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   24-JAN-2024, entry version 178.
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;
RC   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   SwissPalm; O88551; -.
DR   jPOST; O88551; -.
DR   PaxDb; 10090-ENSMUSP00000023154; -.
DR   ProteomicsDB; 285488; -.
DR   Antibodypedia; 3613; 919 antibodies from 44 providers.
DR   DNASU; 12737; -.
DR   Ensembl; ENSMUST00000023154.3; ENSMUSP00000023154.3; ENSMUSG00000022512.4.
DR   GeneID; 12737; -.
DR   KEGG; mmu:12737; -.
DR   UCSC; uc007yuz.2; mouse.
DR   AGR; MGI:1276109; -.
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; 4040914at2759; -.
DR   PhylomeDB; O88551; -.
DR   TreeFam; TF331936; -.
DR   BioGRID-ORCS; 12737; 0 hits in 78 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 208 other cell types or tissues.
DR   ExpressionAtlas; O88551; baseline and differential.
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:0016328; C:lateral plasma membrane; IDA:MGI.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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: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: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:0071346; P:cellular response to type II interferon; 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: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   Gene3D; 1.20.140.150; -; 1.
DR   InterPro; IPR006187; Claudin.
DR   InterPro; IPR003548; Claudin1.
DR   InterPro; IPR017974; Claudin_CS.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; CLAUDIN; 1.
DR   PANTHER; PTHR12002:SF92; CLAUDIN-1; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01077; CLAUDIN.
DR   PRINTS; PR01377; CLAUDIN1.
DR   PROSITE; PS01346; CLAUDIN; 1.
DR   Genevisible; O88551; MM.
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
//