EST6_DROME
ID EST6_DROME Reviewed; 544 AA.
AC P08171; P91646; P91647; P91648; P91649; P91650; P92173; P92195; P92200;
AC Q867G7; Q867V2; Q867Y9; Q868B8; Q86CX4; Q86CX5; Q86CX6; Q86CX7; Q86CX8;
AC Q86CX9; Q86CY0; Q86CY1; Q86CY2; Q86CY3; Q86CY4; Q86CY5; Q86CY6; Q86CY7;
AC Q8SWT4; Q9U797; Q9U798; Q9U799; Q9U7A0; Q9V3U8; Q9XTN6;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Esterase-6;
DE Short=Est-6;
DE EC=3.1.1.1;
DE AltName: Full=Carboxylic-ester hydrolase 6;
DE Short=Carboxylesterase-6;
DE Flags: Precursor;
GN Name=Est-6; Synonyms=EST6; ORFNames=CG6917;
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=Canton-S;
RX PubMed=2105433; DOI=10.1093/oxfordjournals.molbev.a040582;
RA Collet C., Nielsen K.M., Russell R.J., Karl M., Oakeshott J.G.,
RA Richmond R.C.;
RT "Molecular analysis of duplicated esterase genes in Drosophila
RT melanogaster.";
RL Mol. Biol. Evol. 7:9-28(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2493155; DOI=10.1073/pnas.86.4.1426;
RA Cooke P.H., Oakeshott J.G.;
RT "Amino acid polymorphisms for esterase-6 in Drosophila melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1426-1430(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3106966; DOI=10.1073/pnas.84.10.3359;
RA Oakeshott J.G., Collet C., Phillis R.W., Nielsen K.M., Russell R.J.,
RA Chambers G.K., Ross V., Richmond R.C.;
RT "Molecular cloning and characterization of esterase-6, a serine hydrolase
RT of Drosophila.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:3359-3363(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=174F, 357F, 377F, 510S, 517S, 521S, 581F, and 94F;
RX PubMed=10545464; DOI=10.1093/genetics/153.3.1357;
RA Balakirev E.S., Balakirev E.I., Rodriguez-Trelles F., Ayala F.J.;
RT "Molecular evolution of two linked genes, Est-6 and Sod, in Drosophila
RT melanogaster.";
RL Genetics 153:1357-1369(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=F-1461S, F-274F, F-517F, F-531F, F-611F, F-775F, F-96S, S-114S,
RC S-1224F, S-255S, S-2588S, S-26F, S-438S, S-483F, S-498F, S-501S, S-521F,
RC S-549S, S-565F, S-5F, S-968F, and US-255F;
RX PubMed=12034506; DOI=10.1016/s0378-1119(02)00477-8;
RA Balakirev E.S., Balakirev E.I., Ayala F.J.;
RT "Molecular evolution of the Est-6 gene in Drosophila melanogaster:
RT contrasting patterns of DNA variability in adjacent functional regions.";
RL Gene 288:167-177(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Bar-F-77F, Bar-F-79F, Bar-F-7F, Bar-F-93F, Bar-F-96S, Bar-S-119F,
RC Bar-S-158F, Bar-S-19F, Bar-S-24F, Bar-S-44F, Bar-S-48F, Bar-S-60F,
RC Bar-S-78F, Bar-S-80F, Bar-S-86F, Bar-S-89F, Bar-S-95F, Bar-S-99F,
RC Ven-S-10F, Ven-S-11F, Ven-S-12F, Ven-S-13F, Ven-S-14F, Ven-S-15F,
RC Ven-S-16S, Ven-S-17F, Ven-S-18F, Ven-S-1F, Ven-S-20F, Ven-S-21F, Ven-S-22F,
RC Ven-S-23F, Ven-S-2F, Ven-S-3F, Ven-S-4F, Ven-S-5F, Ven-S-7F, Ven-S-8F,
RC Zim-F-H27, Zim-F-H31, Zim-F-S11, Zim-F-S18, Zim-F-S53, Zim-S-44F,
RC Zim-S-H13, Zim-S-H32, Zim-S-S10, Zim-S-S2, Zim-S-S30, and Zim-S-S34;
RX PubMed=14704175; DOI=10.1093/genetics/165.4.1901;
RA Balakirev E.S., Ayala F.J.;
RT "Nucleotide variation of the Est-6 gene region in natural populations of
RT Drosophila melanogaster.";
RL Genetics 165:1901-1914(2003).
