ID   PHOA_PENCH              Reviewed;         412 AA.
AC   P37274;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Phosphate-repressible acid phosphatase;
DE            EC=3.1.3.2;
DE   Flags: Precursor;
GN   Name=PHOA;
OS   Penicillium chrysogenum (Penicillium notatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=5076;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1563629; DOI=10.1016/0378-1119(92)90680-n;
RA   Haas H., Redl B., Friedlin E., Stoeffler G.;
RT   "Isolation and analysis of the Penicillium chrysogenum phoA gene encoding a
RT   secreted phosphate-repressible acid phosphatase.";
RL   Gene 113:129-133(1992).
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.
CC   -!- PTM: The N-terminus is blocked.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M80366; AAA33693.1; -; Genomic_DNA.
DR   PIR; JN0319; JN0319.
DR   AlphaFoldDB; P37274; -.
DR   SMR; P37274; -.
DR   PhylomeDB; P37274; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.720.10; -; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR007312; Phosphoesterase.
DR   PANTHER; PTHR31956; PTHR31956; 1.
DR   Pfam; PF04185; Phosphoesterase; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..412
FT                   /note="Phosphate-repressible acid phosphatase"
FT                   /id="PRO_0000023979"
FT   ACT_SITE        215
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
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        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        332
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   412 AA;  45628 MW;  5659A7F07B1DDFD9 CRC64;
     MLTKQTLLAF VGALALATGT TTTEETPTQA EIDAARATAL PYSPVSNVKG LAFDRFVNIW
     LENTDFEPAA LDENLSKLAK EGILLTNYFA ISHPSQPNYC ASAGGDTFGM DNDDFLQIPS
     NVSTIADLFD TKHISWGEYQ EDMPYAGYQG KRYPLSGPNQ YVRKHNPLVL FNSVTDDAVR
     PRQIKNFTTF YDDLKHHSLP QHMFITPNMT NDAHDTNITV AGNWVDRFLS PLLKNEYFTK
     DSLVLLTFDE GDTYSYPNRV FSFLVGGAIP EHLKGTTDDT FYTHYSIVAS LSANWGLPSL
     GRWDCGANLL KMVADKTGYV NWEVDTSNVY LNETYPGPMS TDNYSSKWAV PATKGKCSAG
     HGIAEVVKNT YHGLQPTYDY ASPVPYDVTS GNNVGIKYHR TLVCILSCSS LS