PRB2_HUMAN
ID PRB2_HUMAN Reviewed; 416 AA.
AC P02812; O00599; P02811; P04281;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 4.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Basic salivary proline-rich protein 2;
DE Short=Salivary proline-rich protein;
DE AltName: Full=Con1 glycoprotein;
DE Contains:
DE RecName: Full=Basic proline-rich peptide IB-1;
DE Contains:
DE RecName: Full=Basic proline-rich peptide P-E;
DE AltName: Full=IB-9;
DE Contains:
DE RecName: Full=Basic proline-rich peptide IB-7;
DE Contains:
DE RecName: Full=Basic proline-rich peptide IB-8c;
DE AltName: Full=Basic peptide P-F;
DE Contains:
DE RecName: Full=Basic proline-rich peptide IB-4;
DE Flags: Precursor;
GN Name=PRB2;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-156.
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP PROTEIN SEQUENCE OF 17-112, PYROGLUTAMATE FORMATION AT GLN-17, AND
RP PHOSPHORYLATION AT SER-24.
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 [4]
RP PROTEIN SEQUENCE OF 52-112.
RC TISSUE=Saliva;
RX PubMed=6924859; DOI=10.1021/bi00268a036;
RA Kauffman D., Wong R., Bennick A., Keller P.;
RT "Basic proline-rich proteins from human parotid saliva: complete covalent
RT structure of protein IB-9 and partial structure of protein IB-6, members of
RT a polymorphic pair.";
RL Biochemistry 21:6558-6562(1982).
RN [5]
RP PROTEIN SEQUENCE OF 52-112.
RC TISSUE=Saliva;
RX PubMed=7118863; DOI=10.1093/oxfordjournals.jbchem.a133900;
RA Isemura S., Saitoh E., Sanada K.;
RT "Fractionation and characterization of basic proline-rich peptides of human
RT parotid saliva and the amino acid sequence of proline-rich peptide P-E.";
RL J. Biochem. 91:2067-2075(1982).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-416, PROTEIN SEQUENCE OF 175-235,
RP GLYCOSYLATION, AND VARIANT SER-274.
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 PROTEIN SEQUENCE OF 113-171; 299-359 AND 361-416.
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 166-416, AND VARIANT SER-274.
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 [9]
RP PROTEIN SEQUENCE OF 299-359.
RC TISSUE=Saliva;
RX PubMed=6874669; DOI=10.1093/jb/93.3.883;
RA Saitoh E., Isemura S., Sanada K.;
RT "Complete amino acid sequence of a basic proline-rich peptide, P-F, from
RT human parotid saliva.";
RL J. Biochem. 93:883-888(1983).
RN [10]
RP 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 [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 ASN-230; SER-232 AND ASN-272, PHOSPHORYLATION AT SER-52,
RP PYROGLUTAMATE FORMATION AT GLN-17, 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 -!- INTERACTION:
CC P02812; Q12797-6: ASPH; NbExp=3; IntAct=EBI-19951389, EBI-12092171;
CC P02812; Q96C03-3: MIEF2; NbExp=3; IntAct=EBI-19951389, EBI-11988931;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: N- and O-glycosylated. In head and neck cancer patients, O-
CC glycosylated with glucosylgalactosyl carbohydrate moiety. This
CC modification would require prior hydroxylation on the lysine residue.
CC {ECO:0000269|PubMed:20879038, ECO:0000269|PubMed:8554050}.
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. Pyroglutamate formation found on at least Gln-398 and Gln-
CC 400. {ECO:0000269|PubMed:18463091}.
CC -!- POLYMORPHISM: The number of repeats is polymorphic and varies among
CC different alleles (PubMed:2851479). {ECO:0000269|PubMed:2851479}.
CC -!- MISCELLANEOUS: Peptides IB-9 and P-E are the same peptide.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC078950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX484538; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; S80905; AAB50686.1; -; Genomic_DNA.
DR EMBL; K03208; AAA60189.1; -; mRNA.
DR CCDS; CCDS41757.2; -.
DR PIR; B40750; PIHUB6.
DR PIR; E25372; PIHUPF.
DR AlphaFoldDB; P02812; -.
DR IntAct; P02812; 4.
DR STRING; 9606.ENSP00000374013; -.
DR GlyGen; P02812; 4 sites.
DR iPTMnet; P02812; -.
DR PhosphoSitePlus; P02812; -.
DR BioMuta; PRB2; -.
DR DMDM; 160409933; -.
DR MassIVE; P02812; -.
DR PaxDb; P02812; -.
DR PeptideAtlas; P02812; -.
DR PRIDE; P02812; -.
DR ProteomicsDB; 51604; -.
DR TopDownProteomics; P02812; -.
DR Antibodypedia; 54442; 16 antibodies from 3 providers.
DR Ensembl; ENST00000389362.6; ENSP00000374013.4; ENSG00000121335.12.
DR MANE-Select; ENST00000389362.6; ENSP00000374013.4; NM_006248.4; NP_006239.3.
