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Basic salivary proline-rich protein 4 (Salivary proline-rich protein Po) (Parotid o protein) (Salivary proline-rich protein II-1) [Cleaved into: Protein N1; Glycosylated protein A; Peptide P-D (Proline-rich peptide IB-5)]

 PRB4_HUMAN              Reviewed;         310 AA.
P10163; A1L439; O00600; P02813; P10161; P10162; P81489;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
14-MAY-2014, sequence version 4.
31-JAN-2018, entry version 123.
RecName: Full=Basic salivary proline-rich protein 4;
Short=Salivary proline-rich protein Po;
AltName: Full=Parotid o protein;
AltName: Full=Salivary proline-rich protein II-1;
Contains:
RecName: Full=Protein N1;
Contains:
RecName: Full=Glycosylated protein A;
Contains:
RecName: Full=Peptide P-D;
AltName: Full=Proline-rich peptide IB-5;
Flags: Precursor;
Name=PRB4;
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 S), AND POLYMORPHISM.
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 L AND S), AND POLYMORPHISM.
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).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE M), AND VARIANT
PRO-272.
TISSUE=Cerebellum;
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).
[5]
PROTEIN SEQUENCE OF 17-112 AND 155-240.
TISSUE=Saliva;
PubMed=8373986;
Kauffman D.L., Keller P.J., Bennick A., Blum M.;
"Alignment of amino acid and DNA sequences of human proline-rich
proteins.";
Crit. Rev. Oral Biol. Med. 4:287-292(1993).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-310 (ALLELE M), AND VARIANT
PRO-272.
PubMed=8554050;
Azen E.A., Amberger E., Fisher S., Prakobphol A., Niece R.L.;
"PRB1, PRB2, and PRB4 coded polymorphisms among human salivary
concanavalin-A binding, II-1, and Po proline-rich proteins.";
Am. J. Hum. Genet. 58:143-153(1996).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-310, AND VARIANT PRO-272.
PubMed=3220251;
Lyons K.M., Stein J.H., Smithies O.;
"Many protein products from a few loci: assignment of human salivary
proline-rich proteins to specific loci.";
Genetics 120:255-265(1988).
[8]
PROTEIN SEQUENCE OF 241-310.
TISSUE=Saliva;
PubMed=6841349;
Saitoh E., Isemura S., Sanada K.;
"Complete amino acid sequence of a basic proline-rich peptide, P-D,
from human parotid saliva.";
J. Biochem. 93:495-502(1983).
[9]
PROTEIN SEQUENCE OF 241-310.
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).
[10]
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).
[11]
GLYCOSYLATION AT ASN-87, PYROGLUTAMATE FORMATION, VARIANTS ALLELE L
AND M, 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).
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: N-glycosylated. {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. Pyroglutamate formation found on at least
Gln-46, Gln-48, Gln-67, Gln-88; Gln-90; Gln-193; Gln-288 Gln-214
and Gln-295, preferentially in diabetic, and head and neck cancer
patients. {ECO:0000269|PubMed:18463091}.
-!- POLYMORPHISM: The number of repeats is polymorphic and varies
among different alleles. Allele S (short), allele M (medium) and
allele L (long) contain 6, 7 and 9 tandem repeats respectively.
{ECO:0000269|PubMed:2851479}.
-!- SEQUENCE CAUTION:
Sequence=CAA30543.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAA30729.1; Type=Erroneous gene model prediction; 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=PRB4";
-----------------------------------------------------------------------
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EMBL; K03207; AAA60188.1; -; mRNA.
EMBL; X07882; CAA30729.1; ALT_SEQ; Genomic_DNA.
EMBL; X07715; CAA30543.1; ALT_SEQ; Genomic_DNA.
EMBL; AC010176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC130386; AAI30387.1; -; mRNA.
EMBL; S80916; AAB50687.2; -; Genomic_DNA.
EMBL; X07704; CAA30542.1; -; Genomic_DNA.
PIR; S03176; PIHUSD.
UniGene; Hs.528651; -.
DisProt; DP00119; -.
iPTMnet; P10163; -.
BioMuta; PRB4; -.
DMDM; 158517854; -.
PeptideAtlas; P10163; -.
PRIDE; P10163; -.
TopDownProteomics; P10163; -.
DisGeNET; 5545; -.
GeneCards; PRB4; -.
H-InvDB; HIX0079490; -.
HGNC; HGNC:9340; PRB4.
MIM; 180990; gene.
neXtProt; NX_P10163; -.
