ID   YNF3_SCHPO              Reviewed;         287 AA.
AC   Q9UUF3; O13635;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 3.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Protein-tyrosine phosphatase family protein C17A3.03c {ECO:0000305};
DE            EC=3.1.-.- {ECO:0000305};
GN   ORFNames=pi043, SPBC17A3.03c;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=10620777;
RX   DOI=10.1002/(sici)1097-0061(20000115)16:1<71::aid-yea505>3.0.co;2-5;
RA   Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K.,
RA   Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y.,
RA   Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.;
RT   "A 38 kb segment containing the cdc2 gene from the left arm of fission
RT   yeast chromosome II: sequence analysis and characterization of the genomic
RT   DNA and cDNAs encoded on the segment.";
RL   Yeast 16:71-80(2000).
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-159, 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       {ECO:0000255}.
CC   -!- CAUTION: Not likely to act as a protein phosphatase. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA21423.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB004537; BAA21423.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CU329671; CAB51762.2; -; Genomic_DNA.
DR   PIR; T39695; T39695.
DR   RefSeq; NP_595585.2; NM_001021481.2.
DR   AlphaFoldDB; Q9UUF3; -.
DR   SMR; Q9UUF3; -.
DR   BioGRID; 276671; 33.
DR   STRING; 284812.Q9UUF3; -.
DR   iPTMnet; Q9UUF3; -.
DR   MaxQB; Q9UUF3; -.
DR   PaxDb; 4896-SPBC17A3-03c-1; -.
DR   EnsemblFungi; SPBC17A3.03c.1; SPBC17A3.03c.1:pep; SPBC17A3.03c.
DR   GeneID; 2540134; -.
DR   KEGG; spo:SPBC17A3.03c; -.
DR   PomBase; SPBC17A3.03c; -.
DR   VEuPathDB; FungiDB:SPBC17A3.03c; -.
DR   eggNOG; KOG1572; Eukaryota.
DR   HOGENOM; CLU_047845_1_1_1; -.
DR   InParanoid; Q9UUF3; -.
DR   PRO; PR:Q9UUF3; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004309; F:exopolyphosphatase activity; IDA:PomBase.
DR   GO; GO:0004427; F:inorganic diphosphate phosphatase activity; IDA:PomBase.
DR   GO; GO:0052840; F:inositol diphosphate tetrakisphosphate diphosphatase activity; IBA:GO_Central.
DR   GO; GO:0052846; F:inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity; IDA:PomBase.
DR   GO; GO:0052847; F:inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity; IDA:PomBase.
DR   GO; GO:0052843; F:inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity; IDA:PomBase.
DR   GO; GO:0052845; F:inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity; IDA:PomBase.
DR   GO; GO:0106211; F:inositol-5-diphosphate-1,3,4,6-tetrakisphosphate diphosphatase activity; ISO:PomBase.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   GO; GO:0071543; P:diphosphoinositol polyphosphate metabolic process; ISO:PomBase.
DR   CDD; cd18538; PFA-DSP_unk; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR004861; Siw14-like.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   PANTHER; PTHR31126:SF78; INOSITOL PHOSPHATASE SIW14; 1.
DR   PANTHER; PTHR31126; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF03162; Y_phosphatase2; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..287
FT                   /note="Protein-tyrosine phosphatase family protein
FT                   C17A3.03c"
FT                   /id="PRO_0000315935"
FT   DOMAIN          85..256
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        189
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   MOD_RES         156
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         159
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   287 AA;  32291 MW;  D261498B24DE12AA CRC64;
     MAIVFPFQLE KKLISITSDR DQISMSIPEV SSHDSCLNDC HSVNSEEQAK PVCCLELNAH
     KDGIKVVDTS NDASTFSNSP LVPDNFGVVY PGIIYRSACP RASNFNFLES LHIRTIISLR
     QEEYSEEDLH YFTKHHINYY HIAMPGSKHR KNDCISSSSN PDISDVDDLV RKTLQLLLNK
     ENWPVLLHCS RGKHRTGIVI GCLRALMNWP VGNRLQEYIS FSHPKEREVD EEYIQNFSSD
     PSLKSSLNDL KRYISDSSSE LADVVLSSES PTVQAATVNE TCRSPGS
//