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Database: UniProt/SWISS-PROT
Entry: PP2C3_SCHPO
LinkDB: PP2C3_SCHPO
Original site: PP2C3_SCHPO 
ID   PP2C3_SCHPO             Reviewed;         414 AA.
AC   Q09173;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   01-MAY-2013, entry version 103.
DE   RecName: Full=Protein phosphatase 2C homolog 3;
DE            Short=PP2C-3;
DE            EC=3.1.3.16;
GN   Name=ptc3; ORFNames=SPAC2G11.07c;
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].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=7859738;
RA   Shiozaki K., Russell P.;
RT   "Counteractive roles of protein phosphatase 2C (PP2C) and a MAP kinase
RT   kinase homolog in the osmoregulation of fission yeast.";
RL   EMBO J. 14:492-502(1995).
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: Has an important role in osmotic stability and cell
CC       shape control. It may negatively regulate the osmosensing signal
CC       transmitted through wis1 map kinase.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit (By
CC       similarity).
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the PP2C family.
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DR   EMBL; L34882; AAA67321.1; -; Genomic_DNA.
DR   EMBL; CU329670; CAA91172.1; -; Genomic_DNA.
DR   PIR; T38573; S62462.
DR   RefSeq; NP_593087.1; NM_001018485.2.
DR   ProteinModelPortal; Q09173; -.
DR   STRING; 4896.SPAC2G11.07c-1; -.
DR   PaxDb; Q09173; -.
DR   PRIDE; Q09173; -.
DR   EnsemblFungi; SPAC2G11.07c.1; SPAC2G11.07c.1:pep; SPAC2G11.07c.
DR   GeneID; 2542008; -.
DR   KEGG; spo:SPAC2G11.07c; -.
DR   PomBase; SPAC2G11.07c; -.
DR   eggNOG; COG0631; -.
DR   HOGENOM; HOG000233896; -.
DR   KO; K14803; -.
DR   OMA; HAGRING; -.
DR   OrthoDB; EOG4RFQ28; -.
DR   NextBio; 20803088; -.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:PomBase.
DR   GO; GO:0000173; P:inactivation of MAPK activity involved in osmosensory signaling pathway; IMP:PomBase.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:PomBase.
DR   Gene3D; 3.60.40.10; -; 1.
DR   InterPro; IPR001932; PP2C-like.
DR   InterPro; IPR000222; PP2C_Mn2_Asp60_BS.
DR   InterPro; IPR015655; Protein_Pase_2C.
DR   PANTHER; PTHR13832; PTHR13832; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-related; 1.
DR   PROSITE; PS01032; PP2C; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN         1    414       Protein phosphatase 2C homolog 3.
FT                                /FTId=PRO_0000057772.
FT   METAL        62     62       Manganese 1 (By similarity).
FT   METAL        62     62       Manganese 2 (By similarity).
FT   METAL        63     63       Manganese 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       230    230       Manganese 2 (By similarity).
FT   METAL       279    279       Manganese 2 (By similarity).
FT   CONFLICT    196    196       K -> T (in Ref. 1; AAA67321).
SQ   SEQUENCE   414 AA;  44857 MW;  EFF3A416625A2B11 CRC64;
     MGQTLSEPVT EKHSVNGSNE FVLYGLSSMQ GWRISMEDAH SAILSMECSA VKDPVDFFAV
     YDGHGGDKVA KWCGSNLPQI LEKNPDFQKG DFVNALKSSF LNADKAILDD DQFHTDPSGC
     TATVVLRVGN KLYCANAGDS RTVLGSKGIA KPLSADHKPS NEAEKARICA AGGFVDFGRV
     NGNLALSRAI GDFEFKNSNL EPEKQIVTAL PDVVVHEITD DDEFVVLACD GIWDCKTSQQ
     VIEFVRRGIV AGTSLEKIAE NLMDNCIASD TETTGLGCDN MTVCIVALLQ ENDKSAWYKK
     IADRVAANDG PCAPPEYAEN HGPGWRSGDN NKKVIVPPNF HQVKLNGSDG YDKDANENSK
     EDDSTNGSLA AGFRWKEHFF PHKAEEENSS SETDIVNSNK DVADDHKEAV SAAD
//
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