PYP3_SCHPO
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 25-MAY-2022, entry version 154.
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; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1464318; DOI=10.1002/j.1460-2075.1992.tb05600.x;
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., 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: Contributes to dephosphorylation of tyrosine 15 of cdc2.
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; 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 AlphaFoldDB; P32587; -.
DR SMR; P32587; -.
DR BioGRID; 277948; 9.
DR STRING; 4896.SPAC11E3.09.1; -.
DR MaxQB; P32587; -.
DR PaxDb; P32587; -.
DR EnsemblFungi; SPAC11E3.09.1; SPAC11E3.09.1:pep; SPAC11E3.09.
DR GeneID; 2541443; -.
DR KEGG; spo:SPAC11E3.09; -.
DR PomBase; SPAC11E3.09; pyp3.
DR VEuPathDB; FungiDB:SPAC11E3.09; -.
DR eggNOG; KOG0791; Eukaryota.
DR HOGENOM; CLU_001645_9_1_1; -.
DR InParanoid; P32587; -.
DR OMA; FYYYKWA; -.
DR PhylomeDB; P32587; -.
DR Reactome; R-SPO-5675221; Negative regulation of MAPK pathway.
DR PRO; PR:P32587; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA: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:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
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; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
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 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; Cytoplasm; Hydrolase; Mitosis;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..303
FT /note="Tyrosine-protein phosphatase 3"
FT /id="PRO_0000094860"
FT DOMAIN 24..292
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 227
FT /note="Phosphocysteine intermediate"
FT /evidence="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
