PPAL_SCHPO
ID PPAL_SCHPO Reviewed; 156 AA.
AC P41893; Q9UTQ3; Q9UUG7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Low molecular weight phosphotyrosine protein phosphatase;
DE EC=3.1.3.48;
DE AltName: Full=Low molecular weight cytosolic acid phosphatase;
DE EC=3.1.3.2;
DE AltName: Full=PTPase;
DE AltName: Full=Small tyrosine phosphatase;
GN Name=stp1; ORFNames=SPAC1071.12c, SPAC926.01c;
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 [MRNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=7961734; DOI=10.1016/s0021-9258(18)46886-x;
RA Mondesert O., Moreno S., Russell P.;
RT "Low molecular weight protein-tyrosine phosphatases are highly conserved
RT between fission yeast and man.";
RL J. Biol. Chem. 269:27996-27999(1994).
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: May contribute to dephosphorylation of 'Tyr-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;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC phosphatase family. {ECO:0000305}.
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DR EMBL; L33929; AAA61930.1; -; mRNA.
DR EMBL; CU329670; CAB59888.1; -; Genomic_DNA.
DR PIR; A55446; A55446.
DR RefSeq; XP_001713094.1; XM_001713042.2.
DR AlphaFoldDB; P41893; -.
DR SMR; P41893; -.
DR BioGRID; 280509; 12.
DR STRING; 4896.SPAC1071.12c.1; -.
DR iPTMnet; P41893; -.
DR MaxQB; P41893; -.
DR PaxDb; P41893; -.
DR PRIDE; P41893; -.
DR EnsemblFungi; SPAC1071.12c.1; SPAC1071.12c.1:pep; SPAC1071.12c.
DR PomBase; SPAC1071.12c; stp1.
DR VEuPathDB; FungiDB:SPAC1071.12c; -.
DR eggNOG; KOG3217; Eukaryota.
DR HOGENOM; CLU_071415_2_0_1; -.
DR InParanoid; P41893; -.
DR OMA; TGSWHVG; -.
DR PhylomeDB; P41893; -.
DR BRENDA; 3.1.3.48; 5613.
DR PRO; PR:P41893; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IDA:PomBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:PomBase.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR InterPro; IPR023485; Ptyr_pPase.
DR InterPro; IPR036196; Ptyr_pPase_sf.
DR InterPro; IPR002115; Tyr_Pase_low_mol_wt_mml.
DR InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR Pfam; PF01451; LMWPc; 1.
DR PRINTS; PR00719; LMWPTPASE.
DR PRINTS; PR00720; MAMMALPTPASE.
DR SMART; SM00226; LMWPc; 1.
DR SUPFAM; SSF52788; SSF52788; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..156
FT /note="Low molecular weight phosphotyrosine protein
FT phosphatase"
FT /id="PRO_0000046564"
FT ACT_SITE 11
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P11064"
FT ACT_SITE 17
FT /evidence="ECO:0000250|UniProtKB:P11064"
FT ACT_SITE 128
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P11064"
SQ SEQUENCE 156 AA; 17391 MW; 536B433655FCB56A CRC64;
MTKNIQVLFV CLGNICRSPM AEAVFRNEVE KAGLEARFDT IDSCGTGAWH VGNRPDPRTL
EVLKKNGIHT KHLARKLSTS DFKNFDYIFA MDSSNLRNIN RVKPQGSRAK VMLFGEYASP
GVSKIVDDPY YGGSDGFGDC YIQLVDFSQN FLKSIA
