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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
- UniProt :accession Q13591
- Entrez Gene :accession 9037