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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
 
 
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