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Reviewed, UniProtKB/Swiss-Prot P82891 (PPAC2_DROME)

Last modified January 19, 2010. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Low molecular weight phosphotyrosine protein phosphatase 2
    EC=3.1.3.48
Alternative name(s):
    Low molecular weight cytosolic acid phosphatase 2
    EC=3.1.3.2
    PTPase 2
Gene names
Name: primo-2
ORF Names: CG31311
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length164 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates By similarity.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

A phosphate monoester + H2O = an alcohol + phosphate.

Subcellular location

Cytoplasm.

Tissue specificity

Cone cells and primary pigment cells in developing pupal retina. Ref.1

Developmental stage

Embryo and adult. Ref.1

Sequence similarities

Belongs to the low molecular weight phosphotyrosine protein phosphatase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processprotein amino acid dephosphorylation

Non-traceable author statement. Source: FlyBase

   Cellular componentcytoplasm

Non-traceable author statement. Source: FlyBase

   Molecular functionacid phosphatase activity

Inferred from electronic annotation. Source: EC

non-membrane spanning protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 164164Low molecular weight phosphotyrosine protein phosphatase 2
PRO_0000046563

Sites

Active site141Nucleophile By similarity
Active site201 By similarity
Active site1301Proton donor By similarity

Experimental info

Mutagenesis141C → S: Complete loss of activity. Ref.1
Sequence conflict311L → V Ref.1
Sequence conflict1111A → V Ref.1

Sequences

Sequence LengthMass (Da)Tools
P82891-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 320485DF557E4CCD

FASTA16418,541
        10         20         30         40         50         60 
MGKRSQKSSV LMVCVGNLCR SPIAEAVMRD LVARAGLQGE WHVESAGIED WHSGHQPDER 

        70         80         90        100        110        120 
ALNVLARHNI EYNGKARVLA PEDFLEFDYI FAMDLSNLAA LRRMAPKGTT AKLLILGNFG 

       130        140        150        160 
LKPDERIIED PYYDIGEASF EEIYRQCSIA CRNFLKQARL KQIM 

« Hide

References

« Hide 'large scale' references
[1]"The Drosophila primo locus encodes two low-molecular-weight tyrosine phosphatases."
Miller D.T., Read R., Rusconi J., Cagan R.L.
Gene 243:1-9(2000) [PubMed: 10675607] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF CYS-14, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Embryo and Pupae.
[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: 10731132] [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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Testis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014297 Genomic DNA. Translation: AAN13590.2.
AY089477 mRNA. Translation: AAL90215.1.
RefSeqNP_001027188.1.
NP_001027189.1.
UniGeneDm.4988

3D structure databases

SMRP82891. Positions 9-157.
ModBaseSearch...

Proteomic databases

PRIDEP82891.

Genome annotation databases

EnsemblFBtr0091745; FBpp0100063; FBgn0040076; Drosophila melanogaster. [Genome view]
FBtr0091746; FBpp0100064; FBgn0040076; Drosophila melanogaster. [Genome view]
GeneID3772427.
KEGGdme:Dmel_CG33747.
UCSCCG33747-RB. d. melanogaster.

Organism-specific databases

CTD3772427.
FlyBaseFBgn0040076. primo-2.

Phylogenomic databases

eggNOGinNOG10293.
InParanoidP82891.
OMAATSGWEH.
OrthoDBEOG9V43FB.
PhylomeDBP82891.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-011492-MONOMER.
DMEL-XXX-02:DMEL-XXX-02-011494-MONOMER.
BRENDA3.1.3.2. 48.
3.1.3.48. 48.

Gene expression databases

GermOnlineCG33747. Drosophila melanogaster.

Family and domain databases

InterProIPR002115. Tyr_Pase_low_mol_wt_mml.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERPTHR11717. Low_mwt_PTPase. 1 hit.
PfamPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSPR00719. LMWPTPASE.
PR00720. MAMMALPTPASE.
SMARTSM00226. LMWPc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio853692.

Entry information

Entry namePPAC2_DROME
AccessionPrimary (citable) accession number: P82891
Secondary accession number(s): Q0KI75, Q9VFR9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: March 1, 2001
Last modified: January 19, 2010
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents