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Database: UniProt
Entry: M9PGI1_DROME
LinkDB: M9PGI1_DROME
Original site: M9PGI1_DROME 
ID   M9PGI1_DROME            Unreviewed;       894 AA.
AC   M9PGI1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=csw {ECO:0000313|EMBL:AGB95020.1,
GN   ECO:0000313|FlyBase:FBgn0000382};
GN   Synonyms=19-106 {ECO:0000313|EMBL:AGB95020.1}, anon-WO03040301.207
GN   {ECO:0000313|EMBL:AGB95020.1}, anon-WO03040301.209
GN   {ECO:0000313|EMBL:AGB95020.1}, anon-WO03040301.219
GN   {ECO:0000313|EMBL:AGB95020.1}, CSW {ECO:0000313|EMBL:AGB95020.1}, Csw
GN   {ECO:0000313|EMBL:AGB95020.1}, csw/SHP-2
GN   {ECO:0000313|EMBL:AGB95020.1}, Csw/Shp2 {ECO:0000313|EMBL:AGB95020.1},
GN   Dmel\CG3954 {ECO:0000313|EMBL:AGB95020.1}, E(sev)1A
GN   {ECO:0000313|EMBL:AGB95020.1}, EG:BACN25G24.2
GN   {ECO:0000313|EMBL:AGB95020.1}, l(1)2Db {ECO:0000313|EMBL:AGB95020.1},
GN   l(1)2Dd {ECO:0000313|EMBL:AGB95020.1}, l(1)csw
GN   {ECO:0000313|EMBL:AGB95020.1}, l(1)G0170
GN   {ECO:0000313|EMBL:AGB95020.1}, l(1)GA114
GN   {ECO:0000313|EMBL:AGB95020.1}, SHP-2 {ECO:0000313|EMBL:AGB95020.1},
GN   Shp-2 {ECO:0000313|EMBL:AGB95020.1}, Shp2/csw
GN   {ECO:0000313|EMBL:AGB95020.1};
GN   ORFNames=CG3954 {ECO:0000313|EMBL:AGB95020.1,
GN   ECO:0000313|FlyBase:FBgn0000382}, Dmel_CG3954
GN   {ECO:0000313|EMBL:AGB95020.1};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:AGB95020.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AGB95020.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Gabor G.L., Abril J.F., Agbayani A.,
RA   An H.J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA   Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA   Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA   Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA   Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA   Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA   Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000313|EMBL:AGB95020.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT   euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|EMBL:AGB95020.1, ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4] {ECO:0000313|EMBL:AGB95020.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA   Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin: a
RT   genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN   [5] {ECO:0000313|EMBL:AGB95020.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:AGB95020.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [7] {ECO:0000313|EMBL:AGB95020.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [8] {ECO:0000313|EMBL:AGB95020.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
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DR   EMBL; AE014298; AGB95020.1; -; Genomic_DNA.
DR   RefSeq; NP_001259174.1; NM_001272245.1.
DR   AlphaFoldDB; M9PGI1; -.
DR   SMR; M9PGI1; -.
DR   DNASU; 45278; -.
DR   EnsemblMetazoa; FBtr0333260; FBpp0305458; FBgn0000382.
DR   GeneID; 45278; -.
DR   AGR; FB:FBgn0000382; -.
DR   CTD; 45278; -.
DR   FlyBase; FBgn0000382; csw.
DR   VEuPathDB; VectorBase:FBgn0000382; -.
DR   GeneTree; ENSGT00940000167235; -.
DR   OMA; VIFQQNT; -.
DR   OrthoDB; 2911650at2759; -.
DR   BioGRID-ORCS; 45278; 2 hits in 3 CRISPR screens.
DR   GenomeRNAi; 45278; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0000382; Expressed in spermathecum and 21 other cell types or tissues.
DR   ExpressionAtlas; M9PGI1; baseline and differential.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0048666; P:neuron development; IEA:UniProt.
DR   CDD; cd14544; PTPc-N11_6; 1.
DR   CDD; cd09931; SH2_C-SH2_SHP_like; 1.
DR   CDD; cd10340; SH2_N-SH2_SHP_like; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   Gene3D; 3.30.505.10; SH2 domain; 2.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR46257; TYROSINE-PROTEIN PHOSPHATASE CORKSCREW; 1.
DR   PANTHER; PTHR46257:SF3; TYROSINE-PROTEIN PHOSPHATASE CORKSCREW; 1.
DR   Pfam; PF00017; SH2; 2.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SMART; SM00252; SH2; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF55550; SH2 domain; 2.
DR   PROSITE; PS50001; SH2; 2.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AGB95020.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..894
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004101865"
FT   DOMAIN          59..154
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          164..258
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          280..698
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          609..689
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          415..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          850..894
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        879..894
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   894 AA;  98260 MW;  3A2C576F86BE0BB5 CRC64;
     MHTPHCAPLF ATVLHCAPLH LPLMTTWYAG QEAPEADHKR HSHNGQWQLT TPICLPTGWF
     HPTISGIEAE KLLQEQGFDG SFLARLSSSN PGAFTLSVRR GNEVTHIKIQ NNGDFFDLYG
     GEKFATLPEL VQYYMENGEL KEKNGQAIEL KQPLICAEPT TERWFHGNLS GKEAEKLILE
     RGKNGSFLVR ESQSKPGDFV LSVRTDDKVT HVMIRWQDKK YDVGGGESFG TLSELIDHYK
     RNPMVETCGT VVHLRQPFNA TRITAAGINA RVEQLVKGGF WEEFESLQQD SRDTFSRNEG
     YKQENRLKNR YRNILPYDHT RVKLLDVEHS VAGAEYINAN YIRLPTDGDL YNMSSSSESL
     NSSVPSCPAC TAAQTQRNCS NCQLQNKTCV QCAVKSAILP YSNCATCSRK SDSLSKHKRS
     ESSASSSPSS GSGSGPGSSG TSGVSSVNGP GTPTNLTSGT AGCLVGLLKR HSNDSSGAVS
     ISMAERERER EREMFKTYIA TQGCLLTQQV NTVTDFWNMV WQENTRVIVM TTKEYERGKE
     KCARYWPDEG RSEQFGHARI QCVSENSTSD YTLREFLVSW RDQPARRIFH YHFQVWPDHG
     VPADPGCVLN FLQDVNTRQS HLAQAGEKPG PICVHCSAGI GRTGTFIVID MILDQIVRNG
     LDTEIDIQRT IQMVRSQRSG LVQTEAQYKF VYYAVQHYIQ TLIARKRAEE QSLQVGREYT
     NIKYTGEIGN DSQRSPLPPA ISSISLVPSK TPLTPTSADL GTGMGLSMGV GMGVGNKHAS
     KQQPPLPVVN CNNNNNGIGN SGCSNGGGSS TTSSSNGSSN GNINALLGGI GLGLGGNMRK
     SNFYSDSLKQ QQQREEQAPA GAAKFKNIPK DMIGLRPPSH APALPPPPTP PRKT
//
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