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Database: UniProt/SWISS-PROT
Entry: PPB_SCHPO
LinkDB: PPB_SCHPO
Original site: PPB_SCHPO 
ID   PPB_SCHPO               Reviewed;         532 AA.
AC   O60109; Q9C427;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   20-JUN-2018, entry version 117.
DE   RecName: Full=Alkaline phosphatase;
DE            EC=3.1.3.1;
GN   ORFNames=SPBC14F5.13c;
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].
RA   Kang S.-W., Lim C.-J.;
RT   "Characterization of alkaline phosphatase gene from
RT   Schizosaccharomyces pombe.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
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   -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
CC       phosphate. {ECO:0000255|PROSITE-ProRule:PRU10042}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the alkaline phosphatase family.
CC       {ECO:0000305}.
DR   EMBL; AF316541; AAK07179.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA19331.1; -; Genomic_DNA.
DR   PIR; T39459; T39459.
DR   RefSeq; NP_596739.1; NM_001022665.2.
DR   ProteinModelPortal; O60109; -.
DR   SMR; O60109; -.
DR   BioGrid; 276470; 13.
DR   STRING; 4896.SPBC14F5.13c.1; -.
DR   MaxQB; O60109; -.
DR   PaxDb; O60109; -.
DR   PRIDE; O60109; -.
DR   EnsemblFungi; SPBC14F5.13c.1; SPBC14F5.13c.1:pep; SPBC14F5.13c.
DR   GeneID; 2539926; -.
DR   KEGG; spo:SPBC14F5.13c; -.
DR   EuPathDB; FungiDB:SPBC14F5.13c; -.
DR   PomBase; SPBC14F5.13c; -.
DR   HOGENOM; HOG000099116; -.
DR   InParanoid; O60109; -.
DR   KO; K01077; -.
DR   OMA; FEIDRRN; -.
DR   OrthoDB; EOG092C1UXR; -.
DR   PhylomeDB; O60109; -.
DR   Reactome; R-SPO-1483166; Synthesis of PA.
DR   Reactome; R-SPO-8935690; Digestion.
DR   PRO; PR:O60109; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:PomBase.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004035; F:alkaline phosphatase activity; ISO:PomBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046496; P:nicotinamide nucleotide metabolic process; ISO:PomBase.
DR   CDD; cd16012; ALP; 1.
DR   Gene3D; 3.40.720.10; -; 2.
DR   InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR018299; Alkaline_phosphatase_AS.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   PANTHER; PTHR11596; PTHR11596; 1.
DR   Pfam; PF00245; Alk_phosphatase; 1.
DR   PRINTS; PR00113; ALKPHPHTASE.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; SSF53649; 2.
DR   PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Magnesium; Membrane; Metal-binding;
KW   Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN         1    532       Alkaline phosphatase.
FT                                /FTId=PRO_0000186165.
FT   TRANSMEM     27     47       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   ACT_SITE    115    115       Phosphoserine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10042}.
FT   METAL        68     68       Magnesium. {ECO:0000250}.
FT   METAL        68     68       Zinc 2. {ECO:0000250}.
FT   METAL       166    166       Magnesium. {ECO:0000250}.
FT   METAL       168    168       Magnesium. {ECO:0000250}.
FT   METAL       306    306       Magnesium. {ECO:0000250}.
FT   METAL       311    311       Zinc 1. {ECO:0000250}.
FT   METAL       315    315       Zinc 1. {ECO:0000250}.
FT   METAL       352    352       Zinc 2. {ECO:0000250}.
FT   METAL       353    353       Zinc 2. {ECO:0000250}.
FT   METAL       456    456       Zinc 1. {ECO:0000250}.
FT   CONFLICT    513    514       PS -> HC (in Ref. 1; AAK07179).
FT                                {ECO:0000305}.
SQ   SEQUENCE   532 AA;  58666 MW;  57A84A66926D545C CRC64;
     MASERDPLLP VHGEGPESPS RRNWKTWIKH GILLILVLST VIFFYFFSSH KSKGTNEKPK
     FVIMMVSDGM GPGSLSMTRS FVETLNDKEG YRLPLDEHLI GSSRTRSSSS LITDSAAGAT
     AFSCANKTYN GAVGVLDNEK PCGTILEAAK EAGYLTGIVV TSRVTDATPA SFSAHAANRF
     MQDLIAEYQV GMGPLGRSVD LLFGGGLCSF LPKSTYRSCR SDNLDLLKYA RKKEGFQILL
     NRTDFDELSN AQLPLLGLFS DYHLSYDIDY QPEVQPKLSE MVETALDVLL NATNEDTSKG
     FFLLIEGSRI DMASHNNDPI AHVYEVMEYN RAFEIASAFV EKNGGSLIST SDHETGGLTV
     GRQVSKKYPE YLWKPQVLSL ALHSIEYLAS AIVNHNQNTL LPYIEQFVLP AIGIPDPNPK
     QIHDIYVARH NIFNLINVLS DIVSVEAQIG WTTHGHTAVD VNVYGVGEVT EHLRGNMENI
     EIGQFMEIYL NVSLSDVTEK LKDAPIHGAP DRPSLVETSF SDRLVGFGAD LF
//
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