PRB4_HUMAN
ID PRB4_HUMAN Reviewed; 310 AA.
AC P10163; A1L439; O00600; P02813; P10161; P10162; P81489;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 4.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Basic salivary proline-rich protein 4;
DE Short=Salivary proline-rich protein Po;
DE AltName: Full=Parotid o protein;
DE AltName: Full=Salivary proline-rich protein II-1;
DE Contains:
DE RecName: Full=Protein N1;
DE Contains:
DE RecName: Full=Glycosylated protein A;
DE Contains:
DE RecName: Full=Peptide P-D;
DE AltName: Full=Proline-rich peptide IB-5;
DE Flags: Precursor;
GN Name=PRB4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE S), AND POLYMORPHISM.
RX PubMed=2993301; DOI=10.1016/s0021-9258(17)39156-1;
RA Maeda N., Kim H.-S., Azen E.A., Smithies O.;
RT "Differential RNA splicing and post-translational cleavages in the human
RT salivary proline-rich protein gene system.";
RL J. Biol. Chem. 260:11123-11130(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES L AND S), AND POLYMORPHISM.
RX PubMed=2851479; DOI=10.1093/genetics/120.1.267;
RA Lyons K.M., Stein J.H., Smithies O.;
RT "Length polymorphisms in human proline-rich protein genes generated by
RT intragenic unequal crossing over.";
RL Genetics 120:267-278(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE M), AND VARIANT PRO-272.
RC TISSUE=Cerebellum;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 17-112 AND 155-240.
RC TISSUE=Saliva;
RX PubMed=8373986; DOI=10.1177/10454411930040030501;
RA Kauffman D.L., Keller P.J., Bennick A., Blum M.;
RT "Alignment of amino acid and DNA sequences of human proline-rich
RT proteins.";
RL Crit. Rev. Oral Biol. Med. 4:287-292(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-310 (ALLELE M), AND VARIANT
RP PRO-272.
RX PubMed=8554050;
RA Azen E.A., Amberger E., Fisher S., Prakobphol A., Niece R.L.;
RT "PRB1, PRB2, and PRB4 coded polymorphisms among human salivary
RT concanavalin-A binding, II-1, and Po proline-rich proteins.";
RL Am. J. Hum. Genet. 58:143-153(1996).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-310, AND VARIANT PRO-272.
RX PubMed=3220251; DOI=10.1093/genetics/120.1.255;
RA Lyons K.M., Stein J.H., Smithies O.;
RT "Many protein products from a few loci: assignment of human salivary
RT proline-rich proteins to specific loci.";
RL Genetics 120:255-265(1988).
RN [8]
RP PROTEIN SEQUENCE OF 241-310.
RC TISSUE=Saliva;
RX PubMed=6841349; DOI=10.1093/oxfordjournals.jbchem.a134204;
RA Saitoh E., Isemura S., Sanada K.;
RT "Complete amino acid sequence of a basic proline-rich peptide, P-D, from
RT human parotid saliva.";
RL J. Biochem. 93:495-502(1983).
RN [9]
RP PROTEIN SEQUENCE OF 241-310.
RC TISSUE=Saliva;
RX PubMed=1849422; DOI=10.1021/bi00228a001;
RA Kauffman D.L., Bennick A., Blum M., Keller P.J.;
RT "Basic proline-rich proteins from human parotid saliva: relationships of
RT the covalent structures of ten proteins from a single individual.";
RL Biochemistry 30:3351-3356(1991).
RN [10]
RP PROTEOLYTIC PROCESSING, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18463091; DOI=10.1074/jbc.m708282200;
RA Helmerhorst E.J., Sun X., Salih E., Oppenheim F.G.;
RT "Identification of Lys-Pro-Gln as a novel cleavage site specificity of
RT saliva-associated proteases.";
RL J. Biol. Chem. 283:19957-19966(2008).
RN [11]
RP GLYCOSYLATION AT ASN-87, PYROGLUTAMATE FORMATION, VARIANTS ALLELE L AND M,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20879038; DOI=10.1002/pmic.201000261;
RA Vitorino R., Alves R., Barros A., Caseiro A., Ferreira R., Lobo M.C.,
RA Bastos A., Duarte J., Carvalho D., Santos L.L., Amado F.L.;
RT "Finding new posttranslational modifications in salivary proline-rich
RT proteins.";
RL Proteomics 10:3732-3742(2010).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20879038}.
CC -!- PTM: Proteolytically cleaved at the tripeptide Xaa-Pro-Gln, where Xaa
CC in the P(3) position is mostly lysine. The endoprotease may be of
CC microbial origin. Pyroglutamate formation found on at least Gln-46,
CC Gln-48, Gln-67, Gln-88; Gln-90; Gln-193; Gln-288 Gln-214 and Gln-295,
CC preferentially in diabetic, and head and neck cancer patients.
CC {ECO:0000269|PubMed:18463091}.
