CLD1_MOUSE
ID CLD1_MOUSE Reviewed; 211 AA.
AC O88551;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Claudin-1;
GN Name=Cldn1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9647647; DOI=10.1083/jcb.141.7.1539;
RA Furuse M., Fujita K., Hiiragi T., Fujimoto K., Tsukita S.;
RT "Claudin-1 and -2: novel integral membrane proteins localizing at tight
RT junctions with no sequence similarity to occludin.";
RL J. Cell Biol. 141:1539-1550(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, Liver, Oviduct, Thymus, and Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=10508613; DOI=10.1016/s0960-9822(99)80452-7;
RA Kubota K., Furuse M., Sasaki H., Sonoda N., Fujita K., Nagafuchi A.,
RA Tsukita S.;
RT "Ca(2+)-independent cell-adhesion activity of claudins, a family of
RT integral membrane proteins localized at tight junctions.";
RL Curr. Biol. 9:1035-1038(1999).
RN [5]
RP INTERACTION WITH CLDN2 AND CLDN3, AND SUBCELLULAR LOCATION.
RX PubMed=10562289; DOI=10.1083/jcb.147.4.891;
RA Furuse M., Sasaki H., Tsukita S.;
RT "Manner of interaction of heterogeneous claudin species within and between
RT tight junction strands.";
RL J. Cell Biol. 147:891-903(1999).
RN [6]
RP INTERACTION WITH TJP1; TJP2 AND TJP3.
RX PubMed=10601346; DOI=10.1083/jcb.147.6.1351;
RA Itoh M., Furuse M., Morita K., Kubota K., Saitou M., Tsukita S.;
RT "Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and
RT ZO-3, with the COOH termini of claudins.";
RL J. Cell Biol. 147:1351-1363(1999).
RN [7]
RP INTERACTION WITH MPDZ.
RX PubMed=11489913; DOI=10.1083/jcb.200103047;
RA Itoh M., Sasaki H., Furuse M., Ozaki H., Kita T., Tsukita S.;
RT "Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism
RT for the recruitment of PAR-3 to tight junctions.";
RL J. Cell Biol. 154:491-497(2001).
RN [8]
RP INTERACTION WITH PATJ.
RX PubMed=12021270; DOI=10.1074/jbc.m201177200;
RA Roh M.H., Liu C.-J., Laurinec S., Margolis B.;
RT "The carboxyl terminus of zona occludens-3 binds and recruits a mammalian
RT homologue of discs lost to tight junctions.";
RL J. Biol. Chem. 277:27501-27509(2002).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11889141; DOI=10.1083/jcb.200110122;
RA Furuse M., Hata M., Furuse K., Yoshida Y., Haratake A., Sugitani Y.,
RA Noda T., Kubo A., Tsukita S.;
RT "Claudin-based tight junctions are crucial for the mammalian epidermal
RT barrier: a lesson from claudin-1-deficient mice.";
RL J. Cell Biol. 156:1099-1111(2002).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION.
RX PubMed=23407391; DOI=10.1038/jid.2012.507;
RA Kirschner N., Rosenthal R., Furuse M., Moll I., Fromm M., Brandner J.M.;
RT "Contribution of tight junction proteins to ion, macromolecule, and water
RT barrier in keratinocytes.";
RL J. Invest. Dermatol. 133:1161-1169(2013).
CC -!- FUNCTION: Claudins function as major constituents of the tight junction
CC complexes that regulate the permeability of epithelia. While some
CC claudin family members play essential roles in the formation of
CC impermeable barriers, others mediate the permeability to ions and small
CC molecules. Often, several claudin family members are coexpressed and
CC interact with each other, and this determines the overall permeability.
CC CLDN1 is required to prevent the paracellular diffusion of small
CC molecules through tight junctions in the epidermis and is required for
CC the normal barrier function of the skin. Required for normal water
CC homeostasis and to prevent excessive water loss through the skin,
CC probably via an indirect effect on the expression levels of other
CC proteins, since CLDN1 itself seems to be dispensable for water barrier
CC formation in keratinocyte tight junctions.
CC {ECO:0000269|PubMed:10508613, ECO:0000269|PubMed:11889141,
CC ECO:0000269|PubMed:23407391}.
CC -!- SUBUNIT: Can form homo- and heteropolymers with other CLDN.
CC Homopolymers interact with CLDN3, but not CLDN2, homopolymers. Directly
CC interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3. Interacts with MPDZ
CC and PATJ. Interacts with OCLN, CD81, CLDN4, CLDN6 and CLDN9 (By
CC similarity). {ECO:0000250|UniProtKB:O95832,
CC ECO:0000269|PubMed:10508613, ECO:0000269|PubMed:10562289,
CC ECO:0000269|PubMed:10601346, ECO:0000269|PubMed:11489913,
CC ECO:0000269|PubMed:12021270}.
CC -!- INTERACTION:
CC O88551; Q8VBX6: Mpdz; NbExp=2; IntAct=EBI-7158428, EBI-8026435;
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:10508613, ECO:0000269|PubMed:10562289,
CC ECO:0000269|PubMed:9647647}. Cell membrane
CC {ECO:0000269|PubMed:11889141}; Multi-pass membrane protein
CC {ECO:0000255}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:O95832}. Note=Associates with CD81 and the
CC CLDN1-CD81 complex localizes to the basolateral cell membrane.
CC {ECO:0000250|UniProtKB:O95832}.
CC -!- TISSUE SPECIFICITY: Detected in epidermis and liver (at protein level).
