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semaphorin-5A; semaphorin-F; sema F (SEMA5A, SEMAF)

Function: - may act as positive axonal guidance cues - binds PLXNB3 Structure: - belongs to the semaphorin family - contains 1 PSI domain - contains 1 sema domain - contains 7 TSP type-1 domains Compartment: - membrane; single-pass type 1 membrane protein

General

glycoprotein membrane protein phosphoprotein semaphorin or semaphorin/collapsin family protein

Properties

SIZE: entity length = 1074 aa MW = 121 kD COMPARTMENT: cellular membrane MOTIF: signal sequence {1-22} Sema {35-484} MOTIF: cysteine residue {C104} MODIFICATION: cysteine residue {C114} Ser phosphorylation site {S106} cysteine residue {C114} MODIFICATION: cysteine residue {C104} cysteine residue {C131} MODIFICATION: cysteine residue {C140} cysteine residue {C140} MODIFICATION: cysteine residue {C131} N-glycosylation site {N142} N-glycosylation site {N168} N-glycosylation site {N227} cysteine residue {C254} MODIFICATION: cysteine residue {C357} N-glycosylation site {N277} cysteine residue {C278} MODIFICATION: cysteine residue {C320} cysteine residue {C320} MODIFICATION: cysteine residue {C278} N-glycosylation site {N323} cysteine residue {C357} MODIFICATION: cysteine residue {C254} N-glycosylation site {N367} N-glycosylation site {N437} cysteine residue {C487} MODIFICATION: cysteine residue {C504} cysteine residue {C496} MODIFICATION: cysteine residue {C513} cysteine residue {C504} MODIFICATION: cysteine residue {C487} cysteine residue {C513} MODIFICATION: cysteine residue {C496} N-glycosylation site {N536} TSP1 module {540-593} MOTIF: N-glycosylation site {N591} TSP1 module {595-651} MOTIF: cysteine residue {C607} MODIFICATION: cysteine residue {C644} cysteine residue {C611} MODIFICATION: cysteine residue {C650} cysteine residue {C622} MODIFICATION: cysteine residue {C634} cysteine residue {C634} MODIFICATION: cysteine residue {C622} cysteine residue {C644} MODIFICATION: cysteine residue {C607} cysteine residue {C650} MODIFICATION: cysteine residue {C611} TSP1 module {653-702} MOTIF: cysteine residue {C665} MODIFICATION: cysteine residue {C696} cysteine residue {C669} MODIFICATION: cysteine residue {C701} cysteine residue {C680} MODIFICATION: cysteine residue {C686} cysteine residue {C686} MODIFICATION: cysteine residue {C680} cysteine residue {C696} MODIFICATION: cysteine residue {C665} cysteine residue {C701} MODIFICATION: cysteine residue {C669} TSP1 module {707-765} MOTIF: N-glycosylation site {N717} TSP1 module {784-839} MOTIF: cysteine residue {C796} MODIFICATION: cysteine residue {C833} cysteine residue {C800} MODIFICATION: cysteine residue {C838} cysteine residue {C811} MODIFICATION: cysteine residue {C823} cysteine residue {C823} MODIFICATION: cysteine residue {C811} cysteine residue {C833} MODIFICATION: cysteine residue {C796} cysteine residue {C838} MODIFICATION: cysteine residue {C800} TSP1 module {841-896} MOTIF: cysteine residue {C853} MODIFICATION: cysteine residue {C890} cysteine residue {C857} MODIFICATION: cysteine residue {C895} cysteine residue {C868} MODIFICATION: cysteine residue {C880} cysteine residue {C880} MODIFICATION: cysteine residue {C868} cysteine residue {C890} MODIFICATION: cysteine residue {C853} cysteine residue {C895} MODIFICATION: cysteine residue {C857} TSP1 module {897-944} MOTIF: N-glycosylation site {N933} transmembrane domain {969-989}

Database Correlations

OMIM 609297 UniProt Q13591 PFAM correlations Entrez Gene 9037 Kegg hsa:9037

References

  1. UniProt :accession Q13591
  2. Entrez Gene :accession 9037