PharmGKB; PA33702; -.
InParanoid; P10163; -.
ChiTaRS; PRB4; human.
GeneWiki; PRB4; -.
GenomeRNAi; 5545; -.
PRO; PR:P10163; -.
Proteomes; UP000005640; Unplaced.
CleanEx; HS_PRB4; -.
GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
InterPro; IPR026086; Pro-rich.
PANTHER; PTHR23203; PTHR23203; 1.
Pfam; PF15240; Pro-rich; 3.
SMART; SM01412; Pro-rich; 2.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Glycoprotein;
Polymorphism; Pyrrolidone carboxylic acid; Reference proteome; Repeat;
Secreted; Signal.
SIGNAL 1 16 {ECO:0000269|PubMed:8373986}.
CHAIN 17 310 Basic salivary proline-rich protein 4.
/FTId=PRO_0000022102.
PEPTIDE 17 39 Protein N1.
/FTId=PRO_0000022103.
CHAIN 40 177 Glycosylated protein A.
/FTId=PRO_0000022104.
CHAIN 241 310 Peptide P-D.
/FTId=PRO_0000022099.
REPEAT 35 55 1.
REPEAT 56 76 2.
REPEAT 77 97 3.
REPEAT 98 118 4.
REPEAT 119 139 5.
REPEAT 140 160 6.
REPEAT 161 181 7.
REPEAT 182 202 8.
REPEAT 203 223 9.
REPEAT 224 234 10; truncated.
REGION 35 234 9.5 X 21 AA tandem repeats of K-P-[EQ]-
[GR]-[PR]-[PR]-P-Q-G-G-N-Q-[PS]-[QH]-
[RG]-[PT]-P-P-[PH]-P-G.
CARBOHYD 66 66 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 87 87 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:20879038}.
CARBOHYD 108 108 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 171 171 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 213 213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 113 154 Missing (in allele M and allele S).
/FTId=VAR_035034.
VARIANT 164 184 Missing (in allele S).
/FTId=VAR_035035.
VARIANT 185 185 R -> G (in dbSNP:rs11054244).
/FTId=VAR_031548.
VARIANT 186 186 P -> R (in dbSNP:rs11054243).
/FTId=VAR_031549.
VARIANT 200 200 P -> H (in dbSNP:rs12308244).
/FTId=VAR_031550.
VARIANT 272 272 A -> P (in dbSNP:rs1052808).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:3220251,
ECO:0000269|PubMed:8554050}.
/FTId=VAR_031551.
CONFLICT 28 28 S -> P (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 31 39 LISGKPEGR -> IIPPKPPG (in Ref. 5; AA
sequence). {ECO:0000305}.
CONFLICT 31 33 LIS -> PPP (in Ref. 6; AAB50687).
{ECO:0000305}.
CONFLICT 37 37 E -> Q (in Ref. 2; CAA30543 and 7;
CAA30542). {ECO:0000305}.
CONFLICT 66 66 N -> D (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 74 94 Missing (in Ref. 7; CAA30542).
{ECO:0000305}.
CONFLICT 96 96 P -> PP (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 101 101 R -> E (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 122 123 SR -> RP (in Ref. 7; CAA30542).
{ECO:0000305}.
CONFLICT 129 129 H -> N (in Ref. 7; CAA30542).
{ECO:0000305}.
CONFLICT 154 174 Missing (in Ref. 7; CAA30542).
{ECO:0000305}.
CONFLICT 169 171 GGN -> QGG (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 192 192 N -> D (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 213 213 N -> D (in Ref. 5; AA sequence).
{ECO:0000305}.
SEQUENCE 310 AA; 31326 MW; 079538A1BC412D0F CRC64;
MLLILLSVAL LALSSAESSS EDVSQEESLF LISGKPEGRR PQGGNQPQRP PPPPGKPQGP
PPQGGNQSQG PPPPPGKPEG RPPQGGNQSQ GPPPHPGKPE RPPPQGGNQS QGPPPHPGKP
ESRPPQGGHQ SQGPPPTPGK PEGPPPQGGN QSQGTPPPPG KPEGRPPQGG NQSQGPPPHP
GKPERPPPQG GNQSHRPPPP PGKPERPPPQ GGNQSQGPPP HPGKPEGPPP QEGNKSRSAR
SPPGKPQGPP QQEGNKPQGP PPPGKPQGPP PAGGNPQQPQ APPAGKPQGP PPPPQGGRPP
RPAQGQQPPQ


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