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ESTP_DROME
ID   ESTP_DROME              Reviewed;         544 AA.
AC   P18167; Q32KD6; Q9VTV0;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Esterase P;
DE            Short=Est-P;
DE            EC=3.1.1.1;
DE   AltName: Full=Carboxylic-ester hydrolase P;
DE            Short=Carboxylesterase-P;
DE   Flags: Precursor;
GN   Name=Est-P; Synonyms=EstP; ORFNames=CG17148;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Canton-S;
RX   PubMed=2105433; DOI=10.1093/oxfordjournals.molbev.a040582;
RA   Collet C., Nielsen K.M., Russell R.J., Karl M., Oakeshott J.G.,
RA   Richmond R.C.;
RT   "Molecular analysis of duplicated esterase genes in Drosophila
RT   melanogaster.";
RL   Mol. Biol. Evol. 7:9-28(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- DEVELOPMENTAL STAGE: Mainly in late larvae.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; M33780; AAA28520.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAF49945.1; -; Genomic_DNA.
DR   EMBL; BT023943; ABB36447.1; -; mRNA.
DR   PIR; B34089; B34089.
DR   RefSeq; NP_788501.1; NM_176323.2.
DR   AlphaFoldDB; P18167; -.
DR   SMR; P18167; -.
DR   IntAct; P18167; 1.
DR   STRING; 7227.FBpp0075736; -.
DR   ESTHER; drome-est6p; Carb_B_Arthropoda.
DR   GlyGen; P18167; 4 sites.
DR   PaxDb; P18167; -.
DR   DNASU; 39393; -.
DR   EnsemblMetazoa; FBtr0076004; FBpp0075736; FBgn0000594.
DR   GeneID; 39393; -.
DR   KEGG; dme:Dmel_CG17148; -.
DR   CTD; 39393; -.
DR   FlyBase; FBgn0000594; Est-P.
DR   VEuPathDB; VectorBase:FBgn0000594; -.
DR   eggNOG; KOG1516; Eukaryota.
DR   GeneTree; ENSGT00940000173305; -.
DR   HOGENOM; CLU_006586_13_2_1; -.
DR   InParanoid; P18167; -.
DR   OMA; WIDLLND; -.
DR   OrthoDB; 754103at2759; -.
DR   PhylomeDB; P18167; -.
DR   Reactome; R-DME-112311; Neurotransmitter clearance.
DR   Reactome; R-DME-1483191; Synthesis of PC.
DR   Reactome; R-DME-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR   Reactome; R-DME-211945; Phase I - Functionalization of compounds.
DR   Reactome; R-DME-8964038; LDL clearance.
DR   Reactome; R-DME-9749641; Aspirin ADME.
DR   BioGRID-ORCS; 39393; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 39393; -.
DR   PRO; PR:P18167; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0000594; Expressed in saliva-secreting gland and 8 other tissues.
DR   Genevisible; P18167; DM.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:FlyBase.
DR   GO; GO:0080030; F:methyl indole-3-acetate esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017171; F:serine hydrolase activity; HDA:FlyBase.
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; Reference proteome; Secreted;
KW   Serine esterase; Signal.
FT   SIGNAL          1..19
FT   CHAIN           20..544
FT                   /note="Esterase P"
FT                   /id="PRO_0000008562"
FT   ACT_SITE        206
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        466
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        456
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        83..102
FT                   /evidence="ECO:0000250"
FT   DISULFID        258..270
FT                   /evidence="ECO:0000250"
FT   DISULFID        514..535
FT                   /evidence="ECO:0000255"
FT   CONFLICT        50
FT                   /note="N -> Y (in Ref. 1; AAA28520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155..156
FT                   /note="FG -> YR (in Ref. 1; AAA28520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        481
FT                   /note="T -> I (in Ref. 1; AAA28520)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   544 AA;  61054 MW;  835FE81D94B46623 CRC64;
     MSIFKRLLCL TLLWIAALES EADPLIVEIT NGKIRGKDNG LYYSYESIPN AEHPTGALRF
     EAPQPYSHHW TDVFNATQSP VECMQWNQFI NENNKLMGDE DCLTVSIYKP KKPNRSSFPV
     VVLLHGGAFM FGSGSIYGHD SIMREGTLLV VKISFGLGPL GFASTGDRHL PGNYGLKDQR
     LALQWIKKNI AHFGGMPDNI VLIGHSAGGA SAHLQLLHED FKHLAKGAIS VSGNALDPWV
     IQQGGRRRAF ELGRIVGCGH TNVSAELKDC LKSKPASDIV SAVRSFLVFS YVPFSAFGPV
     VEPSDAPDAF LTEDPRAVIK SGKFAQVPWA VTYTTEDGGY NAAQLLERNK LTGESWIDLL
     NDRWFDWAPY LLFYRDAKKT IKDMDDLSFD LRQQYLADRR FSVESYWNVQ RMFTDVLFKN
     SVPSAIDLHR KYGKSPVYSF VYDNPTDSGV GQLLSNRTDV HFGTVHGDDF FLIFNTAAYR
     TGIRPDEEVI SKKFIGMLED FALNDKGTLT FGECNFQNNV NSKEYQVLRI SRNACKNEEY
     ARFP
 
 
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