plexin-B1; Semaphorin receptor SEP (PLXNB1 KIAA0407 PLXN5 SEP)

Function: 1) binds a) semaphorin 4D: binding - promotes binding of cytoplasmic ligands b) plexin A1 c) Rho guanine nucleotide exchange factor 11 (ARHGEF11) d) Rho guanine nucleotide exchange factor 12 (ARHGEF12) e) erb B2 f) c-met protein g) macrophage stimulating 1 receptor (MST1R) h) rho6 protein (RND1) i) neuropilin 1 (NRP1) j) neuropilin 2 (NRP2) h) RAC1 that has been activated by GTP binding 2) phosphorylated (after semaphorin 4D binding) by a) erb B2 b) c-met protein 3) rhoA activation 4) changes of the actin cytoskeleton 5) axon guidance 6) invasive growth and cell migration Structure: - monomer, & heterodimer with PLXNB2 after proteolytic processing - proteolytic processing favors heterodimerization with PLXNB2 & SEMA4D binding - belongs to the plexin family - contains 3 IPT/TIG domains - contains 1 Sema domain Compartment: - isoform 1: cell membrane - isoforms 2,3: secreted Alternative splicing: named isoforms=3 Expression: - high expression in fetal kidney - lower expression in fetal brain, lung liver Pathology: - overexpressed & constitutively Tyr phosphorylated in carcinoma cell lines a) colon carcinoma b) hepatocellular carcinoma c) pancreatic carcinoma d) gastric carcinoma - promotion of invasive growth from overexpression & c-MET activation

Properties

SIZE: entity length = 2135 aa MW = 232 kD COMPARTMENT: cellular membrane MOTIF: signal sequence {1-19} Sema {20-479} MOTIF: N-glycosylation site {N31} N-glycosylation site {N334} N-glycosylation site {N543} proline-rich region SITE: 678-829 MOTIF: proline residue (SEVERAL) IPT/TIG 1 {1070-1160} IPT/TIG 2 {1162-1249} MOTIF: N-glycosylation site {N1183} IPT/TIG 3 {1252-1375} MOTIF: N-glycosylation site {N1253} arginine-rich region {1302-1305} MOTIF: arginine residue (SEVERAL) peptide motif {1305-1306} N-glycosylation site {N1330} transmembrane domain {1491-1511} coiled coil {1507-1539}

Database Correlations

OMIM 601053 UniProt O43157 PFAM correlations Entrez Gene 5364 Kegg hsa:5364

References

Uniprot O43157