PRP1_HUMAN
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 03-AUG-2022, entry version 156.
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 PRIDE; P04280; -.
DR ProteomicsDB; 51701; -.
DR TopDownProteomics; P04280; -.
DR DNASU; 5542; -.
DR GeneID; 5542; -.
DR KEGG; hsa:5542; -.
DR UCSC; uc001qzu.2; human.
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; PTHR23203; 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
