PPA3_SCHPO
ID PPA3_SCHPO Reviewed; 463 AA.
AC O60172;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Thiamine-repressible acid phosphatase SPBC21H7.03c;
DE EC=3.1.3.2;
DE Flags: Precursor;
GN ORFNames=SPBC21H7.03c;
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] {ECO:0000312|EMBL:CAA18863.1}
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 [2] {ECO:0000305}
RP INDUCTION.
RX PubMed=16278451; DOI=10.1128/ec.4.11.1840-1850.2005;
RA Jenkins C.C.L., Mata J., Crane R.F., Thomas B., Akoulitchev A., Baehler J.,
RA Norbury C.J.;
RT "Activation of AP-1-dependent transcription by a truncated translation
RT initiation factor.";
RL Eukaryot. Cell 4:1840-1850(2005).
CC -!- FUNCTION: May dephosphorylate thiamine phosphates.
CC {ECO:0000250|UniProtKB:Q01682}.
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 Evidence={ECO:0000250|UniProtKB:Q01682};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:Q01682}.
CC -!- INDUCTION: Repressed by thiamine. {ECO:0000269|PubMed:16278451}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000255}.
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DR EMBL; CU329671; CAA18863.1; -; Genomic_DNA.
DR PIR; T39929; T39929.
DR RefSeq; NP_595928.1; NM_001021836.2.
DR AlphaFoldDB; O60172; -.
DR SMR; O60172; -.
DR STRING; 4896.SPBC21H7.03c.1; -.
DR MaxQB; O60172; -.
DR PaxDb; O60172; -.
DR EnsemblFungi; SPBC21H7.03c.1; SPBC21H7.03c.1:pep; SPBC21H7.03c.
DR GeneID; 2540420; -.
DR KEGG; spo:SPBC21H7.03c; -.
DR PomBase; SPBC21H7.03c; -.
DR VEuPathDB; FungiDB:SPBC21H7.03c; -.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_020880_0_1_1; -.
DR InParanoid; O60172; -.
DR OMA; KSLHSPW; -.
DR PhylomeDB; O60172; -.
DR PRO; PR:O60172; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0003993; F:acid phosphatase activity; IBA:GO_Central.
DR GO; GO:0052745; F:inositol phosphate phosphatase activity; ISS:PomBase.
DR GO; GO:0006112; P:energy reserve metabolic process; NAS:PomBase.
DR GO; GO:0043647; P:inositol phosphate metabolic process; ISS:PomBase.
DR GO; GO:0046434; P:organophosphate catabolic process; ISS: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 2: Evidence at transcript level;
KW Cell wall; Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..463
FT /note="Thiamine-repressible acid phosphatase SPBC21H7.03c"
FT /id="PRO_0000311718"
FT ACT_SITE 69
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P07102"
FT ACT_SITE 341
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P15309"
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 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
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; 52759 MW; 6C41AF422C6D624A CRC64;
MQLCIISLWF LAAFIVNADN VQFEDYESNF FFKEHLGTLS PYHEPYFDGL DSAFPETCEI
QQVHLLQRHG SRNPTGDVTA TDVYSSQYLN NFQEKLLNGS IPVNFSYPEN PLCFIKQWTP
VIDAENADQL SSRGRLELFD LGRQLYQRYY KLFDSYVYDI NTAEQERVVE SAKWFTYGLF
GDKMYEKTNF ILISEGKAAG ANSLSMYNAC PVFKDNNFHK NATDAAHAVW RNIFIEPIVN
RLAKYFDSSY KLTINDVRSL FYICEYEIAI KDHSDFCSIF TPSEFLNFEY DSDLDQAYGG
GPVSEWASTL GGAYINNLAD SLRNVTNPDF DRKVFLAFTH DSNIIPVEAA LGFFPDITPQ
NPLPTDKNIY TYSQKTSSFV PFAGNLITEL FFCSDSKYYV RHLVNQQVYP LIDCGYGPSG
TSDGLCELQA YLNSPIRANS TSNGISIFNT ECQARPTNVT IYF