ID   EST5C_DROMI             Reviewed;         545 AA.
AC   O16169;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Esterase-5C;
DE            Short=Est-5C;
DE            EC=3.1.1.1;
DE   AltName: Full=Carboxylic-ester hydrolase 5C;
DE            Short=Carboxylesterase-5C;
DE   Flags: Precursor;
GN   Name=Est-5C; Synonyms=Est5C;
OS   Drosophila miranda (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7229;
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; AF016109; AAB70220.1; -; Genomic_DNA.
DR   AlphaFoldDB; O16169; -.
DR   SMR; O16169; -.
DR   ESTHER; dromi-est5c; Carb_B_Arthropoda.
DR   MEROPS; S09.947; -.
DR   PRIDE; O16169; -.
DR   FlyBase; FBgn0021336; Dmir\Est-5C.
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..545
FT                   /note="Esterase-5C"
FT                   /id="PRO_0000008558"
FT   ACT_SITE        207
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        467
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        421
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        507
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        515..536
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   545 AA;  60929 MW;  E4676ABBFACD9AFB CRC64;
     MLAARLIILL SFYWLSASAI DPADPLFVDL PHGKIRGRDN GFYYSYESLP YAEPPVGELR
     FEAPQPYKQQ WTDTFDATQP PVTCMQWNQF IFGDNKLAGV EDCLTVSIYK PKNTSQSSFP
     VVAHMHGGAF MFGEARQNGH ENMMREGKLI LVKISYRLGP LGFASTGDAG LSGNFGLKDQ
     RLALLWIKQN IASFGGEPEN IIVVGHSAGG ASVHLQMLRE DFAQVAKAGI SFGGNAMDPW
     VIHRSARGRT FELGRIVGCG QASDSMELKN CLKSKPAGEI VSAVHSFLVF AYVPFAPFGP
     VVESPDAPEA FISQHPVDII KSGKFAQVPW AVTYNTEDGG YNAAVLLEKQ ASSGRELIFD
     LNDHWFDWAP YLLFYRDSMT TIKDMDDYSR KLRQEYLGDR RFSVESYWDL QRLFTDVLYK
     NATELALDLY RKHGKSPVYA FVYDNPANTG IGQFFAKRTD VHFGTVHGDE YFLIFENLAR
     GPEMRSDEEI ISRNFLNMIN DFVLSGNGTM TFGNCVLQDN VGSNKLQLLS ITKNGCENLQ
     LESFP