PPAP_BOVIN
ID PPAP_BOVIN Reviewed; 387 AA.
AC A6H730;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Prostatic acid phosphatase;
DE EC=3.1.3.2 {ECO:0000250|UniProtKB:P15309};
DE AltName: Full=Protein tyrosine phosphatase ACP3;
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:P15309};
DE Flags: Precursor;
GN Name=ACP3; Synonyms=ACPP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A non-specific tyrosine phosphatase that dephosphorylates a
CC diverse number of substrates under acidic conditions (pH 4-6) including
CC alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated
CC proteins. Has lipid phosphatase activity and inactivates
CC lysophosphatidic acid in seminal plasma (By similarity).
CC {ECO:0000250|UniProtKB:P15309}.
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:P15309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-
CC octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:75757; Evidence={ECO:0000250|UniProtKB:P15309};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836;
CC Evidence={ECO:0000250|UniProtKB:P15309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000250|UniProtKB:P15309};
CC -!- SUBUNIT: Homodimer; dimer formation is required for phosphatase
CC activity. {ECO:0000250|UniProtKB:P20646}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P15309}.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; BC146093; AAI46094.1; -; mRNA.
DR RefSeq; NP_001092336.1; NM_001098866.1.
DR AlphaFoldDB; A6H730; -.
DR SMR; A6H730; -.
DR STRING; 9913.ENSBTAP00000015451; -.
DR PaxDb; A6H730; -.
DR Ensembl; ENSBTAT00000015451; ENSBTAP00000015451; ENSBTAG00000011634.
DR GeneID; 504700; -.
DR KEGG; bta:504700; -.
DR CTD; 55; -.
DR VEuPathDB; HostDB:ENSBTAG00000011634; -.
DR VGNC; VGNC:52603; ACP3.
DR eggNOG; KOG3720; Eukaryota.
DR GeneTree; ENSGT00940000160450; -.
DR HOGENOM; CLU_030431_1_1_1; -.
DR InParanoid; A6H730; -.
DR OrthoDB; 1221585at2759; -.
DR TreeFam; TF312893; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000011634; Expressed in zone of skin and 53 other tissues.
DR ExpressionAtlas; A6H730; baseline.
DR GO; GO:0005615; C:extracellular space; ISS:CAFA.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:CAFA.
DR GO; GO:0012506; C:vesicle membrane; ISS:CAFA.
DR GO; GO:0008253; F:5'-nucleotidase activity; ISS:CAFA.
DR GO; GO:0003993; F:acid phosphatase activity; ISS:CAFA.
DR GO; GO:0052642; F:lysophosphatidic acid phosphatase activity; ISS:CAFA.
DR GO; GO:0016791; F:phosphatase activity; ISS:CAFA.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0042131; F:thiamine phosphate phosphatase activity; ISS:CAFA.
DR GO; GO:0046085; P:adenosine metabolic process; ISS:CAFA.
DR GO; GO:0016311; P:dephosphorylation; ISS:CAFA.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007040; P:lysosome organization; IBA:GO_Central.
DR GO; GO:0060168; P:positive regulation of adenosine receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IDA:UniProtKB.
DR GO; GO:0006772; P:thiamine metabolic process; ISS:CAFA.
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 Pfam; PF00328; His_Phos_2; 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 Disulfide bond; Glycoprotein; Hydrolase; Lipid metabolism;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT CHAIN 35..387
FT /note="Prostatic acid phosphatase"
FT /id="PRO_0000356292"
FT ACT_SITE 46
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 292
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20646"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20646"
FT SITE 51
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000250"
FT SITE 140
FT /note="Required for dimerization"
FT /evidence="ECO:0000250|UniProtKB:P20646"
FT SITE 146
FT /note="Required for dimerization"
FT /evidence="ECO:0000250|UniProtKB:P20646"
FT SITE 208
FT /note="Required for structural stability"
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 163..374
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT DISULFID 217..315
FT /evidence="ECO:0000250|UniProtKB:P15309"
FT DISULFID 349..353
FT /evidence="ECO:0000250|UniProtKB:P15309"
SQ SEQUENCE 387 AA; 44622 MW; 67241408CDEC7907 CRC64;
MRNAALLMTR ATSLRLSLLL LLSFLPDLDG GVRAKELRFV TLVFRHGDRS PIETFPNDPI
KESSWPQGFG QLTQLGMAQH YELGQYIRKR YENFLNESYK REQVHVRSTD IDRTLMSAMT
NLAALFPPEG ISIWNPSLPW QPIPVHTVPV SEDQLLYLPF RNCPRFQELQ SETLISEEFQ
KRLQPYKDFI EVLPKLTGYH DQDLLGIWSK VYDPLFCEGV HNFTLPSWAT EDTMTKLKEI
SELSLLSLYG IHKQKEKSRL QGGVLINEIL NHMKSATQPS NRRKLIMYSA HDTTVSGLQM
ALDVYNGILP PYASCHMMEL YFQDGEYFVE MYYRNETRYE PHPLTLPGCT PSCPLAKFVE
LVAPVISQDW SMECAIRNHK GTEDIIN