CC Widely expressed, with highest levels in liver and kidney.
CC {ECO:0000269|PubMed:11889141, ECO:0000269|PubMed:9647647}.
CC -!- DISRUPTION PHENOTYPE: Complete perinatal lethality. Mice are born at
CC the expected Mendelian rate, but die within one day after birth, due to
CC severe defects in the skin barrier function, leading to rapid
CC transepidermal water loss and dehydration.
CC {ECO:0000269|PubMed:11889141}.
CC -!- SIMILARITY: Belongs to the claudin family. {ECO:0000305}.
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DR EMBL; AF072127; AAC27078.1; -; mRNA.
DR EMBL; AK028428; BAC25945.1; -; mRNA.
DR EMBL; AK036762; BAC29567.1; -; mRNA.
DR EMBL; AK036780; BAC29574.1; -; mRNA.
DR EMBL; AK040604; BAC30640.1; -; mRNA.
DR EMBL; AK054207; BAC35693.1; -; mRNA.
DR EMBL; AK081601; BAC38267.1; -; mRNA.
DR EMBL; BC002003; AAH02003.1; -; mRNA.
DR CCDS; CCDS28087.1; -.
DR RefSeq; NP_057883.1; NM_016674.4.
DR AlphaFoldDB; O88551; -.
DR SMR; O88551; -.
DR BioGRID; 198743; 2.
DR IntAct; O88551; 2.
DR MINT; O88551; -.
DR STRING; 10090.ENSMUSP00000023154; -.
DR iPTMnet; O88551; -.
DR PhosphoSitePlus; O88551; -.
DR jPOST; O88551; -.
DR PaxDb; O88551; -.
DR PRIDE; O88551; -.
DR ProteomicsDB; 285488; -.
DR Antibodypedia; 3613; 780 antibodies from 44 providers.
DR DNASU; 12737; -.
DR Ensembl; ENSMUST00000023154; ENSMUSP00000023154; ENSMUSG00000022512.
DR GeneID; 12737; -.
DR KEGG; mmu:12737; -.
DR UCSC; uc007yuz.2; mouse.
DR CTD; 9076; -.
DR MGI; MGI:1276109; Cldn1.
DR VEuPathDB; HostDB:ENSMUSG00000022512; -.
DR eggNOG; ENOG502R7HF; Eukaryota.
DR GeneTree; ENSGT00940000155387; -.
DR HOGENOM; CLU_076370_2_3_1; -.
DR InParanoid; O88551; -.
DR OMA; CCCPQKA; -.
DR OrthoDB; 1244077at2759; -.
DR PhylomeDB; O88551; -.
DR TreeFam; TF331936; -.
DR BioGRID-ORCS; 12737; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Cldn1; mouse.
DR PRO; PR:O88551; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; O88551; protein.
DR Bgee; ENSMUSG00000022512; Expressed in pigmented layer of retina and 206 other tissues.
DR ExpressionAtlas; O88551; baseline and differential.
DR Genevisible; O88551; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IDA:CACAO.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0070160; C:tight junction; IDA:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0001618; F:virus receptor activity; ISO:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0016338; P:calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0034331; P:cell junction maintenance; IMP:ARUK-UCL.
DR GO; GO:0045216; P:cell-cell junction organization; ISO:MGI.
DR GO; GO:1903545; P:cellular response to butyrate; IEA:Ensembl.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0071284; P:cellular response to lead ion; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0008065; P:establishment of blood-nerve barrier; ISO:MGI.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; ISO:MGI.
DR GO; GO:0061436; P:establishment of skin barrier; IMP:UniProtKB.
DR GO; GO:0042538; P:hyperosmotic salinity response; IEA:Ensembl.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:1903348; P:positive regulation of bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; ISO:MGI.
DR GO; GO:0090303; P:positive regulation of wound healing; ISO:MGI.
DR GO; GO:0051259; P:protein complex oligomerization; ISO:MGI.
DR GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0070673; P:response to interleukin-18; ISO:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0061772; P:xenobiotic transport across blood-nerve barrier; ISO:MGI.
DR InterPro; IPR006187; Claudin.
DR InterPro; IPR003548; Claudin1.
DR InterPro; IPR017974; Claudin_CS.
DR InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR PANTHER; PTHR12002; PTHR12002; 1.
DR PANTHER; PTHR12002:SF92; PTHR12002:SF92; 1.
DR Pfam; PF00822; PMP22_Claudin; 1.
DR PRINTS; PR01377; CLAUDIN1.
DR PROSITE; PS01346; CLAUDIN; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Disulfide bond; Membrane; Reference proteome;
KW Tight junction; Transmembrane; Transmembrane helix.
FT CHAIN 1..211
FT /note="Claudin-1"
FT /id="PRO_0000144730"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..163
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 190..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..211
FT /note="Interactions with TJP1, TJP2, TJP3 and PATJ"
FT DISULFID 54..64
FT /evidence="ECO:0000250"
SQ SEQUENCE 211 AA; 22881 MW; BEF896FA62DBB6F0 CRC64;
MANAGLQLLG FILASLGWIG SIVSTALPQW KIYSYAGDNI VTAQAIYEGL WMSCVSQSTG
QIQCKVFDSL LNLNSTLQAT RALMVIGILL GLIAIFVSTI GMKCMRCLED DEVQKMWMAV
IGGIIFLISG LATLVATAWY GNRIVQEFYD PLTPINARYE FGQALFTGWA AASLCLLGGV
LLSCSCPRKT TSYPTPRPYP KPTPSSGKDY V
