P02810
uniprot
P02810
canonical
amino_acid_sequence
MLLILLSVALLAFSSAQDLDEDVSQEDVPLVISDGGDSEQFIDEERQGPPLGGQQSQPSAGDGNQNDGPQQGPPQQGGQQQQGPPPPQGKPQGPPQQGGHPPPPQGRPQGPPQQGGHPRPPRGRPQGPPQQGGHQQGPPPPPPGKPQGPPPQGGRPQGPPQGQSPQ
uniprot
proteins
function
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.
uniprot
proteins
mass_dalton
17015
uniprot
proteins
mutagenesis
MUTAGEN 24; /note="S->A: Decreased phosphorylation by FAM20C; when associated with A-38."; /evidence="ECO:0000269|PubMed:26091039"; MUTAGEN 38; /note="S->A: Decreased phosphorylation by FAM20C; when associated with A-24."; /evidence="ECO:0000269|PubMed:26091039
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved; PRP-2, PRP-1, PIF-S and Db-S yield PRP-4, PRP-3 (protein A), PIF-F and Db-F, respectively. {ECO:0000269|PubMed:18463091}.; PTM: A hexuronic acid was shown to be linked to Ser-33 in about 40% of the polypeptides. Neither the structure of the carbohydrate (whether glucuronic acid or an isomer of), nor the linkage (whether a glycoside or an ester) has been definitely established. {ECO:0000269|PubMed:10858503}.
uniprot
proteins
pubmed
10627138
uniprot
proteins
pubmed
10858503
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15693058
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18463091
uniprot
proteins
pubmed
1849422
uniprot
proteins
pubmed
20879038
uniprot
proteins
pubmed
26091039
uniprot
proteins
pubmed
2993301
uniprot
proteins
pubmed
3009472
uniprot
proteins
pubmed
3196309
uniprot
proteins
pubmed
3687941
uniprot
proteins
pubmed
3710693
uniprot
proteins
pubmed
438215
uniprot
proteins
pubmed
7228490
uniprot
proteins
pubmed
7380845
uniprot
proteins
pubmed
7390979
uniprot
proteins
sequence_length
166
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted.
uniprot
proteins