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Database: UniProt
Entry: B4HWI7_DROSE
LinkDB: B4HWI7_DROSE
Original site: B4HWI7_DROSE 
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
//
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