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Basic salivary proline-rich protein 1 (Salivary proline-rich protein) [Cleaved into: Proline-rich peptide II-2; Basic peptide IB-6; Peptide P-H]

 PRP1_HUMAN              Reviewed;         392 AA.
P04280; G5E9X6; Q08805; Q15186; Q15187; Q15214; Q15215; Q16038;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 3.
25-APR-2018, entry version 133.
RecName: Full=Basic salivary proline-rich protein 1;
Short=Salivary proline-rich protein;
Contains:
RecName: Full=Proline-rich peptide II-2;
Contains:
RecName: Full=Basic peptide IB-6;
Contains:
RecName: Full=Peptide P-H;
Flags: Precursor;
Name=PRB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE M), AND VARIANT ALA-337.
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] (ALLELE M), AND VARIANT ALA-337.
PubMed=8422499; DOI=10.1007/BF00364656;
Kim H.-S., Lyons K.M., Saitoh E., Azen E.A., Smithies O., Maeda N.;
"The structure and evolution of the human salivary proline-rich
protein gene family.";
Mamm. Genome 4:3-14(1993).
[3]
PROTEIN SEQUENCE OF 17-91, AND PYROGLUTAMATE FORMATION AT GLN-17.
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-251 AND 300-392 (ALLELE M),
AND VARIANT ALA-337.
PubMed=6089212; DOI=10.1073/pnas.81.17.5561;
Azen E.A., Lyons K.M., McGonigal T., Barrett N.L., Clements L.S.,
Maeda N., Vanin E.F., Carlson D.M., Smithies O.;
"Clones from the human gene complex coding for salivary proline-rich
proteins.";
Proc. Natl. Acad. Sci. U.S.A. 81:5561-5565(1984).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-392 (ALLELES M AND S),
POLYMORPHISM, AND VARIANT ALA-337.
PubMed=2851479;
Lyons K.M., Stein J.H., Smithies O.;
"Length polymorphisms in human proline-rich protein genes generated by
intragenic unequal crossing over.";
Genetics 120:267-278(1988).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-392 (ALLELES L AND M), AND
VARIANT ALA-337.
PubMed=8317492;
Azen E.A., Latreille P., Niece R.L.;
"PRBI gene variants coding for length and null polymorphisms among
human salivary Ps, PmF, PmS, and Pe proline-rich proteins (PRPs).";
Am. J. Hum. Genet. 53:264-278(1993).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[9]
PROTEIN SEQUENCE OF 275-392, AND SUBCELLULAR LOCATION.
TISSUE=Saliva;
PubMed=3521730; DOI=10.1021/bi00357a013;
Kauffman D., Hofmann T., Bennick A., Keller P.;
"Basic proline-rich proteins from human parotid saliva: complete
covalent structures of proteins IB-1 and IB-6.";
Biochemistry 25:2387-2392(1986).
[10]
PROTEIN SEQUENCE OF 337-392.
TISSUE=Saliva;
PubMed=6671974; DOI=10.1093/oxfordjournals.jbchem.a134553;
Saitoh E., Isemura S., Sanada K.;
"Further fractionation of basic proline-rich peptides from human
parotid saliva and complete amino acid sequence of basic proline-rich
peptide P-H.";
J. Biochem. 94:1991-1999(1983).
[11]
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).
[12]
GLYCOSYLATION AT SER-40; SER-87 AND SER-150, PHOSPHORYLATION AT
SER-40; SER-92 AND SER-150, PYROGLUTAMATE FORMATION AT GLN-17,
IDENTIFICATION BY MASS SPECTROMETRY, AND VARIANTS ALLELE M AND S.
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).
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3521730}.
-!- PTM: O-glycosylated. O-glycosylation on Ser-87 is prevalent in
head and neck cancer patients. O-Glycosylation on Ser-330 has a 5
times prevalence in head and neck cancers.
{ECO:0000269|PubMed:20879038}.
-!- PTM: Proteolytically cleaved at the tripeptide Xaa-Pro-Gln, where
Xaa in the P(3) position is mostly lysine. The endoprotease may be
of microbial origin. {ECO:0000269|PubMed:18463091}.
