ID   PRP1_HUMAN              Reviewed;         392 AA.
AC   P04280; G5E9X6; Q08805; Q15186; Q15187; Q15214; Q15215; Q16038;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 3.
DT   14-DEC-2022, entry version 157.
DE   RecName: Full=Basic salivary proline-rich protein 1;
DE            Short=Salivary proline-rich protein;
DE   Contains:
DE     RecName: Full=Proline-rich peptide II-2;
DE   Contains:
DE     RecName: Full=Basic peptide IB-6;
DE   Contains:
DE     RecName: Full=Peptide P-H;
DE   Flags: Precursor;
GN   Name=PRB1;
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 M), AND VARIANT ALA-337.
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] (ALLELE M), AND VARIANT ALA-337.
RX   PubMed=8422499; DOI=10.1007/bf00364656;
RA   Kim H.-S., Lyons K.M., Saitoh E., Azen E.A., Smithies O., Maeda N.;
RT   "The structure and evolution of the human salivary proline-rich protein
RT   gene family.";
RL   Mamm. Genome 4:3-14(1993).
RN   [3]
RP   PROTEIN SEQUENCE OF 17-91, AND PYROGLUTAMATE FORMATION AT GLN-17.
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-251 AND 300-392 (ALLELE M), AND
RP   VARIANT ALA-337.
RX   PubMed=6089212; DOI=10.1073/pnas.81.17.5561;
RA   Azen E.A., Lyons K.M., McGonigal T., Barrett N.L., Clements L.S., Maeda N.,
RA   Vanin E.F., Carlson D.M., Smithies O.;
RT   "Clones from the human gene complex coding for salivary proline-rich
RT   proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:5561-5565(1984).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-392 (ALLELES M AND S),
RP   POLYMORPHISM, AND VARIANT ALA-337.
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-392 (ALLELES L AND M), AND VARIANT
RP   ALA-337.
RX   PubMed=8317492;
RA   Azen E.A., Latreille P., Niece R.L.;
RT   "PRBI gene variants coding for length and null polymorphisms among human
RT   salivary Ps, PmF, PmS, and Pe proline-rich proteins (PRPs).";
RL   Am. J. Hum. Genet. 53:264-278(1993).
RN   [7]
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PROTEIN SEQUENCE OF 275-392, AND SUBCELLULAR LOCATION.
RC   TISSUE=Saliva;
RX   PubMed=3521730; DOI=10.1021/bi00357a013;
RA   Kauffman D., Hofmann T., Bennick A., Keller P.;
RT   "Basic proline-rich proteins from human parotid saliva: complete covalent
RT   structures of proteins IB-1 and IB-6.";
RL   Biochemistry 25:2387-2392(1986).
RN   [10]
RP   PROTEIN SEQUENCE OF 337-392.
RC   TISSUE=Saliva;
RX   PubMed=6671974; DOI=10.1093/oxfordjournals.jbchem.a134553;
RA   Saitoh E., Isemura S., Sanada K.;
RT   "Further fractionation of basic proline-rich peptides from human parotid
RT   saliva and complete amino acid sequence of basic proline-rich peptide P-
RT   H.";
RL   J. Biochem. 94:1991-1999(1983).
RN   [11]
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   [12]
RP   GLYCOSYLATION AT SER-40; SER-87 AND SER-150, PHOSPHORYLATION AT SER-40;
RP   SER-92 AND SER-150, PYROGLUTAMATE FORMATION AT GLN-17, IDENTIFICATION BY
RP   MASS SPECTROMETRY, AND VARIANTS ALLELE M AND S.
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 {ECO:0000269|PubMed:3521730}.
CC   -!- PTM: O-glycosylated. O-glycosylation on Ser-87 is prevalent in head and
CC       neck cancer patients. O-Glycosylation on Ser-330 has a 5 times
CC       prevalence in head and neck cancers. {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. {ECO:0000269|PubMed:18463091}.
CC   -!- PTM: Pyroglutamate formation occurs on terminal Gln residues of cleaved
CC       peptides. Besides on the N-terminal of mature PBR1, pyroglutamate
CC       formation found on at least Gln-58. {ECO:0000269|PubMed:18463091}.
