F11 receptor

Junctional adhesion molecule A is a protein that in humans is encoded by the F11R gene.[5][6][7] It has also been designated as CD321 (cluster of differentiation 321).

F11R
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesF11R, F11r, 9130004G24, AA638916, ESTM33, JAM, JAM-1, JAM-A, Jcam, Jcam1, Ly106, CD321, JAM1, JAMA, KAT, PAM-1, F11 receptor
External IDsOMIM: 605721 MGI: 1321398 HomoloGene: 14255 GeneCards: F11R
Orthologs
SpeciesHumanMouse
Entrez

50848

16456

Ensembl

ENSG00000158769

ENSMUSG00000038235

UniProt

Q9Y624

O88792

RefSeq (mRNA)

NM_172647

RefSeq (protein)

NP_766235

Location (UCSC)Chr 1: 161 – 161.02 MbChr 1: 171.27 – 171.29 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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 an important regulator of tight junction assembly in epithelia. In addition, the encoded protein can act as (1) a receptor for reovirus, (2) a ligand for the integrin LFA1, involved in leukocyte transmigration, and (3) a platelet receptor. Multiple transcript variants encoding two different isoforms have been found for this gene.[7]

Interactions

F11 receptor has been shown to interact with MLLT4,[8] CASK[8][9] and Tight junction protein 1.[8][10]

References
  1. GRCh38: Ensembl release 89: ENSG00000158769 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000038235 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Ozaki H, Ishii K, Horiuchi H, Arai H, Kawamoto T, Okawa K, Iwamatsu A, Kita T (Jul 1999). "Cutting edge: combined treatment of TNF-alpha and IFN-gamma causes redistribution of junctional adhesion molecule in human endothelial cells". Journal of Immunology. 163 (2): 553–7. doi:10.4049/jimmunol.163.2.553. PMID 10395639. S2CID 255364609.
  6. Naik UP, Ehrlich YH, Kornecki E (Aug 1995). "Mechanisms of platelet activation by a stimulatory antibody: cross-linking of a novel platelet receptor for monoclonal antibody F11 with the Fc gamma RII receptor". The Biochemical Journal. 310 ( Pt 1) (1): 155–62. doi:10.1042/bj3100155. PMC 1135867. PMID 7646439.
  7. "Entrez Gene: F11R F11 receptor".
  8. Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, Pendl GG, Vestweber D (Sep 2000). "Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1". The Journal of Biological Chemistry. 275 (36): 27979–88. doi:10.1074/jbc.M002363200. PMID 10856295.
  9. Martinez-Estrada OM, Villa A, Breviario F, Orsenigo F, Dejana E, Bazzoni G (Mar 2001). "Association of junctional adhesion molecule with calcium/calmodulin-dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells". The Journal of Biological Chemistry. 276 (12): 9291–6. doi:10.1074/jbc.M006991200. PMID 11120739.
  10. Ebnet K, Aurrand-Lions M, Kuhn A, Kiefer F, Butz S, Zander K, Meyer zu Brickwedde MK, Suzuki A, Imhof BA, Vestweber D (Oct 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". Journal of Cell Science. 116 (Pt 19): 3879–91. doi:10.1242/jcs.00704. PMID 12953056.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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