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{{Infobox_gene}}
{{PBB_Controls
'''Junctional adhesion molecule C''' is a [[protein]] that in humans is encoded by the ''JAM3'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: JAM3 junctional adhesion molecule 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=83700| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Gene ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Junctional adhesion molecule 3
| HGNCid = 15532
| Symbol = JAM3
| AltSymbols =; FLJ14529; JAM-C; JAMC
| OMIM = 606871
| ECnumber = 
| Homologene = 11338
| MGIid = 1933825
| GeneAtlas_image1 = PBB_GE_JAM3_212813_at_tn.png
| GeneAtlas_image2 = PBB_GE_JAM3_gnf1h00503_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process =
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 83700
    | Hs_Ensembl = ENSG00000166086
    | Hs_RefseqProtein = NP_116190
    | Hs_RefseqmRNA = NM_032801
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 133444030
    | Hs_GenLoc_end = 133526846
    | Hs_Uniprot = Q9BX67
    | Mm_EntrezGene = 83964
    | Mm_Ensembl = ENSMUSG00000031990
    | Mm_RefseqmRNA = NM_023277
    | Mm_RefseqProtein = NP_075766
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 26846831
    | Mm_GenLoc_end = 26904839
    | Mm_Uniprot = Q9D8B7
  }}
}}
'''Junctional adhesion molecule 3''', also known as '''JAM3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: JAM3 junctional adhesion molecule 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=83700| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
This gene is located on the long arm of [[chromosome 11]] (11q25) on the Watson strand. It is 83,077 bases in length. The encoded protein is 310 [[amino acid]]s long with a predicted [[molecular weight]] of 35.02 kiloDaltons.
{{PBB_Summary
 
| section_title =  
== Function ==
| summary_text = Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is localized in the tight junctions between high endothelial cells. Unlike other proteins in this family, the this protein is unable to adhere to leukocyte cell lines and only forms weak homotypic interactions. The encoded protein is a member of the junctional adhesion molecule protein family and acts as a receptor for another member of this family.<ref name="entrez">{{cite web | title = Entrez Gene: JAM3 junctional adhesion molecule 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=83700| accessdate = }}</ref>
 
}}
[[Tight junction]]s represent one mode of cell-to-cell adhesion in [[epithelial]] or [[endothelial]] cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the [[paracellular]] space. The protein encoded by this [[immunoglobulin superfamily]] gene member is localized in the tight junctions between high endothelial cells. Unlike other proteins in this family, this protein is unable to adhere to [[leukocyte]] cell lines and only forms weak [[wiktionary:homotypic|homotypic]] interactions. The encoded protein is a member of the junctional adhesion molecule protein family and acts as a receptor for another member of this family.<ref name="entrez"/>
 
==Interactions==
 
JAM3 has been shown to [[Protein-protein interaction|interact]] with [[PARD3]].<ref name="pmid12953056">{{cite journal |vauthors=Ebnet K, Aurrand-Lions M, Kuhn A, Kiefer F, Butz S, Zander K, Meyer zu Brickwedde MK, Suzuki A, Imhof BA, Vestweber D | title = The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity | journal = J. Cell Sci. | volume = 116 | issue = Pt 19 | pages = 3879–91 |date=October 2003 | pmid = 12953056 | doi = 10.1242/jcs.00704 }}</ref>
 
