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O88551

- CLD1_MOUSE

UniProt

O88551 - CLD1_MOUSE

Protein

Claudin-1

Gene

Cldn1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    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

    1. identical protein binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. structural molecule activity Source: InterPro

    GO - Biological processi

    1. calcium-independent cell-cell adhesion Source: UniProtKB
    2. cell-cell junction organization Source: Ensembl
    3. establishment of skin barrier Source: UniProtKB

    Names & Taxonomyi

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

    Organism-specific databases

    MGIiMGI:1276109. Cldn1.

    Subcellular locationi

    GO - Cellular componenti

    1. apical plasma membrane Source: MGI
    2. cell junction Source: Reactome
    3. integral component of membrane Source: UniProtKB
    4. integral component of plasma membrane Source: UniProtKB
    5. lateral plasma membrane Source: MGI
    6. plasma membrane Source: MGI
    7. tight junction Source: UniProtKB

    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

    ArrayExpressiO88551.
    BgeeiO88551.
    CleanExiMM_CLDN1.
    GenevestigatoriO88551.

    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

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 77CytoplasmicBy similarity
    Topological domaini29 – 8153ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini103 – 11513CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini137 – 16327ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini185 – 21127CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 2821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei82 – 10221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei116 – 13621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei164 – 18421HelicalSequence AnalysisAdd
    BLAST

    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

    MANAGLQLLG FILASLGWIG SIVSTALPQW KIYSYAGDNI VTAQAIYEGL    50
    WMSCVSQSTG QIQCKVFDSL LNLNSTLQAT RALMVIGILL GLIAIFVSTI 100
    GMKCMRCLED DEVQKMWMAV IGGIIFLISG LATLVATAWY GNRIVQEFYD 150
    PLTPINARYE FGQALFTGWA AASLCLLGGV LLSCSCPRKT TSYPTPRPYP 200
    KPTPSSGKDY V 211
    Length:211
    Mass (Da):22,881
    Last modified:November 1, 1998 - v1
    Checksum:iBEF896FA62DBB6F0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS28087.1.
    RefSeqi NP_057883.1. NM_016674.4.
    UniGenei Mm.289441.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198743. 3 interactions.
    IntActi O88551. 2 interactions.
    MINTi MINT-113174.
    STRINGi 10090.ENSMUSP00000023154.

    PTM databases

    PhosphoSitei O88551.

    Proteomic databases

    PaxDbi O88551.
    PRIDEi O88551.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023154 ; ENSMUSP00000023154 ; ENSMUSG00000022512 .
    GeneIDi 12737.
    KEGGi mmu:12737.
    UCSCi uc007yuz.2. mouse.

    Organism-specific databases

    CTDi 9076.
    MGIi MGI:1276109. Cldn1.

    Phylogenomic databases

    eggNOGi NOG47316.
    HOGENOMi HOG000220937.
    HOVERGENi HBG000643.
    InParanoidi O88551.
    KOi K06087.
    OMAi IYEGLWM.
    OrthoDBi EOG76HQ2T.
    PhylomeDBi O88551.
    TreeFami TF331936.

    Miscellaneous databases

    NextBioi 282042.
    PMAP-CutDB O88551.
    PROi O88551.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O88551.
    Bgeei O88551.
    CleanExi MM_CLDN1.
    Genevestigatori O88551.

    Family and domain databases

    InterProi IPR006187. Claudin.
    IPR003548. Claudin1.
    IPR017974. Claudin_CS.
    IPR004031. PMP22/EMP/MP20/Claudin.
    [Graphical view ]
    PANTHERi PTHR12002. PTHR12002. 1 hit.
    Pfami PF00822. PMP22_Claudin. 1 hit.
    [Graphical view ]
    PRINTSi PR01077. CLAUDIN.
    PR01377. CLAUDIN1.
    PROSITEi PS01346. CLAUDIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 114 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