SEMA3F: Difference between revisions

Jump to navigation Jump to search
m (Robot: Automated text replacement (-{{reflist}} +{{reflist|2}}, -<references /> +{{reflist|2}}, -{{WikiDoc Cardiology Network Infobox}} +))
 
m (Bot: HTTP→HTTPS)
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Semaphorin-3F''' is a [[protein]] that in humans is encoded by the ''SEMA3F'' [[gene]].<ref name="pmid8786119">{{cite journal | vauthors = Xiang RH, Hensel CH, Garcia DK, Carlson HC, Kok K, Daly MC, Kerbacher K, van den Berg A, Veldhuis P, Buys CH, Naylor SL | title = Isolation of the human semaphorin III/F gene (SEMA3F) at chromosome 3p21, a region deleted in lung cancer | journal = Genomics | volume = 32 | issue = 1 | pages = 39–48 |date=Sep 1996 | pmid = 8786119 | pmc =  | doi = 10.1006/geno.1996.0074 }}</ref><ref name="pmid8649831">{{cite journal | vauthors = Roche J, Boldog F, Robinson M, Robinson L, Varella-Garcia M, Swanton M, Waggoner B, Fishel R, Franklin W, Gemmill R, Drabkin H | title = Distinct 3p21.3 deletions in lung cancer and identification of a new human semaphorin | journal = Oncogene | volume = 12 | issue = 6 | pages = 1289–97 |date=Jul 1996 | pmid = 8649831 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SEMA3F sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3F| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6405| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
 
