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Q86BN8

- PTPM1_DROME

UniProt

Q86BN8 - PTPM1_DROME

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Protein
Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1
Gene
Plip, CG10371
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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 activityi

Phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate.
Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei141 – 1411Phosphocysteine intermediate By similarity

GO - Molecular functioni

  1. phosphatidylglycerophosphatase activity Source: UniProtKB-EC
  2. phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Source: RefGenome
  3. protein tyrosine phosphatase activity Source: UniProtKB-EC
  4. protein tyrosine/serine/threonine phosphatase activity Source: FlyBase

GO - Biological processi

  1. ATP catabolic process Source: FlyBase
  2. inositol phosphate dephosphorylation Source: RefGenome
  3. neurogenesis Source: FlyBase
  4. phosphatidylglycerol biosynthetic process Source: UniProtKB-UniPathway
  5. protein dephosphorylation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

ReactomeiREACT_180833. Synthesis of PG.
UniPathwayiUPA00084; UER00504.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Plip
ORF Names:CG10371
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0039111. Plip.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2828Mitochondrion Reviewed prediction
Add
BLAST
Chaini29 – 200172Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1
PRO_0000025426Add
BLAST

Proteomic databases

PaxDbiQ86BN8.
PRIDEiQ86BN8.

Expressioni

Tissue specificityi

Highly enriched in testis.1 Publication

Gene expression databases

BgeeiQ86BN8.

Interactioni

Protein-protein interaction databases

BioGridi67745. 2 interactions.
MINTiMINT-318143.

Structurei

3D structure databases

ProteinModelPortaliQ86BN8.
SMRiQ86BN8. Positions 31-192.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini103 – 18684Tyrosine-protein phosphatase
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG146651.
GeneTreeiENSGT00390000014065.
InParanoidiQ86BN8.
KOiK14165.
OMAiNSSQEWK.
OrthoDBiEOG7KDFCN.
PhylomeDBiQ86BN8.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform B (identifier: Q86BN8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MEMSAAMFAR VSFYPTLLYN VLMEKASARN WYDRIDEHVI LGALPFRSQA    50
NDLIEKENMK AVVSMNEDYE LTAFSNNTEK WRKLGIEFLQ LATTDIFESP 100
NQEKLFRGVE FINKFLPLKQ RIGGLSSSYQ PENVGSVYVH CKAGRTRSAT 150
LVGCYLMMKN GWTPDQAVDH MRKCRPHILL HTKQWDALRL FYTNNVETKS 200
Length:200
Mass (Da):23,156
Last modified:June 1, 2003 - v1
Checksum:iE7B4B6A69CB1CFCD
GO
Isoform A (identifier: Q86BN8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: Missing.

Note: No experimental confirmation available.

Show »
Length:194
Mass (Da):22,535
Checksum:i7C1D7F373CFF2EA7
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 66Missing in isoform A.
VSP_015010

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti186 – 1861D → G in AAL48664. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: AAF56179.1.
AE014297 Genomic DNA. Translation: AAN13956.2.
AY071042 mRNA. Translation: AAL48664.1.
RefSeqiNP_651180.3. NM_142923.3. [Q86BN8-1]
NP_732901.1. NM_170090.2. [Q86BN8-2]
UniGeneiDm.20236.

Genome annotation databases

EnsemblMetazoaiFBtr0084453; FBpp0083844; FBgn0039111. [Q86BN8-1]
GeneIDi42807.
KEGGidme:Dmel_CG10371.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: AAF56179.1 .
AE014297 Genomic DNA. Translation: AAN13956.2 .
AY071042 mRNA. Translation: AAL48664.1 .
RefSeqi NP_651180.3. NM_142923.3. [Q86BN8-1 ]
NP_732901.1. NM_170090.2. [Q86BN8-2 ]
UniGenei Dm.20236.

3D structure databases

ProteinModelPortali Q86BN8.
SMRi Q86BN8. Positions 31-192.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 67745. 2 interactions.
MINTi MINT-318143.

Proteomic databases

PaxDbi Q86BN8.
PRIDEi Q86BN8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0084453 ; FBpp0083844 ; FBgn0039111 . [Q86BN8-1 ]
GeneIDi 42807.
KEGGi dme:Dmel_CG10371.

Organism-specific databases

CTDi 42807.
FlyBasei FBgn0039111. Plip.

Phylogenomic databases

eggNOGi NOG146651.
GeneTreei ENSGT00390000014065.
InParanoidi Q86BN8.
KOi K14165.
OMAi NSSQEWK.
OrthoDBi EOG7KDFCN.
PhylomeDBi Q86BN8.

Enzyme and pathway databases

UniPathwayi UPA00084 ; UER00504 .
Reactomei REACT_180833. Synthesis of PG.

Miscellaneous databases

ChiTaRSi KAT5. drosophila.
GenomeRNAii 42807.
NextBioi 830670.
PROi Q86BN8.

Gene expression databases

Bgeei Q86BN8.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR000340. Dual-sp_phosphatase_cat-dom.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00782. DSPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  3. 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.

Entry informationi

Entry nameiPTPM1_DROME
AccessioniPrimary (citable) accession number: Q86BN8
Secondary accession number(s): Q8SZ90, Q9VCI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2003
Last modified: September 3, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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