CLDN1

CLDN1
Identifiers
Aliases	CLDN1, CLD1, ILVASC, SEMP1, claudin 1
External IDs	OMIM: 603718; MGI: 1276109; HomoloGene: 9620; GeneCards: CLDN1; OMA:CLDN1 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3q28 Start 190,305,707 bp End 190,322,446 bp
Gene location (Mouse) Chr. Chromosome 16 (mouse) Band 16|16 B2 Start 26,175,392 bp End 26,190,591 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in skin of thigh germinal epithelium skin of hip skin of abdomen olfactory zone of nasal mucosa epithelium of nasopharynx left uterine tube right lobe of liver nipple gingival epithelium Top expressed in retinal pigment epithelium decidua molar skin of external ear lip Epithelium of choroid plexus epidermis hair follicle skin of abdomen lumbar spinal ganglion More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding structural molecule activity identical protein binding virus receptor activity Cellular component membrane integral component of membrane cell junction plasma membrane integral component of plasma membrane apical plasma membrane lateral plasma membrane bicellular tight junction cytoplasm basolateral plasma membrane Biological process viral entry into host cell cell-cell junction organization calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules viral process protein homooligomerization protein heterooligomerization establishment of skin barrier bicellular tight junction assembly ageing establishment of blood-nerve barrier response to toxic substance response to lipopolysaccharide hyperosmotic salinity response response to ethanol xenobiotic transport across blood-nerve barrier response to interleukin-18 cellular response to lead ion cellular response to interferon-gamma cellular response to tumor necrosis factor response to dexamethasone cellular response to transforming growth factor beta stimulus establishment of endothelial intestinal barrier liver regeneration positive regulation of bicellular tight junction assembly cellular response to butyrate Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9076 12737 Ensembl ENSG00000163347 ENSMUSG00000022512 UniProt O95832 O88551 RefSeq (mRNA) NM_021101 NM_016674 RefSeq (protein) NP_066924 NP_057883 Location (UCSC) Chr 3: 190.31 – 190.32 Mb Chr 16: 26.18 – 26.19 Mb PubMed search
Wikidata
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Claudin-1 is a protein that in humans is encoded by the CLDN1 gene. It belongs to the group of claudins.

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. These junctions are composed of sets of continuous networking strands in the outwardly facing cytoplasmic leaflet, with complementary grooves in the inwardly facing extracytoplasmic leaflet. The protein encoded by this gene, a member of the claudin family, is an integral membrane protein and a component of tight junction strands. Loss of function mutations result in neonatal ichthyosis-sclerosing cholangitis syndrome.

Interactions

CLDN1 has been shown to interact with CLDN5 and CLDN3.

External links

• Human CLDN1 genome location and CLDN1 gene details page in the UCSC Genome Browser.

Further reading

• Kniesel U, Wolburg H (2000). "Tight junctions of the blood-brain barrier". Cell. Mol. Neurobiol. 20 (1): 57–76. doi:10.1023/A:1006995910836. PMID 10690502. S2CID 26473781.
• Heiskala M, Peterson PA, Yang Y (2001). "The roles of claudin superfamily proteins in paracellular transport". Traffic. 2 (2): 93–8. doi:10.1034/j.1600-0854.2001.020203.x. PMID 11247307. S2CID 12132159.
• Tsukita S, Furuse M, Itoh M (2001). "Multifunctional strands in tight junctions". Nat. Rev. Mol. Cell Biol. 2 (4): 285–93. doi:10.1038/35067088. PMID 11283726. S2CID 36524601.
• Tsukita S, Furuse M (2002). "Claudin-based barrier in simple and stratified cellular sheets". Curr. Opin. Cell Biol. 14 (5): 531–6. doi:10.1016/S0955-0674(02)00362-9. PMID 12231346.
• González-Mariscal L, Betanzos A, Nava P, Jaramillo BE (2003). "Tight junction proteins". Prog. Biophys. Mol. Biol. 81 (1): 1–44. doi:10.1016/S0079-6107(02)00037-8. PMID 12475568.
• Swisshelm K, Macek R, Kubbies M (2005). "Role of claudins in tumorigenesis". Adv. Drug Deliv. Rev. 57 (6): 919–28. doi:10.1016/j.addr.2005.01.006. PMID 15820559.
• King JE, Eugenin EA, Buckner CM, Berman JW (2006). "HIV tat and neurotoxicity". Microbes Infect. 8 (5): 1347–57. doi:10.1016/j.micinf.2005.11.014. PMID 16697675.
• Ye J (2007). "Reliance of host cholesterol metabolic pathways for the life cycle of hepatitis C virus". PLOS Pathog. 3 (8): e108. doi:10.1371/journal.ppat.0030108. PMC 1959368. PMID 17784784.
• Furuse M, Fujita K, Hiiragi T, Fujimoto K, Tsukita S (1998). "Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin". J. Cell Biol. 141 (7): 1539–50. doi:10.1083/jcb.141.7.1539. PMC 2132999. PMID 9647647.
• Swisshelm K, Machl A, Planitzer S, Robertson R, Kubbies M, Hosier S (1999). "SEMP1, a senescence-associated cDNA isolated from human mammary epithelial cells, is a member of an epithelial membrane protein superfamily". Gene. 226 (2): 285–95. doi:10.1016/S0378-1119(98)00553-8. PMID 9931503.
• Furuse M, Sasaki H, Tsukita S (1999). "Manner of interaction of heterogeneous claudin species within and between tight junction strands". J. Cell Biol. 147 (4): 891–903. doi:10.1083/jcb.147.4.891. PMC 2156154. PMID 10562289.
• Itoh M, Furuse M, Morita K, Kubota K, Saitou M, Tsukita S (1999). "Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins". J. Cell Biol. 147 (6): 1351–63. doi:10.1083/jcb.147.6.1351. PMC 2168087. PMID 10601346.
• Krämer F, White K, Kubbies M, Swisshelm K, Weber BH (2000). "Genomic organization of claudin-1 and its assessment in hereditary and sporadic breast cancer". Hum. Genet. 107 (3): 249–56. doi:10.1007/s004390000375. PMID 11071387. S2CID 24898101.
• Miyamori H, Takino T, Kobayashi Y, Tokai H, Itoh Y, Seiki M, Sato H (2001). "Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases". J. Biol. Chem. 276 (30): 28204–11. doi:10.1074/jbc.M103083200. hdl:2297/15688. PMID 11382769.
• Hamazaki Y, Itoh M, Sasaki H, Furuse M, Tsukita S (2002). "Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule". J. Biol. Chem. 277 (1): 455–61. doi:10.1074/jbc.M109005200. hdl:2433/148697. PMID 11689568.
• Liu F, Koval M, Ranganathan S, Fanayan S, Hancock WS, Lundberg EK, Beavis RC, Lane L, Duek P, McQuade L, Kelleher NL, Baker MS (2015). "A systems proteomics view of the endogenous human claudin protein family". J Proteome Res. 15 (2): 339–359. doi:10.1021/acs.jproteome.5b00769. PMC 4777318. PMID 26680015.