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PTEN3 (Phosphatase and tensin homolog) (Phosphatase and tensin homolog, isoform A) (Phosphatase and tensin homolog, isoform E) (EC 3.1.3.-) (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.64) (EC 3.1.3.67)

 Q9V3L4_DROME            Unreviewed;       509 AA.
Q9V3L4; Q9U468;
01-MAY-2000, integrated into UniProtKB/TrEMBL.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 153.
SubName: Full=PTEN3 {ECO:0000313|EMBL:AAD45364.1};
SubName: Full=Phosphatase and tensin homolog {ECO:0000313|EMBL:AAF23235.1};
SubName: Full=Phosphatase and tensin homolog, isoform A {ECO:0000313|EMBL:AAF52887.2};
SubName: Full=Phosphatase and tensin homolog, isoform E {ECO:0000313|EMBL:AAF52889.1};
EC=3.1.3.- {ECO:0000313|EMBL:AAF52887.2, ECO:0000313|EMBL:AAF52889.1};
EC=3.1.3.16 {ECO:0000313|EMBL:AAF52887.2, ECO:0000313|EMBL:AAF52889.1};
EC=3.1.3.48 {ECO:0000313|EMBL:AAF52887.2, ECO:0000313|EMBL:AAF52889.1};
EC=3.1.3.64 {ECO:0000313|EMBL:AAF52887.2, ECO:0000313|EMBL:AAF52889.1};
EC=3.1.3.67 {ECO:0000313|EMBL:AAF52887.2, ECO:0000313|EMBL:AAF52889.1};
Name=Pten {ECO:0000313|EMBL:AAF52887.2,
ECO:0000313|FlyBase:FBgn0026379};
Synonyms=Dmel\CG5671 {ECO:0000313|EMBL:AAF52887.2},
DPTEN {ECO:0000313|EMBL:AAF52887.2},
dPTEN {ECO:0000313|EMBL:AAF52887.2},
dPten {ECO:0000313|EMBL:AAF52887.2},
dpten {ECO:0000313|EMBL:AAF52887.2},
PTEN {ECO:0000313|EMBL:AAF52887.2},
pten {ECO:0000313|EMBL:AAF52887.2},
PTEN3 {ECO:0000313|EMBL:AAF52887.2};
ORFNames=CG5671 {ECO:0000313|EMBL:AAF52887.2,
ECO:0000313|FlyBase:FBgn0026379},
Dmel_CG5671 {ECO:0000313|EMBL:AAF52887.2};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227 {ECO:0000313|EMBL:AAF52887.2, ECO:0000313|Proteomes:UP000000803};
[1] {ECO:0000313|EMBL:AAD45364.1}
NUCLEOTIDE SEQUENCE.
PubMed=10542333; DOI=10.1016/S0167-4781(99)00172-4;
Smith A., Smith A., Alrubaie S., Coehlo C., Leevers S.J., Ashworth A.;
"Alternative splicing of the Drosophila PTEN gene.";
Biochim. Biophys. Acta 1447:313-317(1999).
[2] {ECO:0000313|EMBL:AAF23235.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Oregon-R {ECO:0000313|EMBL:AAF23235.1};
PubMed=10617573; DOI=10.1101/gad.13.24.3244;
Goberdhan D.C., Paricio N., Goodman E.C., Mlodzik M., Wilson C.;
"Drosophila tumor suppressor PTEN controls cell size and number by
antagonizing the Chico/PI3-kinase signaling pathway.";
Genes Dev. 13:3244-3258(1999).
[3] {ECO:0000313|EMBL:AAF52887.2, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L.,
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., 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., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J., 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., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.,
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., WoodageT, 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., Zhu X., Smith H.O.,
Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4] {ECO:0000313|EMBL:AAF52887.2, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537568;
Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
"Finishing a whole-genome shotgun: release 3 of the Drosophila
melanogaster euchromatic genome sequence.";
Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
[5] {ECO:0000313|EMBL:AAF52887.2, ECO:0000313|Proteomes:UP000000803}
GENOME REANNOTATION.
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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., Whitfied E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D., 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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6] {ECO:0000313|EMBL:AAF52887.2, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537573;
Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M.,
Ashburner M., Celniker S.E.;
"The transposable elements of the Drosophila melanogaster euchromatin:
a genomics perspective.";
Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
[7] {ECO:0000313|EMBL:AAF52887.2, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=12537574;
Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
Karpen G.H.;
"Heterochromatic sequences in a Drosophila whole-genome shotgun
assembly.";
Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
[8] {ECO:0000313|EMBL:AAF52887.2, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
Ashburner M., Anxolabehere D.;
"Combined evidence annotation of transposable elements in genome
sequences.";
PLoS Comput. Biol. 1:166-175(2005).
