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EST6_DROMA
ID   EST6_DROMA              Reviewed;         542 AA.
AC   P47982; Q670K3; Q9GNC2; Q9GQA4; Q9GQA5; Q9GQA6;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 84.
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 mauritiana (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7226;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Balakirev E.S., Chechetkin V.R., Lobzin V.V., Ayala F.J.;
RT   "Entropy and GC content in the b-esterase gene cluster of Drosophila
RT   melanogaster subgroup.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-532.
RC   STRAIN=105, 152, 197, 207, Lig72, and Lig74;
RX   PubMed=11102384; DOI=10.1093/genetics/156.4.1913;
RA   Kliman R.M., Andolfatto P., Coyne J.A., Depaulis F., Kreitman M.,
RA   Berry A.J., McCarter J., Wakeley J., Hey J.;
RT   "The population genetics of the origin and divergence of the Drosophila
RT   simulans complex species.";
RL   Genetics 156:1913-1931(2000).
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}.
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DR   EMBL; L10671; AAA03158.1; -; Genomic_DNA.
DR   EMBL; AY695921; AAU05619.1; -; Genomic_DNA.
DR   EMBL; AF284482; AAG28715.1; -; Genomic_DNA.
DR   EMBL; AF284483; AAG28716.1; -; Genomic_DNA.
DR   EMBL; AF284484; AAG28717.1; -; Genomic_DNA.
DR   EMBL; AF284485; AAG28718.1; -; Genomic_DNA.
DR   EMBL; AF284486; AAG28719.1; -; Genomic_DNA.
DR   EMBL; AF284487; AAG28720.1; -; Genomic_DNA.
DR   AlphaFoldDB; P47982; -.
DR   SMR; P47982; -.
DR   ESTHER; droma-este6; Carb_B_Arthropoda.
DR   MEROPS; S09.947; -.
DR   FlyBase; FBgn0012501; Dmau\Est-6.
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..542
FT                   /note="Esterase 6"
FT                   /id="PRO_0000008563"
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"
FT   VARIANT         56
FT                   /note="I -> T (in strain: 197)"
FT   VARIANT         199..201
FT                   /note="ENI -> QNV (in strain: 197)"
FT   VARIANT         302
FT                   /note="L -> M (in strain: Lig72)"
FT   VARIANT         355
FT                   /note="A -> S (in strain: Lig74)"
FT   VARIANT         391
FT                   /note="E -> Q (in strain: Lig74)"
FT   VARIANT         394
FT                   /note="L -> I (in strain: Lig74)"
FT   VARIANT         494
FT                   /note="N -> K (in strain: 197)"
FT   VARIANT         496
FT                   /note="L -> M (in strain: Lig72)"
SQ   SEQUENCE   542 AA;  60890 MW;  3E7ED31DA51E12F1 CRC64;
     MNYVGLIIVL SCLWLGSNAS DPDDPLLVQL PQGKLRGRDN GSYYSYESIP YAEPPIGDLR
     FEAPEPYKQK WSDIFEATKT PVACLQWDQF TPGANKLVGE EDCLTVSIYK PKNSKRSSFP
     VVAHIHGGAF MFGAAWQNGH ENVMREGKFI LVKISYRLGP LGFASTGDRD LPGNYGLKDQ
     RLALKWIKQN IASFGGEPEN ILLIGHSAGG ASVHLQMLRE DFGQLAKAAF SFSGNALDPW
     VVQKGARGRA FELGRNVGCE SSEDSASLKK CLKSKPASEL VTAVRKFLIF SYVPFAPFSP
     VLEPSDAPDA FLTQDPREVI KSGKFGQVPW AVSYVTEDGG YNAALLLKER KSGIAIDDLN
     DRWLELAPYF LFYRDTKTKK DMDDYSRKIK EDYLGNQKFD IESYSELQRL FTDILFKNST
     QESLDLHRKY GKSPAYAYVY DNPAEKGIAQ VLANRTDYDF GTVHGDDYFL IFENFVREVE
     MRPDEEIISR NFINMLADFA SSDNGVLKYG ECAFKNNVGS EKFQLLAIYI DGCQNRQHVE
     FP
 
 
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