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Protein

Claudin-1

Gene

Cldn1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members play essential roles in the formation of impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN1 is required to prevent the paracellular diffusion of small molecules through tight junctions in the epidermis and is required for the normal barrier function of the skin. Required for normal water homeostasis and to prevent excessive water loss through the skin, probably via an indirect effect on the expression levels of other proteins, since CLDN1 itself seems to be dispensable for water barrier formation in keratinocyte tight junctions.3 Publications

GO - Molecular functioni

  • identical protein binding Source: UniProtKB
  • structural molecule activity Source: InterPro

GO - Biological processi

  • calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules Source: UniProtKB
  • cell-cell junction organization Source: MGI
  • establishment of skin barrier Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_349822. Tight junction interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Claudin-1
Gene namesi
Name:Cldn1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1276109. Cldn1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicBy similarity
Transmembranei8 – 2821HelicalSequence AnalysisAdd
BLAST
Topological domaini29 – 8153ExtracellularSequence AnalysisAdd
BLAST
Transmembranei82 – 10221HelicalSequence AnalysisAdd
BLAST
Topological domaini103 – 11513CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei116 – 13621HelicalSequence AnalysisAdd
BLAST
Topological domaini137 – 16327ExtracellularSequence AnalysisAdd
BLAST
Transmembranei164 – 18421HelicalSequence AnalysisAdd
BLAST
Topological domaini185 – 21127CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: MGI
  • bicellular tight junction Source: UniProtKB
  • cell junction Source: CACAO
  • integral component of membrane Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • lateral plasma membrane Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Tight junction

Pathology & Biotechi

Disruption phenotypei

Complete perinatal lethality. Mice are born at the expected Mendelian rate, but die within one day after birth, due to severe defects in the skin barrier function, leading to rapid transepidermal water loss and dehydration.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Claudin-1PRO_0000144730Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 64By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiO88551.
PRIDEiO88551.

PTM databases

PhosphoSiteiO88551.

Miscellaneous databases

PMAP-CutDBO88551.

Expressioni

Tissue specificityi

Detected in epidermis and liver (at protein level). Widely expressed, with highest levels in liver and kidney.2 Publications

Gene expression databases

BgeeiO88551.
CleanExiMM_CLDN1.
ExpressionAtlasiO88551. baseline and differential.
GenevisibleiO88551. MM.

Interactioni

Subunit structurei

Can form homo- and heteropolymers with other CLDN. Homopolymers interact with CLDN3, but not CLDN2, homopolymers. Directly interacts with TJP1/ZO-1, TJP2/ZO-2 and TJP3/ZO-3. Interacts with MPDZ and INADL.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MpdzQ8VBX62EBI-7158428,EBI-8026435

Protein-protein interaction databases

BioGridi198743. 3 interactions.
IntActiO88551. 2 interactions.
MINTiMINT-113174.
STRINGi10090.ENSMUSP00000023154.

Structurei

3D structure databases

ProteinModelPortaliO88551.
SMRiO88551. Positions 4-185.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni210 – 2112Interactions with TJP1, TJP2, TJP3 and INADL

Sequence similaritiesi

Belongs to the claudin family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG47316.
HOGENOMiHOG000220937.
HOVERGENiHBG000643.
InParanoidiO88551.
KOiK06087.
OMAiIYEGLWM.
OrthoDBiEOG76HQ2T.
PhylomeDBiO88551.
TreeFamiTF331936.

Family and domain databases

InterProiIPR006187. Claudin.
IPR003548. Claudin1.
IPR017974. Claudin_CS.
IPR004031. PMP22/EMP/MP20/Claudin.
[Graphical view]
PANTHERiPTHR12002. PTHR12002. 1 hit.
PfamiPF00822. PMP22_Claudin. 1 hit.
[Graphical view]
PRINTSiPR01077. CLAUDIN.
PR01377. CLAUDIN1.
PROSITEiPS01346. CLAUDIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88551-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANAGLQLLG FILASLGWIG SIVSTALPQW KIYSYAGDNI VTAQAIYEGL
60 70 80 90 100
WMSCVSQSTG QIQCKVFDSL LNLNSTLQAT RALMVIGILL GLIAIFVSTI
110 120 130 140 150
GMKCMRCLED DEVQKMWMAV IGGIIFLISG LATLVATAWY GNRIVQEFYD
160 170 180 190 200
PLTPINARYE FGQALFTGWA AASLCLLGGV LLSCSCPRKT TSYPTPRPYP
210
KPTPSSGKDY V
Length:211
Mass (Da):22,881
Last modified:November 1, 1998 - v1
Checksum:iBEF896FA62DBB6F0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF072127 mRNA. Translation: AAC27078.1.
AK028428 mRNA. Translation: BAC25945.1.
AK036762 mRNA. Translation: BAC29567.1.
AK036780 mRNA. Translation: BAC29574.1.
AK040604 mRNA. Translation: BAC30640.1.
AK054207 mRNA. Translation: BAC35693.1.
AK081601 mRNA. Translation: BAC38267.1.
BC002003 mRNA. Translation: AAH02003.1.
CCDSiCCDS28087.1.
RefSeqiNP_057883.1. NM_016674.4.
UniGeneiMm.289441.

