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.
Functionedit
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.[5]
Loss-of-function mutations in this gene cause a rare syndrome - autosomal recessive hemorrhagic destruction of the brain, subependymal calcification and congenital cataracts.[7]
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000166086 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000031990 - Ensembl, May 2017
^"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.
^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.
^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. PMC3951164. PMID 23255084.
Further readingedit
Muller WA (2003). "Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response". Trends Immunol. 24 (6): 327–34. doi:10.1016/S1471-4906(03)00117-0. PMID 12810109.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Arrate MP, Rodriguez JM, Tran TM, et al. (2002). "Cloning of human junctional adhesion molecule 3 (JAM3) and its identification as the JAM2 counter-receptor". J. Biol. Chem. 276 (49): 45826–32. doi:10.1074/jbc.M105972200. PMID 11590146.
Aurrand-Lions M, Johnson-Leger C, Wong C, et al. (2002). "Heterogeneity of endothelial junctions is reflected by differential expression and specific subcellular localization of the three JAM family members". Blood. 98 (13): 3699–707. doi:10.1182/blood.V98.13.3699. PMID 11739175. S2CID 29405220.
Liang TW, Chiu HH, Gurney A, et al. (2002). "Vascular endothelial-junctional adhesion molecule (VE-JAM)/JAM 2 interacts with T, NK, and dendritic cells through JAM 3". J. Immunol. 168 (4): 1618–26. doi:10.4049/jimmunol.168.4.1618. PMID 11823489.
Phillips HM, Renforth GL, Spalluto C, et al. (2002). "Narrowing the critical region within 11q24-qter for hypoplastic left heart and identification of a candidate gene, JAM3, expressed during cardiogenesis". Genomics. 79 (4): 475–8. doi:10.1006/geno.2002.6742. PMID 11944976.
Cunningham SA, Rodriguez JM, Arrate MP, et al. (2002). "JAM2 interacts with alpha4beta1. Facilitation by JAM3". J. Biol. Chem. 277 (31): 27589–92. doi:10.1074/jbc.C200331200. PMID 12070135.
Santoso S, Sachs UJ, Kroll H, et al. (2002). "The junctional adhesion molecule 3 (JAM-3) on human platelets is a counterreceptor for the leukocyte integrin Mac-1". J. Exp. Med. 196 (5): 679–91. doi:10.1084/jem.20020267. PMC2194005. PMID 12208882.
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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC139241. PMID 12477932.
Ebnet K, Aurrand-Lions M, Kuhn A, et al. (2004). "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.
Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC403697. PMID 12975309.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Zen K, Babbin BA, Liu Y, et al. (2005). "JAM-C is a component of desmosomes and a ligand for CD11b/CD18-mediated neutrophil transepithelial migration". Mol. Biol. Cell. 15 (8): 3926–37. doi:10.1091/mbc.E04-04-0317. PMC491847. PMID 15194813.
Zhang Z, Henzel WJ (2005). "Signal peptide prediction based on analysis of experimentally verified cleavage sites". Protein Sci. 13 (10): 2819–24. doi:10.1110/ps.04682504. PMC2286551. PMID 15340161.
Chavakis T, Keiper T, Matz-Westphal R, et al. (2005). "The junctional adhesion molecule-C promotes neutrophil transendothelial migration in vitro and in vivo". J. Biol. Chem. 279 (53): 55602–8. doi:10.1074/jbc.M404676200. PMID 15485832.
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. PMC528928. PMID 15489334.
Aurrand-Lions M, Lamagna C, Dangerfield JP, et al. (2005). "Junctional adhesion molecule-C regulates the early influx of leukocytes into tissues during inflammation". J. Immunol. 174 (10): 6406–15. doi:10.4049/jimmunol.174.10.6406. PMID 15879142.
Santoso S, Orlova VV, Song K, et al. (2006). "The homophilic binding of junctional adhesion molecule-C mediates tumor cell-endothelial cell interactions". J. Biol. Chem. 280 (43): 36326–33. doi:10.1074/jbc.M505059200. PMID 16118203.
This article on a gene on human chromosome 11 is a stub. You can help Wikipedia by expanding it.
