PPA_ASPFI
ID PPA_ASPFI Reviewed; 614 AA.
AC Q12546;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Acid phosphatase;
DE EC=3.1.3.2;
DE AltName: Full=APase6;
DE AltName: Full=pH 6-optimum acid phosphatase;
DE Flags: Precursor;
GN Name=aphA;
OS Aspergillus ficuum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=5058;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 66876 / DSM 932 / SRRC 265 / NRRL 3135;
RX PubMed=7557398; DOI=10.1016/0378-1119(95)00298-k;
RA Mullaney E.J., Daly C.B., Ehrlich K.C., Ullah A.H.J.;
RT "The Aspergillus niger (ficuum) aphA gene encodes a pH 6.0-optimum acid
RT phosphatase.";
RL Gene 162:117-121(1995).
RN [2]
RP PROTEIN SEQUENCE OF 23-605.
RC STRAIN=ATCC 66876 / DSM 932 / SRRC 265 / NRRL 3135;
RX PubMed=8074654; DOI=10.1006/bbrc.1994.2166;
RA Ullah A.H.J., Mullaney E.M., Dischinger H.C. Jr.;
RT "The complete primary structure elucidation of Aspergillus ficuum (niger),
RT pH 6.0, optimum acid phosphatase by Edman degradation.";
RL Biochem. Biophys. Res. Commun. 203:182-189(1994).
RN [3]
RP PROTEIN SEQUENCE OF 23-56, AND CHARACTERIZATION.
RC STRAIN=ATCC 66876 / DSM 932 / SRRC 265 / NRRL 3135;
RX PubMed=3375203; DOI=10.1080/00327488808062512;
RA Ullah A.H.J., Cummins B.J.;
RT "Aspergillus ficuum extracellular pH 6.0 optimum acid phosphatase:
RT purification, N-terminal amino acid sequence, and biochemical
RT characterization.";
RL Prep. Biochem. 18:37-65(1988).
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 -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000305};
CC -!- ACTIVITY REGULATION: Competitively inhibited by phosphomycin and
CC inorganic orthophosphate.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6. Inactive above pH 6.7.;
CC Temperature dependence:
CC Optimum temperature is 63 degrees Celsius.;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Glycosylated; probably with N-linked high-mannose
CC oligosaccharides.
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DR EMBL; U18553; AAA91632.1; -; Genomic_DNA.
DR PIR; JC2545; JC2545.
DR AlphaFoldDB; Q12546; -.
DR SMR; Q12546; -.
DR PRIDE; Q12546; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd00063; FN3; 1.
DR CDD; cd00839; MPP_PAPs; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR014390; Acid_Pase_Asper.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041792; MPP_PAP.
DR InterPro; IPR039331; PPA-like.
DR InterPro; IPR008963; Purple_acid_Pase-like_N.
DR InterPro; IPR015914; Purple_acid_Pase_N.
DR InterPro; IPR025733; Purple_acid_PPase_C_dom.
DR PANTHER; PTHR22953; PTHR22953; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF14008; Metallophos_C; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR PIRSF; PIRSF000900; Acid_Ptase_Asper; 1.
DR SUPFAM; SSF49363; SSF49363; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW Copper; Direct protein sequencing; Glycoprotein; Hydrolase; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:3375203,
FT ECO:0000269|PubMed:8074654"
FT CHAIN 23..605
FT /note="Acid phosphatase"
FT /id="PRO_0000023997"
FT PROPEP 606..614
FT /id="PRO_0000023998"
FT DOMAIN 80..176
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 614 AA; 67211 MW; 7016738F63C62EBE CRC64;
MKGTAASALL VALSATAAQA RPVVDERFPY TGPAVPIGDW VDPTINGNGK GFPRLVEPPA
VKPATANPRN NVNVISLSYI PKGMHIHYQT PFGLGQLPAV RWGKDPRNLN STAQGYSHTY
DRTPSCSQVK AVTQCSQFFH EVSIDGLEPD TTYYYQIPAA NGTTQSEVLS FKTSRPAGHP
GSFSVAVLND MGYTNAHGTH KQLVKAATEG TAFAWHGGDL SYADDWYSGI LACADDWPVC
YNGTSSTLPG GGPLPEEYKK PLPAGEIPDQ GGPQGGDMSV LYESNWDLWQ QWLNNVTLKI
PYMVLPGNHE ASCAEFDGPH NILTAYLNDD IANGTAPTDN LTYYSCPPSQ RNFTAYQHRF
RMPGPETGGV GNFWYSFDYG LAHFVSIDGE TDFANSPEWN FAEDVTGNET LPSESETFIT
DSGPFGNVNG SVHETKSYEQ WHWLQQDLAK VDRSKTPWVI VMSHRPMYSS AYSSYQLHVR
EAFEGLLLKY GVDAYLSGHI HWYERLYPLG ANGTIDTAAI VNNNTYYAHN GKSITHIING
MAGNIESHSE FSDGEGLTNI TALLDKVHYG FSKLTIFNET ALKWELIRGD DGTVGDSLTL
LKPSHVAGGK KLHS
