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Salivary acidic proline-rich phosphoprotein 1/2 (Db-s) (PRP-1/PRP-2) (Parotid acidic protein) (Pa) (Parotid double-band protein) (Parotid isoelectric focusing variant protein) (PIF-S) (Parotid proline-rich protein 1/2) (Pr1/Pr2) (Protein C) [Cleaved into: Salivary acidic proline-rich phosphoprotein 1/2; Salivary acidic proline-rich phosphoprotein 3/4 (Db-F) (PIF-F) (PRP-3/PRP-4) (Protein A); Peptide P-C]

 PRPC_HUMAN              Reviewed;         166 AA.
P02810; A2VCM0; A3KN66; A5D902; B2RMW2; Q4VBP2; Q53XA2; Q6P2F6;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 2.
27-SEP-2017, entry version 158.
RecName: Full=Salivary acidic proline-rich phosphoprotein 1/2;
AltName: Full=Db-s;
AltName: Full=PRP-1/PRP-2;
AltName: Full=Parotid acidic protein;
Short=Pa;
AltName: Full=Parotid double-band protein;
AltName: Full=Parotid isoelectric focusing variant protein;
Short=PIF-S;
AltName: Full=Parotid proline-rich protein 1/2;
AltName: Full=Pr1/Pr2;
AltName: Full=Protein C;
Contains:
RecName: Full=Salivary acidic proline-rich phosphoprotein 1/2;
Contains:
RecName: Full=Salivary acidic proline-rich phosphoprotein 3/4;
AltName: Full=Db-F;
AltName: Full=PIF-F;
AltName: Full=PRP-3/PRP-4;
AltName: Full=Protein A;
Contains:
RecName: Full=Peptide P-C;
Flags: Precursor;
Name=PRH1;
and
Name=PRH2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELES PRH1-PIF AND PRH2-1).
PubMed=2993301;
Maeda N., Kim H.-S., Azen E.A., Smithies O.;
"Differential RNA splicing and post-translational cleavages in the
human salivary proline-rich protein gene system.";
J. Biol. Chem. 260:11123-11130(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES PRH1-PIF AND PRH2-1).
PubMed=3009472;
Kim H.-S., Maeda N.;
"Structures of two HaeIII-type genes in the human salivary proline-
rich protein multigene family.";
J. Biol. Chem. 261:6712-6718(1986).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE PRH2-1).
TISSUE=Salivary gland;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE PRH1-PIF), AND
VARIANT ASN-66.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELES PRH1-DB; PRH1-PIF;
PRH2-1 AND PRH2-2).
TISSUE=Thyroid;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 17-166 (PROTEIN C).
TISSUE=Saliva;
PubMed=7380845;
Wong R.S.C., 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. 255:5943-5948(1980).
[7]
PROTEIN SEQUENCE OF 17-166 (PRP-2).
TISSUE=Saliva;
PubMed=3710693;
Schlesinger D.H., Hay D.I.;
"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. 27:373-379(1986).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-166 (ALLELES PRH1-PIF; PRH1-PA
AND PRH1-DB).
PubMed=3687941;
Azen E.A., Kim H.S., 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. 41:1035-1047(1987).
[9]
PROTEIN SEQUENCE OF 17-166 (PRP-1 TO PRP-4; PIF-F AND PIF-S), AND
PYROGLUTAMATE FORMATION AT GLN-17.
TISSUE=Saliva;
PubMed=3196309; DOI=10.1042/bj2550015;
Hay D.I., Bennick A., Schlesinger D.H., Minaguchi K.,
Madapallimattam G., Schluckebier S.K.;
"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. 255:15-21(1988).
[10]
PROTEIN SEQUENCE OF 17-122 (PROTEIN A).
TISSUE=Saliva;
PubMed=438215;
Wong R.S.C., Hofmann T., Bennick A.;
"The complete primary structure of a proline-rich phosphoprotein from
human saliva.";
J. Biol. Chem. 254:4800-4808(1979).
[11]
PROTEIN SEQUENCE OF 17-122 (PROTEIN A).