-!- PTM: Pyroglutamate formation occurs on terminal Gln residues of
cleaved peptides. Besides on the N-terminal of mature PBR1,
pyroglutamate formation found on at least Gln-58.
{ECO:0000269|PubMed:18463091}.
-!- POLYMORPHISM: The number of repeats is polymorphic and varies
among different alleles. The sequence shown is that of allele L
(long). There are allele M (medium) and allele S (short) which
contain 12 and 9 approximate tandem repeats repectively.
{ECO:0000269|PubMed:2851479}.
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EMBL; K03204; AAA60185.1; -; mRNA.
EMBL; K03205; AAA60186.1; -; mRNA.
EMBL; K03206; AAA60187.1; -; mRNA.
EMBL; S52986; AAA13341.2; -; Genomic_DNA.
EMBL; M97220; AAB05816.1; -; Genomic_DNA.
EMBL; K02575; AAA36502.1; -; Genomic_DNA.
EMBL; K02576; AAA36503.1; -; Genomic_DNA.
EMBL; X07516; CAA30394.2; -; Genomic_DNA.
EMBL; X07517; CAA30395.2; -; Genomic_DNA.
EMBL; S62928; AAB27288.2; -; Genomic_DNA.
EMBL; S62941; AAB27289.1; -; Genomic_DNA.
EMBL; AC010176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC078950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC126171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471094; EAW96233.1; -; Genomic_DNA.
PIR; B40750; PIHUB6.
PIR; C38355; C38355.
PIR; D40750; D40750.
RefSeq; NP_005030.2; NM_005039.3.
RefSeq; NP_955385.1; NM_199353.2.
RefSeq; NP_955386.1; NM_199354.2.
UniGene; Hs.631726; -.
ProteinModelPortal; P04280; -.
BioGrid; 111534; 4.
STRING; 9606.ENSP00000420826; -.
iPTMnet; P04280; -.
PhosphoSitePlus; P04280; -.
BioMuta; PRB1; -.
PaxDb; P04280; -.
PeptideAtlas; P04280; -.
PRIDE; P04280; -.
TopDownProteomics; P04280; -.
GeneID; 5542; -.
KEGG; hsa:5542; -.
CTD; 5542; -.
DisGeNET; 5542; -.
EuPathDB; HostDB:ENSG00000251655.6; -.
GeneCards; PRB1; -.
HGNC; HGNC:9337; PRB1.
MIM; 180989; gene.
neXtProt; NX_P04280; -.
PharmGKB; PA33699; -.
InParanoid; P04280; -.
KO; K13911; -.
GeneWiki; PRB1; -.
GenomeRNAi; 5542; -.
PRO; PR:P04280; -.
Proteomes; UP000005640; Unplaced.
Bgee; ENSG00000251655; -.
CleanEx; HS_PRB1; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
InterPro; IPR026086; Pro-rich.
PANTHER; PTHR23203; PTHR23203; 6.
Pfam; PF15240; Pro-rich; 3.
SMART; SM01412; Pro-rich; 2.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Glycoprotein;
Phosphoprotein; Polymorphism; Pyrrolidone carboxylic acid;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 16 {ECO:0000269|PubMed:1849422}.
CHAIN 17 392 Basic salivary proline-rich protein 1.
/FTId=PRO_0000022129.
CHAIN 17 91 Proline-rich peptide II-2.
/FTId=PRO_0000372441.
CHAIN 275 392 Basic peptide IB-6.
/FTId=PRO_0000022130.
CHAIN 337 392 Peptide P-H.
/FTId=PRO_0000022131.
REPEAT 53 72 1.
REPEAT 73 92 2.
REPEAT 93 112 3.
REPEAT 114 133 4.
REPEAT 134 153 5.
REPEAT 154 173 6.
REPEAT 175 194 7.
REPEAT 195 214 8.
REPEAT 215 234 9.
REPEAT 236 255 10.
REPEAT 256 275 11.
REPEAT 276 295 12.
REPEAT 297 316 13.
REPEAT 317 336 14.
REPEAT 338 357 15.
REGION 53 357 15 X 20 AA approximate tandem repeats of
P-P-G-K-P-Q-G-P-P-[PAQ]-Q-[GE]-[GD]-
[NKS]-[KSQRN]-[PRQS]-[QS] [GPS]-[PQAR]-
[PSR].
