PYP2_SCHPO
ID PYP2_SCHPO Reviewed; 711 AA.
AC P32586; Q9UR59; Q9UU64;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 162.
DE RecName: Full=Tyrosine-protein phosphatase 2;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphatase 2;
DE Short=PTPase 2;
GN Name=pyp2; ORFNames=SPAC19D5.01;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1448087; DOI=10.1128/mcb.12.12.5571-5580.1992;
RA Ottilie S., Chernoff J., Hannig G., Hoffman C.S., Erikson R.L.;
RT "The fission yeast genes pyp1+ and pyp2+ encode protein tyrosine
RT phosphatases that negatively regulate mitosis.";
RL Mol. Cell. Biol. 12:5571-5580(1992).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 285-437.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 485-519.
RX PubMed=1668885;
RA Yanagida M., Yamano H., Stone E.M., Kinoshita N., Yoshida T., Shiozaki K.;
RT "Protein phosphatases in cell division: how vital are they?";
RL Princess Takamatsu Symp. 22:137-144(1991).
RN [6]
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).
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; S51320; AAB24544.1; -; Genomic_DNA.
DR EMBL; X59599; CAA42167.1; -; mRNA.
DR EMBL; AB027789; BAA87093.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB16711.1; -; Genomic_DNA.
DR PIR; S28391; S28391.
DR PIR; T45160; T45160.
DR RefSeq; NP_594899.1; NM_001020328.2.
DR AlphaFoldDB; P32586; -.
DR SMR; P32586; -.
DR BioGRID; 278675; 64.
DR IntAct; P32586; 1.
DR STRING; 4896.SPAC19D5.01.1; -.
DR iPTMnet; P32586; -.
DR PaxDb; P32586; -.
DR EnsemblFungi; SPAC19D5.01.1; SPAC19D5.01.1:pep; SPAC19D5.01.
DR GeneID; 2542200; -.
DR KEGG; spo:SPAC19D5.01; -.
DR PomBase; SPAC19D5.01; pyp2.
DR VEuPathDB; FungiDB:SPAC19D5.01; -.
DR eggNOG; KOG0789; Eukaryota.
DR HOGENOM; CLU_386439_0_0_1; -.
DR InParanoid; P32586; -.
DR OMA; DYSFPLR; -.
DR PhylomeDB; P32586; -.
DR Reactome; R-SPO-5675221; Negative regulation of MAPK pathway.
DR PRO; PR:P32586; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; 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: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; IDA:PomBase.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
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 SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 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;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..711
FT /note="Tyrosine-protein phosphatase 2"
FT /id="PRO_0000094859"
FT DOMAIN 21..130
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 433..698
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 275..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 630
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT CONFLICT 271..275
FT /note="IVGNA -> NRRQC (in Ref. 2; CAA42167)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="I -> M (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="E -> N (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="H -> D (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="R -> P (in Ref. 2; CAA42167)"
FT /evidence="ECO:0000305"
FT CONFLICT 668..670
FT /note="FNC -> IQL (in Ref. 2; CAA42167)"
FT /evidence="ECO:0000305"
FT CONFLICT 675..676
FT /note="RS -> DT (in Ref. 2; CAA42167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 711 AA; 79356 MW; 15A12CDAE13D341E CRC64;
MLHLLSKDEF NSTLKSFEEQ TESVSWIIDL RLHSKYAVSH IKNAINVSLP TALLRRPSFD
IGKVFACIKC NVKVSLDEIN AIFLYDSSMA GMNRIYDLVQ KFRRGGYSKK IYLLSNGFEA
FASSHPDAIV STEMVKESVP YKIDINENCK LDILHLSDPS AVSTPISPDY SFPLRVPINI
PPPLCTPSVV SDTFSEFASH AEYPGFSGLT PFSIHSPTAS SVRSCQSIYG SPLSPPNSAF
QAEMPYFPIS PAISCASSCP STPDEQKNFF IVGNAPQQTP ARPSLRSVPS YPSSNNQRRP
SASRVRSFSN YVKSSNVVNP SLSQASLEII PRKSMKRDSN AQNDGTSTMT SKLKPSVGLS
NTRDAPKPGG LRRANKPCFN KETKGSIFSK ENKGPFTCNP WGAKKVSPPP CEVLADLNTA
SIFYKFKRLE EMEMTRSLAF NDSKSDWCCL ASSRSTSISR KNRYTDIVPY DKTRVRLAVP
KGCSDYINAS HIDVGNKKYI ACQAPKPGTL LDFWEMVWHN SGTNGVIVML TNLYEAGSEK
CSQYWPDNKD HALCLEGGLR ISVQKYETFE DLKVNTHLFR LDKPNGPPKY IHHFWVHTWF
DKTHPDIESI TGIIRCIDKV PNDGPMFVHC SAGVGRTGTF IAVDQILQVP KNILPKTTNL
EDSKDFIFNC VNSLRSQRMK MVQNFEQFKF LYDVVDYLNS GVNQASKPLM T
