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Showing Protein Salivary acidic proline-rich phosphoprotein 1/2 (HMDBP07956)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP07956
Secondary Accession Numbers
  • 13667
Name Salivary acidic proline-rich phosphoprotein 1/2
Synonyms
  1. Db-F
  2. Db-s
  3. PIF-F
  4. PIF-S
  5. PRP-1/PRP-2
  6. PRP-3/PRP-4
  7. Pa
  8. Parotid acidic protein
  9. Parotid double-band protein
  10. Parotid isoelectric focusing variant protein
  11. Parotid proline-rich protein 1/2
  12. Peptide P-C
  13. Pr1/Pr2
  14. Protein A
  15. Protein C
  16. Salivary acidic proline-rich phosphoprotein 1/2
  17. Salivary acidic proline-rich phosphoprotein 3/4
Gene Name PRH1
Protein Type Unknown
Biological Properties
General Function Involved in protein binding
Specific Function PRP's act as highly potent inhibitors of crystal growth of calcium phosphates. They provide a protective and reparative environment for dental enamel which is important for the integrity of the teeth
Pathways Not Available
Reactions Not Available
GO Classification Not Available
Cellular Location
  1. Secreted
Gene Properties
Chromosome Location Chromosome:1
Locus 12p13.2
SNPs PRH1
Gene Sequence 
>501 bp
ATGCTTCTGATTCTGCTGTCAGTGGCCCTGCTGGCCTTCAGCTCAGCTCAGGACTTAGAT
GAAGATGTCAGCCAAGAAGACGTTCCCTTGGTAATATCAGATGGAGGAGACTCTGAGCAG
TTCATAGATGAGGAGCGTCAGGGACCACCTTTGGGAGGACAGCAATCTCAACCCTCTGCT
GGTGATGGGAACCAGGATGATGGCCCTCAGCAGGGACCACCCCAACAAGGAGGCCAGCAG
CAACAAGGTCCACCACCTCCTCAGGGAAAGCCACAAGGACCACCCCAACAGGGAGGCCAT
CCCCCTCCTCCTCAAGGAAGGCCACAAGGACCACCCCAACAGGGAGGCCATCCCCGTCCT
CCTCGAGGAAGGCCACAAGGACCACCCCAACAGGGAGGCCATCAGCAAGGTCCTCCCCCA
CCTCCTCCTGGAAAGCCCCAGGGACCACCTCCCCAAGGGGGCCGCCCACAAGGACCTCCA
CAGGGGCAGTCTCCTCAGTAA
Protein Properties
Number of Residues 166
Molecular Weight 17016.5
Theoretical pI 4.43
Pfam Domain Function Not Available
Signals
  • 1-16
Transmembrane Regions
  • None
Protein Sequence 
>Salivary acidic proline-rich phosphoprotein 1/2
MLLILLSVALLAFSSAQDLDEDVSQEDVPLVISDGGDSEQFIDEERQGPPLGGQQSQPSA
GDGNQDDGPQQGPPQQGGQQQQGPPPPQGKPQGPPQQGGHPPPPQGRPQGPPQQGGHPRP
PRGRPQGPPQQGGHQQGPPPPPPGKPQGPPPQGGRPQGPPQGQSPQ
GenBank ID Protein 66267613
UniProtKB/Swiss-Prot ID P02810
UniProtKB/Swiss-Prot Entry Name PRPC_HUMAN
PDB IDs Not Available
GenBank Gene ID BC095488
GeneCard ID PRH1
GenAtlas ID PRH1
HGNC ID HGNC:9366
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  3. Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. doi: 10.1021/ac801708p. [PubMed:19007248 ]
  4. Maeda N, Kim HS, Azen EA, Smithies O: Differential RNA splicing and post-translational cleavages in the human salivary proline-rich protein gene system. J Biol Chem. 1985 Sep 15;260(20):11123-30. [PubMed:2993301 ]
  5. Kim HS, Maeda N: Structures of two HaeIII-type genes in the human salivary proline-rich protein multigene family. J Biol Chem. 1986 May 25;261(15):6712-8. [PubMed:3009472 ]
  6. Wong RS, Bennick A: The primary structure of a salivary calcium-binding proline-rich phosphoprotein (protein C), a possible precursor of a related salivary protein A. J Biol Chem. 1980 Jun 25;255(12):5943-8. [PubMed:7380845 ]
  7. Schlesinger DH, Hay DI: Complete covalent structure of a proline-rich phosphoprotein, PRP-2, an inhibitor of calcium phosphate crystal growth from human parotid saliva. Int J Pept Protein Res. 1986 Apr;27(4):373-9. [PubMed:3710693 ]
  8. Azen EA, Kim HS, Goodman P, Flynn S, Maeda N: Alleles at the PRH1 locus coding for the human salivary-acidic proline-rich proteins Pa, Db, and PIF. Am J Hum Genet. 1987 Dec;41(6):1035-47. [PubMed:3687941 ]
  9. Hay DI, Bennick A, Schlesinger DH, Minaguchi K, Madapallimattam G, Schluckebier SK: The primary structures of six human salivary acidic proline-rich proteins (PRP-1, PRP-2, PRP-3, PRP-4, PIF-s and PIF-f). Biochem J. 1988 Oct 1;255(1):15-21. [PubMed:3196309 ]
  10. Wong RS, Hofmann T, Bennick A: The complete primary structure of a proline-rich phosphoprotein from human saliva. J Biol Chem. 1979 Jun 10;254(11):4800-8. [PubMed:438215 ]
  11. Schlesinger DH, Hay DI: Primary structure of the active tryptic fragments of human and monkey salivary anionic proline-rich proteins. Int J Pept Protein Res. 1981 Jan;17(1):34-41. [PubMed:7228490 ]
  12. Inzitari R, Cabras T, Onnis G, Olmi C, Mastinu A, Sanna MT, Pellegrini MG, Castagnola M, Messana I: Different isoforms and post-translational modifications of human salivary acidic proline-rich proteins. Proteomics. 2005 Feb;5(3):805-15. [PubMed:15693058 ]
  13. Isemura S, Saitoh E, Sanada K: The amino acid sequence of a salivary proline-rich peptide, P-C, and its relation to a salivary proline-rich phosphoprotein, protein C. J Biochem. 1980 Apr;87(4):1071-7. [PubMed:7390979 ]
  14. Kauffman DL, Bennick A, Blum M, Keller PJ: Basic proline-rich proteins from human parotid saliva: relationships of the covalent structures of ten proteins from a single individual. Biochemistry. 1991 Apr 9;30(14):3351-6. [PubMed:1849422 ]
  15. Jonsson AP, Griffiths WJ, Bratt P, Johansson I, Stromberg N, Jornvall H, Bergman T: A novel Ser O-glucuronidation in acidic proline-rich proteins identified by tandem mass spectrometry. FEBS Lett. 2000 Jun 16;475(2):131-4. [PubMed:10858503 ]
  16. Azen EA: A frequent mutation in the acidic proline-rich protein gene, PRH2, causing a Q147K change closely adjacent to the bacterial binding domain of the cognate salivary PRP (Pr1') in Afro-Americans. Mutations in brief no. 154. Online. Hum Mutat. 1998;12(1):72. [PubMed:10627138 ]