PYP1_SCHPO
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 03-AUG-2022, entry version 166.
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=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; M63257; AAA35328.1; -; mRNA.
DR EMBL; CU329670; CAA97367.1; -; Genomic_DNA.
DR PIR; A40449; A40449.
DR RefSeq; NP_594885.1; NM_001020314.2.
DR AlphaFoldDB; P27574; -.
DR SMR; P27574; -.
DR BioGRID; 279130; 245.
DR STRING; 4896.SPAC26F1.10c.1; -.
DR iPTMnet; P27574; -.
DR MaxQB; P27574; -.
DR PaxDb; P27574; -.
DR PRIDE; P27574; -.
DR EnsemblFungi; SPAC26F1.10c.1; SPAC26F1.10c.1:pep; SPAC26F1.10c.
DR GeneID; 2542677; -.
DR KEGG; spo:SPAC26F1.10c; -.
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; YIACQGS; -.
DR PhylomeDB; P27574; -.
DR Reactome; R-SPO-5675221; Negative regulation of MAPK pathway.
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:0005634; C:nucleus; 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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1903753; P:negative regulation of p38MAPK cascade; IMP:PomBase.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; IGI:PomBase.
DR Gene3D; 3.40.250.10; -; 1.
DR Gene3D; 3.90.190.10; -; 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 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; SSF52799; 1.
DR SUPFAM; SSF52821; SSF52821; 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