jam3, junctional, adhesion, molecule, protein, that, humans, encoded, gene, identifiersaliases, jamc, junctional, adhesion, molecule, 3external, idsomim, 606871, 1933825, homologene, 11338, genecards, gene, location, human, chromosome, human, band11q25start134. Junctional adhesion molecule C is a protein that in humans is encoded by the JAM3 gene 5 JAM3IdentifiersAliasesJAM3 JAM 2 JAM 3 JAM C JAMC junctional adhesion molecule 3External IDsOMIM 606871 MGI 1933825 HomoloGene 11338 GeneCards JAM3Gene location Human Chr Chromosome 11 human 1 Band11q25Start134 069 071 bp 1 End134 152 001 bp 1 Gene location Mouse Chr Chromosome 9 mouse 2 Band9 9 A4Start27 008 680 bp 2 End27 066 717 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed incorpus callosuminferior ganglion of vagus nerveolfactory bulbglobus pallidusinternal globus pallidusexternal globus pallidustrigeminal ganglionsaphenous veinsubthalamic nucleusmiddle frontal gyrusTop expressed insciatic nervespermatocytelensutriclespermatidextraocular muscleneural tubemedial ganglionic eminencestria vascularissacculeMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionprotein homodimerization activity integrin binding protein binding protein heterodimerization activityCellular componentintegral component of membrane membrane cell cell contact zone cell cell junction bicellular tight junction plasma membrane desmosome Schmidt Lanterman incisure extracellular region cell junction paranodal junction extracellular space Golgi apparatus integral component of plasma membraneBiological processneutrophil homeostasis regulation of neutrophil chemotaxis regulation of actin cytoskeleton organization by cell cell adhesion myeloid progenitor cell differentiation adaptive immune response axon regeneration transmission of nerve impulse leukocyte migration involved in inflammatory response extracellular matrix organization cell adhesion angiogenesis spermatogenesis establishment of cell polarity spermatid development myelination cell matrix adhesion cell migration leukocyte migration cell differentiationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez8370083964EnsemblENSG00000166086ENSMUSG00000031990UniProtQ9BX67Q9D8B7RefSeq mRNA NM 032801NM 001205329NM 023277RefSeq protein NP 001192258NP 116190NP 075766Location UCSC Chr 11 134 07 134 15 MbChr 9 27 01 27 07 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Gene 2 Function 3 Interactions 4 Clinical significance 5 References 6 Further readingGene editThis 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 editTight 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 5 Interactions editJAM3 has been shown to interact with PARD3 6 Clinical significance editLoss of function mutations in this gene cause a rare syndrome autosomal recessive hemorrhagic destruction of the brain subependymal calcification and congenital cataracts 7 References edit a b c GRCh38 Ensembl release 89 ENSG00000166086 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000031990 Ensembl May 2017 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 a b Entrez Gene JAM3 junctional adhesion molecule 3 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 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 PMC 3951164 PMID 23255084 Further reading editMuller WA 2003 Leukocyte endothelial cell interactions in leukocyte transmigration and the inflammatory response Trends Immunol 24 6 327 34 doi 10 1016 S1471 4906 03 00117 0 PMID 12810109 Maruyama K Sugano S 1994 Oligo capping a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides Gene 138 1 2 171 4 doi 10 1016 0378 1119 94 90802 8 PMID 8125298 Suzuki Y Yoshitomo Nakagawa K Maruyama K et al 1997 Construction and characterization of a full length enriched and a 5 end enriched cDNA library Gene 200 1 2 149 56 doi 10 1016 S0378 1119 97 00411 3 PMID 9373149 Arrate MP Rodriguez JM Tran TM et al 2002 Cloning of human junctional adhesion molecule 3 JAM3 and its identification as the JAM2 counter receptor J Biol Chem 276 49 45826 32 doi 10 1074 jbc M105972200 PMID 11590146 Aurrand Lions M Johnson Leger C Wong C et al 2002 Heterogeneity of endothelial junctions is reflected by differential expression and specific subcellular localization of the three JAM family members Blood 98 13 3699 707 doi 10 1182 blood V98 13 3699 PMID 11739175 S2CID 29405220 Liang TW Chiu HH Gurney A et al 2002 Vascular endothelial junctional adhesion molecule VE JAM JAM 2 interacts with T NK and dendritic cells through JAM 3 J Immunol 168 4 1618 26 doi 10 4049 jimmunol 168 4 1618 PMID 11823489 Phillips HM Renforth GL Spalluto C et al 2002 Narrowing the critical region within 11q24 qter for hypoplastic left heart and identification of a candidate gene JAM3 expressed during cardiogenesis Genomics 79 4 475 8 doi 10 1006 geno 2002 6742 PMID 11944976 Cunningham SA Rodriguez JM Arrate MP et al 2002 JAM2 interacts with alpha4beta1 Facilitation by JAM3 J Biol Chem 277 31 27589 92 doi 10 1074 jbc C200331200 PMID 12070135 Santoso S Sachs UJ Kroll H et al 2002 The junctional adhesion molecule 3 JAM 3 on human platelets is a counterreceptor for the leukocyte integrin Mac 1 J Exp Med 196 5 679 91 doi 10 1084 jem 20020267 PMC 2194005 PMID 12208882 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 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 Ebnet K Aurrand Lions M Kuhn A et al 2004 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 Clark HF Gurney AL Abaya E et al 2003 The secreted protein discovery initiative SPDI a large scale effort to identify novel human secreted and transmembrane proteins a bioinformatics assessment Genome Res 13 10 2265 70 doi 10 1101 gr 1293003 PMC 403697 PMID 12975309 Ota T Suzuki Y Nishikawa T et al 2004 Complete sequencing and characterization of 21 243 full length human cDNAs Nat Genet 36 1 40 5 doi 10 1038 ng1285 PMID 14702039 Zen K Babbin BA Liu Y et al 2005 JAM C is a component of desmosomes and a ligand for CD11b CD18 mediated neutrophil transepithelial migration Mol Biol Cell 15 8 3926 37 doi 10 1091 mbc E04 04 0317 PMC 491847 PMID 15194813 Zhang Z Henzel WJ 2005 Signal peptide prediction based on analysis of experimentally verified cleavage sites Protein Sci 13 10 2819 24 doi 10 1110 ps 04682504 PMC 2286551 PMID 15340161 Chavakis T Keiper T Matz Westphal R et al 2005 The junctional adhesion molecule C promotes neutrophil transendothelial migration in vitro and in vivo J Biol Chem 279 53 55602 8 doi 10 1074 jbc M404676200 PMID 15485832 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 PMC 528928 PMID 15489334 Aurrand Lions M Lamagna C Dangerfield JP et al 2005 Junctional adhesion molecule C regulates the early influx of leukocytes into tissues during inflammation J Immunol 174 10 6406 15 doi 10 4049 jimmunol 174 10 6406 PMID 15879142 Santoso S Orlova VV Song K et al 2006 The homophilic binding of junctional adhesion molecule C mediates tumor cell endothelial cell interactions J Biol Chem 280 43 36326 33 doi 10 1074 jbc M505059200 PMID 16118203 nbsp This article on a gene on human chromosome 11 is a stub You can help Wikipedia by expanding it vte Retrieved from https en 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