F11 receptor

Protein-coding gene in the species Homo sapiens
F11R
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1NBQ, 3EOY, 3TSZ, 4ODB

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; OMA:F11R - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for F11R
Genomic location for F11R
Band1q23.3Start160,995,211 bp[1]
End161,021,343 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for F11R
Genomic location for F11R
Band1 H3|1 79.43 cMStart171,265,103 bp[2]
End171,292,171 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • olfactory zone of nasal mucosa

  • right lung

  • rectum

  • islet of Langerhans

  • upper lobe of left lung

  • mucosa of transverse colon

  • minor salivary glands

  • gallbladder

  • skin of abdomen

  • left lobe of thyroid gland
Top expressed in
  • saccule

  • otic placode

  • corneal stroma

  • left lung lobe

  • otic vesicle

  • lactiferous gland

  • choroid plexus of fourth ventricle

  • transitional epithelium of urinary bladder

  • epithelium of stomach

  • large intestine
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • PDZ domain binding
  • virus receptor activity
  • protein binding
  • cadherin binding
Cellular component
  • integral component of membrane
  • membrane
  • cell-cell junction
  • bicellular tight junction
  • plasma membrane
  • slit diaphragm
  • extracellular exosome
  • cytoplasmic vesicle
  • cell junction
Biological process
  • regulation of actin cytoskeleton reorganization
  • cell differentiation
  • establishment of endothelial intestinal barrier
  • epithelial cell differentiation
  • actomyosin structure organization
  • extracellular matrix organization
  • regulation of membrane permeability
  • regulation of cytokine production
  • positive regulation of GTPase activity
  • positive regulation of blood pressure
  • cell adhesion
  • negative regulation of GTPase activity
  • bicellular tight junction assembly
  • viral entry into host cell
  • intestinal absorption
  • response to radiation
  • inflammatory response
  • viral process
  • transforming growth factor beta receptor signaling pathway
  • leukocyte migration
  • protein localization to plasma membrane
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

50848

16456

Ensembl

ENSG00000158769

ENSMUSG00000038235

UniProt

Q9Y624

O88792

RefSeq (mRNA)
NM_016946
NM_144501
NM_144502
NM_144503
NM_144504

NM_001348091
NM_001382727
NM_001382730
NM_001382733
NM_001382734

NM_172647

RefSeq (protein)
NP_058642
NP_001335020
NP_001369656
NP_001369659
NP_001369662

NP_001369663

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

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).

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. ^ a b c GRCh38: Ensembl release 89: ENSG00000158769 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "Entrez Gene: F11R F11 receptor".
  8. ^ a b c 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

  • Muller WA (Jun 2003). "Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response". Trends in Immunology. 24 (6): 327–34. doi:10.1016/S1471-4906(03)00117-0. PMID 12810109.
  • Bazzoni G (Oct 2003). "The JAM family of junctional adhesion molecules". Current Opinion in Cell Biology. 15 (5): 525–30. doi:10.1016/S0955-0674(03)00104-2. PMID 14519386.
  • Naik UP, Eckfeld K (2004). "Junctional adhesion molecule 1 (JAM-1)". Journal of Biological Regulators and Homeostatic Agents. 17 (4): 341–7. PMID 15065765.
  • Kornecki E, Walkowiak B, Naik UP, Ehrlich YH (Jun 1990). "Activation of human platelets by a stimulatory monoclonal antibody". The Journal of Biological Chemistry. 265 (17): 10042–8. doi:10.1016/S0021-9258(19)38776-9. PMID 2351647.
  • Williams LA, Martin-Padura I, Dejana E, Hogg N, Simmons DL (Dec 1999). "Identification and characterisation of human Junctional Adhesion Molecule (JAM)". Molecular Immunology. 36 (17): 1175–88. doi:10.1016/S0161-5890(99)00122-4. PMID 10698320.
  • Sobocka MB, Sobocki T, Banerjee P, Weiss C, Rushbrook JI, Norin AJ, Hartwig J, Salifu MO, Markell MS, Babinska A, Ehrlich YH, Kornecki E (Apr 2000). "Cloning of the human platelet F11 receptor: a cell adhesion molecule member of the immunoglobulin superfamily involved in platelet aggregation". Blood. 95 (8): 2600–9. doi:10.1182/blood.V95.8.2600. PMID 10753840.
  • Liu Y, Nusrat A, Schnell FJ, Reaves TA, Walsh S, Pochet M, Parkos CA (Jul 2000). "Human junction adhesion molecule regulates tight junction resealing in epithelia". Journal of Cell Science. 113 ( Pt 13) (13): 2363–74. doi:10.1242/jcs.113.13.2363. PMID 10852816.
  • 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.
  • Bazzoni G, Martinez-Estrada OM, Orsenigo F, Cordenonsi M, Citi S, Dejana E (Jul 2000). "Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin". The Journal of Biological Chemistry. 275 (27): 20520–6. doi:10.1074/jbc.M905251199. PMID 10877843.
  • Gupta SK, Pillarisetti K, Ohlstein EH (Jul 2000). "Platelet agonist F11 receptor is a member of the immunoglobulin superfamily and identical with junctional adhesion molecule (JAM): regulation of expression in human endothelial cells and macrophages". IUBMB Life. 50 (1): 51–6. doi:10.1080/15216540050176593. PMID 11087121. S2CID 37733691.
  • 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.
  • Naik UP, Naik MU, Eckfeld K, Martin-DeLeon P, Spychala J (Feb 2001). "Characterization and chromosomal localization of JAM-1, a platelet receptor for a stimulatory monoclonal antibody". Journal of Cell Science. 114 (Pt 3): 539–47. doi:10.1242/jcs.114.3.539. PMID 11171323.
  • Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Research. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
  • Barton ES, Forrest JC, Connolly JL, Chappell JD, Liu Y, Schnell FJ, Nusrat A, Parkos CA, Dermody TS (Feb 2001). "Junction adhesion molecule is a receptor for reovirus". Cell. 104 (3): 441–51. doi:10.1016/S0092-8674(01)00231-8. PMID 11239401. S2CID 17095289.
  • Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S (Sep 2000). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Reports. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
  • Ebnet K, Suzuki A, Horikoshi Y, Hirose T, Meyer Zu Brickwedde MK, Ohno S, Vestweber D (Jul 2001). "The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM)". The EMBO Journal. 20 (14): 3738–48. doi:10.1093/emboj/20.14.3738. PMC 125258. PMID 11447115.
  • Itoh M, Sasaki H, Furuse M, Ozaki H, Kita T, Tsukita S (Aug 2001). "Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions". The Journal of Cell Biology. 154 (3): 491–7. doi:10.1083/jcb.200103047. PMC 2196413. PMID 11489913.
  • Hamazaki Y, Itoh M, Sasaki H, Furuse M, Tsukita S (Jan 2002). "Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule". The Journal of Biological Chemistry. 277 (1): 455–61. doi:10.1074/jbc.M109005200. hdl:2433/148697. PMID 11689568.

External links

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

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  • 1nbq: Crystal Structure of Human Junctional Adhesion Molecule Type 1
    1nbq: Crystal Structure of Human Junctional Adhesion Molecule Type 1
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