ID   PPA1_SCHPO              Reviewed;         453 AA.
AC   P08091; Q9UTX1;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Acid phosphatase;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=pho1; ORFNames=SPBP4G3.02;
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].
RX   PubMed=3005272; DOI=10.1016/s0021-9258(17)35876-3;
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 acid
RT   phosphatase from Schizosaccharomyces pombe.";
RL   J. Biol. Chem. 261:2936-2941(1986).
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 88-285.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
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: Secreted, cell wall.
CC   -!- INDUCTION: Repressed by phosphate and weakly by thiamine.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; M11857; AAA35321.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAB68657.1; -; Genomic_DNA.
DR   EMBL; AB027949; BAA87253.1; -; Genomic_DNA.
DR   PIR; A25326; A25326.
DR   RefSeq; NP_596847.1; NM_001023870.2.
DR   AlphaFoldDB; P08091; -.
DR   SMR; P08091; -.
DR   BioGRID; 277850; 21.
DR   STRING; 284812.P08091; -.
DR   GlyCosmos; P08091; 9 sites, No reported glycans.
DR   iPTMnet; P08091; -.
DR   MaxQB; P08091; -.
DR   PaxDb; 4896-SPBP4G3-02-1; -.
DR   EnsemblFungi; SPBP4G3.02.1; SPBP4G3.02.1:pep; SPBP4G3.02.
DR   GeneID; 2541339; -.
DR   KEGG; spo:SPBP4G3.02; -.
DR   PomBase; SPBP4G3.02; pho1.
DR   VEuPathDB; FungiDB:SPBP4G3.02; -.
DR   eggNOG; KOG1382; Eukaryota.
DR   HOGENOM; CLU_020880_3_1_1; -.
DR   InParanoid; P08091; -.
DR   OMA; YERYHEL; -.
DR   PhylomeDB; P08091; -.
DR   PRO; PR:P08091; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0030287; C:cell wall-bounded periplasmic space; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR   GO; GO:0005576; C:extracellular region; IDA:PomBase.
DR   GO; GO:0009277; C:fungal-type cell wall; ISO:PomBase.
DR   GO; GO:0016020; C:membrane; IDA:PomBase.
DR   GO; GO:0003993; F:acid phosphatase activity; IMP:PomBase.
DR   GO; GO:0046434; P:organophosphate catabolic process; IMP:PomBase.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR016274; Histidine_acid_Pase_euk.
DR   PANTHER; PTHR20963:SF56; ACID PHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 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; Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT   CHAIN           19..453
FT                   /note="Acid phosphatase"
FT                   /id="PRO_0000023951"
FT   ACT_SITE        69
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        331
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        243
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        410
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        443
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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
//