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source = 
| PDB =
| Name = Sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3F
| HGNCid = 10728
| Symbol = SEMA3F
| AltSymbols =; SEMA-IV; SEMA4; SEMAK; sema IV
| OMIM = 601124
| ECnumber =
| Homologene = 20885
| MGIid = 1096347
  | GeneAtlas_image1 = PBB_GE_SEMA3F_35666_at_tn.png
| GeneAtlas_image2 = PBB_GE_SEMA3F_206832_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_SEMA3F_209730_at_tn.png
| Function = {{GNF_GO|id=GO:0045499 |text = chemorepellant activity}}  
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0001755 |text = neural crest cell migration}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0050919 |text = negative chemotaxis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6405
    | Hs_Ensembl = ENSG00000001617
    | Hs_RefseqProtein = NP_004177
    | Hs_RefseqmRNA = NM_004186
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 50167528
    | Hs_GenLoc_end = 50201511
    | Hs_Uniprot = Q13275
    | Mm_EntrezGene = 20350
    | Mm_Ensembl = ENSMUSG00000034684
    | Mm_RefseqmRNA = NM_011349
    | Mm_RefseqProtein = NP_035479
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 107539603
    | Mm_GenLoc_end = 107568576
    | Mm_Uniprot = O88632
  }}
}}
'''Sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3F''', also known as '''SEMA3F''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SEMA3F sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3F| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6405| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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]<ref name="entrez">{{cite web | title = Entrez Gene: SEMA3F sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3F| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6405| accessdate = }}</ref>
| summary_text = The [[semaphorin]]s 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]<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Goshima Y, Nakamura F, Strittmatter P, Strittmatter SM |title=Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33. |journal=Nature |volume=376 |issue= 6540 |pages= 509-14 |year= 1995 |pmid= 7637782 |doi= 10.1038/376509a0 }}
*{{cite journal  | vauthors=Goshima Y, Nakamura F, Strittmatter P, Strittmatter SM |title=Collapsin-induced growth cone collapse mediated by an intracellular protein related to UNC-33. |journal=Nature |volume=376 |issue= 6540 |pages= 509–14 |year= 1995 |pmid= 7637782 |doi= 10.1038/376509a0 }}
*{{cite journal  | author=Kolodkin AL, Matthes DJ, Goodman CS |title=The semaphorin genes encode a family of transmembrane and secreted growth cone guidance molecules. |journal=Cell |volume=75 |issue= 7 |pages= 1389-99 |year= 1994 |pmid= 8269517 |doi=  }}
*{{cite journal  | vauthors=Kolodkin AL, Matthes DJ, Goodman CS |title=The semaphorin genes encode a family of transmembrane and secreted growth cone guidance molecules. |journal=Cell |volume=75 |issue= 7 |pages= 1389–99 |year= 1994 |pmid= 8269517 |doi=10.1016/0092-8674(93)90625-Z }}
*{{cite journal  | author=Luo Y, Raible D, Raper JA |title=Collapsin: a protein in brain that induces the collapse and paralysis of neuronal growth cones. |journal=Cell |volume=75 |issue= 2 |pages= 217-27 |year= 1993 |pmid= 8402908 |doi=  }}
*{{cite journal  | vauthors=Luo Y, Raible D, Raper JA |title=Collapsin: a protein in brain that induces the collapse and paralysis of neuronal growth cones. |journal=Cell |volume=75 |issue= 2 |pages= 217–27 |year= 1993 |pmid= 8402908 |doi=10.1016/0092-8674(93)80064-L }}
*{{cite journal | author=Sekido Y, Bader S, Latif F, ''et al.'' |title=Human semaphorins A(V) and IV reside in the 3p21.3 small cell lung cancer deletion region and demonstrate distinct expression patterns. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 9 |pages= 4120-5 |year= 1996 |pmid= 8633026 |doi=  }}
*{{cite journal   |vauthors=Sekido Y, Bader S, Latif F, etal |title=Human semaphorins A(V) and IV reside in the 3p21.3 small cell lung cancer deletion region and demonstrate distinct expression patterns. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 9 |pages= 4120–5 |year= 1996 |pmid= 8633026 |doi=10.1073/pnas.93.9.4120  | pmc=39497 }}
