Q86BN8 (PTPM1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Plip
ORF Names:	CG10371

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	200 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 phosphoprotein + H2O = a protein + 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.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from mutant phenotype PubMed 21304887. Source: FlyBase inositol phosphate dephosphorylation Inferred from Biological aspect of Ancestor. Source: RefGenome neurogenesis Inferred from mutant phenotype PubMed 21549331. Source: FlyBase peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC phosphatidylglycerol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phosphatidylglycerophosphatase activity Inferred from electronic annotation. Source: EC phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC protein tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 28	28	Mitochondrion Potential
	Chain	29 – 200	172	Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1		PRO_0000025426
Regions
	Domain	103 – 186	84	Tyrosine-protein phosphatase
Sites
	Active site	141	1	Phosphocysteine intermediate By similarity
Natural variations
	Alternative sequence	1 – 6	6	Missing in isoform A.		VSP_015010
Experimental info
	Sequence conflict	186	1	D → G in AAL48664. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform B [UniParc]. Last modified June 1, 2003. Version 1. Checksum: E7B4B6A69CB1CFCD	FASTA	200	23,156
	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
	Isoform A [UniParc]. Checksum: 7C1D7F373CFF2EA7	FASTA	194	22,535
	10 20 30 40 50 60 MFARVSFYPT LLYNVLMEKA SARNWYDRID EHVILGALPF RSQANDLIEK ENMKAVVSMN 70 80 90 100 110 120 EDYELTAFSN NTEKWRKLGI EFLQLATTDI FESPNQEKLF RGVEFINKFL PLKQRIGGLS 130 140 150 160 170 180 SSYQPENVGS VYVHCKAGRT RSATLVGCYL MMKNGWTPDQ AVDHMRKCRP HILLHTKQWD 190 ALRLFYTNNV ETKS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
RefSeq	NP_651180.3. NM_142923.3. NP_732901.1. NM_170090.2.
UniGene	Dm.20236.
3D structure databases
ProteinModelPortal	Q86BN8.
SMR	Q86BN8. Positions 31-192.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-318143.
Proteomic databases
PaxDb	Q86BN8.
PRIDE	Q86BN8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0084453; FBpp0083844; FBgn0039111.
GeneID	42807.
KEGG	dme:Dmel_CG10371.
Organism-specific databases
CTD	42807.
FlyBase	FBgn0039111. Plip.
Phylogenomic databases
eggNOG	NOG146651.
GeneTree	ENSGT00390000014065.
InParanoid	Q86BN8.
KO	K14165.
OMA	TDIFESP.
OrthoDB	EOG4FJ6RZ.
PhylomeDB	Q86BN8.
Enzyme and pathway databases
UniPathway	UPA00084; UER00504.
Gene expression databases
Bgee	Q86BN8.
GermOnline	CG10371. Drosophila melanogaster.
Family and domain databases
InterPro	IPR000340. Dual-sp_phosphatase_cat-dom. IPR024950. DUSP. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. [Graphical view]
PANTHER	PTHR10159. PTHR10159. 1 hit.
Pfam	PF00782. DSPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50054. TYR_PHOSPHATASE_DUAL. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	KAT5. drosophila.
GenomeRNAi	42807.
NextBio	830670.

Entry information

Entry name

PTPM1_DROME

Accession

Primary (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:	May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project