ID B4HWI7_DROSE Unreviewed; 514 AA.
AC B4HWI7;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=GM11890 {ECO:0000313|EMBL:EDW52382.1};
GN Name=Dsec\GM11890 {ECO:0000313|EMBL:EDW52382.1};
GN ORFNames=Dsec_GM11890 {ECO:0000313|EMBL:EDW52382.1};
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238 {ECO:0000313|Proteomes:UP000001292};
RN [1] {ECO:0000313|EMBL:EDW52382.1, ECO:0000313|Proteomes:UP000001292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25
RC {ECO:0000313|Proteomes:UP000001292};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000256|ARBA:ARBA00007881}.
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DR EMBL; CH480818; EDW52382.1; -; Genomic_DNA.
DR RefSeq; XP_002036459.1; XM_002036423.1.
DR AlphaFoldDB; B4HWI7; -.
DR SMR; B4HWI7; -.
DR STRING; 7238.B4HWI7; -.
DR EnsemblMetazoa; FBtr0194875; FBpp0193367; FBgn0166831.
DR GeneID; 6611942; -.
DR KEGG; dse:6611942; -.
DR HOGENOM; CLU_020105_5_1_1; -.
DR OMA; FWLNTYF; -.
DR OrthoDB; 5477362at2759; -.
DR PhylomeDB; B4HWI7; -.
DR Proteomes; UP000001292; Unassembled WGS sequence.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0010008; C:endosome membrane; IEA:EnsemblMetazoa.
DR GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:EnsemblMetazoa.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:EnsemblMetazoa.
DR GO; GO:0006914; P:autophagy; IEA:EnsemblMetazoa.
DR GO; GO:0071711; P:basement membrane organization; IEA:EnsemblMetazoa.
DR GO; GO:0035212; P:cell competition in a multicellular organism; IEA:EnsemblMetazoa.
DR GO; GO:0031104; P:dendrite regeneration; IEA:EnsemblMetazoa.
DR GO; GO:0007032; P:endosome organization; IEA:EnsemblMetazoa.
DR GO; GO:0007425; P:epithelial cell fate determination, open tracheal system; IEA:EnsemblMetazoa.
DR GO; GO:0030707; P:follicle cell of egg chamber development; IEA:EnsemblMetazoa.
DR GO; GO:0002164; P:larval development; IEA:EnsemblMetazoa.
DR GO; GO:0035069; P:larval midgut histolysis; IEA:EnsemblMetazoa.
DR GO; GO:0055088; P:lipid homeostasis; IEA:EnsemblMetazoa.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0048542; P:lymph gland development; IEA:EnsemblMetazoa.
DR GO; GO:0035011; P:melanotic encapsulation of foreign target; IEA:EnsemblMetazoa.
DR GO; GO:0048681; P:negative regulation of axon regeneration; IEA:EnsemblMetazoa.
DR GO; GO:0030308; P:negative regulation of cell growth; IEA:EnsemblMetazoa.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:EnsemblMetazoa.
DR GO; GO:0045792; P:negative regulation of cell size; IEA:EnsemblMetazoa.
DR GO; GO:0042690; P:negative regulation of crystal cell differentiation; IEA:EnsemblMetazoa.
DR GO; GO:0045571; P:negative regulation of imaginal disc growth; IEA:EnsemblMetazoa.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0035204; P:negative regulation of lamellocyte differentiation; IEA:EnsemblMetazoa.
DR GO; GO:0010888; P:negative regulation of lipid storage; IEA:EnsemblMetazoa.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IEA:EnsemblMetazoa.
DR GO; GO:0046621; P:negative regulation of organ growth; IEA:EnsemblMetazoa.
DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:EnsemblMetazoa.
DR GO; GO:0045614; P:negative regulation of plasmatocyte differentiation; IEA:EnsemblMetazoa.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:EnsemblMetazoa.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:EnsemblMetazoa.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:EnsemblMetazoa.
DR GO; GO:0008104; P:protein localization; IEA:EnsemblMetazoa.
DR GO; GO:0010506; P:regulation of autophagy; IEA:EnsemblMetazoa.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:EnsemblMetazoa.
DR GO; GO:1901888; P:regulation of cell junction assembly; IEA:EnsemblMetazoa.
DR GO; GO:0008360; P:regulation of cell shape; IEA:EnsemblMetazoa.
DR GO; GO:0050773; P:regulation of dendrite development; IEA:EnsemblMetazoa.
DR GO; GO:0090175; P:regulation of establishment of planar polarity; IEA:EnsemblMetazoa.
DR GO; GO:0035206; P:regulation of hemocyte proliferation; IEA:EnsemblMetazoa.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IEA:EnsemblMetazoa.
DR GO; GO:0042594; P:response to starvation; IEA:EnsemblMetazoa.
DR GO; GO:0042052; P:rhabdomere development; IEA:EnsemblMetazoa.
DR CDD; cd14509; PTP_PTEN; 1.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR045101; PTP_PTEN.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR12305; PHOSPHATASE WITH HOMOLOGY TO TENSIN; 1.
DR PANTHER; PTHR12305:SF81; PHOSPHATIDYLINOSITOL 3,4,5-TRISPHOSPHATE 3-PHOSPHATASE AND DUAL-SPECIFICITY PROTEIN PHOSPHATASE PTEN; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM01301; PTPlike_phytase; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 3: Inferred from homology;
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000001292}.
FT DOMAIN 21..193
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 110..167
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 181..337
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
SQ SEQUENCE 514 AA; 58952 MW; DB694C29BE0A6BB3 CRC64;
MANTISLMSN VIRNVVSKKR IRYKEKGYNL DLTYINDNII AMGYPAPDKL EGLFRNRLED
VFKLLEENHA QHYKVYNLCS ERSYDVDKFH GRVAVYPFDD HNPPTIELIQ RFCSDVDLWL
KEDSSNVVAV HCKAGKGRTG TMICAYLVYS GLKKSADEAL AWYDEKRTKD RKGVTIPSQR
RYVQYFSKLV CSSVPYSKVS LNVCEIRFSE SSCVQNLGTV ECSVSVLHDS ATENSKPDIL
KTFAIDFQES FVLTIKPSLP VSGDVKFKLT QKSPDKIIGH FWLNTYFVRN YSLCESNGTV
NKYIHTLSKS EIDDVHKDSE HKRFSEEFKI SIVFEAENFS NDVQAEASEK ERNENVLNFE
RSDYDSLRPN CYTEKKVLTA IVNDNTAKSQ TIETLDHKDI VTKIQYDTST NSKNTSTACK
RKQPNSKTLL PSLNDSTKEE IKRNHIFNQP SIKKTDLIKW QNSEVHITSD TRSINENKNI
NYNSYITCKQ SSPKFNCGTE DGEEDWESGE STYL
//