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
//