CC   -!- POLYMORPHISM: The number of repeats is polymorphic and varies among
CC       different alleles. The sequence shown is that of allele L (long). There
CC       are allele M (medium) and allele S (short) which contain 12 and 9
CC       approximate tandem repeats repectively. {ECO:0000269|PubMed:2851479}.
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DR   EMBL; K03204; AAA60185.1; -; mRNA.
DR   EMBL; K03205; AAA60186.1; -; mRNA.
DR   EMBL; K03206; AAA60187.1; -; mRNA.
DR   EMBL; S52986; AAA13341.2; -; Genomic_DNA.
DR   EMBL; M97220; AAB05816.1; -; Genomic_DNA.
DR   EMBL; K02575; AAA36502.1; -; Genomic_DNA.
DR   EMBL; K02576; AAA36503.1; -; Genomic_DNA.
DR   EMBL; X07516; CAA30394.2; -; Genomic_DNA.
DR   EMBL; X07517; CAA30395.2; -; Genomic_DNA.
DR   EMBL; S62928; AAB27288.2; -; Genomic_DNA.
DR   EMBL; S62941; AAB27289.1; -; Genomic_DNA.
DR   EMBL; AC010176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC078950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC126171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471094; EAW96233.1; -; Genomic_DNA.
DR   PIR; B40750; PIHUB6.
DR   PIR; C38355; C38355.
DR   PIR; D40750; D40750.
DR   RefSeq; NP_005030.2; NM_005039.3.
DR   RefSeq; NP_955385.1; NM_199353.2.
DR   RefSeq; NP_955386.1; NM_199354.2.
DR   AlphaFoldDB; P04280; -.
DR   BioGRID; 111534; 19.
DR   STRING; 9606.ENSP00000420826; -.
DR   GlyGen; P04280; 4 sites.
DR   iPTMnet; P04280; -.
DR   PhosphoSitePlus; P04280; -.
DR   BioMuta; PRB1; -.
DR   MassIVE; P04280; -.
DR   PaxDb; P04280; -.
DR   PeptideAtlas; P04280; -.
DR   ProteomicsDB; 51701; -.
DR   TopDownProteomics; P04280; -.
DR   DNASU; 5542; -.
DR   GeneID; 5542; -.
DR   KEGG; hsa:5542; -.
DR   UCSC; uc001qzu.2; human.
DR   AGR; HGNC:9337; -.
DR   CTD; 5542; -.
DR   DisGeNET; 5542; -.
DR   GeneCards; PRB1; -.
DR   HGNC; HGNC:9337; PRB1.
DR   MIM; 180989; gene.
DR   neXtProt; NX_P04280; -.
DR   PharmGKB; PA33699; -.
DR   eggNOG; ENOG502QS37; Eukaryota.
DR   InParanoid; P04280; -.
DR   PathwayCommons; P04280; -.
DR   BioGRID-ORCS; 5542; 68 hits in 967 CRISPR screens.
DR   ChiTaRS; PRB1; human.
DR   GeneWiki; PRB1; -.
DR   GenomeRNAi; 5542; -.
DR   Pharos; P04280; Tdark.
DR   PRO; PR:P04280; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; P04280; protein.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR026086; Pro-rich.
DR   PANTHER; PTHR23203; PROLINE-RICH PROTEIN; 6.
DR   Pfam; PF15240; Pro-rich; 2.