DR UCSC; uc010shk.2; human.
DR GeneCards; PRB2; -.
DR HGNC; HGNC:9338; PRB2.
DR HPA; ENSG00000121335; Tissue enriched (salivary).
DR MIM; 168810; gene.
DR neXtProt; NX_P02812; -.
DR OpenTargets; ENSG00000121335; -.
DR VEuPathDB; HostDB:ENSG00000121335; -.
DR eggNOG; ENOG502SEXN; Eukaryota.
DR GeneTree; ENSGT00730000111783; -.
DR HOGENOM; CLU_054768_0_0_1; -.
DR InParanoid; P02812; -.
DR PathwayCommons; P02812; -.
DR SignaLink; P02812; -.
DR ChiTaRS; PRB2; human.
DR Pharos; P02812; Tdark.
DR PRO; PR:P02812; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P02812; protein.
DR Bgee; ENSG00000121335; Expressed in caudate nucleus and 87 other tissues.
DR ExpressionAtlas; P02812; baseline and differential.
DR Genevisible; P02812; HS.
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:0000255"
FT CHAIN 17..416
FT /note="Basic salivary proline-rich protein 2"
FT /id="PRO_0000022095"
FT CHAIN 17..112
FT /note="Basic proline-rich peptide IB-1"
FT /id="PRO_0000097038"
FT CHAIN 52..112
FT /note="Basic proline-rich peptide P-E"
FT /id="PRO_0000395485"
FT CHAIN 113..171
FT /note="Basic proline-rich peptide IB-7"
FT /id="PRO_0000372439"
FT CHAIN 299..359
FT /note="Basic proline-rich peptide IB-8c"
FT /id="PRO_0000022096"
FT CHAIN 361..416
FT /note="Basic proline-rich peptide IB-4"
FT /id="PRO_0000372440"
FT REPEAT 53..72
FT /note="1"
FT REPEAT 74..93
FT /note="2"
FT REPEAT 94..113
FT /note="3"
FT REPEAT 114..133
FT /note="4"
FT REPEAT 135..154
FT /note="5"
FT REPEAT 155..174
FT /note="6"
FT REPEAT 176..195
FT /note="7"
FT REPEAT 197..216
FT /note="8"
FT REPEAT 217..236
FT /note="9"
FT REPEAT 238..257
FT /note="10"
FT REPEAT 259..278
FT /note="11"
FT REPEAT 279..298
FT /note="12"
FT REPEAT 300..319
FT /note="13"
FT REPEAT 321..340
FT /note="14"
FT REPEAT 341..360
FT /note="15"
FT REGION 19..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..360
FT /note="15 X 20 AA approximate tandem repeats of P-P-G-K-P-
FT Q-G-P-P-P-Q-G-[GD]-[NKS]-[KSQ]-[PRS]-[QRS] [GPS]-[PSAR]-
FT [PSR]"
FT COMPBIAS 43..163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..225
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..287
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..349
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..416
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:20879038,
FT ECO:0000269|PubMed:3521730"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:3521730"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20879038"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20879038"
FT CARBOHYD 232
FT /note="O-linked (Hex) serine"
FT /evidence="ECO:0000269|PubMed:20879038"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20879038"
FT VARIANT 233
FT /note="Q -> R (in dbSNP:rs34305575)"
FT /id="VAR_061693"
FT VARIANT 274
FT /note="P -> S (in dbSNP:rs10845349)"
FT /evidence="ECO:0000269|PubMed:2993301,
FT ECO:0000269|PubMed:8554050"
FT /id="VAR_019695"
FT CONFLICT 68
FT /note="P -> S (in Ref. 2; BX484538)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="K -> R (in Ref. 4; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="Q -> P (in Ref. 2; BX484538)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="G -> D (in Ref. 8; AAA60189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 40809 MW; 9D9BEF42B1053780 CRC64;
MLLILLSVAL LALSSAQNLN EDVSQEESPS LIAGNPQGAP PQGGNKPQGP PSPPGKPQGP
PPQGGNQPQG PPPPPGKPQG PPPQGGNKPQ GPPPPGKPQG PPPQGDKSRS PRSPPGKPQG
PPPQGGNQPQ GPPPPPGKPQ GPPPQGGNKP QGPPPPGKPQ GPPPQGDNKS RSSRSPPGKP
QGPPPQGGNQ PQGPPPPPGK PQGPPPQGGN KPQGPPPPGK PQGPPPQGDN KSQSARSPPG
KPQGPPPQGG NQPQGPPPPP GKPQGPPPQG GNKPQGPPPP GKPQGPPPQG GSKSRSSRSP
PGKPQGPPPQ GGNQPQGPPP PPGKPQGPPP QGGNKPQGPP PPGKPQGPPP QGGSKSRSAR
SPPGKPQGPP QQEGNNPQGP PPPAGGNPQQ PQAPPAGQPQ GPPRPPQGGR PSRPPQ
