Detail Information for IndEnz0018001484
IED ID IndEnz0018001484
Enzyme Type ID peroxidase001484
Protein Name Basic salivary proline-rich protein 3
Parotid salivary glycoprotein G1
Proline-rich protein G1
Gene Name PRB3
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MLLILLSVALLALSSAQSLNEDVSQEESPSVISGKPEGRRPQGGNQPQRTPPPPGKPEGRPPQGGNQSQGPPPRPGKPEGPPPQGGNQSQGPPPRPGKPEGQPPQGGNQSQGPPPRPGKPEGPPPQGGNQSQGPPPRPGKPEGPPPQGGNQSQGPPPHPGKPEGPPPQGGNQSQGPPPRPGKPEGPPPQGGNQSQGPPPRPGKPEGPPPQGGNQSQGPPPRPGKPEGSPSQGGNKPQGPPPHPGKPQGPPPQEGNKPQRPPPPGRPQGPPPPGGNPQQPLPPPAGKPQGPPPPPQGGRPHRPPQGQPPQ
Enzyme Length 309
Uniprot Accession Number Q04118
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Acts as a receptor for the Gram-negative bacterium F.nucleatum. {ECO:0000269|PubMed:1894623}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (4); Erroneous translation (1); Glycosylation (10); Modified residue (2); Natural variant (3); Region (2); Repeat (10); Sequence conflict (13); Signal peptide (1)
Keywords Direct protein sequencing;Disulfide bond;Glycoprotein;Phosphoprotein;Pyrrolidone carboxylic acid;Reference proteome;Repeat;Secreted;Signal
Interact With O43681; Q96AL5; P30405; Q96EQ0; Q99961; Q969Z0
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue MOD_RES 17; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:20879038; MOD_RES 24; /note=Phosphoserine; /evidence=ECO:0000269|PubMed:20879038
Post Translational Modification PTM: The Gl-8 variant contains an interchain disulfide bond with salivary peroxidase.; PTM: N- and O-glycosylated; contains about 50% carbohydrate. This is composed of highly fucosylated N-linked saccharides, the major structure is a biantennary asialosaccharide containing 2 fucose residues on one antenna and an unsubstituted terminal lactosamine sequence on the other. The Gram-negative bacterium F.nucleatum binds to carbohydrates containing unsubstituted GalBeta1,4GlcNAc residues. N-glycosylation on Asn-87 is prevalent in head and neck cancer patients. {ECO:0000269|PubMed:1894623, ECO:0000269|PubMed:20879038}.; PTM: Proteolytically cleaved at the tripeptide Xaa-Pro-Gln, where Xaa in the P(3) position is mostly lysine. The endoprotease may be of microbial origin. Besides on the N-terminal of mature PRB3, pyroglutamate formation found on at least Gln-67, Gln-88, Gln-214 and Gln-295. {ECO:0000269|PubMed:18463091}.
Signal Peptide SIGNAL 1..16; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 24135847;
Motif
Gene Encoded By
Mass 30,980
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda