Prostatic acid phosphatase

Details

Name
Prostatic acid phosphatase
Synonyms
  • 3.1.3.2
  • 5'-NT
  • 5'-nucleotidase
  • Ecto-5'-nucleotidase
  • PAP
  • Thiamine monophosphatase
  • TMPase
Gene Name
ACPP
Organism
Humans
Amino acid sequence
>lcl|BSEQ0002193|Prostatic acid phosphatase
MRAAPLLLARAASLSLGFLFLLFFWLDRSVLAKELKFVTLVFRHGDRSPIDTFPTDPIKE
SSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNL
AALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKR
LHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSE
LSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMAL
DVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELV
GPVIPQDWSTECMTTNSHQGTEDSTD
Number of residues
386
Molecular Weight
44565.715
Theoretical pI
6.19
GO Classification
Functions
5'-nucleotidase activity / acid phosphatase activity / identical protein binding / lysophosphatidic acid phosphatase activity / phosphatase activity / thiamine phosphate phosphatase activity
Processes
adenosine metabolic process / dephosphorylation / nucleotide metabolic process / positive regulation of adenosine receptor signaling pathway / purine nucleobase metabolic process / regulation of sensory perception of pain / thiamine metabolic process
Components
extracellular exosome / extracellular space / filopodium / integral component of membrane / intracellular / lysosomal membrane / nucleus / plasma membrane / vesicle membrane
General Function
Thiamine phosphate phosphatase activity
Specific 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.Isoform 2: the cellular form also has ecto-5'-nucleotidase activity in dorsal root ganglion (DRG) neurons. Generates adenosine from AMP which acts as a pain suppressor. Acts as a tumor suppressor of prostate cancer through dephosphorylation of ERBB2 and deactivation of MAPK-mediated signaling.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0016316|Prostatic acid phosphatase (ACPP)
ATGAGAGCTGCACCCCTCCTCCTGGCCAGGGCAGCAAGCCTTAGCCTTGGCTTCTTGTTT
CTGCTTTTTTTCTGGCTAGACCGAAGTGTACTAGCCAAGGAGTTGAAGTTTGTGACTTTG
GTGTTTCGGCATGGAGACCGAAGTCCCATTGACACCTTTCCCACTGACCCCATAAAGGAA
TCCTCATGGCCACAAGGATTTGGCCAACTCACCCAGCTGGGCATGGAGCAGCATTATGAA
CTTGGAGAGTATATAAGAAAGAGATATAGAAAATTCTTGAATGAGTCCTATAAACATGAA
CAGGTTTATATTCGAAGCACAGACGTTGACCGGACTTTGATGAGTGCTATGACAAACCTG
GCAGCCCTGTTTCCCCCAGAAGGTGTCAGCATCTGGAATCCTATCCTACTCTGGCAGCCC
ATCCCGGTGCACACAGTTCCTCTTTCTGAAGATCAGTTGCTATACCTGCCTTTCAGGAAC
TGCCCTCGTTTTCAAGAACTTGAGAGTGAGACTTTGAAATCAGAGGAATTCCAGAAGAGG
CTGCACCCTTATAAGGATTTTATAGCTACCTTGGGAAAACTTTCAGGATTACATGGCCAG
GACCTTTTTGGAATTTGGAGTAAAGTCTACGACCCTTTATATTGTGAGAGTGTTCACAAT
TTCACTTTACCCTCCTGGGCCACTGAGGACACCATGACTAAGTTGAGAGAATTGTCAGAA
TTGTCCCTCCTGTCCCTCTATGGAATTCACAAGCAGAAAGAGAAATCTAGGCTCCAAGGG
GGTGTCCTGGTCAATGAAATCCTCAATCACATGAAGAGAGCAACTCAGATACCAAGCTAC
AAAAAACTCATCATGTATTCTGCGCATGACACTACTGTGAGTGGCCTACAGATGGCGCTA
GATGTTTACAACGGACTCCTTCCTCCCTATGCTTCTTGCCACTTGACGGAATTGTACTTT
GAGAAGGGGGAGTACTTTGTGGAGATGTACTATCGGAATGAGACGCAGCACGAGCCGTAT
CCCCTCATGCTACCTGGCTGCAGCCCCAGCTGTCCTCTGGAGAGGTTTGCTGAGCTGGTT
GGCCCTGTGATCCCTCAAGACTGGTCCACGGAGTGTATGACCACAAACAGCCATCAAGGT
ACTGAAGACAGTACAGATTAG
Chromosome Location
3
Locus
3q21-q23
External Identifiers
ResourceLink
UniProtKB IDP15309
UniProtKB Entry NamePPAP_HUMAN
GenBank Protein ID189613
GenBank Gene IDM97589
GenAtlas IDACPP
HGNC IDHGNC:125
General References
  1. Sharief FS, Li SS: Structure of human prostatic acid phosphatase gene. Biochem Biophys Res Commun. 1992 May 15;184(3):1468-76. [Article]
  2. Van Etten RL, Davidson R, Stevis PE, MacArthur H, Moore DL: Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase. J Biol Chem. 1991 Feb 5;266(4):2313-9. [Article]
  3. Sharief FS, Lee H, Leuderman MM, Lundwall A, Deaven LL, Lee CL, Li SS: Human prostatic acid phosphatase: cDNA cloning, gene mapping and protein sequence homology with lysosomal acid phosphatase. Biochem Biophys Res Commun. 1989 Apr 14;160(1):79-86. [Article]
  4. Vihko P, Virkkunen P, Henttu P, Roiko K, Solin T, Huhtala ML: Molecular cloning and sequence analysis of cDNA encoding human prostatic acid phosphatase. FEBS Lett. 1988 Aug 29;236(2):275-81. [Article]
  5. Tailor PG, Govindan MV, Patel PC: Nucleotide sequence of human prostatic acid phosphatase determined from a full-length cDNA clone. Nucleic Acids Res. 1990 Aug 25;18(16):4928. [Article]
