PPAC_YEAST
ID PPAC_YEAST Reviewed; 467 AA.
AC P38693; D3DLH0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Acid phosphatase PHO12;
DE EC=3.1.3.2;
DE Flags: Precursor;
GN Name=PHO12; OrderedLocusNames=YHR215W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
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 -!- INDUCTION: S.cerevisiae has 2 types of acid phosphatase: one is
CC constitutive and the other is repressible by inorganic phosphate.
CC -!- PTM: Glycosylated during secretion across the membrane.
CC -!- MISCELLANEOUS: Present with 3290 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; U00029; AAB69729.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06914.1; -; Genomic_DNA.
DR PIR; S48996; S48996.
DR RefSeq; NP_012087.1; NM_001179346.1.
DR AlphaFoldDB; P38693; -.
DR SMR; P38693; -.
DR BioGRID; 36650; 26.
DR DIP; DIP-1325N; -.
DR IntAct; P38693; 2.
DR MINT; P38693; -.
DR STRING; 4932.YHR215W; -.
DR MaxQB; P38693; -.
DR PaxDb; P38693; -.
DR PRIDE; P38693; -.
DR EnsemblFungi; YHR215W_mRNA; YHR215W; YHR215W.
DR GeneID; 856625; -.
DR KEGG; sce:YHR215W; -.
DR SGD; S000001258; PHO12.
DR VEuPathDB; FungiDB:YHR215W; -.
DR eggNOG; KOG1382; Eukaryota.
DR GeneTree; ENSGT00390000018409; -.
DR HOGENOM; CLU_020880_3_1_1; -.
DR InParanoid; P38693; -.
DR BioCyc; YEAST:YHR215W-MON; -.
DR PRO; PR:P38693; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38693; protein.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0003993; F:acid phosphatase activity; 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:0000250"
FT CHAIN 18..467
FT /note="Acid phosphatase PHO12"
FT /id="PRO_0000023957"
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 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 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 467 AA; 52700 MW; BEC606CDF39B845B CRC64;
MLKSAVYSIL AASLVNAGTI PLGKLSDIDK IGTQTEIFPF LGGSGPYYSF PGDYGISRDL
PESCEMKQVQ MVGRHGERYP TVSKAKSIMT TWYKLSNYTG QFSGALSFLN DDYEFFIRDT
KNLEMETTLA NSVNVLNPYT GEMNAKRHAR DFLAQYGYMV ENQTSFAVFT SNSNRCHDTA
QYFIDGLGDK FNISLQTISE AESAGANTLS AHHSCPAWDD DVNDDILKKY DTKYLSGIAK
RLNKENKGLN LTSSDANTFF AWCAYEINAR GYSDICNIFT KDELVRFSYG QDLETYYQTG
PGYDVVRSVG ANLFNASVKL LKESEVQDQK VWLSFTHDTD ILNYLTTIGI IDDQNNLTAE
HVPFMENTFH RSWYVPQGAR VYTEKFQCSN DTYVRYVIND AVVPIETCST GPGFSCEIND
FYGYAEKRVA GTDFLKVCNV SSVSNSTELT FFWDWNTKHY NDTLLKQ
