Semaphorin-3F is a
protein that in humans is encoded by the SEMA3Fgene.[5][6][7]
The
semaphorins are a family of proteins that are involved in signaling. All the family members have a secretion signal, a 500-amino acid sema domain, and 16 conserved cysteine residues (Kolodkin et al., 1993). Sequence comparisons have grouped the secreted semaphorins into 3 general classes (classes 2, 3 and V), all of which also have an immunoglobulin domain. The semaphorin 3 family, consisting of human semaphorins 3A-G (SEMA3A; MIM 603961), chicken collapsin, and mouse semaphorins 3A-G, all have a basic domain at the C terminus. Chicken collapsin contributes to path finding by axons during development by inhibiting extension of growth cones (Luo et al., 1993) through an interaction with a collapsin response mediator protein of relative molecular mass 62K (CRMP62) (Goshima et al., 1995), a putative homolog of an axonal guidance associated UNC33 gene product (MIM 601168). SEMA3F is a secreted member of the semaphorin III family.[supplied by OMIM][7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Xiang RH, Hensel CH, Garcia DK, Carlson HC, Kok K, Daly MC, Kerbacher K, van den Berg A, Veldhuis P, Buys CH, Naylor SL (Sep 1996). "Isolation of the human semaphorin III/F gene (SEMA3F) at chromosome 3p21, a region deleted in lung cancer". Genomics. 32 (1): 39–48.
doi:
10.1006/geno.1996.0074.
PMID8786119.
^Roche J, Boldog F, Robinson M, Robinson L, Varella-Garcia M, Swanton M, Waggoner B, Fishel R, Franklin W, Gemmill R, Drabkin H (Jul 1996). "Distinct 3p21.3 deletions in lung cancer and identification of a new human semaphorin". Oncogene. 12 (6): 1289–97.
PMID8649831.
Pope SN, Lee IR (2005). "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin". J. Steroid Biochem. Mol. Biol. 94 (1–3): 203–8.
doi:
10.1016/j.jsbmb.2005.01.007.
PMID15862967.
S2CID9746088.
Semaphorin-3F is a
protein that in humans is encoded by the SEMA3Fgene.[5][6][7]
The
semaphorins are a family of proteins that are involved in signaling. All the family members have a secretion signal, a 500-amino acid sema domain, and 16 conserved cysteine residues (Kolodkin et al., 1993). Sequence comparisons have grouped the secreted semaphorins into 3 general classes (classes 2, 3 and V), all of which also have an immunoglobulin domain. The semaphorin 3 family, consisting of human semaphorins 3A-G (SEMA3A; MIM 603961), chicken collapsin, and mouse semaphorins 3A-G, all have a basic domain at the C terminus. Chicken collapsin contributes to path finding by axons during development by inhibiting extension of growth cones (Luo et al., 1993) through an interaction with a collapsin response mediator protein of relative molecular mass 62K (CRMP62) (Goshima et al., 1995), a putative homolog of an axonal guidance associated UNC33 gene product (MIM 601168). SEMA3F is a secreted member of the semaphorin III family.[supplied by OMIM][7]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Xiang RH, Hensel CH, Garcia DK, Carlson HC, Kok K, Daly MC, Kerbacher K, van den Berg A, Veldhuis P, Buys CH, Naylor SL (Sep 1996). "Isolation of the human semaphorin III/F gene (SEMA3F) at chromosome 3p21, a region deleted in lung cancer". Genomics. 32 (1): 39–48.
doi:
10.1006/geno.1996.0074.
PMID8786119.
^Roche J, Boldog F, Robinson M, Robinson L, Varella-Garcia M, Swanton M, Waggoner B, Fishel R, Franklin W, Gemmill R, Drabkin H (Jul 1996). "Distinct 3p21.3 deletions in lung cancer and identification of a new human semaphorin". Oncogene. 12 (6): 1289–97.
PMID8649831.
Pope SN, Lee IR (2005). "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin". J. Steroid Biochem. Mol. Biol. 94 (1–3): 203–8.
doi:
10.1016/j.jsbmb.2005.01.007.
PMID15862967.
S2CID9746088.