ID   EST5A_DROPE             Reviewed;         548 AA.
AC   O16173;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Esterase-5A;
DE            Short=Est-5A;
DE            EC=3.1.1.1;
DE   AltName: Full=Carboxylic-ester hydrolase 5A;
DE            Short=Carboxylesterase-5A;
DE   Flags: Precursor;
GN   Name=Est-5A; Synonyms=Est5A;
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9475741; DOI=10.1093/genetics/148.1.305;
RA   King L.M.;
RT   "The role of gene conversion in determining sequence variation and
RT   divergence in the Est-5 gene family in Drosophila pseudoobscura.";
RL   Genetics 148:305-315(1998).
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AF016111; AAB70224.1; -; Genomic_DNA.
DR   AlphaFoldDB; O16173; -.
DR   SMR; O16173; -.
DR   STRING; 7234.FBpp0189270; -.
DR   ESTHER; drope-est5a; Carb_B_Arthropoda.
DR   MEROPS; S09.947; -.
DR   eggNOG; KOG1516; Eukaryota.
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   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:0000255"
FT   CHAIN           20..548
FT                   /note="Esterase-5A"
FT                   /id="PRO_0000008553"
FT   ACT_SITE        210
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        479
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        87..106
FT                   /evidence="ECO:0000250"
FT   DISULFID        262..274
FT                   /evidence="ECO:0000250"
FT   DISULFID        518..539
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   548 AA;  61556 MW;  D10ED7A9223BC60D CRC64;
     MHLVRWLICL IQLWIQLGAA GSVTLLDPLL IEIPNGKLRG RDNGHYYSYE AIPYAEPPTG
     ELRFEVPKPY KQQWTNTFDA TQPPVLCMQW NQFINGTNKL LGVEDCLTVS VYRPKNSSRN
     NFPVVANLHG GAFMFGGPSQ YGHENIMREG SVILVTIGYR LGPLGFVSTG DADLSGNFGL
     KDQRLALLWI KQNIASFGGE PENILVVGHS AGGASVHLQM LREDFSKVAK AAISFSGNSL
     DPWVIQQGLR GRAFELGRIV GCGQASDSVT LKKCLKSKPA IEIVSAVRSF LVFSYVPFTP
     FGPAIESPDA PEAFITHHPI DIIKRGKFSQ VPWAVTYTTE DGGYNAALLL EKQASSGREL
     IVDLNDRWFD WAPYLLFYRD SMTTIKDMDD YSRKLRQEYL GDRRFSVESY WDVQRMFTDL
     LFKNSVTVSV DLHRKYGKSP VYAFVYDNPS EVGVGQILSG RNDVYFGTVH GDDVFLIFNV
     SFVPANRRPD EEIISRNFIK MLEYFALSTD DTMAYGDCVF QNNVGSKHMQ LLSITRDGCE
     NKQLNFFI