PTP3_DICDI
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 03-AUG-2022, entry version 117.
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 (Slime mold).
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}.
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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.DDB0214986; -.
DR PaxDb; P54637; -.
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; TLAMHNT; -.
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:0016791; F:phosphatase activity; IDA:dictyBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:dictyBase.
DR GO; GO:0016311; P:dephosphorylation; IDA:dictyBase.
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:0006470; P:protein dephosphorylation; IEA:InterPro.
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 Gene3D; 3.90.190.10; -; 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 Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 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