RN [7]
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 [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-538.
RC STRAIN=178.7, 709.6, DPF-13, DPF-2, DPF-30, DPF-46, DPF-62, DPF-77,
RC DPF-82.1, EM-10, MA-10.2, MA-4.2, MA-4.4, VC-805, and VC-815;
RX PubMed=8978045; DOI=10.1093/genetics/144.4.1565;
RA Hasson E., Eanes W.F.;
RT "Contrasting histories of three gene regions associated with In(3L)Payne of
RT Drosophila melanogaster.";
RL Genetics 144:1565-1575(1996).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-42; ASN-420 AND ASN-456, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
CC -!- FUNCTION: Transferred from the ejaculatory bulbs of males to the female
CC genitals upon copulation, plays an important role in the reproductive
CC biology.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+);
CC Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10039};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the ejaculatory bulbs of
CC male.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM11419.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M33780; AAA28519.1; -; Genomic_DNA.
DR EMBL; J04167; AAA28518.1; -; Genomic_DNA.
DR EMBL; M15961; AAA28517.1; -; mRNA.
DR EMBL; AF147095; AAD39958.1; -; Genomic_DNA.
DR EMBL; AF147096; AAD39959.1; -; Genomic_DNA.
DR EMBL; AF147097; AAD39960.1; -; Genomic_DNA.
DR EMBL; AF147098; AAD39961.1; -; Genomic_DNA.
DR EMBL; AF147099; AAD39962.1; -; Genomic_DNA.
DR EMBL; AF147100; AAD39963.1; -; Genomic_DNA.
DR EMBL; AF147101; AAD39964.1; -; Genomic_DNA.
DR EMBL; AF147102; AAD39965.1; -; Genomic_DNA.
DR EMBL; AF217624; AAF61043.1; -; Genomic_DNA.
DR EMBL; AF217625; AAF61044.1; -; Genomic_DNA.
DR EMBL; AF217626; AAF61045.1; -; Genomic_DNA.
DR EMBL; AF217627; AAF61046.1; -; Genomic_DNA.
DR EMBL; AF217628; AAF61047.1; -; Genomic_DNA.
DR EMBL; AF217629; AAF61048.1; -; Genomic_DNA.
DR EMBL; AF217630; AAF61049.1; -; Genomic_DNA.
DR EMBL; AF217631; AAF61050.1; -; Genomic_DNA.
DR EMBL; AF217632; AAF61051.1; -; Genomic_DNA.
DR EMBL; AF217633; AAF61052.1; -; Genomic_DNA.
DR EMBL; AF217634; AAF61053.1; -; Genomic_DNA.
DR EMBL; AF217635; AAF61054.1; -; Genomic_DNA.
DR EMBL; AF217636; AAF61055.1; -; Genomic_DNA.
DR EMBL; AF217637; AAF61056.1; -; Genomic_DNA.
DR EMBL; AF217638; AAF61057.1; -; Genomic_DNA.
DR EMBL; AF217639; AAF61058.1; -; Genomic_DNA.
DR EMBL; AF217640; AAF61059.1; -; Genomic_DNA.
DR EMBL; AF217641; AAF61060.1; -; Genomic_DNA.
DR EMBL; AF217642; AAF61061.1; -; Genomic_DNA.
DR EMBL; AF217643; AAF61062.1; -; Genomic_DNA.
DR EMBL; AF217644; AAF61063.1; -; Genomic_DNA.
DR EMBL; AF217645; AAF61064.1; -; Genomic_DNA.
DR EMBL; AY247664; AAP20953.1; -; Genomic_DNA.
DR EMBL; AY247665; AAP20954.1; -; Genomic_DNA.
DR EMBL; AY247666; AAP20955.1; -; Genomic_DNA.
DR EMBL; AY247667; AAP20956.1; -; Genomic_DNA.
DR EMBL; AY247668; AAP20957.1; -; Genomic_DNA.
