ESTS_DROVI
ID ESTS_DROVI Reviewed; 542 AA.
AC Q05487;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Esterase S;
DE Short=Est-S;
DE EC=3.1.1.1;
DE AltName: Full=Carboxylic-ester hydrolase S;
DE Short=Carboxylesterase-S;
DE Flags: Precursor;
GN Name=EstS;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2783177;
RA Sergeev P.V., Castillo J.E., Peunova N.I., Yenikolopov G.N.;
RT "Primary structure of the esterase s gene from Drosophila virilis.";
RL Bioorg. Khim. 15:839-843(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8346032; DOI=10.1093/nar/21.15.3545;
RA Sergeev P.V., Yenikolopov G.N., Peunova N.I., Kuzin B.A., Khechumian R.A.,
RA Korochkin L.I., Georgiev G.P.;
RT "Regulation of tissue-specific expression of the esterase S gene in
RT Drosophila virilis.";
RL Nucleic Acids Res. 21:3545-3551(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 -!- TISSUE SPECIFICITY: Specifically expressed in the ejaculatory bulbs of
CC male.
CC -!- DEVELOPMENTAL STAGE: In the male, it appears 3 days after emergence in
CC the imago stage and reaches maximum levels by the 10th day.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; X70351; CAA49809.1; -; Genomic_DNA.
DR PIR; JN0438; JN0438.
DR AlphaFoldDB; Q05487; -.
DR SMR; Q05487; -.
DR STRING; 7244.FBpp0224488; -.
DR ESTHER; drovi-estes; 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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Secreted; Serine esterase; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..542
FT /note="Esterase S"
FT /id="PRO_0000008565"
FT ACT_SITE 204
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 81..100
FT /evidence="ECO:0000250"
FT DISULFID 256..268
FT /evidence="ECO:0000250"
FT DISULFID 507..528
FT /evidence="ECO:0000255"
SQ SEQUENCE 542 AA; 61070 MW; 9134648A7B573F84 CRC64;
MTQILLPIAL LCLFAASTLS NPLLVELPNG ELRGRDNGFY YSYESIPYAE PPIDDLCLEE
PRPYTERWEN TFDATRPPVD CLQWSQLISQ PNKLTGSEDC LTVSIYKPKN LTRISFPVVA
HIFGGGWSFG AAIDDGVRPF SSSGNVIVVK TTTEWERLGF MSTGDSVIPG NFGLKDQRLA
IKWIRNNIAR FGGDPHNIIL LGFSTGGSSV HLQLMHKEYG QLVKGAISIS GTATVPWAVQ
ANARDLAFRY GKLLGCNNPK NSRELKDCLK KTDAEEFVST LRHLQVFDYV PFGPFGPVVE
SPEVESPFLT ELPLDTIRSG NFAQVPWLAS YTPENGIYNA ALLLAKDANG KERIEELNTR
WNELAPYFLA YPYTLKRSEM NAHSQKLKYQ YLGYKNFSVV NYFDVQRLFT NELYKKGIEL
SLDSHRKHGA SPVYAYVYDN PADKSLAQFL AKRSDISLGT GMGDDYYLLM NNPLREPLRA
DEKIVSWKLV KMVEDFAAHE TLVYDDCVFP NNLGKKKFQL VVIGRNYCKQ LEVESFARHG
VQ