MOD_RES 17 17 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:1849422,
ECO:0000269|PubMed:20879038}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000250|UniProtKB:P02812}.
MOD_RES 40 40 Phosphoserine; alternate.
{ECO:0000269|PubMed:20879038}.
MOD_RES 92 92 Phosphoserine.
{ECO:0000269|PubMed:20879038}.
MOD_RES 150 150 Phosphoserine; alternate.
{ECO:0000269|PubMed:20879038}.
CARBOHYD 40 40 O-linked (Hex) serine; alternate.
{ECO:0000269|PubMed:20879038}.
CARBOHYD 87 87 O-linked (HexNAc...) serine.
{ECO:0000269|PubMed:20879038}.
CARBOHYD 150 150 O-linked (Hex) serine; alternate.
{ECO:0000269|PubMed:20879038}.
CARBOHYD 330 330 O-linked (HexNAc...) serine.
VARIANT 93 153 Missing (in allele M).
/FTId=VAR_019693.
VARIANT 106 319 Missing. {ECO:0000269|PubMed:20879038}.
/FTId=VAR_005562.
VARIANT 106 299 Missing.
/FTId=VAR_005561.
VARIANT 134 255 Missing (in allele S).
/FTId=VAR_019694.
VARIANT 337 337 S -> A. {ECO:0000269|PubMed:2851479,
ECO:0000269|PubMed:2993301,
ECO:0000269|PubMed:6089212,
ECO:0000269|PubMed:8317492,
ECO:0000269|PubMed:8422499}.
/FTId=VAR_080188.
CONFLICT 18 33 NLNEDVSQEESPSLIA -> SCVGFYSVFLFSLCPL (in
Ref. 4; AAA36502). {ECO:0000305}.
CONFLICT 40 40 S -> P (in Ref. 4; AAA36502).
{ECO:0000305}.
CONFLICT 85 86 DK -> GKR (in Ref. 4; AAA36502).
{ECO:0000305}.
CONFLICT 128 128 K -> R (in Ref. 5; CAA30395).
{ECO:0000305}.
CONFLICT 216 217 PG -> R (in Ref. 4; AAA36502).
{ECO:0000305}.
CONFLICT 271 271 R -> Q (in Ref. 6; AAB27288).
{ECO:0000305}.
CONFLICT 274 274 Q -> R (in Ref. 5; CAA30395).
{ECO:0000305}.
CONFLICT 278 278 G -> R (in Ref. 5; CAA30395).
{ECO:0000305}.
CONFLICT 307 307 Q -> T (in Ref. 4; AAA36503).
{ECO:0000305}.
CONFLICT 326 326 A -> P (in Ref. 6; AAB27289).
{ECO:0000305}.
CONFLICT 330 330 S -> C (in Ref. 4; AAA36503).
{ECO:0000305}.
CONFLICT 385 386 GR -> DK (in Ref. 4; AAA36503).
{ECO:0000305}.
SEQUENCE 392 AA; 38562 MW; 31F4D7B21F335CAF CRC64;
MLLILLSVAL LALSSAQNLN EDVSQEESPS LIAGNPQGPS PQGGNKPQGP PPPPGKPQGP
PPQGGNKPQG PPPPGKPQGP PPQGDKSRSP RSPPGKPQGP PPQGGNQPQG PPPPPGKPQG
PPPQGGNKPQ GPPPPGKPQG PPPQGDKSQS PRSPPGKPQG PPPQGGNQPQ GPPPPPGKPQ
GPPPQGGNKP QGPPPPGKPQ GPPPQGDKSQ SPRSPPGKPQ GPPPQGGNQP QGPPPPPGKP
QGPPQQGGNR PQGPPPPGKP QGPPPQGDKS RSPQSPPGKP QGPPPQGGNQ PQGPPPPPGK
PQGPPPQGGN KPQGPPPPGK PQGPPAQGGS KSQSARSPPG KPQGPPQQEG NNPQGPPPPA
GGNPQQPQAP PAGQPQGPPR PPQGGRPSRP PQ


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