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Q86BN8 (PTPM1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1

EC=3.1.3.27
Alternative name(s):
PTEN-like protein
Protein-tyrosine phosphatase mitochondrial 1-like protein
EC=3.1.3.16
EC=3.1.3.48
Gene names
Name:Plip
ORF Names:CG10371
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Lipid phosphatase that may mediate dephosphorylation of mitochondrial proteins By similarity. Protein phosphatase that may mediate dephosphorylation of mitochondrial proteins By similarity. Does not dephosphorylate Akt.

Catalytic activity

Phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate.

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Pathway

Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.

Subcellular location

Mitochondrion inner membrane By similarity.

Tissue specificity

Highly enriched in testis. Ref.4

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: Q86BN8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform A (identifier: Q86BN8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion Potential
Chain29 – 200172Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1
PRO_0000025426

Regions

Domain103 – 18684Tyrosine-protein phosphatase

Sites

Active site1411Phosphocysteine intermediate By similarity

Natural variations

Alternative sequence1 – 66Missing in isoform A.
VSP_015010

Experimental info

Sequence conflict1861D → G in AAL48664. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform B [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: E7B4B6A69CB1CFCD

FASTA20023,156
        10         20         30         40         50         60 
MEMSAAMFAR VSFYPTLLYN VLMEKASARN WYDRIDEHVI LGALPFRSQA NDLIEKENMK 

        70         80         90        100        110        120 
AVVSMNEDYE LTAFSNNTEK WRKLGIEFLQ LATTDIFESP NQEKLFRGVE FINKFLPLKQ 

       130        140        150        160        170        180 
RIGGLSSSYQ PENVGSVYVH CKAGRTRSAT LVGCYLMMKN GWTPDQAVDH MRKCRPHILL 

       190        200 
HTKQWDALRL FYTNNVETKS 

« Hide

Isoform A [UniParc].

Checksum: 7C1D7F373CFF2EA7
Show »

FASTA19422,535

References

« Hide 'large scale' references
[1]"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.
[2]"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, ALTERNATIVE SPLICING.
Strain: Berkeley.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
Strain: Berkeley.
Tissue: Embryo.
[4]"A PTEN-like phosphatase with a novel substrate specificity."
Pagliarini D.J., Worby C.A., Dixon J.E.
J. Biol. Chem. 279:38590-38596(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: LACK OF ACTIVITY TOWARD AKT, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014297 Genomic DNA. Translation: AAF56179.1.
AE014297 Genomic DNA. Translation: AAN13956.2.
AY071042 mRNA. Translation: AAL48664.1.
RefSeqNP_651180.3. NM_142923.3.
NP_732901.1. NM_170090.2.
UniGeneDm.20236.

3D structure databases

ProteinModelPortalQ86BN8.
SMRQ86BN8. Positions 31-192.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid67745. 2 interactions.
MINTMINT-318143.

Proteomic databases

PaxDbQ86BN8.
PRIDEQ86BN8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0084453; FBpp0083844; FBgn0039111.
GeneID42807.
KEGGdme:Dmel_CG10371.

Organism-specific databases

CTD42807.
FlyBaseFBgn0039111. Plip.

Phylogenomic databases

eggNOGNOG146651.
GeneTreeENSGT00390000014065.
InParanoidQ86BN8.
KOK14165.
OMANSSQEWK.
OrthoDBEOG7KDFCN.
PhylomeDBQ86BN8.

Enzyme and pathway databases

UniPathwayUPA00084; UER00504.

Gene expression databases

BgeeQ86BN8.

Family and domain databases

InterProIPR000340. Dual-sp_phosphatase_cat-dom.
IPR024950. DUSP.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKAT5. drosophila.
GenomeRNAi42807.
NextBio830670.
PROQ86BN8.

Entry information

Entry namePTPM1_DROME
AccessionPrimary (citable) accession number: Q86BN8
Secondary accession number(s): Q8SZ90, Q9VCI6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

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