*{{cite journal  | author=Roche J, Boldog F, Robinson M, ''et al.'' |title=Distinct 3p21.3 deletions in lung cancer and identification of a new human semaphorin. |journal=Oncogene |volume=12 |issue= 6 |pages= 1289-97 |year= 1996 |pmid= 8649831 |doi=  }}
*{{cite journal  | vauthors=Chen H, He Z, Bagri A, Tessier-Lavigne M |title=Semaphorin-neuropilin interactions underlying sympathetic axon responses to class III semaphorins. |journal=Neuron |volume=21 |issue= 6 |pages= 1283–90 |year= 1999 |pmid= 9883722 |doi=10.1016/S0896-6273(00)80648-0 }}
*{{cite journal | author=Xiang RH, Hensel CH, Garcia DK, ''et al.'' |title=Isolation of the human semaphorin III/F gene (SEMA3F) at chromosome 3p21, a region deleted in lung cancer. |journal=Genomics |volume=32 |issue= 1 |pages= 39-48 |year= 1996 |pmid= 8786119 |doi= 10.1006/geno.1996.0074 }}
*{{cite journal   |vauthors=Hirsch E, Hu LJ, Prigent A, etal |title=Distribution of semaphorin IV in adult human brain. |journal=Brain Res. |volume=823 |issue= 1-2 |pages= 67–79 |year= 1999 |pmid= 10095013 |doi=10.1016/S0006-8993(99)01103-8  }}
*{{cite journal  | author=Chen H, He Z, Bagri A, Tessier-Lavigne M |title=Semaphorin-neuropilin interactions underlying sympathetic axon responses to class III semaphorins. |journal=Neuron |volume=21 |issue= 6 |pages= 1283-90 |year= 1999 |pmid= 9883722 |doi=  }}
*{{cite journal  | vauthors=Brambilla E, Constantin B, Drabkin H, Roche J |title=Semaphorin SEMA3F localization in malignant human lung and cell lines: A suggested role in cell adhesion and cell migration. |journal=Am. J. Pathol. |volume=156 |issue= 3 |pages= 939–50 |year= 2000 |pmid= 10702410 |doi= 10.1016/S0002-9440(10)64962-0| pmc=1876858 }}
*{{cite journal | author=Hirsch E, Hu LJ, Prigent A, ''et al.'' |title=Distribution of semaphorin IV in adult human brain. |journal=Brain Res. |volume=823 |issue= 1-2 |pages= 67-79 |year= 1999 |pmid= 10095013 |doi=  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Brambilla E, Constantin B, Drabkin H, Roche J |title=Semaphorin SEMA3F localization in malignant human lung and cell lines: A suggested role in cell adhesion and cell migration. |journal=Am. J. Pathol. |volume=156 |issue= 3 |pages= 939-50 |year= 2000 |pmid= 10702410 |doi=  }}
*{{cite journal   |vauthors=Nasarre P, Constantin B, Rouhaud L, etal |title=Semaphorin SEMA3F and VEGF have opposing effects on cell attachment and spreading. |journal=Neoplasia |volume=5 |issue= 1 |pages= 83–92 |year= 2003 |pmid= 12659673 |doi= 10.1016/s1476-5586(03)80020-9| pmc=1502125 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Lantuéjoul S, Constantin B, Drabkin H, etal |title=Expression of VEGF, semaphorin SEMA3F, and their common receptors neuropilins NP1 and NP2 in preinvasive bronchial lesions, lung tumours, and cell lines. |journal=J. Pathol. |volume=200 |issue= 3 |pages= 336–47 |year= 2003 |pmid= 12845630 |doi= 10.1002/path.1367 }}
*{{cite journal | author=Nasarre P, Constantin B, Rouhaud L, ''et al.'' |title=Semaphorin SEMA3F and VEGF have opposing effects on cell attachment and spreading. |journal=Neoplasia |volume=5 |issue= 1 |pages= 83-92 |year= 2003 |pmid= 12659673 |doi=  }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Lantuéjoul S, Constantin B, Drabkin H, ''et al.'' |title=Expression of VEGF, semaphorin SEMA3F, and their common receptors neuropilins NP1 and NP2 in preinvasive bronchial lesions, lung tumours, and cell lines. |journal=J. Pathol. |volume=200 |issue= 3 |pages= 336-47 |year= 2003 |pmid= 12845630 |doi= 10.1002/path.1367 }}
*{{cite journal   |vauthors=Bielenberg DR, Hida Y, Shimizu A, etal |title=Semaphorin 3F, a chemorepulsant for endothelial cells, induces a poorly vascularized, encapsulated, nonmetastatic tumor phenotype. |journal=J. Clin. Invest. |volume=114 |issue= 9 |pages= 1260–71 |year= 2004 |pmid= 15520858 |doi= 10.1172/JCI21378  | pmc=524226 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Gu C, Yoshida Y, Livet J, etal |title=Semaphorin 3E and plexin-D1 control vascular pattern independently of neuropilins. |journal=Science |volume=307 |issue= 5707 |pages= 265–8 |year= 2005 |pmid= 15550623 |doi= 10.1126/science.1105416 }}
