ID   PYP2_SCHPO              Reviewed;         711 AA.
AC   P32586; Q9UR59; Q9UU64;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 169.
DE   RecName: Full=Tyrosine-protein phosphatase 2;
DE            EC=3.1.3.48;
DE   AltName: Full=Protein-tyrosine phosphatase 2;
DE            Short=PTPase 2;
GN   Name=pyp2; ORFNames=SPAC19D5.01;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1464319; DOI=10.1002/j.1460-2075.1992.tb05601.x;
RA   Millar J.B.A., Russell P., Dixon J.E., Guan K.L.;
RT   "Negative regulation of mitosis by two functionally overlapping PTPases in
RT   fission yeast.";
RL   EMBO J. 11:4943-4952(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1448087; DOI=10.1128/mcb.12.12.5571-5580.1992;
RA   Ottilie S., Chernoff J., Hannig G., Hoffman C.S., Erikson R.L.;
RT   "The fission yeast genes pyp1+ and pyp2+ encode protein tyrosine
RT   phosphatases that negatively regulate mitosis.";
RL   Mol. Cell. Biol. 12:5571-5580(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 285-437.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE OF 485-519.
RX   PubMed=1668885;
RA   Yanagida M., Yamano H., Stone E.M., Kinoshita N., Yoshida T., Shiozaki K.;
RT   "Protein phosphatases in cell division: how vital are they?";
RL   Princess Takamatsu Symp. 22:137-144(1991).
RN   [6]
RP   CHARACTERIZATION.
RX   PubMed=7657164; DOI=10.1101/gad.9.17.2117;
RA   Millar J.B.A., Buck V., Wilkinson M.G.;
RT   "Pyp1 and Pyp2 PTPases dephosphorylate an osmosensing MAP kinase
RT   controlling cell size at division in fission yeast.";
RL   Genes Dev. 9:2117-2130(1995).
CC   -!- FUNCTION: Plays a role in inhibiting the onset of mitosis.
CC       Dephosphorylates sty1/spc1 and wis1/spc2/sty2.
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   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000305}.
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DR   EMBL; S51320; AAB24544.1; -; Genomic_DNA.
DR   EMBL; X59599; CAA42167.1; -; mRNA.
DR   EMBL; AB027789; BAA87093.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB16711.1; -; Genomic_DNA.
DR   PIR; S28391; S28391.
DR   PIR; T45160; T45160.
DR   RefSeq; NP_594899.1; NM_001020328.2.
DR   AlphaFoldDB; P32586; -.
DR   SMR; P32586; -.
DR   BioGRID; 278675; 65.
DR   IntAct; P32586; 1.
DR   STRING; 284812.P32586; -.
DR   iPTMnet; P32586; -.
DR   PaxDb; 4896-SPAC19D5-01-1; -.
DR   EnsemblFungi; SPAC19D5.01.1; SPAC19D5.01.1:pep; SPAC19D5.01.
DR   GeneID; 2542200; -.
DR   KEGG; spo:SPAC19D5.01; -.
DR   PomBase; SPAC19D5.01; pyp2.
DR   VEuPathDB; FungiDB:SPAC19D5.01; -.
DR   eggNOG; KOG0789; Eukaryota.
DR   HOGENOM; CLU_386439_0_0_1; -.
DR   InParanoid; P32586; -.
DR   OMA; FWEMIWH; -.
DR   PhylomeDB; P32586; -.
DR   Reactome; R-SPO-5675221; Negative regulation of MAPK pathway.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   PRO; PR:P32586; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0033550; F:MAP kinase tyrosine phosphatase activity; IDA:PomBase.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:PomBase.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:1903753; P:negative regulation of p38MAPK cascade; IDA:PomBase.
DR   CDD; cd01446; DSP_MapKP; 1.
DR   CDD; cd18533; PTP_fungal; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
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:SF557; TYROSINE-PROTEIN PHOSPHATASE 2; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Hydrolase; Mitosis;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..711
FT                   /note="Tyrosine-protein phosphatase 2"
FT                   /id="PRO_0000094859"
FT   DOMAIN          21..130
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT   DOMAIN          433..698
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          275..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          329..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        630
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
FT   CONFLICT        271..275
FT                   /note="IVGNA -> NRRQC (in Ref. 2; CAA42167)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        487
FT                   /note="I -> M (in Ref. 5)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        515
FT                   /note="E -> N (in Ref. 5)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        519
FT                   /note="H -> D (in Ref. 5)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        636
FT                   /note="R -> P (in Ref. 2; CAA42167)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        668..670
FT                   /note="FNC -> IQL (in Ref. 2; CAA42167)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        675..676
FT                   /note="RS -> DT (in Ref. 2; CAA42167)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   711 AA;  79356 MW;  15A12CDAE13D341E CRC64;
     MLHLLSKDEF NSTLKSFEEQ TESVSWIIDL RLHSKYAVSH IKNAINVSLP TALLRRPSFD
     IGKVFACIKC NVKVSLDEIN AIFLYDSSMA GMNRIYDLVQ KFRRGGYSKK IYLLSNGFEA
     FASSHPDAIV STEMVKESVP YKIDINENCK LDILHLSDPS AVSTPISPDY SFPLRVPINI
     PPPLCTPSVV SDTFSEFASH AEYPGFSGLT PFSIHSPTAS SVRSCQSIYG SPLSPPNSAF
     QAEMPYFPIS PAISCASSCP STPDEQKNFF IVGNAPQQTP ARPSLRSVPS YPSSNNQRRP
     SASRVRSFSN YVKSSNVVNP SLSQASLEII PRKSMKRDSN AQNDGTSTMT SKLKPSVGLS
     NTRDAPKPGG LRRANKPCFN KETKGSIFSK ENKGPFTCNP WGAKKVSPPP CEVLADLNTA
     SIFYKFKRLE EMEMTRSLAF NDSKSDWCCL ASSRSTSISR KNRYTDIVPY DKTRVRLAVP
     KGCSDYINAS HIDVGNKKYI ACQAPKPGTL LDFWEMVWHN SGTNGVIVML TNLYEAGSEK
     CSQYWPDNKD HALCLEGGLR ISVQKYETFE DLKVNTHLFR LDKPNGPPKY IHHFWVHTWF
     DKTHPDIESI TGIIRCIDKV PNDGPMFVHC SAGVGRTGTF IAVDQILQVP KNILPKTTNL
     EDSKDFIFNC VNSLRSQRMK MVQNFEQFKF LYDVVDYLNS GVNQASKPLM T
//