PPA3_YEAST
ID PPA3_YEAST Reviewed; 467 AA.
AC P24031; D6VQ93;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Constitutive acid phosphatase;
DE EC=3.1.3.2;
DE Flags: Precursor;
GN Name=PHO3; OrderedLocusNames=YBR092C; ORFNames=YBR0813;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6093051; DOI=10.1093/nar/12.20.7721;
RA Bajwa W., Meyhack B., Rudolph H., Schweingruber A.-M., Hinnen A.;
RT "Structural analysis of the two tandemly repeated acid phosphatase genes in
RT yeast.";
RL Nucleic Acids Res. 12:7721-7739(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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 -!- MISCELLANEOUS: Present with 952 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; X01080; CAA25557.1; -; Genomic_DNA.
DR EMBL; X78993; CAA55597.1; -; Genomic_DNA.
DR EMBL; Z35961; CAA85045.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07213.1; -; Genomic_DNA.
DR PIR; S48259; PABYCC.
DR RefSeq; NP_009650.1; NM_001178440.1.
DR AlphaFoldDB; P24031; -.
DR SMR; P24031; -.
DR BioGRID; 32798; 74.
DR STRING; 4932.YBR092C; -.
DR iPTMnet; P24031; -.
DR MaxQB; P24031; -.
DR PaxDb; P24031; -.
DR PRIDE; P24031; -.
DR EnsemblFungi; YBR092C_mRNA; YBR092C; YBR092C.
DR GeneID; 852389; -.
DR KEGG; sce:YBR092C; -.
DR SGD; S000000296; PHO3.
DR VEuPathDB; FungiDB:YBR092C; -.
DR eggNOG; KOG1382; Eukaryota.
DR GeneTree; ENSGT00390000018409; -.
DR HOGENOM; CLU_020880_3_1_1; -.
DR InParanoid; P24031; -.
DR OMA; TGEMDAK; -.
DR BioCyc; YEAST:YBR092C-MON; -.
DR BRENDA; 3.1.3.2; 984.
DR PRO; PR:P24031; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P24031; protein.
DR GO; GO:0030287; C:cell wall-bounded periplasmic space; IMP:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0003993; F:acid phosphatase activity; IMP:SGD.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IDA:SGD.
DR GO; GO:0042723; P:thiamine-containing compound metabolic process; IDA:SGD.
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 Glycoprotein; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..467
FT /note="Constitutive acid phosphatase"
FT /id="PRO_0000023953"
FT ACT_SITE 75
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 338
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
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 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 219..221
FT /note="DED -> MKT (in Ref. 1; CAA25557)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 52777 MW; 05FBB80DEB41B0FF CRC64;
MFKSVVYSVL AAALVNAGTI PLGELADVAK IGTQEDIFPF LGGAGPYFSF PGDYGISRDL
PEGCEMKQLQ MLARHGERYP TYSKGATIMK TWYKLSNYTR QFNGSLSFLN DDYEFFIRDD
DDLEMETTFA NSDNVLNPYT GEMDAKRHAR EFLAQYGYMF ENQTSFPIFA ASSERVHDTA
QYFIDGLGDQ FNISLQTVSE AMSAGANTLS AGNACPGWDE DANDDILDKY DTTYLDDIAK
RLNKENKGLN LTSKDANTLF AWCAYELNAR GYSDVCDIFT EDELVRYSYG QDLVSFYQDG
PGYDMIRSVG ANLFNATLKL LKQSETQDLK VWLSFTHDTD ILNYLTTAGI IDDKNNLTAE
YVPFMGNTFH KSWYVPQGAR VYTEKFQCSN DTYVRYVIND AVVPIETCST GPGFSCEIND
FYDYAEKRVA GTDFLKVCNV SSVSNVTELT FYWDWNTTHY NDTLLKQ
