HSP22_DROME
ID HSP22_DROME Reviewed; 174 AA.
AC P02515; A4V1Q5; Q95SZ4; Q9VSX1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 4.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Heat shock protein 22;
GN Name=Hsp22; ORFNames=CG4460;
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].
RC STRAIN=Oregon-R;
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, Larva, and Pupae;
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 THR-152, 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).
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; J01098; AAA28635.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50290.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11962.1; -; Genomic_DNA.
DR EMBL; AY060412; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY119034; AAM50894.1; -; mRNA.
DR PIR; A02918; HHFF22.
DR PIR; A20647; A20647.
DR RefSeq; NP_001027114.1; NM_001031943.3.
DR RefSeq; NP_001027115.1; NM_001031944.2.
DR AlphaFoldDB; P02515; -.
DR SMR; P02515; -.
DR BioGRID; 534173; 172.
DR STRING; 7227.FBpp0100010; -.
DR iPTMnet; P02515; -.
DR PaxDb; P02515; -.
DR PRIDE; P02515; -.
DR EnsemblMetazoa; FBtr0100558; FBpp0100010; FBgn0001223.
DR EnsemblMetazoa; FBtr0100559; FBpp0100011; FBgn0001223.
DR GeneID; 3772576; -.
DR KEGG; dme:Dmel_CG4460; -.
DR CTD; 3772576; -.
DR FlyBase; FBgn0001223; Hsp22.
DR VEuPathDB; VectorBase:FBgn0001223; -.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000166889; -.
DR HOGENOM; CLU_095001_3_0_1; -.
DR InParanoid; P02515; -.
DR OMA; MFWRMAE; -.
DR PhylomeDB; P02515; -.
DR Reactome; R-DME-3371571; HSF1-dependent transactivation.
DR BioGRID-ORCS; 3772576; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 3772576; -.
DR PRO; PR:P02515; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0001223; Expressed in seminal fluid secreting gland and 12 other tissues.
DR Genevisible; P02515; DM.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:FlyBase.
DR GO; GO:0042802; F:identical protein 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:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IDA:FlyBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP: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..174
FT /note="Heat shock protein 22"
FT /id="PRO_0000125963"
FT DOMAIN 44..154
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 152..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT CONFLICT 44
FT /note="Q -> H (in Ref. 1; AAA28635 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="F -> L (in Ref. 1; AAA28635 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="A -> P (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="G -> A (in Ref. 1; AAA28635 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 109..111
FT /note="RRF -> GRY (in Ref. 1; AAA28635)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="E -> D (in Ref. 1; AAA28635)"
FT /evidence="ECO:0000305"
FT CONFLICT 123..128
FT /note="TSTLSS -> SSSLSD (in Ref. 1; AAA28635)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="N -> K (in Ref. 1; AAA28635 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="A -> T (in Ref. 1; AAA28635 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 174 AA; 19763 MW; 57DE84D754516B7E CRC64;
MRSLPMFWRM AEEMARMPRL SSPFHAFFHE PPVWSVALPR NWQQIARWQE QEFAPPATVN
KDGYKLTLDV KDYSELKVKV LDESVVLVEG KSEQQEAEQG GYSSRHFLRR FVLPEGYEAD
KVTSTLSSDG VLTISVPNPP GVQETLKERE VTIEQTGEPA KKSAEEPNDK AASQ
