ID   PPA1_SCHPO              Reviewed;         453 AA.
AC   P08091;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   16-JUN-2009, entry version 71.
DE   RecName: Full=Acid phosphatase;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=pho1; ORFNames=SPBP4G3.02;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=86140050; PubMed=3005272;
RA   Elliott S., Chang C., Schweingruber M.E., Schaller J., Rickli E.E.,
RA   Carbon J.;
RT   "Isolation and characterization of the structural gene for secreted
RT   acid phosphatase from Schizosaccharomyces pombe.";
RL   J. Biol. Chem. 261:2936-2941(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; 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.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall.
CC   -!- INDUCTION: Repressed by phosphate and weakly by thiamine.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
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DR   EMBL; M11857; AAA35321.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAB68657.1; -; Genomic_DNA.
DR   PIR; A25326; A25326.
DR   RefSeq; NP_596847.1; -.
DR   HSSP; P34755; 1QFX.
DR   GeneID; 2541339; -.
DR   KEGG; spo:SPBP4G3.02; -.
DR   NMPDR; fig|4896.1.peg.2713; -.
DR   GeneDB_Spombe; SPBP4G3.02; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-004819-MON; -.
DR   BRENDA; 3.1.3.2; 653.
DR   ArrayExpress; P08091; -.
DR   GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:GeneDB_SPombe.
DR   GO; GO:0009897; C:external side of plasma membrane; NAS:GeneDB_SPombe.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:EC.
DR   InterPro; IPR000560; Histidine_acid_Pase.
DR   InterPro; IPR016274; Histidine_acid_Pase_euk.
DR   Pfam; PF00328; Acid_phosphat_A; 1.
DR   PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   2: Evidence at transcript level;
KW   Cell wall; Complete proteome; Glycoprotein; Hydrolase; Secreted;
KW   Signal.
FT   SIGNAL        1     18
FT   CHAIN        19    453       Acid phosphatase.
FT                                /FTId=PRO_0000023951.
FT   ACT_SITE     69     69       Nucleophile (By similarity).
FT   ACT_SITE    331    331       Proton donor (By similarity).
FT   CARBOHYD     95     95       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    151    151       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    183    183       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    193    193       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    243    243       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    319    319       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    410    410       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    429    429       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    443    443       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   453 AA;  50557 MW;  7CF891256EB154D1 CRC64;
     MFLQNLFLGF LAVVCANAQF AEFTAFDGKF DFKEHLTSRS PYHKPYFYGP SIDFPTTCKI
     KQVHTLQRHG SRNPTGGNAA FDAVGIANFQ QRLLNGSVPI DYSVSGNPLS FVPTWTPVIE
     AANADALSSS GRVELFDMGR QFYERYHELF NASTYNIYTA AQQRVVDSAL WYGYGMFGED
     VHNFTNYILV SENATAGSNS LSSYNACPAS DADDFTTPAL EAWRNVYMPP IRQRLNPYFS
     NYNLTNDDIL NLYGICSYEI ALQDYSEFCK LFNSVDFLNF EYEGDLSFSY GMGNSVKWGS
     IFGGAYANSL ANSLRSVENN TQQVFFAFTH DANIIPVETA LGFFTDNTPE NPLPTSYQVH
     SHSMKASEFV PFAGNLITEL FQCEDSKYYV RHLVNEEVFP LSDCGFGPSN TSDGMCELYA
     YLNSPVRVNG TSNGIQNFDT LCNASAVAAV YPY
//