ID PTP2_DICDI Reviewed; 377 AA.
AC P34138; Q54YM9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE RecName: Full=Tyrosine-protein phosphatase 2;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine-phosphate phosphohydrolase 2;
DE Short=PTPA;
GN Name=ptpB; Synonyms=ptp2; ORFNames=DDB_G0277865;
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=AX4;
RX PubMed=8226777; DOI=10.1016/s0021-9258(18)41581-5;
RA Ramalingam R., Shaw D.R., Ennis H.;
RT "Cloning and functional expression of a Dictyostelium discoideum protein
RT tyrosine phosphatase.";
RL J. Biol. Chem. 268:22680-22685(1993).
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 -!- 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 -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
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DR EMBL; L15420; AAA33242.1; -; mRNA.
DR EMBL; AAFI02000023; EAL68105.1; -; Genomic_DNA.
DR PIR; A48711; A48711.
DR RefSeq; XP_642173.1; XM_637081.1.
DR AlphaFoldDB; P34138; -.
DR SMR; P34138; -.
DR STRING; 44689.P34138; -.
DR PaxDb; 44689-DDB0214985; -.
DR EnsemblProtists; EAL68105; EAL68105; DDB_G0277865.
DR GeneID; 8621380; -.
DR KEGG; ddi:DDB_G0277865; -.
DR dictyBase; DDB_G0277865; ptpB.
DR eggNOG; KOG0792; Eukaryota.
DR HOGENOM; CLU_001645_9_1_1; -.
DR InParanoid; P34138; -.
DR OMA; RFCYLAI; -.
DR PhylomeDB; P34138; -.
DR Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:P34138; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0016791; F:phosphatase activity; IDA:dictyBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
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:SF449; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE GAMMA; 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 Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..377
FT /note="Tyrosine-protein phosphatase 2"
FT /id="PRO_0000094887"
FT DOMAIN 27..347
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 77..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 281
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
SQ SEQUENCE 377 AA; 43488 MW; 5B08F6EB54829FD9 CRC64;
MDESFDAFEI KPNSSIIEHF NNHPTCIDKE FNFILQKTEL RALETDKFRS ALEAKNKLKN
RYSNVLPFEE TRVKINIDDD DDDEDDNEDD IIVSNNNNNN NNNEKRIKRN SIGSSGQSDV
MSNSSDEEDH GGSGDEGTTL SDYINASFIN NGTYICTQGP LLNTIVDFWK MIWEQNSNII
VMLTREEENF KTKCDKYWPD KDEERYGNFI VKFDNNITIP DILIRREFTL ENLKDNKTRK
IYHFQYTTWP DHGTPVSTTG FLKFVSFVDH EKRSGPIVVH CSAGIGRSGT FVAIHSIVAK
FAKHYDEKKQ APSINLPKLV VEMRNERPGM VQTRDQYRFC YLAISEAMNT VLKKEQKKRK
GLSYSYSSIP LTGPEHD
//