== Clinical significance ==
 
Mutations in this gene have been associated with a rare syndrome - autosomal recessive hemorrhagic destruction of the brain, subependymal calcification and congenital cataracts.<ref name="pmid23255084">{{cite journal |vauthors=Akawi NA, Canpolat FE, White SM, Quilis-Esquerra J, Sanchez MM, Gamundi MJ, Mochida GH, Walsh CA, Ali BR, Al-Gazali L | title = Delineation of the Clinical, Molecular and Cellular Aspects of Novel JAM3 Mutations Underlying the Autosomal Recessive Hemorrhagic Destruction of the Brain, Subependymal Calcification and Congenital Cataracts | journal = Hum. Mutat. | volume = 34| issue = 3| pages = 498–505|date=December 2012 | pmid = 23255084 | doi = 10.1002/humu.22263 }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | author=Muller WA |title=Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response. |journal=Trends Immunol. |volume=24 |issue= 6 |pages= 327–34 |year= 2003 |pmid= 12810109 |doi=10.1016/S1471-4906(03)00117-0 }}
| citations =
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal  | author=Muller WA |title=Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response. |journal=Trends Immunol. |volume=24 |issue= 6 |pages= 327-34 |year= 2003 |pmid= 12810109 |doi=  }}
*{{cite journal   |vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, etal |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal   |vauthors=Arrate MP, Rodriguez JM, Tran TM, etal |title=Cloning of human junctional adhesion molecule 3 (JAM3) and its identification as the JAM2 counter-receptor. |journal=J. Biol. Chem. |volume=276 |issue= 49 |pages= 45826–32 |year= 2002 |pmid= 11590146 |doi= 10.1074/jbc.M105972200 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal   |vauthors=Aurrand-Lions M, Johnson-Leger C, Wong C, etal |title=Heterogeneity of endothelial junctions is reflected by differential expression and specific subcellular localization of the three JAM family members. |journal=Blood |volume=98 |issue= 13 |pages= 3699–707 |year= 2002 |pmid= 11739175 |doi=10.1182/blood.V98.13.3699 }}
*{{cite journal | author=Arrate MP, Rodriguez JM, Tran TM, ''et al.'' |title=Cloning of human junctional adhesion molecule 3 (JAM3) and its identification as the JAM2 counter-receptor. |journal=J. Biol. Chem. |volume=276 |issue= 49 |pages= 45826-32 |year= 2002 |pmid= 11590146 |doi= 10.1074/jbc.M105972200 }}
*{{cite journal   |vauthors=Liang TW, Chiu HH, Gurney A, etal |title=Vascular endothelial-junctional adhesion molecule (VE-JAM)/JAM 2 interacts with T, NK, and dendritic cells through JAM 3. |journal=J. Immunol. |volume=168 |issue= 4 |pages= 1618–26 |year= 2002 |pmid= 11823489 |doi=  10.4049/jimmunol.168.4.1618}}
*{{cite journal | author=Aurrand-Lions M, Johnson-Leger C, Wong C, ''et al.'' |title=Heterogeneity of endothelial junctions is reflected by differential expression and specific subcellular localization of the three JAM family members. |journal=Blood |volume=98 |issue= 13 |pages= 3699-707 |year= 2002 |pmid= 11739175 |doi=  }}
*{{cite journal   |vauthors=Phillips HM, Renforth GL, Spalluto C, etal |title=Narrowing the critical region within 11q24-qter for hypoplastic left heart and identification of a candidate gene, JAM3, expressed during cardiogenesis. |journal=Genomics |volume=79 |issue= 4 |pages= 475–8 |year= 2002 |pmid= 11944976 |doi= 10.1006/geno.2002.6742 }}
*{{cite journal | author=Liang TW, Chiu HH, Gurney A, ''et al.'' |title=Vascular endothelial-junctional adhesion molecule (VE-JAM)/JAM 2 interacts with T, NK, and dendritic cells through JAM 3. |journal=J. Immunol. |volume=168 |issue= 4 |pages= 1618-26 |year= 2002 |pmid= 11823489 |doi=  }}
*{{cite journal   |vauthors=Cunningham SA, Rodriguez JM, Arrate MP, etal |title=JAM2 interacts with alpha4beta1. Facilitation by JAM3. |journal=J. Biol. Chem. |volume=277 |issue= 31 |pages= 27589–92 |year= 2002 |pmid= 12070135 |doi= 10.1074/jbc.C200331200 }}
*{{cite journal | author=Phillips HM, Renforth GL, Spalluto C, ''et al.'' |title=Narrowing the critical region within 11q24-qter for hypoplastic left heart and identification of a candidate gene, JAM3, expressed during cardiogenesis. |journal=Genomics |volume=79 |issue= 4 |pages= 475-8 |year= 2002 |pmid= 11944976 |doi= 10.1006/geno.2002.6742 }}
*{{cite journal   |vauthors=Santoso S, Sachs UJ, Kroll H, etal |title=The junctional adhesion molecule 3 (JAM-3) on human platelets is a counterreceptor for the leukocyte integrin Mac-1. |journal=J. Exp. Med. |volume=196 |issue= 5 |pages= 679–91 |year= 2002 |pmid= 12208882 |doi=10.1084/jem.20020267  | pmc=2194005 }}
