PPA2_SCHPO
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 03-AUG-2022, entry version 153.
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; 4896.SPBC428.03c.1; -.
DR MaxQB; Q01682; -.
DR PaxDb; Q01682; -.
DR PRIDE; Q01682; -.
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; ILYHLGG; -.
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:0009228; P:thiamine biosynthetic process; IMP:PomBase.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; -; 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 Pfam; PF00328; His_Phos_2; 1.
DR PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR SUPFAM; SSF53254; SSF53254; 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
