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Database: UniProt
Entry: P32587
LinkDB: P32587
Original site: P32587 
ID   PYP3_SCHPO              Reviewed;         303 AA.
AC   P32587;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   29-OCT-2014, entry version 109.
DE   RecName: Full=Tyrosine-protein phosphatase 3;
DE            EC=3.1.3.48;
DE   AltName: Full=Protein-tyrosine phosphatase 3;
DE            Short=PTPase 3;
GN   Name=pyp3; ORFNames=SPAC11E3.09;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1464318;
RA   Millar J.B.A., Lenaers G., Russell P.;
RT   "Pyp3 PTPase acts as a mitotic inducer in fission yeast.";
RL   EMBO J. 11:4933-4941(1992).
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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Contributes to dephosphorylation of tyrosine 15 of cdc2.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00160}.
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DR   EMBL; X69994; CAA49609.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAB11188.1; -; Genomic_DNA.
DR   PIR; S28392; S28392.
DR   RefSeq; NP_594934.1; NM_001020365.2.
DR   ProteinModelPortal; P32587; -.
DR   BioGrid; 277948; 8.
DR   MINT; MINT-4688440; -.
DR   STRING; 4896.SPAC11E3.09-1; -.
DR   MaxQB; P32587; -.
DR   EnsemblFungi; SPAC11E3.09.1; SPAC11E3.09.1:pep; SPAC11E3.09.
DR   GeneID; 2541443; -.
DR   KEGG; spo:SPAC11E3.09; -.
DR   PomBase; SPAC11E3.09; -.
DR   eggNOG; COG5599; -.
DR   InParanoid; P32587; -.
DR   KO; K01104; -.
DR   OMA; NANQELQ; -.
DR   OrthoDB; EOG7R573B; -.
DR   PhylomeDB; P32587; -.
DR   NextBio; 20802545; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:PomBase.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:PomBase.
DR   GO; GO:0007067; P:mitotic nuclear division; IEA:UniProtKB-KW.
DR   GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:GOC.
DR   GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:PomBase.
DR   GO; GO:0007165; P:signal transduction; IC:PomBase.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Complete proteome; Cytoplasm; Hydrolase;
KW   Mitosis; Protein phosphatase; Reference proteome.
FT   CHAIN         1    303       Tyrosine-protein phosphatase 3.
FT                                /FTId=PRO_0000094860.
FT   DOMAIN       24    292       Tyrosine-protein phosphatase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00160}.
FT   ACT_SITE    227    227       Phosphocysteine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00160,
FT                                ECO:0000255|PROSITE-ProRule:PRU10044}.
SQ   SEQUENCE   303 AA;  34583 MW;  6ED642C818B32791 CRC64;
     MSFKEVSTEN GVLTPLITIK EKAYMIIEGL NEEEIELLNT RLPKLSKKAL ARNRYSNIVP
     YENTRVRLDP MWKEACDYIN ASIVKIPSGK TFIATQGPTS NSIDVFWKMV WQSVPKSGII
     VMLTKLRERH RLKCDIYWPV ELFETLNIGD LSVILVKVYT LTSLNEVQVR EFELNKDGVK
     KKILHFYYNG WPDFGAPHTF SLLSLTRYIK SLSYSPDFET APIIVHCSAG CGRTGTFMAL
     FEILSQTDDS TSTSKFEVDN IANIVSSLRS QRMQSVQSVD QLVFLYTVSQ ELLQGKEFLL
     PQL
//
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