  6. Sharief FS, Li SS: Nucleotide sequence of human prostatic acid phosphatase ACPP gene, including seven Alu repeats. Biochem Mol Biol Int. 1994 Jun;33(3):561-5. [Article]
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  10. Risley JM, Van Etten RL: Structures of the carbohydrate moieties of human prostatic acid phosphatase elucidated by H1 nuclear magnetic resonance spectroscopy. Arch Biochem Biophys. 1987 Nov 1;258(2):404-12. [Article]
  11. Zhang Z, Ostanin K, Van Etten RL: Covalent modification and site-directed mutagenesis of an active site tryptophan of human prostatic acid phosphatase. Acta Biochim Pol. 1997;44(4):659-72. [Article]
  12. Tanaka M, Kishi Y, Takanezawa Y, Kakehi Y, Aoki J, Arai H: Prostatic acid phosphatase degrades lysophosphatidic acid in seminal plasma. FEBS Lett. 2004 Jul 30;571(1-3):197-204. [Article]
  13. Quintero IB, Araujo CL, Pulkka AE, Wirkkala RS, Herrala AM, Eskelinen EL, Jokitalo E, Hellstrom PA, Tuominen HJ, Hirvikoski PP, Vihko PT: Prostatic acid phosphatase is not a prostate specific target. Cancer Res. 2007 Jul 15;67(14):6549-54. [Article]
  14. Munch J, Rucker E, Standker L, Adermann K, Goffinet C, Schindler M, Wildum S, Chinnadurai R, Rajan D, Specht A, Gimenez-Gallego G, Sanchez PC, Fowler DM, Koulov A, Kelly JW, Mothes W, Grivel JC, Margolis L, Keppler OT, Forssmann WG, Kirchhoff F: Semen-derived amyloid fibrils drastically enhance HIV infection. Cell. 2007 Dec 14;131(6):1059-71. [Article]
  15. Schroder B, Wrocklage C, Pan C, Jager R, Kosters B, Schafer H, Elsasser HP, Mann M, Hasilik A: Integral and associated lysosomal membrane proteins. Traffic. 2007 Dec;8(12):1676-86. Epub 2007 Sep 26. [Article]
  16. Hong S, Klein EA, Das Gupta J, Hanke K, Weight CJ, Nguyen C, Gaughan C, Kim KA, Bannert N, Kirchhoff F, Munch J, Silverman RH: Fibrils of prostatic acid phosphatase fragments boost infections with XMRV (xenotropic murine leukemia virus-related virus), a human retrovirus associated with prostate cancer. J Virol. 2009 Jul;83(14):6995-7003. doi: 10.1128/JVI.00268-09. Epub 2009 Apr 29. [Article]
  17. Hauber I, Hohenberg H, Holstermann B, Hunstein W, Hauber J: The main green tea polyphenol epigallocatechin-3-gallate counteracts semen-mediated enhancement of HIV infection. Proc Natl Acad Sci U S A. 2009 Jun 2;106(22):9033-8. doi: 10.1073/pnas.0811827106. Epub 2009 May 18. [Article]
  18. Roan NR, Sowinski S, Munch J, Kirchhoff F, Greene WC: Aminoquinoline surfen inhibits the action of SEVI (semen-derived enhancer of viral infection). J Biol Chem. 2010 Jan 15;285(3):1861-9. doi: 10.1074/jbc.M109.066167. Epub 2009 Nov 6. [Article]
  19. Chuang TD, Chen SJ, Lin FF, Veeramani S, Kumar S, Batra SK, Tu Y, Lin MF: Human prostatic acid phosphatase, an authentic tyrosine phosphatase, dephosphorylates ErbB-2 and regulates prostate cancer cell growth. J Biol Chem. 2010 Jul 30;285(31):23598-606. doi: 10.1074/jbc.M109.098301. Epub 2010 May 24. [Article]
  20. Graddis TJ, McMahan CJ, Tamman J, Page KJ, Trager JB: Prostatic acid phosphatase expression in human tissues. Int J Clin Exp Pathol. 2011 Mar;4(3):295-306. Epub 2011 Mar 22. [Article]
  21. LaCount MW, Handy G, Lebioda L: Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase. J Biol Chem. 1998 Nov 13;273(46):30406-9. [Article]
  22. Jakob CG, Lewinski K, Kuciel R, Ostrowski W, Lebioda L: Crystal structure of human prostatic acid phosphatase . Prostate. 2000 Feb 15;42(3):211-8. [Article]
  23. Ortlund E, LaCount MW, Lebioda L: Crystal structures of human prostatic acid phosphatase in complex with a phosphate ion and alpha-benzylaminobenzylphosphonic acid update the mechanistic picture and offer new insights into inhibitor design. Biochemistry. 2003 Jan 21;42(2):383-9. [Article]
  24. Nanga RP, Brender JR, Vivekanandan S, Popovych N, Ramamoorthy A: NMR structure in a membrane environment reveals putative amyloidogenic regions of the SEVI precursor peptide PAP(248-286). J Am Chem Soc. 2009 Dec 16;131(49):17972-9. doi: 10.1021/ja908170s. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03390(2R,3R)-2,3-Dihydroxy-4-oxo-4-(propylamino)butanoic acidexperimentalunknownDetails
DB03577Alpha-Benzyl-Aminobenzyl-Phosphonic AcidexperimentalunknownDetails
DB06688Sipuleucel-Tapproved, investigationalyesotherDetails