DR   SMART; SM01412; Pro-rich; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Phosphoprotein;
KW   Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:1849422"
FT   CHAIN           17..392
FT                   /note="Basic salivary proline-rich protein 1"
FT                   /id="PRO_0000022129"
FT   CHAIN           17..91
FT                   /note="Proline-rich peptide II-2"
FT                   /id="PRO_0000372441"
FT   CHAIN           275..392
FT                   /note="Basic peptide IB-6"
FT                   /id="PRO_0000022130"
FT   CHAIN           337..392
FT                   /note="Peptide P-H"
FT                   /id="PRO_0000022131"
FT   REPEAT          53..72
FT                   /note="1"
FT   REPEAT          73..92
FT                   /note="2"
FT   REPEAT          93..112
FT                   /note="3"
FT   REPEAT          114..133
FT                   /note="4"
FT   REPEAT          134..153
FT                   /note="5"
FT   REPEAT          154..173
FT                   /note="6"
FT   REPEAT          175..194
FT                   /note="7"
FT   REPEAT          195..214
FT                   /note="8"
FT   REPEAT          215..234
FT                   /note="9"
FT   REPEAT          236..255
FT                   /note="10"
FT   REPEAT          256..275
FT                   /note="11"
FT   REPEAT          276..295
FT                   /note="12"
FT   REPEAT          297..316
FT                   /note="13"
FT   REPEAT          317..336
FT                   /note="14"
FT   REPEAT          338..357
FT                   /note="15"
FT   REGION          19..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..357
FT                   /note="15 X 20 AA approximate tandem repeats of P-P-G-K-P-
FT                   Q-G-P-P-[PAQ]-Q-[GE]-[GD]-[NKS]-[KSQRN]-[PRQS]-[QS] [GPS]-
FT                   [PQAR]-[PSR]"
FT   COMPBIAS        19..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..324
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..392
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         17
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:1849422,
FT                   ECO:0000269|PubMed:20879038"
FT   MOD_RES         40
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000269|PubMed:20879038"
FT   MOD_RES         92
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:20879038"
FT   MOD_RES         150
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000269|PubMed:20879038"
FT   CARBOHYD        40
FT                   /note="O-linked (Hex) serine; alternate"
FT                   /evidence="ECO:0000269|PubMed:20879038"
FT   CARBOHYD        87
FT                   /note="O-linked (HexNAc...) serine"
FT                   /evidence="ECO:0000269|PubMed:20879038"
FT   CARBOHYD        150
FT                   /note="O-linked (Hex) serine; alternate"
FT                   /evidence="ECO:0000269|PubMed:20879038"
FT   CARBOHYD        330
FT                   /note="O-linked (HexNAc...) serine"
FT   VARIANT         93..153
FT                   /note="Missing (in allele M)"
FT                   /id="VAR_019693"
FT   VARIANT         106..319
FT                   /note="Missing"
FT                   /evidence="ECO:0000269|PubMed:20879038"
FT                   /id="VAR_005562"
FT   VARIANT         106..299
FT                   /note="Missing"
FT                   /id="VAR_005561"
FT   VARIANT         134..255
FT                   /note="Missing (in allele S)"
FT                   /id="VAR_019694"
FT   VARIANT         337
FT                   /note="S -> A"
FT                   /evidence="ECO:0000269|PubMed:2851479,
FT                   ECO:0000269|PubMed:2993301, ECO:0000269|PubMed:6089212,
FT                   ECO:0000269|PubMed:8317492, ECO:0000269|PubMed:8422499"
FT                   /id="VAR_080188"
FT   CONFLICT        18..33
FT                   /note="NLNEDVSQEESPSLIA -> SCVGFYSVFLFSLCPL (in Ref. 4;
FT                   AAA36502)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        40
FT                   /note="S -> P (in Ref. 4; AAA36502)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        85..86
FT                   /note="DK -> GKR (in Ref. 4; AAA36502)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        128
FT                   /note="K -> R (in Ref. 5; CAA30395)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216..217
FT                   /note="PG -> R (in Ref. 4; AAA36502)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        271
FT                   /note="R -> Q (in Ref. 6; AAB27288)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        274
FT                   /note="Q -> R (in Ref. 5; CAA30395)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        278
FT                   /note="G -> R (in Ref. 5; CAA30395)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        307
FT                   /note="Q -> T (in Ref. 4; AAA36503)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        326
FT                   /note="A -> P (in Ref. 6; AAB27289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        330
FT                   /note="S -> C (in Ref. 4; AAA36503)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        385..386
FT                   /note="GR -> DK (in Ref. 4; AAA36503)"
FT                   /evidence="ECO:0000305"
SQ   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
//