DR EMBL; AY247669; AAP20958.1; -; Genomic_DNA.
DR EMBL; AY247670; AAP20959.1; -; Genomic_DNA.
DR EMBL; AY247671; AAP20960.1; -; Genomic_DNA.
DR EMBL; AY247672; AAP20961.1; -; Genomic_DNA.
DR EMBL; AY247673; AAP20962.1; -; Genomic_DNA.
DR EMBL; AY247674; AAP20963.1; -; Genomic_DNA.
DR EMBL; AY247675; AAP20964.1; -; Genomic_DNA.
DR EMBL; AY247676; AAP20965.1; -; Genomic_DNA.
DR EMBL; AY247677; AAP20966.1; -; Genomic_DNA.
DR EMBL; AY247678; AAP20967.1; -; Genomic_DNA.
DR EMBL; AY247679; AAP20968.1; -; Genomic_DNA.
DR EMBL; AY247680; AAP20969.1; -; Genomic_DNA.
DR EMBL; AY247681; AAP20970.1; -; Genomic_DNA.
DR EMBL; AY247682; AAP20971.1; -; Genomic_DNA.
DR EMBL; AY247683; AAP20972.1; -; Genomic_DNA.
DR EMBL; AY247684; AAP20973.1; -; Genomic_DNA.
DR EMBL; AY247685; AAP20974.1; -; Genomic_DNA.
DR EMBL; AY247686; AAP20975.1; -; Genomic_DNA.
DR EMBL; AY247687; AAP20976.1; -; Genomic_DNA.
DR EMBL; AY247688; AAP20977.1; -; Genomic_DNA.
DR EMBL; AY247689; AAP20978.1; -; Genomic_DNA.
DR EMBL; AY247690; AAP20979.1; -; Genomic_DNA.
DR EMBL; AY247691; AAP20980.1; -; Genomic_DNA.
DR EMBL; AY247692; AAP20981.1; -; Genomic_DNA.
DR EMBL; AY247693; AAP20982.1; -; Genomic_DNA.
DR EMBL; AY247694; AAP20983.1; -; Genomic_DNA.
DR EMBL; AY247695; AAP20984.1; -; Genomic_DNA.
DR EMBL; AY247696; AAP20985.1; -; Genomic_DNA.
DR EMBL; AY247697; AAP20986.1; -; Genomic_DNA.
DR EMBL; AY247698; AAP20987.1; -; Genomic_DNA.
DR EMBL; AY247699; AAP20988.1; -; Genomic_DNA.
DR EMBL; AY247700; AAP20989.1; -; Genomic_DNA.
DR EMBL; AY247701; AAP20990.1; -; Genomic_DNA.
DR EMBL; AY247702; AAP20991.1; -; Genomic_DNA.
DR EMBL; AY247703; AAP20992.1; -; Genomic_DNA.
DR EMBL; AY247704; AAP20993.1; -; Genomic_DNA.
DR EMBL; AY247705; AAP20994.1; -; Genomic_DNA.
DR EMBL; AY247706; AAP20995.1; -; Genomic_DNA.
DR EMBL; AY247707; AAP20996.1; -; Genomic_DNA.
DR EMBL; AY247708; AAP20997.1; -; Genomic_DNA.
DR EMBL; AY247709; AAP20998.1; -; Genomic_DNA.
DR EMBL; AY247710; AAP20999.1; -; Genomic_DNA.
DR EMBL; AY247711; AAP21000.1; -; Genomic_DNA.
DR EMBL; AY247712; AAP21001.1; -; Genomic_DNA.
DR EMBL; AY247713; AAP21002.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49946.1; -; Genomic_DNA.
DR EMBL; AY095091; AAM11419.1; ALT_SEQ; mRNA.
DR EMBL; U57474; AAB46692.1; -; Genomic_DNA.
DR EMBL; U57475; AAB46693.1; -; Genomic_DNA.
DR EMBL; U57476; AAB46694.1; -; Genomic_DNA.
DR EMBL; U57477; AAB46695.1; -; Genomic_DNA.
DR EMBL; U57478; AAB46696.1; -; Genomic_DNA.
