ID   PMP1_SCHPO              Reviewed;         278 AA.
AC   O13453;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Tyrosine-protein phosphatase pmp1;
DE            EC=3.1.3.48;
GN   Name=pmp1; ORFNames=SPBC1685.01;
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], AND FUNCTION.
RX   PubMed=9427748; DOI=10.1093/emboj/17.1.140;
RA   Sugiura R., Toda T., Shuntoh H., Yanagida M., Kuno T.;
RT   "pmp1+, a suppressor of calcineurin deficiency, encodes a novel MAP kinase
RT   phosphatase in fission yeast.";
RL   EMBO J. 17:140-148(1998).
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).
CC   -!- FUNCTION: Dual specificity phosphatase that dephosphorylates MAP kinase
CC       pmk1 on a Tyr. Has a role in chloride ion homeostasis by inactivating
CC       this pmk1 MAP kinase pathway. {ECO:0000269|PubMed:9427748}.
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;
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class dual specificity subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D82022; BAA22897.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA20049.1; -; Genomic_DNA.
DR   PIR; T39517; T39517.
DR   RefSeq; NP_595205.1; NM_001021111.2.
DR   AlphaFoldDB; O13453; -.
DR   SMR; O13453; -.
DR   BioGRID; 276563; 95.
DR   IntAct; O13453; 1.
DR   STRING; 4896.SPBC1685.01.1; -.
DR   iPTMnet; O13453; -.
DR   MaxQB; O13453; -.
DR   PaxDb; O13453; -.
DR   EnsemblFungi; SPBC1685.01.1; SPBC1685.01.1:pep; SPBC1685.01.
DR   GeneID; 2540019; -.
DR   KEGG; spo:SPBC1685.01; -.
DR   PomBase; SPBC1685.01; pmp1.
DR   VEuPathDB; FungiDB:SPBC1685.01; -.
DR   eggNOG; KOG1716; Eukaryota.
DR   HOGENOM; CLU_1001704_0_0_1; -.
DR   InParanoid; O13453; -.
DR   OMA; INCQMGI; -.
DR   PhylomeDB; O13453; -.
DR   Reactome; R-SPO-112409; RAF-independent MAPK1/3 activation.
DR   Reactome; R-SPO-202670; ERKs are inactivated.
DR   Reactome; R-SPO-5675221; Negative regulation of MAPK pathway.
DR   PRO; PR:O13453; -.
DR   Proteomes; UP000002485; Chromosome II.
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:0033550; F:MAP kinase tyrosine phosphatase activity; IDA:PomBase.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IBA:GO_Central.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:1903138; P:negative regulation of cell wall integrity MAPK cascade; EXP:PomBase.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; IBA:GO_Central.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Hydrolase; Protein phosphatase; Reference proteome.
FT   CHAIN           1..278
FT                   /note="Tyrosine-protein phosphatase pmp1"
FT                   /id="PRO_0000094917"
FT   DOMAIN          60..214
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          217..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..232
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..278
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        158
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   278 AA;  31628 MW;  0EA71219ED32483F CRC64;
     MSQKLPPLKI YTSQLPLVSH KNMLENEEEA SHSQLFTPCP VPPSFPKASK PNSNQPYPNG
     PVCIYPPNIY LYAKPTMPII QSFDVVINVA KEVLHPFRTD GRHYRDSKHN LDIQVFDHIE
     YVHIHWDHDT QFALELDKLV SFVAYNAMQL NKKVLINCQM GISRSACLMI AFIMKTLNLN
     VSDAYEYVKE RSPWIGPNMS LIFQLSEYQQ IIRKNSSQGP YQSSSLKQSK RKSEGNLLFP
     EKPHSAQLPL VSPSTSESSM FTNLRRTRSS GSISNDAS