Schlesinger D.H., Hay D.I.;
"Complete primary structure of a proline-rich phosphoprotein (PRP-4),
a potent inhibitor of calcium phosphate precipitation in human parotid
saliva.";
(In) Gross E., Meienhofer J. (eds.);
Peptides: structure and biological function (Proceedings of the 6th
American peptide symposium), pp.133-136, Pierce Chemical Co., Rockford
Il. (1979).
[12]
PROTEIN SEQUENCE OF 17-46 (PROTEIN C).
TISSUE=Saliva;
PubMed=7228490;
Schlesinger D.H., Hay D.I.;
"Primary structure of the active tryptic fragments of human and monkey
salivary anionic proline-rich proteins.";
Int. J. Pept. Protein Res. 17:34-41(1981).
[13]
PROTEIN SEQUENCE OF 17-46 (PROTEIN DB-S), PROTEIN SEQUENCE OF 91-97
(PROTEIN DB-S), IDENTIFICATION BY MASS SPECTROMETRY OF PIF-S; PIF-F;
DB-S; DB-F; PA; PRP-1 TO PRP4 AND PEPTIDE P-C, AND PHOSPHORYLATION AT
SER-24; SER-33 AND SER-38.
TISSUE=Saliva;
PubMed=15693058; DOI=10.1002/pmic.200401156;
Inzitari R., Cabras T., Onnis G., Olmi C., Mastinu A., Sanna M.T.,
Pellegrini M.G., Castagnola M., Messana I.;
"Different isoforms and post-translational modifications of human
salivary acidic proline-rich proteins.";
Proteomics 5:805-815(2005).
[14]
PROTEIN SEQUENCE OF 123-166 (PEPTIDE P-C).
TISSUE=Saliva;
PubMed=7390979;
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. 87:1071-1077(1980).
[15]
PROTEIN SEQUENCE OF 123-166.
TISSUE=Saliva;
PubMed=1849422; DOI=10.1021/bi00228a001;
Kauffman D.L., Bennick A., Blum M., Keller P.J.;
"Basic proline-rich proteins from human parotid saliva: relationships
of the covalent structures of ten proteins from a single individual.";
Biochemistry 30:3351-3356(1991).
[16]
GLYCOSYLATION AT SER-33, PHOSPHORYLATION AT SER-24 AND SER-38, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10858503; DOI=10.1016/S0014-5793(00)01645-8;
Jonsson A.P., Griffiths W.J., Bratt P., Johansson I., Stroemberg N.,
Joernvall H., Bergman T.;
"A novel Ser O-glucuronidation in acidic proline-rich proteins
identified by tandem mass spectrometry.";
FEBS Lett. 475:131-134(2000).
[17]
PROTEOLYTIC PROCESSING, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18463091; DOI=10.1074/jbc.M708282200;
Helmerhorst E.J., Sun X., Salih E., Oppenheim F.G.;
"Identification of Lys-Pro-Gln as a novel cleavage site specificity of
saliva-associated proteases.";
J. Biol. Chem. 283:19957-19966(2008).
[18]
GLYCOSYLATION AT SER-38, PHOSPHORYLATION AT SER-38, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=20879038; DOI=10.1002/pmic.201000261;
Vitorino R., Alves R., Barros A., Caseiro A., Ferreira R., Lobo M.C.,
Bastos A., Duarte J., Carvalho D., Santos L.L., Amado F.L.;
"Finding new posttranslational modifications in salivary proline-rich
proteins.";
Proteomics 10:3732-3742(2010).
[19]
PHOSPHORYLATION AT SER-24 AND SER-38, AND MUTAGENESIS OF SER-24 AND
SER-38.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[20]
VARIANT PRH2-3 LYS-163.
PubMed=10627138;
DOI=10.1002/(SICI)1098-1004(1998)12:1<72::AID-HUMU18>3.0.CO;2-W;
Azen E.A.;
"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.";
Hum. Mutat. 12:72-72(1998).
-!- 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.
-!- INTERACTION:
Q8IXL6:FAM20C; NbExp=2; IntAct=EBI-738601, EBI-7147442;
Q8TAX7:MUC7; NbExp=2; IntAct=EBI-738601, EBI-738582;
-!- SUBCELLULAR LOCATION: Secreted.