DR EMBL; U57479; AAB46697.1; -; Genomic_DNA.
DR EMBL; U57480; AAB46698.1; -; Genomic_DNA.
DR EMBL; U57481; AAB46699.1; -; Genomic_DNA.
DR EMBL; U57482; AAB46700.1; -; Genomic_DNA.
DR EMBL; U57483; AAB46701.1; -; Genomic_DNA.
DR EMBL; U57484; AAB46702.1; -; Genomic_DNA.
DR EMBL; U57485; AAB46703.1; -; Genomic_DNA.
DR EMBL; U57486; AAB46704.1; -; Genomic_DNA.
DR EMBL; U57487; AAB46705.1; -; Genomic_DNA.
DR EMBL; U57488; AAB46706.1; -; Genomic_DNA.
DR PIR; A28022; A28022.
DR PIR; A34089; A34089.
DR PIR; A40122; A40122.
DR PIR; A41426; A41426.
DR PIR; B40122; B40122.
DR PIR; B41426; B41426.
DR PIR; C41426; C41426.
DR PIR; D41426; D41426.
DR PIR; E41426; E41426.
DR PIR; F41426; F41426.
DR PIR; G41426; G41426.
DR PIR; H41426; H41426.
DR PIR; I41426; I41426.
DR RefSeq; NP_001261749.1; NM_001274820.1.
DR RefSeq; NP_788500.1; NM_176322.3.
DR PDB; 5THM; X-ray; 2.15 A; A=22-544.
DR PDBsum; 5THM; -.
DR AlphaFoldDB; P08171; -.
DR SMR; P08171; -.
DR BioGRID; 64746; 1.
DR DIP; DIP-21801N; -.
DR IntAct; P08171; 1.
DR STRING; 7227.FBpp0305575; -.
DR ESTHER; drome-este6; Carb_B_Arthropoda.
DR MEROPS; S09.947; -.
DR GlyGen; P08171; 4 sites.
DR iPTMnet; P08171; -.
DR PaxDb; P08171; -.
DR DNASU; 39392; -.
DR EnsemblMetazoa; FBtr0076003; FBpp0075735; FBgn0000592.
DR EnsemblMetazoa; FBtr0333383; FBpp0305575; FBgn0000592.
DR GeneID; 39392; -.
DR KEGG; dme:Dmel_CG6917; -.
DR CTD; 39392; -.
DR FlyBase; FBgn0000592; Est-6.
DR VEuPathDB; VectorBase:FBgn0000592; -.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000173305; -.
DR HOGENOM; CLU_006586_13_2_1; -.
DR InParanoid; P08171; -.
DR OMA; NGHENFM; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; P08171; -.
DR BioCyc; MetaCyc:MON-20460; -.
DR Reactome; R-DME-112311; Neurotransmitter clearance.
DR Reactome; R-DME-1483191; Synthesis of PC.
DR Reactome; R-DME-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Reactome; R-DME-211945; Phase I - Functionalization of compounds.
DR Reactome; R-DME-8964038; LDL clearance.
DR Reactome; R-DME-9749641; Aspirin ADME.
DR SignaLink; P08171; -.
DR BioGRID-ORCS; 39392; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39392; -.
DR PRO; PR:P08171; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000592; Expressed in head capsule and 20 other tissues.
DR ExpressionAtlas; P08171; baseline and differential.
DR Genevisible; P08171; DM.
DR GO; GO:0005576; C:extracellular region; IDA:FlyBase.
DR GO; GO:0005615; C:extracellular space; HDA:FlyBase.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:FlyBase.
DR GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR GO; GO:0017171; F:serine hydrolase activity; HDA:FlyBase.
DR GO; GO:0034338; F:short-chain carboxylesterase activity; IDA:FlyBase.
DR GO; GO:0007619; P:courtship behavior; IMP:FlyBase.
DR GO; GO:0007618; P:mating; TAS:FlyBase.
DR GO; GO:1901575; P:organic substance catabolic process; IDA:FlyBase.
DR GO; GO:0030728; P:ovulation; TAS:FlyBase.
DR GO; GO:0042811; P:pheromone biosynthetic process; IDA:FlyBase.