[9] {ECO:0000313|EMBL:AAF52887.2}
NUCLEOTIDE SEQUENCE.
Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
Svirskas R., Rubin G.;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
[10] {ECO:0000313|EMBL:AAF52887.2}
NUCLEOTIDE SEQUENCE.
Berkeley Drosophila Genome Project;
Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E.,
Yu C., Rubin G.;
"Drosophila melanogaster release 4 sequence.";
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[11] {ECO:0000313|EMBL:AAF52887.2, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569856; DOI=10.1126/science.1139815;
Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
"The Release 5.1 annotation of Drosophila melanogaster
heterochromatin.";
Science 316:1586-1591(2007).
[12] {ECO:0000313|EMBL:AAF52887.2, ECO:0000313|Proteomes:UP000000803}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
PubMed=17569867; DOI=10.1126/science.1139816;
Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
Dimitri P., Karpen G.H., Celniker S.E.;
"Sequence finishing and mapping of Drosophila melanogaster
heterochromatin.";
Science 316:1625-1628(2007).
[13] {ECO:0000313|EMBL:AAF52887.2}
NUCLEOTIDE SEQUENCE.
FlyBase;
Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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EMBL; AF161259; AAD45364.1; -; mRNA.
EMBL; AF201904; AAF23235.1; -; Genomic_DNA.
EMBL; AE014134; AAF52887.2; -; Genomic_DNA.
EMBL; AE014134; AAF52889.1; -; Genomic_DNA.
RefSeq; NP_599147.1; NM_134320.3.
RefSeq; NP_599148.1; NM_134321.3.
UniGene; Dm.1417; -.
MINT; MINT-1030801; -.
EnsemblMetazoa; FBtr0089901; FBpp0088840; FBgn0026379.
EnsemblMetazoa; FBtr0089905; FBpp0088844; FBgn0026379.
GeneID; 43991; -.
UCSC; CG5671-RA; d. melanogaster.
CTD; 5728; -.
FlyBase; FBgn0026379; Pten.
eggNOG; KOG2283; Eukaryota.
eggNOG; COG2453; LUCA.
GeneTree; ENSGT00760000119113; -.
OrthoDB; EOG091G09VG; -.
Reactome; R-DME-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-DME-1855204; Synthesis of IP3 and IP4 in the cytosol.
Reactome; R-DME-199418; Negative regulation of the PI3K/AKT network.
Reactome; R-DME-202424; Downstream TCR signaling.
Reactome; R-DME-5689880; Ub-specific processing proteases.
Reactome; R-DME-8948747; Regulation of PTEN localization.
Reactome; R-DME-8948751; Regulation of PTEN stability and activity.
GenomeRNAi; 43991; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0026379; -.
GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
GO; GO:0005634; C:nucleus; ISS:FlyBase.
GO; GO:0003779; F:actin binding; ISS:FlyBase.
GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; ISS:FlyBase.
GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IGI:FlyBase.
GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IMP:FlyBase.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:FlyBase.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; ISS:FlyBase.
GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
GO; GO:0009887; P:animal organ morphogenesis; IMP:FlyBase.
GO; GO:0006915; P:apoptotic process; IMP:FlyBase.
GO; GO:0006914; P:autophagy; IMP:FlyBase.
GO; GO:0071711; P:basement membrane organization; IMP:FlyBase.
GO; GO:0035212; P:cell competition in a multicellular organism; IMP:FlyBase.
GO; GO:0008283; P:cell proliferation; IMP:FlyBase.
GO; GO:0009987; P:cellular process; IMP:FlyBase.
GO; GO:0034613; P:cellular protein localization; IMP:FlyBase.
GO; GO:0007010; P:cytoskeleton organization; IMP:FlyBase.
GO; GO:0031104; P:dendrite regeneration; IMP:FlyBase.
GO; GO:0007425; P:epithelial cell fate determination, open tracheal system; IMP:FlyBase.
GO; GO:0008286; P:insulin receptor signaling pathway; IGI:FlyBase.
GO; GO:0002164; P:larval development; IMP:FlyBase.
GO; GO:0035069; P:larval midgut histolysis; IGI:FlyBase.
