ID   PPA2_SCHPO              Reviewed;         463 AA.
AC   Q01682; Q9UU70;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Thiamine-repressible acid phosphatase pho4;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=pho4; ORFNames=SPBC428.03c;
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], AND PROTEIN SEQUENCE OF 19-30.
RX   PubMed=2249257; DOI=10.1007/bf00318392;
RA   Yang J., Schweingruber M.E.;
RT   "The structural gene coding for thiamin-repressible acid phosphatase in
RT   Schizosaccharomyces pombe.";
RL   Curr. Genet. 18:269-272(1990).
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 1-71.
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   -!- FUNCTION: May dephosphorylate thiamine phosphates.
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 thiamine.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; X56939; CAA40258.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA22278.1; -; Genomic_DNA.
DR   EMBL; AB027777; BAA87081.1; -; Genomic_DNA.
DR   PIR; S14119; S14119.
DR   RefSeq; NP_595181.1; NM_001021089.2.
DR   AlphaFoldDB; Q01682; -.
DR   SMR; Q01682; -.
DR   BioGRID; 277132; 16.
DR   STRING; 284812.Q01682; -.
DR   GlyCosmos; Q01682; 9 sites, No reported glycans.
DR   iPTMnet; Q01682; -.
DR   MaxQB; Q01682; -.
DR   PaxDb; 4896-SPBC428-03c-1; -.
DR   EnsemblFungi; SPBC428.03c.1; SPBC428.03c.1:pep; SPBC428.03c.
DR   GeneID; 2540606; -.
DR   KEGG; spo:SPBC428.03c; -.
DR   PomBase; SPBC428.03c; pho4.
DR   VEuPathDB; FungiDB:SPBC428.03c; -.
DR   eggNOG; KOG1382; Eukaryota.
DR   HOGENOM; CLU_020880_0_1_1; -.
DR   InParanoid; Q01682; -.
DR   OMA; GTSPWCG; -.
DR   PhylomeDB; Q01682; -.
DR   BRENDA; 3.1.3.100; 5613.
DR   PRO; PR:Q01682; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0030287; C:cell wall-bounded periplasmic space; ISO:PomBase.
DR   GO; GO:0005576; C:extracellular region; ISO:PomBase.
DR   GO; GO:0009277; C:fungal-type cell wall; ISO:PomBase.
DR   GO; GO:0003993; F:acid phosphatase activity; IMP:PomBase.
DR   GO; GO:0016791; F:phosphatase activity; IDA:PomBase.
DR   GO; GO:0042131; F:thiamine phosphate phosphatase activity; IMP:PomBase.
DR   GO; GO:0036172; P:thiamine salvage; 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   1: Evidence at protein level;
KW   Cell wall; Direct protein sequencing; Glycoprotein; Hydrolase;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:2249257"
FT   CHAIN           19..463
FT                   /note="Thiamine-repressible acid phosphatase pho4"
FT                   /id="PRO_0000023952"
FT   ACT_SITE        69
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        341
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        328
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        439
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        458
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   463 AA;  52119 MW;  F48EAFF8BB6B234A CRC64;
     MKLSGISLWL LAASIVHAGK SQFEAFENEF YFKDHLGTIS VYHEPYFNGP TTSFPESCAI
     KQVHLLQRHG SRNPTGDDTA TDVSSAQYID IFQNKLLNGS IPVNFSYPEN PLYFVKHWTP
     VIKAENADQL SSSGRIELFD LGRQVFERYY ELFDTDVYDI NTAAQERVVD SAEWFSYGMF
     GDDMQNKTNF IVLPEDDSAG ANSLAMYYSC PVYEDNNIDE NTTEAAHTSW RNVFLKPIAN
     RLNKYFDSGY NLTVSDVRSL YYICVYEIAL RDNSDFCSLF TPSEFLNFEY DSDLDYAYWG
     GPASEWASTL GGAYVNNLAN NLRKGVNNAS DRKVFLAFTH DSQIIPVEAA LGFFPDITPE
     HPLPTDKNIF TYSLKTSSFV PFAGNLITEL FLCSDNKYYV RHLVNQQVYP LTDCGYGPSG
     ASDGLCELSA YLNSSVRVNS TSNGIANFNS QCQAHSTNVT VYY
//