PRB3_HUMAN
ID PRB3_HUMAN Reviewed; 309 AA.
AC Q04118; Q15188; Q4VAY3; Q4VAY4; Q7M4M9; Q9UCT9;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Basic salivary proline-rich protein 3;
DE AltName: Full=Parotid salivary glycoprotein G1;
DE AltName: Full=Proline-rich protein G1;
DE Flags: Precursor;
GN Name=PRB3;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE L), AND VARIANT GLN-186.
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-309 (ALLELE S), VARIANT GL-8
RP CYS-53, INTERACTION WITH SALIVARY PEROXIDASE, AND DISULFIDE BOND.
RX PubMed=2171329;
RA Azen E.A., Minaguchi K., Latreille P., Kim H.-S.;
RT "Alleles at the PRB3 locus coding for a disulfide-bonded human salivary
RT proline-rich glycoprotein (Gl 8) and a null in an Ashkenazi Jew.";
RL Am. J. Hum. Genet. 47:686-697(1990).
RN [4]
RP PROTEIN SEQUENCE OF 68-92; 110-127; 131-148; 173-190 AND 194-211, FUNCTION,
RP AND GLYCOSYLATION.
RC TISSUE=Saliva;
RX PubMed=1894623; DOI=10.1016/s0021-9258(19)47381-x;
RA Gillece-Castro B.L., Prakobphol A., Burlingame A.L., Leffler H.,
RA Fisher S.J.;
RT "Structure and bacterial receptor activity of a human salivary proline-rich
RT glycoprotein.";
RL J. Biol. Chem. 266:17358-17368(1991).
RN [5]
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 [6]
RP GLYCOSYLATION AT ASN-87; SER-89 AND ASN-255, PYROGLUTAMATE FORMATION AT
RP GLN-17, PHOSPHORYLATION AT SER-24, 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 -!- FUNCTION: Acts as a receptor for the Gram-negative bacterium
CC F.nucleatum. {ECO:0000269|PubMed:1894623}.
CC -!- SUBUNIT: The Gl-8 variant forms a disulfide-bonded heterodimer with
CC salivary perodixase.
CC -!- INTERACTION:
CC Q04118; O43681: GET3; NbExp=3; IntAct=EBI-13360404, EBI-2515857;
CC Q04118; Q96AL5: PBX3; NbExp=3; IntAct=EBI-13360404, EBI-741171;
CC Q04118; P30405: PPIF; NbExp=3; IntAct=EBI-13360404, EBI-5544229;
CC Q04118; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-13360404, EBI-744081;
CC Q04118; Q99961: SH3GL1; NbExp=3; IntAct=EBI-13360404, EBI-697911;
CC Q04118; Q969Z0: TBRG4; NbExp=3; IntAct=EBI-13360404, EBI-702328;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: The Gl-8 variant contains an interchain disulfide bond with
CC salivary peroxidase.
CC -!- PTM: N- and O-glycosylated; contains about 50% carbohydrate. This is
CC composed of highly fucosylated N-linked saccharides, the major
CC structure is a biantennary asialosaccharide containing 2 fucose
CC residues on one antenna and an unsubstituted terminal lactosamine
CC sequence on the other. The Gram-negative bacterium F.nucleatum binds to
CC carbohydrates containing unsubstituted GalBeta1,4GlcNAc residues. N-
CC glycosylation on Asn-87 is prevalent in head and neck cancer patients.
CC {ECO:0000269|PubMed:1894623, 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. Besides on the N-terminal of mature PRB3,
CC pyroglutamate formation found on at least Gln-67, Gln-88, Gln-214 and
CC Gln-295. {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 is an allele S (short) which contains 6 tandem repeats.
CC {ECO:0000269|PubMed:2851479}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA30477.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; X07637; CAA30477.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X07881; CAA30728.1; -; Genomic_DNA.
DR EMBL; BC096209; AAH96209.1; -; mRNA.
DR EMBL; BC096210; AAH96210.1; -; mRNA.
DR EMBL; BC096211; AAH96211.1; -; mRNA.
DR PIR; A36298; A36298.
DR PIR; B36298; B36298.
DR PIR; S10889; S10889.
DR AlphaFoldDB; Q04118; -.
DR IntAct; Q04118; 14.
DR STRING; 9606.ENSP00000442626; -.
DR GlyGen; Q04118; 10 sites.
DR iPTMnet; Q04118; -.
DR PhosphoSitePlus; Q04118; -.
DR BioMuta; PRB3; -.
DR DMDM; 229462763; -.
DR MassIVE; Q04118; -.
DR PeptideAtlas; Q04118; -.
DR PRIDE; Q04118; -.
DR ProteomicsDB; 58235; -.