-!- 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: An 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}.
-!- POLYMORPHISM: Sequence shown is that of allele PRH2-2, also known
as PR-2; Allele PRH2-1 is also known as PR-1 or protein C, and
allele PRH2-3 as PR-1'. The PRH1-DB allele (about 16% of the
population) has an insertion of 21 repeated amino acids compared
to the more frequent PRH1-PIF allele (68%). In contrast to all
other PRH1 and PRH2 alleles, the PRH1-PA allele (16%) is not
proteolytically cleaved.
-!- SEQUENCE CAUTION:
Sequence=AAI28193.1; Type=Erroneous termination; Positions=167; Note=Translated as stop.; Evidence={ECO:0000305};
Sequence=AAI41917.1; Type=Erroneous termination; Positions=167; Note=Translated as stop.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=PRH1";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=PRH2";
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EMBL; K03202; AAA60183.1; -; mRNA.
EMBL; K03203; AAA60184.1; -; mRNA.
EMBL; M13057; AAA98807.1; -; Genomic_DNA.
EMBL; M13058; AAA98808.1; -; Genomic_DNA.
EMBL; BX641094; CAE46044.1; -; mRNA.
EMBL; CH471094; EAW96214.1; -; Genomic_DNA.
EMBL; CH471094; EAW96219.1; -; Genomic_DNA.
EMBL; BC095488; AAH95488.1; -; mRNA.
EMBL; BC128192; AAI28193.1; ALT_SEQ; mRNA.
EMBL; BC133676; AAI33677.1; -; mRNA.
EMBL; BC136499; AAI36500.1; -; mRNA.
EMBL; BC141916; AAI41917.1; ALT_SEQ; mRNA.
CCDS; CCDS8636.1; -.
PIR; A25372; PIHUSC.
PIR; B25372; B25372.
RefSeq; NP_001103683.1; NM_001110213.1.
RefSeq; NP_001278243.1; NM_001291314.1.
RefSeq; NP_001278244.1; NM_001291315.1.
UniGene; Hs.408153; -.
UniGene; Hs.656965; -.
UniGene; Hs.731575; -.
ProteinModelPortal; P02810; -.
IntAct; P02810; 4.
STRING; 9606.ENSP00000371271; -.
iPTMnet; P02810; -.
PhosphoSitePlus; P02810; -.
BioMuta; PRH1; -.
DMDM; 131008; -.
EPD; P02810; -.
MaxQB; P02810; -.
PaxDb; P02810; -.
PeptideAtlas; P02810; -.
PRIDE; P02810; -.
TopDownProteomics; P02810; -.
DNASU; 5554; -.
Ensembl; ENST00000381847; ENSP00000371271; ENSG00000134551.
Ensembl; ENST00000396400; ENSP00000379682; ENSG00000134551.
Ensembl; ENST00000572141; ENSP00000458690; ENSG00000272803.
Ensembl; ENST00000575657; ENSP00000461041; ENSG00000272803.
Ensembl; ENST00000622570; ENSP00000481810; ENSG00000275679.
Ensembl; ENST00000622848; ENSP00000483458; ENSG00000275679.
GeneID; 5554; -.
GeneID; 5555; -.
KEGG; hsa:5554; -.
KEGG; hsa:5555; -.
UCSC; uc001qzi.5; human.
CTD; 5554; -.
CTD; 5555; -.
DisGeNET; 5554; -.
DisGeNET; 5555; -.
EuPathDB; HostDB:ENSG00000134551.12; -.
GeneCards; PRH1; -.
GeneCards; PRH2; -.
H-InvDB; HIX0026359; -.
H-InvDB; HIX0026397; -.
H-InvDB; HIX0079411; -.
HGNC; HGNC:9366; PRH1.
HGNC; HGNC:9367; PRH2.
MIM; 168730; gene.
MIM; 168790; gene.
neXtProt; NX_P02810; -.
PharmGKB; PA33738; -.
eggNOG; ENOG410IUYX; Eukaryota.
eggNOG; ENOG4110PRV; LUCA.
InParanoid; P02810; -.
KO; K13910; -.
