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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
 
 
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