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semaphorin-5B (SEMA5B, KIAA1445, SEMAG, UNQ5867/PRO34001)

Function: - positive role in axonal guidance cues (putative) Structure: - belongs to the semaphorin family - contains 1 PSI domain - contains 1 Sema domain - contains 7 TSP type-1 domains Compartment: membrane Alternative splicing: named isoforms=2

General

glycoprotein membrane protein semaphorin or semaphorin/collapsin family protein

Properties

SIZE: MW = 120 kD entity length = 1093 aa COMPARTMENT: cellular membrane MOTIF: signal sequence {1-26} Sema {45-495} MOTIF: N-glycosylation site {N59} N-glycosylation site {N95} cysteine residue {C114} MODIFICATION: cysteine residue {C124} cysteine residue {C124} MODIFICATION: cysteine residue {C114} cysteine residue {C141} MODIFICATION: cysteine residue {C150} cysteine residue {C150} MODIFICATION: cysteine residue {C141} N-glycosylation site {N157} N-glycosylation site {N178} cysteine residue {C264} MODIFICATION: cysteine residue {C367} N-glycosylation site {N287} cysteine residue {C288} MODIFICATION: cysteine residue {C330} cysteine residue {C330} MODIFICATION: cysteine residue {C288} N-glycosylation site {N333} cysteine residue {C367} MODIFICATION: cysteine residue {C264} N-glycosylation site {N378} N-glycosylation site {N532} N-glycosylation site {N539} N-glycosylation site {N547} TSP type-1 1 {551-605} MOTIF: N-glycosylation site {N602} TSP type-1 2 {606-662} MOTIF: cysteine residue {C618} MODIFICATION: cysteine residue {C655} cysteine residue {C622} MODIFICATION: cysteine residue {C661} cysteine residue {C633} MODIFICATION: cysteine residue {C645} cysteine residue {C645} MODIFICATION: cysteine residue {C633} cysteine residue {C655} MODIFICATION: cysteine residue {C618} cysteine residue {C661} MODIFICATION: cysteine residue {C622} TSP type-1 3 {664-713} MOTIF: cysteine residue {C676} MODIFICATION: cysteine residue {C707} cysteine residue {C680} MODIFICATION: cysteine residue {C712} cysteine residue {C691} MODIFICATION: cysteine residue {C697} cysteine residue {C697} MODIFICATION: cysteine residue {C691} cysteine residue {C707} MODIFICATION: cysteine residue {C676} cysteine residue {C712} MODIFICATION: cysteine residue {C680} TSP type-1 4 {721-776} MOTIF: N-glycosylation site {N728} TSP type-1 5 {795-850} MOTIF: cysteine residue {C807} MODIFICATION: cysteine residue {C844} cysteine residue {C811} MODIFICATION: cysteine residue {C849} cysteine residue {C822} MODIFICATION: cysteine residue {C834} cysteine residue {C834} MODIFICATION: cysteine residue {C822} cysteine residue {C844} MODIFICATION: cysteine residue {C807} cysteine residue {C849} MODIFICATION: cysteine residue {C811} TSP type-1 6 {852-907} MOTIF: cysteine residue {C864} MODIFICATION: cysteine residue {C901} cysteine residue {C868} MODIFICATION: cysteine residue {C906} cysteine residue {C879} MODIFICATION: cysteine residue {C891} cysteine residue {C891} MODIFICATION: cysteine residue {C879} cysteine residue {C901} MODIFICATION: cysteine residue {C864} cysteine residue {C906} MODIFICATION: cysteine residue {C868} TSP type-1 7 {908-952} MOTIF: N-glycosylation site {N944} transmembrane domain {979-999}

Database Correlations

UniProt Q9P283 PFAM correlations Entrez Gene 54437

References

UniProt :accession Q9P283