GO; GO:0007436; P:larval salivary gland morphogenesis; IMP:FlyBase.
GO; GO:0055088; P:lipid homeostasis; IMP:FlyBase.
GO; GO:0019915; P:lipid storage; IMP:FlyBase.
GO; GO:0035011; P:melanotic encapsulation of foreign target; IMP:FlyBase.
GO; GO:0007552; P:metamorphosis; IMP:FlyBase.
GO; GO:0048681; P:negative regulation of axon regeneration; IMP:FlyBase.
GO; GO:0045786; P:negative regulation of cell cycle; TAS:FlyBase.
GO; GO:0030308; P:negative regulation of cell growth; NAS:FlyBase.
GO; GO:0045792; P:negative regulation of cell size; TAS:FlyBase.
GO; GO:0045926; P:negative regulation of growth; TAS:FlyBase.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; TAS:FlyBase.
GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:FlyBase.
GO; GO:0046621; P:negative regulation of organ growth; IMP:FlyBase.
GO; GO:0016322; P:neuron remodeling; IMP:FlyBase.
GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; TAS:FlyBase.
GO; GO:0006470; P:protein dephosphorylation; IMP:FlyBase.
GO; GO:0010506; P:regulation of autophagy; IMP:FlyBase.
GO; GO:0051726; P:regulation of cell cycle; IMP:FlyBase.
GO; GO:1901888; P:regulation of cell junction assembly; IMP:FlyBase.
GO; GO:0008360; P:regulation of cell shape; IMP:FlyBase.
GO; GO:0008361; P:regulation of cell size; IMP:FlyBase.
GO; GO:0050773; P:regulation of dendrite development; IMP:FlyBase.
GO; GO:0090175; P:regulation of establishment of planar polarity; IMP:FlyBase.
GO; GO:0035206; P:regulation of hemocyte proliferation; IMP:FlyBase.
GO; GO:0040014; P:regulation of multicellular organism growth; IMP:FlyBase.
GO; GO:0046620; P:regulation of organ growth; NAS:FlyBase.
GO; GO:0042594; P:response to starvation; IMP:FlyBase.
GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
GO; GO:0007525; P:somatic muscle development; IMP:FlyBase.
GO; GO:0009888; P:tissue development; IMP:FlyBase.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR014020; Tensin_C2-dom.
InterPro; IPR029023; Tensin_phosphatase.
InterPro; IPR016130; Tyr_Pase_AS.
Pfam; PF00782; DSPc; 1.
Pfam; PF10409; PTEN_C2; 1.
SMART; SM01326; PTEN_C2; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS51182; C2_TENSIN; 1.
PROSITE; PS51181; PPASE_TENSIN; 1.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
2: Evidence at transcript level;
Complete proteome {ECO:0000313|Proteomes:UP000000803};
Hydrolase {ECO:0000313|EMBL:AAF52887.2};
Reference proteome {ECO:0000313|Proteomes:UP000000803}.
DOMAIN 21 193 Phosphatase tensin-type.
{ECO:0000259|PROSITE:PS51181}.
DOMAIN 181 337 C2 tensin-type.
{ECO:0000259|PROSITE:PS51182}.
SEQUENCE 509 AA; 58432 MW; A618527D9EFF9020 CRC64;
MANTISLMSN VIRNVVSKKR IRYKEKGYDL DLTYINDNII AMGYPAPDKL EGLFRNRLED
VFKLLEENHA QHYKIYNLCS ERSYDVAKFR GRVAVYPFDD HNPPTIELIQ RFCSDVDMWL
KEDSSNVVAV HCKAGKGRTG TMICAYLVFS GIKKSADEAL AWYDEKRTKD RKGVTIPSQR
RYVQYFSKLV CSSVPYSKVS LNVCEIRFSE SSCVQNLGMV ECSISVLHDS ATENAKPDRL
KTLPIDFQKS FVLTIKPSIP VSGDVKFELT KKSPDKIICH FWLNTFFVRN YSPCESDGTV
NKYIHTLSKS EIDDVHKDSE HKRFSEEFKI SIVFEAENFS NDVQAEASEK ERNENVLNFE
RSDYDSLSPN CYAEKKVLTA IVNDNTTKSQ TIETLDHKDI VTKIQYDTST NSKNTSTACK
RKQPNSKTLL PSLNDSTKEE IKRNHIFNQP SIKKTDLIKW QNSEVHITSD TRSINENKNI
NYNSYITCKQ SSPKFNCGTE DGEEDWESE


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