ID   PYP1_SCHPO              Reviewed;         550 AA.
AC   P27574;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   04-NOV-2026, entry version 182.
DE   RecName: Full=Tyrosine-protein phosphatase 1;
DE            EC=3.1.3.48;
DE   AltName: Full=Protein-tyrosine phosphatase 1;
DE            Short=PTPase 1;
GN   Name=pyp1; ORFNames=SPAC26F1.10c;
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 [MRNA].
RX   PubMed=1849659; DOI=10.1073/pnas.88.8.3455;
RA   Ottilie S., Chernoff J., Hannig G., Hoffman C.S., Erikson R.L.;
RT   "A fission-yeast gene encoding a protein with features of protein-tyrosine-
RT   phosphatases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:3455-3459(1991).
RN   [2]
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   [3]
RP   CHARACTERIZATION.
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   [4]
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).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318 AND SER-320, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Plays a role in inhibiting the onset of mitosis.
CC       Dephosphorylates sty1/spc1 and wis1/spc2/sty2.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-tyrosyl-[protein] + H2O = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978; 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; M63257; AAA35328.1; -; mRNA.
DR   EMBL; CU329670; CAA97367.1; -; Genomic_DNA.
DR   PIR; A40449; A40449.
DR   RefSeq; NP_594885.1; NM_001020314.3.
DR   AlphaFoldDB; P27574; -.
DR   SMR; P27574; -.
DR   BioGRID; 279130; 245.
DR   FunCoup; P27574; 27.
DR   STRING; 284812.P27574; -.
DR   iPTMnet; P27574; -.
DR   PaxDb; 284812-P27574; -.
DR   GeneID; 2542677; -.
DR   KEGG; spo:2542677; -.
DR   PomBase; SPAC26F1.10c; pyp1.
DR   VEuPathDB; FungiDB:SPAC26F1.10c; -.
DR   eggNOG; KOG0789; Eukaryota.
DR   HOGENOM; CLU_493601_0_0_1; -.
DR   InParanoid; P27574; -.
DR   OMA; ACCADKN; -.
DR   PhylomeDB; P27574; -.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   PRO; PR:P27574; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0140453; C:protein aggregate center; IDA: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:1903753; P:negative regulation of p38MAPK cascade; IMP:PomBase.
DR   GO; GO:1900744; P:regulation of p38MAPK cascade; IGI:PomBase.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd18533; PTP_fungal; 1.
DR   FunFam; 3.90.190.10:FF:000294; Tyrosine-protein phosphatase 2; 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; IPR050348; Protein-Tyr_Phosphatase.
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:SF529; TYROSINE-PROTEIN PHOSPHATASE 1; 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   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 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; Phosphoprotein;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..550
FT                   /note="Tyrosine-protein phosphatase 1"
FT                   /id="PRO_0000094858"
FT   DOMAIN          260..539
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        470
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
FT   MOD_RES         318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         320
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   550 AA;  61588 MW;  5DB770AEAAA59F03 CRC64;
     MNFSNGSKSS TFTIAPSGSC IALPPQRGVA TSKYAVHASC LQEYLDKEAW KDDTLIIDLR
     PVSEFSKSRI KGSVNLSLPA TLIKRPAFSV ARIISNLHDV DDKRDFQNWQ EFSSILVCVP
     AWIANYVTNA EVIGEKFRKE SYSGDFGILD LDYSKVSGKY PSVIDNSPVK SKLGALPSAR
     PRLSYSAAQT APISLSSEGS DYFSRPPPTP NVAGLSLNNF FCPLPENKDN KSSPFGSATV
     QTPCLHSVPD AFTNPDVATL YQKFLRLQSL EHQRLVSCSD RNSQWSTVDS LSNTSYKKNR
     YTDIVPYNCT RVHLKRTSPS ELDYINASFI KTETSNYIAC QGSISRSISD FWHMVWDNVE
     NIGTIVMLGS LFEAGREMCT AYWPSNGIGD KQVYGDYCVK QISEENVDNS RFILRKFEIQ
     NANFPSVKKV HHYQYPNWSD CNSPENVKSM VEFLKYVNNS HGSGNTIVHC SAGVGRTGTF
     IVLDTILRFP ESKLSGFNPS VADSSDVVFQ LVDHIRKQRM KMVQTFTQFK YVYDLIDSLQ
     KSQVHFPVLT
//