L2EFL_DROME
ID L2EFL_DROME Reviewed; 187 AA.
AC P82147; Q8MLQ9;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein lethal(2)essential for life;
DE AltName: Full=Protein Efl21;
GN Name=l(2)efl; ORFNames=CG4533;
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] (ISOFORM LONG).
RC STRAIN=Oregon-R;
RA Czaja J., Kurzik-Dumke U.;
RT "Tissue specificity and subcellular localisation of the Efl21 protein
RT encoded by the heat shock related gene l(2)efl.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG), AND CHARACTERIZATION.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=7890160; DOI=10.1016/0378-1119(94)00827-f;
RA Kurzik-Dumke U., Lohmann E.;
RT "Sequence of the new Drosophila melanogaster small heat-shock-related gene,
RT lethal(2) essential for life [l(2)efl], at locus 59F4,5.";
RL Gene 154:171-175(1995).
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, AND ALTERNATIVE SPLICING.
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] (ISOFORMS LONG AND SHORT).
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).
CC -!- FUNCTION: Vital role in embryonic development.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P82147-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P82147-2; Sequence=VSP_002420, VSP_002421;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed during embryogenesis with no
CC sign of tissue specificity in expression up to stage 16.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development. Highest
CC expression during larval development.
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; AJ250883; CAB60198.1; -; Genomic_DNA.
DR EMBL; X77635; CAB55438.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF47041.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68267.1; -; Genomic_DNA.
DR EMBL; AY047516; AAK77248.1; -; mRNA.
DR EMBL; BT001462; AAN71217.1; ALT_SEQ; mRNA.
DR PIR; S42032; S42032.
DR RefSeq; NP_001261156.1; NM_001274227.1. [P82147-1]
DR RefSeq; NP_523827.1; NM_079103.3. [P82147-1]
DR AlphaFoldDB; P82147; -.
DR SMR; P82147; -.
DR BioGRID; 63343; 13.
DR DIP; DIP-18793N; -.
DR IntAct; P82147; 4.
DR STRING; 7227.FBpp0072009; -.
DR PaxDb; P82147; -.
DR PRIDE; P82147; -.
DR DNASU; 37744; -.
DR EnsemblMetazoa; FBtr0072100; FBpp0072009; FBgn0011296. [P82147-1]
DR EnsemblMetazoa; FBtr0336685; FBpp0307666; FBgn0011296. [P82147-1]
DR GeneID; 37744; -.
DR KEGG; dme:Dmel_CG4533; -.
DR FlyBase; FBgn0011296; l(2)efl.
DR VEuPathDB; VectorBase:FBgn0011296; -.
DR eggNOG; KOG3591; Eukaryota.
DR GeneTree; ENSGT00940000166889; -.
DR HOGENOM; CLU_095001_1_0_1; -.
DR InParanoid; P82147; -.
DR OMA; RPSFMRW; -.
DR PhylomeDB; P82147; -.
DR Reactome; R-DME-3371571; HSF1-dependent transactivation.
DR BioGRID-ORCS; 37744; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 37744; -.
DR PRO; PR:P82147; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0011296; Expressed in crop (Drosophila) and 27 other tissues.
DR ExpressionAtlas; P82147; baseline and differential.
DR Genevisible; P82147; DM.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
DR GO; GO:0030018; C:Z disc; IDA:FlyBase.
DR GO; GO:0051082; F:unfolded protein binding; ISM:FlyBase.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISM:FlyBase.
DR GO; GO:0042026; P:protein refolding; IDA:FlyBase.
DR GO; GO:0010998; P:regulation of translational initiation by eIF2 alpha phosphorylation; IMP:FlyBase.
DR GO; GO:0009408; P:response to heat; IDA:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; 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 PIRSF; PIRSF036514; Sm_HSP_B1; 1.
DR PRINTS; PR00299; ACRYSTALLIN.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS01031; SHSP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Reference proteome;
KW Stress response.
FT CHAIN 1..187
FT /note="Protein lethal(2)essential for life"
FT /id="PRO_0000125969"
FT DOMAIN 61..170
FT /note="sHSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00285"
FT REGION 151..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 131..145
FT /note="DVNPDTVTSSLSSDG -> ESEFHQQNRKYAKRV (in isoform
FT Short)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_002420"
FT VAR_SEQ 146..187
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_002421"
SQ SEQUENCE 187 AA; 21309 MW; FF1742AD4E29EEDB CRC64;
MSVVPLMFRD WWDELDFPMR TSRLLDQHFG QGLKRDDLMS SVWNSRPTVL RSGYLRPWHT
NSLQKQESGS TLNIDSEKFE VILDVQQFSP SEITVKVADK FVIVEGKHEE KQDEHGYVSR
QFSRRYQLPS DVNPDTVTSS LSSDGLLTIK APMKALPPPQ TERLVQITQT GPSSKEDNAK
KVETSTA
