ID PTP3_DICDI Reviewed; 990 AA. AC P54637; Q54SY3; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 04-DEC-2007, sequence version 2. DT 27-MAR-2024, entry version 122. DE RecName: Full=Tyrosine-protein phosphatase 3; DE EC=3.1.3.48; DE AltName: Full=Protein-tyrosine-phosphate phosphohydrolase 3; GN Name=ptpC; Synonyms=ptp3; ORFNames=DDB_G0282145; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=AX3; RX PubMed=8628311; DOI=10.1128/mcb.16.5.2431; RA Gamper M., Howard P.K., Hunter T., Firtel R.A.; RT "Multiple roles of the novel protein tyrosine phosphatase PTP3 during RT Dictyostelium growth and development."; RL Mol. Cell. Biol. 16:2431-2444(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). CC -!- FUNCTION: Seems to dephosphorylate a protein of 130 kDa (p130). CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU10044}; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: In the anterior-like and prestalk cell types. CC -!- DEVELOPMENTAL STAGE: Expressed at moderate levels during growth and CC development. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non- CC receptor class subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U38197; AAC47041.1; -; mRNA. DR EMBL; AAFI02000045; EAL66352.1; -; Genomic_DNA. DR RefSeq; XP_640326.1; XM_635234.1. DR AlphaFoldDB; P54637; -. DR SMR; P54637; -. DR STRING; 44689.P54637; -. DR PaxDb; 44689-DDB0214986; -. DR EnsemblProtists; EAL66352; EAL66352; DDB_G0282145. DR GeneID; 8623427; -. DR KEGG; ddi:DDB_G0282145; -. DR dictyBase; DDB_G0282145; ptpC. DR eggNOG; KOG0789; Eukaryota. DR HOGENOM; CLU_301777_0_0_1; -. DR InParanoid; P54637; -. DR OMA; SHNDLDN; -. DR PRO; PR:P54637; -. DR Proteomes; UP000002195; Chromosome 3. DR GO; GO:0005829; C:cytosol; IDA:dictyBase. DR GO; GO:0005768; C:endosome; IDA:dictyBase. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:dictyBase. DR GO; GO:0019722; P:calcium-mediated signaling; IMP:dictyBase. DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro. DR GO; GO:0035556; P:intracellular signal transduction; IMP:dictyBase. DR GO; GO:1904893; P:negative regulation of receptor signaling pathway via STAT; IMP:dictyBase. DR GO; GO:0034504; P:protein localization to nucleus; IMP:dictyBase. DR GO; GO:1903013; P:response to differentiation-inducing factor 1; IDA:dictyBase. DR GO; GO:0006970; P:response to osmotic stress; IMP:dictyBase. DR CDD; cd00047; PTPc; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR000242; PTP_cat. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR003595; Tyr_Pase_cat. DR InterPro; IPR000387; Tyr_Pase_dom. DR PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1. DR PANTHER; PTHR19134:SF555; TYROSINE-PROTEIN PHOSPHATASE 3; 1. DR Pfam; PF00102; Y_phosphatase; 1. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00194; PTPc; 1. DR SMART; SM00404; PTPc_motif; 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; PS50055; TYR_PHOSPHATASE_PTP; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Hydrolase; Protein phosphatase; Reference proteome. FT CHAIN 1..990 FT /note="Tyrosine-protein phosphatase 3" FT /id="PRO_0000094888" FT DOMAIN 422..715 FT /note="Tyrosine-protein phosphatase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160" FT REGION 47..88 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 100..193 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 246..414 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 431..452 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 786..814 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 834..990 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 246..412 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 834..966 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 967..981 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 650 FT /note="Phosphocysteine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160, FT ECO:0000255|PROSITE-ProRule:PRU10044" FT CONFLICT 187 FT /note="Missing (in Ref. 1; AAC47041)" FT /evidence="ECO:0000305" SQ SEQUENCE 990 AA; 110110 MW; 123EAF31B9ED0AF4 CRC64; MISSSMSYRH STNSVYTLNP HLNIPISTST TIPPTSFYAN NTPEMIQSQS ENTNTNNINN SSSNINNNNN NTPDSMSMST SLSSSPSVSF NHLDLNSINN KINNNTTTNN NNNNNNNNDD KFDTNALKLS NTMIIKNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNSNS NIEINVPSIQ FDNEPAMEVD SVAPLNVPSN HTRTTLAMHN TKSLSTSNIG LLNILPNQQS SSSSSLSSTT TTTTTTSSSL LMPQSLFNNS TYNNHHNNNN SSNAGIVGGL NGSTSSLPTQ AQVQLQQMQQ QMQQHQQHQY KKANLSSLST VVDNNLNNNP MNTSTSSPAQ PNASPFSFSS SSLFSNSSLS NSGSGSASTT STSTSSSNSM SSSPPPSLKT SFSQLDEDRE KMRLEFEMIK KPEMASKKSH KHHQRHYSHN DLDNRKHDEE KFFSALQPNN YGKNRYHDVL PNESTRVRLT PIESGDGDYI NANYINGEVP NSYRYYIACQ APLPSTIKDF WRMVWEERSS VIVCLTKLEE NGKKKADVYY PETSQAQEYG SFWIHLHKKV MFKDIGVSSL HLYKKGEEFP REVVLLHYTQ WPDCGAPPSS SHIRTLSVMV NTFKARGSAK NTNGPVIVHC SAGIGRSGTF ISININMAKI ERFGNDPSQM NISIKDSVLE LRRQRRGMVQ TLDQYIFIFK VINDVLTDMG IRSLSSPSKR RSCEMIKSTP MPRLDISIPP PLTFTPKDFQ SSISPSTDMI ASLSIITQMT QTLKFPPQQQ QDNPFSKSSI KISPSPLNST NISIPKNQQF QHPFQIQPQL DLNLQQQQQQ SSQQLNDNPP LNMSSNSIKF PPVTSLSSCH LFEDSKNNDN NNKQQQQQQQ QQQKNNQQCS GFSHFLNNNN NNDNNGSSGG GFNGSFLFNS NNSGSSSTNS ECSNNNKNNN NNSNNNNNNN NNKNSDNNGT KDKDENDSCE SPRVTPIKCF //