Genome annotation databases

EnsembliENSMUST00000023154; ENSMUSP00000023154; ENSMUSG00000022512.
GeneIDi12737.
KEGGimmu:12737.
UCSCiuc007yuz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF072127 mRNA. Translation: AAC27078.1.
AK028428 mRNA. Translation: BAC25945.1.
AK036762 mRNA. Translation: BAC29567.1.
AK036780 mRNA. Translation: BAC29574.1.
AK040604 mRNA. Translation: BAC30640.1.
AK054207 mRNA. Translation: BAC35693.1.
AK081601 mRNA. Translation: BAC38267.1.
BC002003 mRNA. Translation: AAH02003.1.
CCDSiCCDS28087.1.
RefSeqiNP_057883.1. NM_016674.4.
UniGeneiMm.289441.

3D structure databases

ProteinModelPortaliO88551.
SMRiO88551. Positions 4-185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198743. 3 interactions.
IntActiO88551. 2 interactions.
MINTiMINT-113174.
STRINGi10090.ENSMUSP00000023154.

PTM databases

PhosphoSiteiO88551.

Proteomic databases

PaxDbiO88551.
PRIDEiO88551.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023154; ENSMUSP00000023154; ENSMUSG00000022512.
GeneIDi12737.
KEGGimmu:12737.
UCSCiuc007yuz.2. mouse.

Organism-specific databases

CTDi9076.
MGIiMGI:1276109. Cldn1.

Phylogenomic databases

eggNOGiNOG47316.
HOGENOMiHOG000220937.
HOVERGENiHBG000643.
InParanoidiO88551.
KOiK06087.
OMAiIYEGLWM.
OrthoDBiEOG76HQ2T.
PhylomeDBiO88551.
TreeFamiTF331936.

Enzyme and pathway databases

ReactomeiREACT_349822. Tight junction interactions.

Miscellaneous databases

NextBioi282042.
PMAP-CutDBO88551.
PROiO88551.
SOURCEiSearch...

Gene expression databases

BgeeiO88551.
CleanExiMM_CLDN1.
ExpressionAtlasiO88551. baseline and differential.
GenevisibleiO88551. MM.

Family and domain databases

InterProiIPR006187. Claudin.
IPR003548. Claudin1.
IPR017974. Claudin_CS.
IPR004031. PMP22/EMP/MP20/Claudin.
[Graphical view]
PANTHERiPTHR12002. PTHR12002. 1 hit.
PfamiPF00822. PMP22_Claudin. 1 hit.
[Graphical view]
PRINTSiPR01077. CLAUDIN.
PR01377. CLAUDIN1.
PROSITEiPS01346. CLAUDIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin."
    Furuse M., Fujita K., Hiiragi T., Fujimoto K., Tsukita S.
    J. Cell Biol. 141:1539-1550(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic head, Liver, Oviduct, Thymus and Vagina.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  4. "Ca(2+)-independent cell-adhesion activity of claudins, a family of integral membrane proteins localized at tight junctions."
    Kubota K., Furuse M., Sasaki H., Sonoda N., Fujita K., Nagafuchi A., Tsukita S.
    Curr. Biol. 9:1035-1038(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
  5. "Manner of interaction of heterogeneous claudin species within and between tight junction strands."
    Furuse M., Sasaki H., Tsukita S.
    J. Cell Biol. 147:891-903(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLDN2 AND CLDN3, SUBCELLULAR LOCATION.
  6. "Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins."
    Itoh M., Furuse M., Morita K., Kubota K., Saitou M., Tsukita S.
    J. Cell Biol. 147:1351-1363(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TJP1; TJP2 AND TJP3.
  7. "Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions."
    Itoh M., Sasaki H., Furuse M., Ozaki H., Kita T., Tsukita S.
    J. Cell Biol. 154:491-497(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MPDZ.
  8. "The carboxyl terminus of zona occludens-3 binds and recruits a mammalian homologue of discs lost to tight junctions."
    Roh M.H., Liu C.-J., Laurinec S., Margolis B.
    J. Biol. Chem. 277:27501-27509(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INADL.
  9. "Claudin-based tight junctions are crucial for the mammalian epidermal barrier: a lesson from claudin-1-deficient mice."
    Furuse M., Hata M., Furuse K., Yoshida Y., Haratake A., Sugitani Y., Noda T., Kubo A., Tsukita S.
    J. Cell Biol. 156:1099-1111(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  10. "Contribution of tight junction proteins to ion, macromolecule, and water barrier in keratinocytes."
    Kirschner N., Rosenthal R., Furuse M., Moll I., Fromm M., Brandner J.M.
    J. Invest. Dermatol. 133:1161-1169(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCLD1_MOUSE
AccessioniPrimary (citable) accession number: O88551
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: June 24, 2015
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.