DR GO; GO:0046008; P:regulation of female receptivity, post-mating; TAS:FlyBase.
DR GO; GO:0046662; P:regulation of oviposition; TAS:FlyBase.
DR GO; GO:0019953; P:sexual reproduction; HEP:FlyBase.
DR GO; GO:0046693; P:sperm storage; TAS:FlyBase.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Reference proteome; Secreted; Serine esterase; Signal.
FT SIGNAL 1..21
FT CHAIN 22..544
FT /note="Esterase-6"
FT /id="PRO_0000008561"
FT ACT_SITE 209
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 466
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 86..105
FT /evidence="ECO:0000250"
FT DISULFID 261..273
FT /evidence="ECO:0000250"
FT DISULFID 514..535
FT /evidence="ECO:0000255"
FT VARIANT 10
FT /note="I -> T (in strain: 178.7, 357F, 517S, Bar-F-77F,
FT Bar-F-79F, Bar-F-96S, DPF-13, DPF-30, DPF-82.1, EM-10, F-
FT 274F, F-517F, F-1461S, MA-4.4 and Zim-F-H31)"
FT VARIANT 24
FT /note="T -> I (in strain: 178.7, 377F, 357F, 517S, Bar-F-
FT 79F, DPF-13, DPF-30, DPF-82.1, EM-10, F-274F, F-517F, F-
FT 775F, F-1461S, MA-4.4, Ven-S-13F, Zim-F-H27, Zim-F-H31,
FT Zim-F-S11, Zim-F-S18, Zim-F-S53, Zim-S-S2, Zim-S-S30 and
FT Zim-S-S34)"
FT VARIANT 33
FT /note="P -> S (in strain: Zim-S-H13)"
FT VARIANT 58
FT /note="T -> I (in strain: 178.7, 357F, 517S, Bar-F-77F,
FT Bar-F-79F, Bar-F-96S, DPF-13, DPF-30, DPF-82.1, EM-10, F-
FT 274F, F-1461S, MA-4.2, VC-805, Ven-S-1F, Ven-S-2F, Ven-S-
FT 3F, Ven-S-11F, Ven-S-21F, Zim-F-H31, Zim-F-S18 and Zim-S-
FT S10)"
FT VARIANT 120
FT /note="S -> T (in strain: DPF-2 and 521S)"
FT VARIANT 258
FT /note="N -> D (in strain: 178.7, 357F, 517S, 709.6, Bar-F-
FT 7F, Bar-F-77F, Bar-F-79F, Bar-F-93F, Bar-F-96S, DPF-13,
FT DPF-30, DPF-46, DPF-77, DPF-82.1, EM-10, F-96S, F-274F, F-
FT 517F, F-531F, F-611F, F-775F, F-1461S, MA-4.2, Zim-F-H27,
FT Zim-F-H31, Zim-F-S11, Zim-F-S18 and Zim-F-S53)"
FT VARIANT 268
FT /note="T -> A (in strain: 174F, 178.7, 357F, 517S, 709.6,
FT Bar-F-7F, Bar-F-77F, Bar-F-79F, Bar-F-93F, Bar-F-96S, Bar-
FT S-24F, Bar-S-60F, Bar-S-78F, Bar-S-89F, Bar-S-99F, Bar-S-
FT 95F, DPF-13, DPF-30, DPF-46, DPF-77, DPF-82.1, EM-10, F-
FT 96S, F-274F, F-517F, F-531F, S-549S, F-611F, F-775F, F-
FT 1461S, MA-4.2, S-114S, S-2588S, VC-815, Ven-S-1F, Ven-S-2F,
FT Ven-S-3F, Ven-S-4F, Ven-S-11F, Ven-S-21F, Zim-F-H27, Zim-F-
FT H31, Zim-F-S11, Zim-F-S18, Zim-F-S53, Zim-S-S34 and Zim-S-
FT 44F)"
FT VARIANT 276
FT /note="S -> P (in strain: VC-805)"
FT VARIANT 309
FT /note="A -> V (in strain: Ven-S-13F)"
FT VARIANT 356
FT /note="I -> T (in strain: F-775F)"
FT VARIANT 363
FT /note="E -> D (in strain: F-775F)"
FT VARIANT 371
FT /note="Y -> H (in strain: F-775F)"
FT VARIANT 376
FT /note="R -> G (in strain: Zim-S-S34)"
FT VARIANT 394
FT /note="E -> D (in strain: Ven-S-13F and Zim-F-S18)"
FT VARIANT 397
FT /note="G -> R (in strain: US-255F)"
FT VARIANT 409
FT /note="L -> V (in strain: 357F, 517S, Bar-F-7F, Bar-F-77F,