DR TopDownProteomics; Q04118; -.
DR Antibodypedia; 71505; 16 antibodies from 7 providers.
DR Ensembl; ENST00000381842.7; ENSP00000371264.3; ENSG00000197870.13.
DR UCSC; uc058lgs.1; human.
DR GeneCards; PRB3; -.
DR HGNC; HGNC:9339; PRB3.
DR HPA; ENSG00000197870; Tissue enriched (salivary).
DR MIM; 168840; gene.
DR neXtProt; NX_Q04118; -.
DR PharmGKB; PA33701; -.
DR VEuPathDB; HostDB:ENSG00000197870; -.
DR eggNOG; ENOG502SEXN; Eukaryota.
DR InParanoid; Q04118; -.
DR PathwayCommons; Q04118; -.
DR SignaLink; Q04118; -.
DR Pharos; Q04118; Tdark.
DR PRO; PR:Q04118; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q04118; protein.
DR Bgee; ENSG00000197870; Expressed in olfactory segment of nasal mucosa and 85 other tissues.
DR ExpressionAtlas; Q04118; baseline and differential.
DR Genevisible; Q04118; HS.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; NAS:UniProtKB.
DR InterPro; IPR026086; Pro-rich.
DR PANTHER; PTHR23203; PTHR23203; 4.
DR Pfam; PF15240; Pro-rich; 2.
DR SMART; SM01412; Pro-rich; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..309
FT /note="Basic salivary proline-rich protein 3"
FT /id="PRO_0000022097"
FT REPEAT 53..73
FT /note="1"
FT REPEAT 74..94
FT /note="2"
FT REPEAT 95..115
FT /note="3"
FT REPEAT 116..136
FT /note="4"
FT REPEAT 137..157
FT /note="5"
FT REPEAT 158..178
FT /note="6"
FT REPEAT 179..199
FT /note="7"
FT REPEAT 200..220
FT /note="8"
FT REPEAT 221..241
FT /note="9"
FT REPEAT 242..262
FT /note="10"
FT REGION 17..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..262
FT /note="10 X 21 AA tandem repeats of [RH]-P-G-K-P-[EQ]-G-
FT [PQS]-P-[PS]-Q-[GE]-G-N-[QK]-[SP]-[QR]-[GR]-P-P-P"
FT COMPBIAS 17..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..101
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..226
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..309
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 MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20879038"
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 89
FT /note="O-linked (Hex) serine"
FT /evidence="ECO:0000269|PubMed:20879038"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
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 255
FT /note="N-linked (Hex) asparagine; atypical"
FT /evidence="ECO:0000269|PubMed:20879038"
FT VARIANT 53
FT /note="P -> C (in Gl-8; requires 2 nucleotide
FT substitutions)"
FT /evidence="ECO:0000269|PubMed:2171329"
FT /id="VAR_019696"
FT VARIANT 158..220
FT /note="Missing (in allele S)"
FT /id="VAR_055031"
FT VARIANT 186
FT /note="P -> Q (in dbSNP:rs113564509)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_055032"
FT CONFLICT 40
FT /note="R -> P (in Ref. 1; CAA30728)"
FT /evidence="ECO:0000305"
FT CONFLICT 47..53
FT /note="PQRTPPP -> SQGPPPR (in Ref. 1; CAA30728)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="P -> S (in Ref. 1; CAA30477)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="R -> P (in Ref. 1; CAA30728)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="P -> Q (in Ref. 1; CAA30728)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="Q -> P (in Ref. 1; CAA30728)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="K -> E (in Ref. 1; CAA30728)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="R -> H (in Ref. 1; CAA30728)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="H -> R (in Ref. 1; CAA30728 and 2; AAH96211)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="Q -> R (in Ref. 1; CAA30728)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="G -> R (in Ref. 1; CAA30728/CAA30477)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 30980 MW; A8FCBEBA784618C6 CRC64;
MLLILLSVAL LALSSAQSLN EDVSQEESPS VISGKPEGRR PQGGNQPQRT PPPPGKPEGR
PPQGGNQSQG PPPRPGKPEG PPPQGGNQSQ GPPPRPGKPE GQPPQGGNQS QGPPPRPGKP
EGPPPQGGNQ SQGPPPRPGK PEGPPPQGGN QSQGPPPHPG KPEGPPPQGG NQSQGPPPRP
GKPEGPPPQG GNQSQGPPPR PGKPEGPPPQ GGNQSQGPPP RPGKPEGSPS QGGNKPQGPP
PHPGKPQGPP PQEGNKPQRP PPPGRPQGPP PPGGNPQQPL PPPAGKPQGP PPPPQGGRPH
RPPQGQPPQ