*{{cite journal  | author=Bielenberg DR, Hida Y, Shimizu A, ''et al.'' |title=Semaphorin 3F, a chemorepulsant for endothelial cells, induces a poorly vascularized, encapsulated, nonmetastatic tumor phenotype. |journal=J. Clin. Invest. |volume=114 |issue= 9 |pages= 1260-71 |year= 2004 |pmid= 15520858 |doi= 10.1172/JCI200421378 }}
*{{cite journal  | vauthors=Pope SN, Lee IR |title=Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin. |journal=J. Steroid Biochem. Mol. Biol. |volume=94 |issue= 1-3 |pages= 203–8 |year= 2005 |pmid= 15862967 |doi= 10.1016/j.jsbmb.2005.01.007 }}
*{{cite journal | author=Gu C, Yoshida Y, Livet J, ''et al.'' |title=Semaphorin 3E and plexin-D1 control vascular pattern independently of neuropilins. |journal=Science |volume=307 |issue= 5707 |pages= 265-8 |year= 2005 |pmid= 15550623 |doi= 10.1126/science.1105416 }}
*{{cite journal   |vauthors=Kusy S, Nasarre P, Chan D, etal |title=Selective suppression of in vivo tumorigenicity by semaphorin SEMA3F in lung cancer cells. |journal=Neoplasia |volume=7 |issue= 5 |pages= 457–65 |year= 2005 |pmid= 15967098 |doi=10.1593/neo.04721  | pmc=1501157  }}
*{{cite journal | author=Pope SN, Lee IR |title=Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin. |journal=J. Steroid Biochem. Mol. Biol. |volume=94 |issue= 1-3 |pages= 203-8 |year= 2005 |pmid= 15862967 |doi= 10.1016/j.jsbmb.2005.01.007 }}
*{{cite journal   |vauthors=Futamura M, Kamino H, Miyamoto Y, etal |title=Possible role of semaphorin 3F, a candidate tumor suppressor gene at 3p21.3, in p53-regulated tumor angiogenesis suppression. |journal=Cancer Res. |volume=67 |issue= 4 |pages= 1451–60 |year= 2007 |pmid= 17308083 |doi= 10.1158/0008-5472.CAN-06-2485 }}
*{{cite journal | author=Kusy S, Nasarre P, Chan D, ''et al.'' |title=Selective suppression of in vivo tumorigenicity by semaphorin SEMA3F in lung cancer cells. |journal=Neoplasia |volume=7 |issue= 5 |pages= 457-65 |year= 2005 |pmid= 15967098 |doi= }}
*{{cite journal   |vauthors=Guttmann-Raviv N, Shraga-Heled N, Varshavsky A, etal |title=Semaphorin-3A and semaphorin-3F work together to repel endothelial cells and to inhibit their survival by induction of apoptosis. |journal=J. Biol. Chem. |volume=282 |issue= 36 |pages= 26294–305 |year= 2007 |pmid= 17569671 |doi= 10.1074/jbc.M609711200 }}
*{{cite journal  | author=Futamura M, Kamino H, Miyamoto Y, ''et al.'' |title=Possible role of semaphorin 3F, a candidate tumor suppressor gene at 3p21.3, in p53-regulated tumor angiogenesis suppression. |journal=Cancer Res. |volume=67 |issue= 4 |pages= 1451-60 |year= 2007 |pmid= 17308083 |doi= 10.1158/0008-5472.CAN-06-2485 }}
*{{cite journal  | vauthors=Menon L, Mihailescu MR |title=Interactions of the G quartet forming semaphorin 3F RNA with the RGG box domain of the fragile X protein family. |journal=Nucleic Acids Res. |volume=35 |issue= 16 |pages= 5379–92 |year= 2007 |pmid= 17693432 |doi= 10.1093/nar/gkm581 | pmc=2018618 }}
*{{cite journal | author=Guttmann-Raviv N, Shraga-Heled N, Varshavsky A, ''et al.'' |title=Semaphorin-3A and semaphorin-3F work together to repel endothelial cells and to inhibit their survival by induction of apoptosis. |journal=J. Biol. Chem. |volume=282 |issue= 36 |pages= 26294-305 |year= 2007 |pmid= 17569671 |doi= 10.1074/jbc.M609711200 }}
*{{cite journal  | author=Menon L, Mihailescu MR |title=Interactions of the G quartet forming semaphorin 3F RNA with the RGG box domain of the fragile X protein family. |journal=Nucleic Acids Res. |volume=35 |issue= 16 |pages= 5379-92 |year= 2007 |pmid= 17693432 |doi= 10.1093/nar/gkm581 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{WikiDoc Sources}}
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
 
 
{{gene-3-stub}}

Latest revision as of 06:05, 11 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Semaphorin-3F is a protein that in humans is encoded by the SEMA3F gene.[1][2][3]

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][3]

References

  1. 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. PMID 8786119.
  2. 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. PMID 8649831.
  3. 3.0 3.1 "Entrez Gene: SEMA3F sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3F".

Further reading