FT Bar-F-79F, Bar-F-93F, Bar-F-96S, DPF-13, DPF-30, F-96S, F-
FT 274F, F-517F, F-1461S, S-114S, S-549S, S-2588S, VC-805,
FT Ven-S-4F, Zim-S-S2, Zim-S-S30 and Zim-S-S34)"
FT VARIANT 441
FT /note="V -> I (in strain: Zim-F-S53)"
FT VARIANT 492
FT /note="R -> K (in strain: 94F, 174F, Bar-S-24F, Bar-S-89F,
FT Bar-S-99F, Bar-S-95F, Bar-S-60F, F-531F, F-611F, MA-4.2,
FT Zim-F-H27, Zim-F-S18 and Zim-S-44F)"
FT VARIANT 500
FT /note="D -> N (in strain: Zim-F-S18, Zim-S-H32 and Zim-S-
FT S2)"
FT VARIANT 508
FT /note="S -> A (in strain: 357F, 517S, Bar-F-79F, Bar-S-78F,
FT DPF-13, DPF-30, F-96S, F-517F, F-1461S, MA-4.2, VC-805,
FT Ven-S-1F, Ven-S-2F, Ven-S-3F, Ven-S-11F, Ven-S-21F and Zim-
FT F-S11)"
FT CONFLICT 519
FT /note="N -> S (in Ref. 3; AAA28517)"
FT /evidence="ECO:0000305"
FT CONFLICT 534..544
FT /note="GCQNRQHVEFP -> AARIGSMWNFRKLHE (in Ref. 3;
FT AAA28517)"
FT /evidence="ECO:0000305"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 43..52
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:5THM"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 161..165
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:5THM"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 248..258
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 279..284
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 318..322
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 361..372
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 384..389
FT /evidence="ECO:0007829|PDB:5THM"
FT TURN 394..398
FT /evidence="ECO:0007829|PDB:5THM"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 406..417
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 419..430
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 437..443
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 450..455
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:5THM"
FT TURN 466..469
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 470..473
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 477..479
FT /evidence="ECO:0007829|PDB:5THM"
FT HELIX 485..503
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 526..531
FT /evidence="ECO:0007829|PDB:5THM"
FT STRAND 534..539
FT /evidence="ECO:0007829|PDB:5THM"
SQ SEQUENCE 544 AA; 61125 MW; 5D99B80DF588F268 CRC64;
MNYVGLGLII VLSCLWLGSN ASDTDDPLLV QLPQGKLRGR DNGSYYSYES IPYAEPPTGD
LRFEAPEPYK QKWSDIFDAT KTPVACLQWD QFTPGANKLV GEEDCLTVSV YKPKNSKRNS
FPVVAHIHGG AFMFGAAWQN GHENVMREGK FILVKISYRL GPLGFVSTGD RDLPGNYGLK
DQRLALKWIK QNIASFGGEP QNVLLVGHSA GGASVHLQML REDFGQLARA AFSFSGNALD
PWVIQKGARG RAFELGRNVG CESAEDSTSL KKCLKSKPAS ELVTAVRKFL IFSYVPFAPF
SPVLEPSDAP DAIITQDPRD VIKSGKFGQV PWAVSYVTED GGYNAALLLK ERKSGIVIDD
LNERWLELAP YLLFYRDTKT KKDMDDYSRK IKQEYIGNQR FDIESYSELQ RLFTDILFKN
STQESLDLHR KYGKSPAYAY VYDNPAEKGI AQVLANRTDY DFGTVHGDDY FLIFENFVRD
VEMRPDEQII SRNFINMLAD FASSDNGSLK YGECDFKDNV GSEKFQLLAI YIDGCQNRQH
VEFP
