SEMA3F

From Wikipedia, the free encyclopedia


Sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3F
Identifiers
Symbol(s) SEMA3F; SEMA-IV; SEMA4; SEMAK; sema IV
External IDs OMIM: 601124 MGI: 1096347 HomoloGene: 20885
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 6405 20350
Ensembl ENSG00000001617 ENSMUSG00000034684
Uniprot Q13275 O88632
Refseq NM_004186 (mRNA)
NP_004177 (protein)		 NM_011349 (mRNA)
NP_035479 (protein)
Location Chr 3: 50.17 - 50.2 Mb Chr 9: 107.54 - 107.57 Mb
Pubmed search [1] [2]

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]

[edit] References

  1. ^ a b Entrez Gene: SEMA3F sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3F.

[edit] 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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