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Prostatic acid phosphatase (EC 3.1.3.2)

 PPAP_BOVIN              Reviewed;         387 AA.
A6H730;
16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
24-JUL-2007, sequence version 1.
07-JUN-2017, entry version 62.
RecName: Full=Prostatic acid phosphatase;
EC=3.1.3.2;
Flags: Precursor;
Name=ACPP;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Fetal skin;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: A non-specific tyrosine phosphatase that
dephosphorylates a diverse number of substrates under acidic
conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate
monoesters and phosphorylated proteins. Has lipid phosphatase
activity and inactivates lysophosphatidic acid in seminal plasma
(By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate.
-!- SUBUNIT: Homodimer; dimer formation is required for phosphatase
activity. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P15309}.
-!- SIMILARITY: Belongs to the histidine acid phosphatase family.
{ECO:0000305}.
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EMBL; BC146093; AAI46094.1; -; mRNA.
RefSeq; NP_001092336.1; NM_001098866.1.
UniGene; Bt.61011; -.
ProteinModelPortal; A6H730; -.
SMR; A6H730; -.
STRING; 9913.ENSBTAP00000015451; -.
PaxDb; A6H730; -.
PRIDE; A6H730; -.
Ensembl; ENSBTAT00000015451; ENSBTAP00000015451; ENSBTAG00000011634.
GeneID; 504700; -.
KEGG; bta:504700; -.
CTD; 55; -.
eggNOG; KOG3720; Eukaryota.
eggNOG; ENOG410ZVBQ; LUCA.
GeneTree; ENSGT00530000062956; -.
HOGENOM; HOG000231439; -.
HOVERGEN; HBG002203; -.
InParanoid; A6H730; -.
KO; K19283; -.
OMA; YGIHKQK; -.
OrthoDB; EOG091G09FA; -.
TreeFam; TF312893; -.
Reactome; R-BTA-6798695; Neutrophil degranulation.
Proteomes; UP000009136; Chromosome 1.
Bgee; ENSBTAG00000011634; -.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0030175; C:filopodium; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:Ensembl.
GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0012506; C:vesicle membrane; ISS:UniProtKB.
GO; GO:0008253; F:5'-nucleotidase activity; ISS:UniProtKB.
GO; GO:0003993; F:acid phosphatase activity; ISS:UniProtKB.
GO; GO:0052642; F:lysophosphatidic acid phosphatase activity; ISS:UniProtKB.
GO; GO:0016791; F:phosphatase activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0042131; F:thiamine phosphate phosphatase activity; ISS:UniProtKB.
GO; GO:0046085; P:adenosine metabolic process; ISS:UniProtKB.
GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
GO; GO:0009117; P:nucleotide metabolic process; IEA:Ensembl.
GO; GO:0060168; P:positive regulation of adenosine receptor signaling pathway; IMP:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
GO; GO:0006144; P:purine nucleobase metabolic process; IEA:Ensembl.
GO; GO:0051930; P:regulation of sensory perception of pain; IDA:UniProtKB.
GO; GO:0006772; P:thiamine metabolic process; ISS:UniProtKB.
CDD; cd07061; HP_HAP_like; 1.
Gene3D; 3.40.50.1240; -; 1.
InterPro; IPR033379; Acid_Pase_AS.
InterPro; IPR000560; His_Pase_clade-2.
InterPro; IPR029033; His_PPase_superfam.
Pfam; PF00328; His_Phos_2; 1.
SUPFAM; SSF53254; SSF53254; 1.
PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein; Hydrolase;
Reference proteome; Secreted; Signal.
SIGNAL 1 34 {ECO:0000255}.
CHAIN 35 387 Prostatic acid phosphatase.
/FTId=PRO_0000356292.
ACT_SITE 46 46 Nucleophile. {ECO:0000250}.
ACT_SITE 292 292 Proton donor. {ECO:0000305}.
BINDING 45 45 Substrate. {ECO:0000250}.
BINDING 49 49 Substrate. {ECO:0000250}.
BINDING 113 113 Substrate. {ECO:0000250}.
BINDING 291 291 Substrate. {ECO:0000250}.
SITE 51 51 Important for substrate specificity.
{ECO:0000250}.
SITE 208 208 Required for structural stability.
{ECO:0000250}.
CARBOHYD 96 96 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 222 222 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 335 335 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 163 374 {ECO:0000250}.
DISULFID 217 315 {ECO:0000250}.
DISULFID 349 353 {ECO:0000250}.
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


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