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semaphorin-6A; semaphorin VIA; sema VIA; semaphorin-6A-1; SEMA6A-1 (SEMA6A, KIAA1368, SEMAQ)

Function: - cell surface receptor for PLXNA2 - role in cell-cell signaling - required for normal granule cell migration in the developing cerebellum - promotes reorganization of the actin cytoskeleton - role in axon guidance in the developing CNS - can act as repulsive axon guidance cue - repulsive action towards migrating granular neurons - may play a role in channeling sympathetic axons into the sympathetic chains & controlling the temporal sequence of sympathetic target innervation - active as a homodimer or oligomer - the SEMA6A homodimer interacts with a PLXNA2 homodimer, giving rise to a heterotetramer (putative) - interacts with EVL Structure: - belongs to the semaphorin family - contains 1 PSI domain - contains 1 sema domain Compartment: - plasma membrane; single-pass type 1 membrane protein Alternative splicing: named isoforms=2

General

glycoprotein human longevity protein membrane protein semaphorin or semaphorin/collapsin family protein

Properties

SIZE: entity length = 1030 aa MW = 114 kD COMPARTMENT: cellular membrane MOTIF: signal sequence {1-18} Sema {24-512} MOTIF: N-glycosylation site {N33} N-glycosylation site {N49} N-glycosylation site {N65} cysteine residue {C107} MODIFICATION: cysteine residue {C117} cysteine residue {C117} MODIFICATION: cysteine residue {C107} cysteine residue {C135} MODIFICATION: cysteine residue {C144} cysteine residue {C144} MODIFICATION: cysteine residue {C135} cysteine residue {C258} MODIFICATION: cysteine residue {C369} N-glycosylation site {N282} cysteine residue {C283} MODIFICATION: cysteine residue {C328} cysteine residue {C328} MODIFICATION: cysteine residue {C283} cysteine residue {C369} MODIFICATION: cysteine residue {C258} N-glycosylation site {N434} N-glycosylation site {N461} cysteine residue {C477} MODIFICATION: cysteine residue {C506} cysteine residue {C506} MODIFICATION: cysteine residue {C477} cysteine residue {C515} MODIFICATION: cysteine residue {C533} cysteine residue {C521} MODIFICATION: cysteine residue {C568} cysteine residue {C525} MODIFICATION: cysteine residue {C542} cysteine residue {C533} MODIFICATION: cysteine residue {C515} cysteine residue {C542} MODIFICATION: cysteine residue {C525} cysteine residue {C568} MODIFICATION: cysteine residue {C521} transmembrane domain {650-670} proline-rich region SITE: 792-819 MOTIF: proline residue (SEVERAL)

Database Correlations

OMIM 605885 UniProt Q9H2E6 PFAM correlations Entrez Gene 57556 Kegg hsa:57556

References

  1. UniProt :accession Q9H2E6
  2. Entrez Gene :accession 57556