SEMA3F

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Sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3F
Identifiers
Symbols SEMA3F ; SEMA-IV; SEMA4; SEMAK; sema IV
External IDs Template:OMIM5 Template:MGI HomoloGene20885
RNA expression pattern
File:PBB GE SEMA3F 35666 at tn.png
File:PBB GE SEMA3F 206832 s at tn.png
File:PBB GE SEMA3F 209730 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3F, also known as SEMA3F, is a human gene.[1]

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, all of which also have an immunoglobulin domain. The semaphorin III family, consisting of human semaphorin III (SEMA3A; MIM 603961), chicken collapsin, and mouse semaphorins A, D, and E, 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][1]

References

  1. 1.0 1.1 "Entrez Gene: SEMA3F sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3F".

Further reading

  • Goshima Y, Nakamura F, Strittmatter P, Strittmatter SM (1995). "Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33". Nature. 376 (6540): 509–14. doi:10.1038/376509a0. PMID 7637782.
  • Kolodkin AL, Matthes DJ, Goodman CS (1994). "The semaphorin genes encode a family of transmembrane and secreted growth cone guidance molecules". Cell. 75 (7): 1389–99. PMID 8269517.
  • Luo Y, Raible D, Raper JA (1993). "Collapsin: a protein in brain that induces the collapse and paralysis of neuronal growth cones". Cell. 75 (2): 217–27. PMID 8402908.
  • Sekido Y, Bader S, Latif F; et al. (1996). "Human semaphorins A(V) and IV reside in the 3p21.3 small cell lung cancer deletion region and demonstrate distinct expression patterns". Proc. Natl. Acad. Sci. U.S.A. 93 (9): 4120–5. PMID 8633026.
  • Roche J, Boldog F, Robinson M; et al. (1996). "Distinct 3p21.3 deletions in lung cancer and identification of a new human semaphorin". Oncogene. 12 (6): 1289–97. PMID 8649831.
  • Xiang RH, Hensel CH, Garcia DK; et al. (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. PMID 8786119.
  • Chen H, He Z, Bagri A, Tessier-Lavigne M (1999). "Semaphorin-neuropilin interactions underlying sympathetic axon responses to class III semaphorins". Neuron. 21 (6): 1283–90. PMID 9883722.
  • Hirsch E, Hu LJ, Prigent A; et al. (1999). "Distribution of semaphorin IV in adult human brain". Brain Res. 823 (1–2): 67–79. PMID 10095013.
  • Brambilla E, Constantin B, Drabkin H, Roche J (2000). "Semaphorin SEMA3F localization in malignant human lung and cell lines: A suggested role in cell adhesion and cell migration". Am. J. Pathol. 156 (3): 939–50. PMID 10702410.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Nasarre P, Constantin B, Rouhaud L; et al. (2003). "Semaphorin SEMA3F and VEGF have opposing effects on cell attachment and spreading". Neoplasia. 5 (1): 83–92. PMID 12659673.
  • Lantuéjoul S, Constantin B, Drabkin H; et al. (2003). "Expression of VEGF, semaphorin SEMA3F, and their common receptors neuropilins NP1 and NP2 in preinvasive bronchial lesions, lung tumours, and cell lines". J. Pathol. 200 (3): 336–47. doi:10.1002/path.1367. PMID 12845630.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Bielenberg DR, Hida Y, Shimizu A; et al. (2004). "Semaphorin 3F, a chemorepulsant for endothelial cells, induces a poorly vascularized, encapsulated, nonmetastatic tumor phenotype". J. Clin. Invest. 114 (9): 1260–71. doi:10.1172/JCI200421378. PMID 15520858.
  • Gu C, Yoshida Y, Livet J; et al. (2005). "Semaphorin 3E and plexin-D1 control vascular pattern independently of neuropilins". Science. 307 (5707): 265–8. doi:10.1126/science.1105416. PMID 15550623.
  • 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. PMID 15862967.
  • Kusy S, Nasarre P, Chan D; et al. (2005). "Selective suppression of in vivo tumorigenicity by semaphorin SEMA3F in lung cancer cells". Neoplasia. 7 (5): 457–65. PMID 15967098.
  • Futamura M, Kamino H, Miyamoto Y; et al. (2007). "Possible role of semaphorin 3F, a candidate tumor suppressor gene at 3p21.3, in p53-regulated tumor angiogenesis suppression". Cancer Res. 67 (4): 1451–60. doi:10.1158/0008-5472.CAN-06-2485. PMID 17308083.
  • Guttmann-Raviv N, Shraga-Heled N, Varshavsky A; et al. (2007). "Semaphorin-3A and semaphorin-3F work together to repel endothelial cells and to inhibit their survival by induction of apoptosis". J. Biol. Chem. 282 (36): 26294–305. doi:10.1074/jbc.M609711200. PMID 17569671.
  • Menon L, Mihailescu MR (2007). "Interactions of the G quartet forming semaphorin 3F RNA with the RGG box domain of the fragile X protein family". Nucleic Acids Res. 35 (16): 5379–92. doi:10.1093/nar/gkm581. PMID 17693432.

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