ID   EST6_DROSI              Reviewed;         542 AA.
AC   Q08662;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 92.
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;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8375665; DOI=10.1007/bf02424448;
RA   Karotam J., Delves A.C., Oakeshott J.G.;
RT   "Conservation and change in structural and 5' flanking sequences of
RT   esterase 6 in sibling Drosophila species.";
RL   Genetica 88:11-28(1993).
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   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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; L10670; AAA18250.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q08662; -.
DR   SMR; Q08662; -.
DR   ESTHER; drosi-este6; Carb_B_Arthropoda.
DR   MEROPS; S09.947; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034338; F:short-chain carboxylesterase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0007619; P:courtship behavior; IEA:EnsemblMetazoa.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:EnsemblMetazoa.
DR   GO; GO:0042811; P:pheromone biosynthetic process; IEA:EnsemblMetazoa.
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   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Hydrolase; Secreted; Serine esterase; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..542
FT                   /note="Esterase 6"
FT                   /id="PRO_0000008564"
FT   ACT_SITE        207
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        464
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        418
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        454
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        84..103
FT                   /evidence="ECO:0000250"
FT   DISULFID        259..271
FT                   /evidence="ECO:0000250"
FT   DISULFID        512..533
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   542 AA;  60831 MW;  F3AF3016C3770680 CRC64;
     MNYVGLIIVL SCLWLGSNAS DPDDPLLVQL PQGKLRGRDN GSYYSYESIP YAEPPTGDLR
     FEAPEPYKQK WSDIFDATKT PVACLQWDQF TPGANKLVGE EDCLTVSIYK PKNSKRSTFP
     VVAHIHGGAF MFGAAWQNGH ENVMREGKFI LVKISYRLGP LGFASTGDRD LPGNYGLKDQ
     RLALKWIKQN IASFGGEPQN VLLIGHSAGG ASVHLQMLRE DFGQLAKAAF SFSGNALDPW
     VVQKGARGRA FELGRNVGCE SAEDSASLKK CLKSKSASEL VTAVRKFLIF SYVPFAPFSP
     VLEPSDAPDA ILTQDPREVI KSGKFGQVPW AVSYVTEDGG YNAALLLKER KSGIVIDDLN
     DRWLELAPYF LFYRDTKTKK DMDDYSRKIK EDYLGNQKFD IESYSELQRL FTDILFKNST
     QESLDLHRKY GKSPAYAYVY DNPAEKGIAQ VLANRTDYDF GTVHGDDYFL IFENFVREVE
     MRPDEEIISR NFINMLADFA SSDNGVLKYG ECAFKNNVGS EKFQLLAIYI DGCQNRQHVE
     FP