CLDN1

Claudin-1 is a protein that in humans is encoded by the CLDN1 gene.[5][6] It belongs to the group of claudins.

CLDN1
Identifiers
Aliases	CLDN1, CLD1, ILVASC, SEMP1, claudin 1
External IDs	OMIM: 603718 MGI: 1276109 HomoloGene: 9620 GeneCards: CLDN1
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3q28 Start 190,305,707 bp[1] End 190,322,446 bp[1]
Gene location (Mouse) Chr. Chromosome 16 (mouse)[2] Band 16|16 B2 Start 26,356,642 bp[2] End 26,371,841 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • structural molecule activity • identical protein binding • virus receptor activity Cellular component • membrane • integral component of membrane • cell junction • cell membrane • integral component of plasma membrane • apical plasma membrane • lateral plasma membrane • bicellular tight junction • cytoplasm • basolateral plasma membrane Biological process • viral entry • cell-cell junction organization • calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules • GO:0022415 viral process • protein homooligomerization • protein heterooligomerization • establishment of skin barrier • bicellular tight junction assembly • aging • establishment of blood-nerve barrier • response to toxic substance • response to lipopolysaccharide • hyperosmotic salinity response • response to ethanol • drug 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: 26.36 – 26.37 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/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. 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.[7]

Interactions

CLDN1 has been shown to interact with CLDN5[8] and CLDN3.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000163347 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022512 - 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. Halford S, Spencer P, Greenwood J, Winton H, Hunt DM, Adamson P (Jun 2000). "Assignment of claudin-1 (CLDN1) to human chromosome 3q28-->q29 with somatic cell hybrids". Cytogenet. Cell Genet. 88 (3–4): 217. doi:10.1159/000015553. PMID 10828592. S2CID 8896678.
6. Morita K, Furuse M, Fujimoto K, Tsukita S (Mar 1999). "Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands". Proc. Natl. Acad. Sci. U.S.A. 96 (2): 511–6. Bibcode:1999PNAS...96..511M. doi:10.1073/pnas.96.2.511. PMC 15167. PMID 9892664.
7. "Entrez Gene: CLDN1 claudin 1".
8. Coyne CB, Gambling TM, Boucher RC, Carson JL, Johnson LG (Nov 2003). "Role of claudin interactions in airway tight junctional permeability". Am. J. Physiol. Lung Cell Mol. Physiol. 285 (5): L1166-78. doi:10.1152/ajplung.00182.2003. PMID 12909588.

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. 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. 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.