PVH1_SCHPO
ID PVH1_SCHPO Reviewed; 330 AA.
AC O13632;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Tyrosine-protein phosphatase yvh1;
DE Short=PTPase yvh1;
DE EC=3.1.3.48;
GN Name=yvh1; ORFNames=pi040, SPBC17A3.06;
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].
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).
CC -!- FUNCTION: May be directly involved in signal transduction and/or cell
CC cycle regulation. It is necessary for maintaining growth rate or spore
CC germination. Could show both activity toward tyrosine-protein phosphate
CC as well as with serine-protein phosphate (By similarity).
CC {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class dual specificity subfamily. {ECO:0000305}.
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DR EMBL; AB004537; BAA21420.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB51765.1; -; Genomic_DNA.
DR PIR; T39698; T39698.
DR RefSeq; NP_595588.1; NM_001021484.2.
DR AlphaFoldDB; O13632; -.
DR SMR; O13632; -.
DR BioGRID; 276683; 99.
DR STRING; 4896.SPBC17A3.06.1; -.
DR MaxQB; O13632; -.
DR PaxDb; O13632; -.
DR EnsemblFungi; SPBC17A3.06.1; SPBC17A3.06.1:pep; SPBC17A3.06.
DR GeneID; 2540146; -.
DR KEGG; spo:SPBC17A3.06; -.
DR PomBase; SPBC17A3.06; -.
DR VEuPathDB; FungiDB:SPBC17A3.06; -.
DR eggNOG; KOG1716; Eukaryota.
DR HOGENOM; CLU_023312_0_1_1; -.
DR InParanoid; O13632; -.
DR OMA; RIMLNTQ; -.
DR PhylomeDB; O13632; -.
DR PRO; PR:O13632; -.
DR Proteomes; UP000002485; Chromosome II.
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; ISO:PomBase.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0000027; P:ribosomal large subunit assembly; ISO:PomBase.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR InterPro; IPR016278; DUSP12.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF00782; DSPc; 1.
DR PIRSF; PIRSF000941; DUSP12; 1.
DR SMART; SM00195; DSPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Nucleus; Protein phosphatase; Reference proteome;
KW Stress response.
FT CHAIN 1..330
FT /note="Tyrosine-protein phosphatase yvh1"
FT /id="PRO_0000314761"
FT DOMAIN 45..187
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 131
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 330 AA; 38006 MW; DBF64E7FAEBA1E84 CRC64;
MSNKSAWQPQ FDEIHSSVQE AEGFLQSSND VQKAIDEVHY PDSLNDLSEI SKNLYISSWK
TASELVSTSD KGIDYTLSAM SINPNLSVPE QQHLWLQIED SSSQNILQYF EKSNKFIAFA
LSKNAKVLVH CFAGISRSVT LVAAYLMKEN NWNTEEALSH INERRSGISP NANFLRQLRV
YFECNYQLDR SLRPYRQWLF RRYGDFAVLN TRVPSEVAYA ETVRARAGQL ELRCKKCRFV
LASSDYLVSH EPKDENNYSH TRCTHYFLEP IRWMQPELEL GNLEGRFDCP KCNSKIGSYK
WQGLQCSCLQ WVCPALSILQ SRVDAVRKLG
