ID B4M154_DROVI Unreviewed; 513 AA.
AC B4M154;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE SubName: Full=Uncharacterized protein, isoform A {ECO:0000313|EMBL:EDW67465.1};
DE EC=3.1.3.- {ECO:0000313|EMBL:EDW67465.1};
DE EC=3.1.3.48 {ECO:0000313|EMBL:EDW67465.1};
GN Name=Dvir\GJ24161 {ECO:0000313|EMBL:EDW67465.1};
GN ORFNames=Dvir_GJ24161 {ECO:0000313|EMBL:EDW67465.1};
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244 {ECO:0000313|EMBL:EDW67465.1, ECO:0000313|Proteomes:UP000008792};
RN [1] {ECO:0000313|EMBL:EDW67465.1, ECO:0000313|Proteomes:UP000008792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
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 protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily.
CC {ECO:0000256|ARBA:ARBA00008601}.
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DR EMBL; CH940650; EDW67465.1; -; Genomic_DNA.
DR RefSeq; XP_002053945.1; XM_002053909.2.
DR AlphaFoldDB; B4M154; -.
DR SMR; B4M154; -.
DR STRING; 7244.B4M154; -.
DR EnsemblMetazoa; FBtr0240086; FBpp0238578; FBgn0211245.
DR GeneID; 6630955; -.
DR KEGG; dvi:6630955; -.
DR eggNOG; KOG1716; Eukaryota.
DR HOGENOM; CLU_048492_0_0_1; -.
DR InParanoid; B4M154; -.
DR OMA; NHKDYPN; -.
DR OrthoDB; 53899at2759; -.
DR PhylomeDB; B4M154; -.
DR Proteomes; UP000008792; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:EnsemblMetazoa.
DR GO; GO:0005794; C:Golgi apparatus; IEA:EnsemblMetazoa.
DR GO; GO:0008579; F:JUN kinase phosphatase activity; IEA:EnsemblMetazoa.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:EnsemblMetazoa.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblMetazoa.
DR GO; GO:0008362; P:chitin-based embryonic cuticle biosynthetic process; IEA:EnsemblMetazoa.
DR GO; GO:0046844; P:chorion micropyle formation; IEA:EnsemblMetazoa.
DR GO; GO:0048749; P:compound eye development; IEA:EnsemblMetazoa.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:EnsemblMetazoa.
DR GO; GO:0071907; P:determination of digestive tract left/right asymmetry; IEA:EnsemblMetazoa.
DR GO; GO:0046843; P:dorsal appendage formation; IEA:EnsemblMetazoa.
DR GO; GO:0007391; P:dorsal closure; IEA:EnsemblMetazoa.
DR GO; GO:0048615; P:embryonic anterior midgut (ectodermal) morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0008544; P:epidermis development; IEA:EnsemblMetazoa.
DR GO; GO:0030707; P:follicle cell of egg chamber development; IEA:EnsemblMetazoa.
DR GO; GO:0007561; P:imaginal disc eversion; IEA:EnsemblMetazoa.
DR GO; GO:0046529; P:imaginal disc fusion, thorax closure; IEA:EnsemblMetazoa.
DR GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0007254; P:JNK cascade; IEA:EnsemblMetazoa.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:EnsemblMetazoa.
DR GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0070303; P:negative regulation of stress-activated protein kinase signaling cascade; IEA:EnsemblMetazoa.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IEA:EnsemblMetazoa.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:EnsemblMetazoa.
DR GO; GO:0050778; P:positive regulation of immune response; IEA:EnsemblMetazoa.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:EnsemblMetazoa.
DR GO; GO:0009306; P:protein secretion; IEA:EnsemblMetazoa.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IEA:EnsemblMetazoa.
DR GO; GO:0042060; P:wound healing; IEA:EnsemblMetazoa.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR PANTHER; PTHR10159; DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR10159:SF528; PUCKERED, ISOFORM A; 1.
DR Pfam; PF00782; DSPc; 1.
DR SMART; SM00195; DSPc; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EDW67465.1};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000008792}.
FT DOMAIN 132..272
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50054"
FT DOMAIN 193..251
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 13..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 54594 MW; 3F179363F3B63B0B CRC64;
MCVCETSNSS YNYNNNSNNT ATSTTRNCCE RDGDSNSVSH KSEMKMRIKR EAPCLLLFMP
IQNNNNNNNR IGANHKDYPN NKRSRENLAC DEQQLTATST STAAMNVGSN GGRTPPLMRS
CSSPAVYDIE THPASPVFPH LLLGNGRDAD DPSSVGANCV LNVTCQSPSE SHLQGLKYMQ
IPASDTPHQN IKQYFQEAFD FIEDARKTGS RVLLHCHAGI SRSATIAIAY VMRYKSLSLL
EAYKLVKVAR PIISPNLNFM GQLLELEQSL RKSGVLAPLP VTPVASSQSP QVPLAATTSQ
LVEQPEQEAA AAVAHLAPTS RPLHSKSKSD SEAMDEDVYD YDDVDSGAGS FAGSNCSSRL
TSPPVTPDET PCTSAAAAAT ELDSPCSNSS SGIYSMSASR PFSAPNSYAA ATPAPAATTA
APALLSPSRP LALFKRNSPV KLRLNLESNY TPNIPKSISC ISIHNASLRS PLQREAPATP
SCEAAPTTPG DNNCSSSSST SNNNNLVAAT SSD
//