*{{cite journal | author=Cunningham SA, Rodriguez JM, Arrate MP, ''et al.'' |title=JAM2 interacts with alpha4beta1. Facilitation by JAM3. |journal=J. Biol. Chem. |volume=277 |issue= 31 |pages= 27589-92 |year= 2002 |pmid= 12070135 |doi= 10.1074/jbc.C200331200 }}
*{{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=Santoso S, Sachs UJ, Kroll H, ''et al.'' |title=The junctional adhesion molecule 3 (JAM-3) on human platelets is a counterreceptor for the leukocyte integrin Mac-1. |journal=J. Exp. Med. |volume=196 |issue= 5 |pages= 679-91 |year= 2002 |pmid= 12208882 |doi=  }}
*{{cite journal   |vauthors=Ebnet K, Aurrand-Lions M, Kuhn A, etal |title=The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity. |journal=J. Cell Sci. |volume=116 |issue= Pt 19 |pages= 3879–91 |year= 2004 |pmid= 12953056 |doi= 10.1242/jcs.00704 }}
*{{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=Clark HF, Gurney AL, Abaya E, etal |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265–70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 | pmc=403697 }}
*{{cite journal | author=Ebnet K, Aurrand-Lions M, Kuhn A, ''et al.'' |title=The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity. |journal=J. Cell. Sci. |volume=116 |issue= Pt 19 |pages= 3879-91 |year= 2004 |pmid= 12953056 |doi= 10.1242/jcs.00704 }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
*{{cite journal   |vauthors=Zen K, Babbin BA, Liu Y, etal |title=JAM-C is a component of desmosomes and a ligand for CD11b/CD18-mediated neutrophil transepithelial migration. |journal=Mol. Biol. Cell |volume=15 |issue= 8 |pages= 3926–37 |year= 2005 |pmid= 15194813 |doi= 10.1091/mbc.E04-04-0317 | pmc=491847 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  |vauthors=Zhang Z, Henzel WJ |title=Signal peptide prediction based on analysis of experimentally verified cleavage sites. |journal=Protein Sci. |volume=13 |issue= 10 |pages= 2819–24 |year= 2005 |pmid= 15340161 |doi= 10.1110/ps.04682504 | pmc=2286551 }}
*{{cite journal | author=Zen K, Babbin BA, Liu Y, ''et al.'' |title=JAM-C is a component of desmosomes and a ligand for CD11b/CD18-mediated neutrophil transepithelial migration. |journal=Mol. Biol. Cell |volume=15 |issue= 8 |pages= 3926-37 |year= 2005 |pmid= 15194813 |doi= 10.1091/mbc.E04-04-0317 }}
*{{cite journal   |vauthors=Chavakis T, Keiper T, Matz-Westphal R, etal |title=The junctional adhesion molecule-C promotes neutrophil transendothelial migration in vitro and in vivo. |journal=J. Biol. Chem. |volume=279 |issue= 53 |pages= 55602–8 |year= 2005 |pmid= 15485832 |doi= 10.1074/jbc.M404676200 }}
*{{cite journal  | author=Zhang Z, Henzel WJ |title=Signal peptide prediction based on analysis of experimentally verified cleavage sites. |journal=Protein Sci. |volume=13 |issue= 10 |pages= 2819-24 |year= 2005 |pmid= 15340161 |doi= 10.1110/ps.04682504 }}
*{{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=Chavakis T, Keiper T, Matz-Westphal R, ''et al.'' |title=The junctional adhesion molecule-C promotes neutrophil transendothelial migration in vitro and in vivo. |journal=J. Biol. Chem. |volume=279 |issue= 53 |pages= 55602-8 |year= 2005 |pmid= 15485832 |doi= 10.1074/jbc.M404676200 }}
*{{cite journal   |vauthors=Aurrand-Lions M, Lamagna C, Dangerfield JP, etal |title=Junctional adhesion molecule-C regulates the early influx of leukocytes into tissues during inflammation. |journal=J. Immunol. |volume=174 |issue= 10 |pages= 6406–15 |year= 2005 |pmid= 15879142 |doi=  10.4049/jimmunol.174.10.6406}}
*{{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=Santoso S, Orlova VV, Song K, etal |title=The homophilic binding of junctional adhesion molecule-C mediates tumor cell-endothelial cell interactions. |journal=J. Biol. Chem. |volume=280 |issue= 43 |pages= 36326–33 |year= 2006 |pmid= 16118203 |doi= 10.1074/jbc.M505059200 }}
*{{cite journal | author=Aurrand-Lions M, Lamagna C, Dangerfield JP, ''et al.'' |title=Junctional adhesion molecule-C regulates the early influx of leukocytes into tissues during inflammation. |journal=J. Immunol. |volume=174 |issue= 10 |pages= 6406-15 |year= 2005 |pmid= 15879142 |doi=  }}
*{{cite journal | author=Santoso S, Orlova VV, Song K, ''et al.'' |title=The homophilic binding of junctional adhesion molecule-C mediates tumor cell-endothelial cell interactions. |journal=J. Biol. Chem. |volume=280 |issue= 43 |pages= 36326-33 |year= 2006 |pmid= 16118203 |doi= 10.1074/jbc.M505059200 }}
}}
{{refend}}
{{refend}}


