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P18167 (ESTP_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Esterase P
Short name=Est-P
EC=3.1.1.1
Alternative name(s):
Carboxylic-ester hydrolase P
Short name=Carboxylesterase-P
Gene names
Name:Est-P
Synonyms:EstP
ORF Names:CG17148
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›

Protein attributes

Sequence length544 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

A carboxylic ester + H2O = an alcohol + a carboxylate.

Subunit structure

Monomer.

Subcellular location

Secreted.

Developmental stage

Mainly in late larvae.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Chain20 – 544525Esterase P
PRO_0000008562

Sites

Active site2061Acyl-ester intermediate By similarity
Active site4661Charge relay system By similarity

Amino acid modifications

Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation1141N-linked (GlcNAc...) Potential
Glycosylation2621N-linked (GlcNAc...) Potential
Glycosylation4561N-linked (GlcNAc...) Potential
Disulfide bond83 ↔ 102 By similarity
Disulfide bond258 ↔ 270 By similarity
Disulfide bond514 ↔ 535 Potential

Experimental info

Sequence conflict501N → Y in AAA28520. Ref.1
Sequence conflict155 – 1562FG → YR in AAA28520. Ref.1
Sequence conflict4811T → I in AAA28520. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P18167 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: 835FE81D94B46623

FASTA54461,054
        10         20         30         40         50         60 
MSIFKRLLCL TLLWIAALES EADPLIVEIT NGKIRGKDNG LYYSYESIPN AEHPTGALRF 

        70         80         90        100        110        120 
EAPQPYSHHW TDVFNATQSP VECMQWNQFI NENNKLMGDE DCLTVSIYKP KKPNRSSFPV 

       130        140        150        160        170        180 
VVLLHGGAFM FGSGSIYGHD SIMREGTLLV VKISFGLGPL GFASTGDRHL PGNYGLKDQR 

       190        200        210        220        230        240 
LALQWIKKNI AHFGGMPDNI VLIGHSAGGA SAHLQLLHED FKHLAKGAIS VSGNALDPWV 

       250        260        270        280        290        300 
IQQGGRRRAF ELGRIVGCGH TNVSAELKDC LKSKPASDIV SAVRSFLVFS YVPFSAFGPV 

       310        320        330        340        350        360 
VEPSDAPDAF LTEDPRAVIK SGKFAQVPWA VTYTTEDGGY NAAQLLERNK LTGESWIDLL 

       370        380        390        400        410        420 
NDRWFDWAPY LLFYRDAKKT IKDMDDLSFD LRQQYLADRR FSVESYWNVQ RMFTDVLFKN 

       430        440        450        460        470        480 
SVPSAIDLHR KYGKSPVYSF VYDNPTDSGV GQLLSNRTDV HFGTVHGDDF FLIFNTAAYR 

       490        500        510        520        530        540 
TGIRPDEEVI SKKFIGMLED FALNDKGTLT FGECNFQNNV NSKEYQVLRI SRNACKNEEY 


ARFP

« Hide

References

« Hide 'large scale' references
[1]"Molecular analysis of duplicated esterase genes in Drosophila melanogaster."
Collet C., Nielsen K.M., Russell R.J., Karl M., Oakeshott J.G., Richmond R.C.
Mol. Biol. Evol. 7:9-28(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Canton-S.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Larva and Pupae.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M33780 Genomic DNA. Translation: AAA28520.1.
AE014296 Genomic DNA. Translation: AAF49945.1.
BT023943 mRNA. Translation: ABB36447.1.
PIRB34089.
RefSeqNP_788501.1. NM_176323.2.
UniGeneDm.31153.

3D structure databases

ProteinModelPortalP18167.
SMRP18167. Positions 23-502.
ModBaseSearch...

Proteomic databases

PRIDEP18167.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0076004; FBpp0075736; FBgn0000594.
GeneID39393.
KEGGdme:Dmel_CG17148.

Organism-specific databases

CTD39393.
FlyBaseFBgn0000594. Est-P.

Phylogenomic databases

eggNOGCOG2272.
GeneTreeENSGT00700000104419.
InParanoidP18167.
KOK01044.
OMAPRNATER.
OrthoDBEOG4DBRVQ.
PhylomeDBP18167.

Gene expression databases

BgeeP18167.
GermOnlineCG17148. Drosophila melanogaster.

Family and domain databases

InterProIPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamPF00135. COesterase. 1 hit.
[Graphical view]
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi39393.
NextBio813419.

Entry information

Entry nameESTP_DROME
AccessionPrimary (citable) accession number: P18167
Secondary accession number(s): Q32KD6, Q9VTV0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: June 21, 2005
Last modified: May 1, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents