; dme:Dmel_CG4183; -.
DR CTD; 39075; -.
DR FlyBase; FBgn0001225; Hsp26.
DR VEuPathDB; VectorBase:FBgn0001225; -.
DR eggNOG; KOG3591; Eukaryota.
DR HOGENOM; CLU_095001_1_1_1; -.
DR InParanoid; P02517; -.
DR OMA; LSPWQCP; -.
DR OrthoDB; 1187096at2759; -.
DR PhylomeDB; P02517; -.
DR Reactome; R-DME-3371571; HSF1-dependent transactivation.
DR SignaLink; P02517; -.
DR BioGRID-ORCS; 39075; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Hsp26; fly.
DR GenomeRNAi; 39075; -.
DR PRO; PR:P02517; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0001225; Expressed in oocyte and 45 other tissues.
DR ExpressionAtlas; P02517; baseline and differential.
DR Genevisible; P02517; DM.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0017022; F:myosin binding; IPI:FlyBase.
DR GO; GO:0051082; F:unfolded protein binding; IDA:FlyBase.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:FlyBase.
DR GO; GO:0009631; P:cold acclimation; IEP: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..208
FT /note="Heat shock protein 26"
FT /id="PRO_0000125965"
FT DOMAIN 71..179
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 187..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 35
FT /note="L -> LL (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="E -> D (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 208 AA; 22994 MW; 75781CB2C309E33C CRC64;
MSLSTLLSLV DELQEPRSPI YELGLGLHPH SRYVLPLGTQ QRRSINGCPC ASPICPSSPA
GQVLALRREM ANRNDIHWPA TAHVGKDGFQ VCMDVAQFKP SELNVKVVDD SILVEGKHEE
RQDDHGHIMR HFVRRYKVPD GYKAEQVVSQ LSSDGVLTVS IPKPQAVEDK SKERIIQIQQ
VGPAHLNVKA NESEVKGKEN GAPNGKDK