CC -!- POLYMORPHISM: The number of repeats is polymorphic and varies among
CC different alleles. Allele S (short), allele M (medium) and allele L
CC (long) contain 6, 7 and 9 tandem repeats respectively.
CC {ECO:0000269|PubMed:2851479}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA30543.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA30729.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; K03207; AAA60188.1; -; mRNA.
DR EMBL; X07882; CAA30729.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X07715; CAA30543.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC010176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC130386; AAI30387.1; -; mRNA.
DR EMBL; S80916; AAB50687.2; -; Genomic_DNA.
DR EMBL; X07704; CAA30542.1; -; Genomic_DNA.
DR PIR; S03176; PIHUSD.
DR AlphaFoldDB; P10163; -.
DR BioGRID; 111536; 3.
DR STRING; 9606.ENSP00000279575; -.
DR GlyGen; P10163; 8 sites.
DR iPTMnet; P10163; -.
DR BioMuta; PRB4; -.
DR DMDM; 158517854; -.
DR MassIVE; P10163; -.
DR PeptideAtlas; P10163; -.
DR PRIDE; P10163; -.
DR TopDownProteomics; P10163; -.
DR GeneCards; PRB4; -.
DR HGNC; HGNC:9340; PRB4.
DR MIM; 180990; gene.
DR neXtProt; NX_P10163; -.
DR PharmGKB; PA33702; -.
DR eggNOG; ENOG502RU4G; Eukaryota.
DR InParanoid; P10163; -.
DR PathwayCommons; P10163; -.
DR SIGNOR; P10163; -.
DR GeneWiki; PRB4; -.
DR Pharos; P10163; Tdark.
DR PRO; PR:P10163; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; P10163; protein.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR DisProt; DP00119; -.
DR InterPro; IPR026086; Pro-rich.
DR PANTHER; PTHR23203; PTHR23203; 5.
DR Pfam; PF15240; Pro-rich; 2.
DR SMART; SM01412; Pro-rich; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Pyrrolidone carboxylic acid;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:8373986"
FT CHAIN 17..310
FT /note="Basic salivary proline-rich protein 4"
FT /id="PRO_0000022102"
FT PEPTIDE 17..39
FT /note="Protein N1"
FT /id="PRO_0000022103"
FT CHAIN 40..177
FT /note="Glycosylated protein A"
FT /id="PRO_0000022104"
FT CHAIN 241..310
FT /note="Peptide P-D"
FT /id="PRO_0000022099"
FT REPEAT 35..55
FT /note="1"
FT REPEAT 56..76
FT /note="2"
FT REPEAT 77..97
FT /note="3"
FT REPEAT 98..118
FT /note="4"
FT REPEAT 119..139
FT /note="5"
FT REPEAT 140..160
FT /note="6"
FT REPEAT 161..181
FT /note="7"
FT REPEAT 182..202
FT /note="8"
FT REPEAT 203..223
FT /note="9"
FT REPEAT 224..234
FT /note="10; truncated"
FT REGION 14..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..234
FT /note="9.5 X 21 AA tandem repeats of K-P-[EQ]-[GR]-[PR]-
FT [PR]-P-Q-G-G-N-Q-[PS]-[QH]-[RG]-[PT]-P-P-[PH]-P-G"
FT COMPBIAS 45..122
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..229
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..310
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20879038"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 113..154
FT /note="Missing (in allele M and allele S)"
FT /id="VAR_035034"
FT VARIANT 164..184
FT /note="Missing (in allele S)"
FT /id="VAR_035035"
FT VARIANT 185
FT /note="R -> G (in dbSNP:rs11054244)"
FT /id="VAR_031548"
FT VARIANT 186
FT /note="P -> R (in dbSNP:rs11054243)"
FT /id="VAR_031549"
FT VARIANT 200
FT /note="P -> H (in dbSNP:rs12308244)"
FT /id="VAR_031550"
FT VARIANT 272
FT /note="A -> P (in dbSNP:rs1052808)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:3220251, ECO:0000269|PubMed:8554050"
FT /id="VAR_031551"
FT CONFLICT 28
FT /note="S -> P (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 31..39
FT /note="LISGKPEGR -> IIPPKPPG (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 31..33
FT /note="LIS -> PPP (in Ref. 6; AAB50687)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="E -> Q (in Ref. 2; CAA30543 and 7; CAA30542)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="N -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 74..94
FT /note="Missing (in Ref. 7; CAA30542)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="P -> PP (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="R -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 122..123
FT /note="SR -> RP (in Ref. 7; CAA30542)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="H -> N (in Ref. 7; CAA30542)"
FT /evidence="ECO:0000305"
FT CONFLICT 154..174
FT /note="Missing (in Ref. 7; CAA30542)"
FT /evidence="ECO:0000305"
FT CONFLICT 169..171
FT /note="GGN -> QGG (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="N -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="N -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ 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