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Revision as of 20:09, 8 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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

Junctional adhesion molecule C is a protein that in humans is encoded by the JAM3 gene.[1]

Gene

This gene is located on the long arm of chromosome 11 (11q25) on the Watson strand. It is 83,077 bases in length. The encoded protein is 310 amino acids long with a predicted molecular weight of 35.02 kiloDaltons.

Function

Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is localized in the tight junctions between high endothelial cells. Unlike other proteins in this family, this protein is unable to adhere to leukocyte cell lines and only forms weak homotypic interactions. The encoded protein is a member of the junctional adhesion molecule protein family and acts as a receptor for another member of this family.[1]

Interactions

JAM3 has been shown to interact with PARD3.[2]

Clinical significance

Mutations in this gene have been associated with a rare syndrome - autosomal recessive hemorrhagic destruction of the brain, subependymal calcification and congenital cataracts.[3]

References

  1. ↑ 1.0 1.1 "Entrez Gene: JAM3 junctional adhesion molecule 3".
  2. ↑ Ebnet K, Aurrand-Lions M, Kuhn A, Kiefer F, Butz S, Zander K, Meyer zu Brickwedde MK, Suzuki A, Imhof BA, Vestweber D (October 2003). "The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity". J. Cell Sci. 116 (Pt 19): 3879–91. doi:10.1242/jcs.00704. PMID 12953056.
  3. ↑ Akawi NA, Canpolat FE, White SM, Quilis-Esquerra J, Sanchez MM, Gamundi MJ, Mochida GH, Walsh CA, Ali BR, Al-Gazali L (December 2012). "Delineation of the Clinical, Molecular and Cellular Aspects of Novel JAM3 Mutations Underlying the Autosomal Recessive Hemorrhagic Destruction of the Brain, Subependymal Calcification and Congenital Cataracts". Hum. Mutat. 34 (3): 498–505. doi:10.1002/humu.22263. PMID 23255084.

Further reading


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