OrthoDB; EOG091G1ACT; -.
SIGNOR; P02810; -.
GeneWiki; PRH1; -.
PRO; PR:P02810; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000134551; -.
CleanEx; HS_PRH2; -.
Genevisible; P02810; HS.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
InterPro; IPR026086; Pro-rich.
PANTHER; PTHR23203; PTHR23203; 1.
Pfam; PF15240; Pro-rich; 1.
SMART; SM01412; Pro-rich; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Glycoprotein; Phosphoprotein; Polymorphism;
Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted;
Signal.
SIGNAL 1 16 {ECO:0000269|PubMed:15693058,
ECO:0000269|PubMed:3196309,
ECO:0000269|PubMed:3710693,
ECO:0000269|PubMed:438215,
ECO:0000269|PubMed:7228490,
ECO:0000269|PubMed:7380845,
ECO:0000269|Ref.11}.
CHAIN 17 166 Salivary acidic proline-rich
phosphoprotein 1/2.
/FTId=PRO_0000022137.
CHAIN 17 122 Salivary acidic proline-rich
phosphoprotein 3/4.
/FTId=PRO_0000022138.
CHAIN 123 166 Peptide P-C.
/FTId=PRO_0000022139.
REGION 17 46 Inhibits hydroxyapatite formation, binds
to hydroxyapatite and calcium.
MOD_RES 17 17 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:3196309}.
MOD_RES 24 24 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:10858503,
ECO:0000269|PubMed:15693058,
ECO:0000269|PubMed:26091039}.
MOD_RES 33 33 Phosphoserine; alternate.
{ECO:0000269|PubMed:15693058}.
MOD_RES 38 38 Phosphoserine; by FAM20C; alternate.
{ECO:0000269|PubMed:10858503,
ECO:0000269|PubMed:15693058,
ECO:0000269|PubMed:20879038,
ECO:0000269|PubMed:26091039}.
CARBOHYD 33 33 O-linked (GlcA) serine; alternate.
{ECO:0000269|PubMed:10858503}.
CARBOHYD 38 38 O-linked (GlcA) serine; alternate.
{ECO:0000269|PubMed:20879038}.
VARIANT 20 20 D -> N (in allele PRH1-PIF, allele PRH1-
PA and allele PRH1-DB; dbSNP:rs1130404).
/FTId=VAR_005563.
VARIANT 42 42 I -> L (in allele PRH1-PA and allele
PRH1-DB; dbSNP:rs2923234).
/FTId=VAR_023240.
VARIANT 66 66 D -> N (in allele PRH2-1;
dbSNP:rs1049112). {ECO:0000269|Ref.4}.
/FTId=VAR_005564.
VARIANT 97 97 Q -> QGGQQQQGPPPPQGKPQGPPQQ (in allele
PRH1-DB).
/FTId=VAR_023241.
VARIANT 119 119 R -> C (in allele PRH1-PA; interferes
with proteolytic cleavage at Arg-122).
/FTId=VAR_023242.
VARIANT 163 163 Q -> K (in allele PRH2-3;
dbSNP:rs74062407).
{ECO:0000269|PubMed:10627138}.
/FTId=VAR_005565.
MUTAGEN 24 24 S->A: Decreased phosphorylation by
FAM20C; when associated with A-38.
{ECO:0000269|PubMed:26091039}.
MUTAGEN 38 38 S->A: Decreased phosphorylation by
FAM20C; when associated with A-24.
{ECO:0000269|PubMed:26091039}.
CONFLICT 41 41 F -> P (in Ref. 11; AA sequence).
{ECO:0000305}.
SEQUENCE 166 AA; 17016 MW; A7DF62BF94E3C3EF CRC64;
MLLILLSVAL LAFSSAQDLD EDVSQEDVPL VISDGGDSEQ FIDEERQGPP LGGQQSQPSA
GDGNQDDGPQ QGPPQQGGQQ QQGPPPPQGK PQGPPQQGGH PPPPQGRPQG PPQQGGHPRP
PRGRPQGPPQ QGGHQQGPPP PPPGKPQGPP PQGGRPQGPP QGQSPQ


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