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P09803

- CADH1_MOUSE

UniProt

P09803 - CADH1_MOUSE

Protein

Cadherin-1

Gene

Cdh1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7 By similarity.By similarity
    E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi259 – 2591Calcium 1
    Metal bindingi259 – 2591Calcium 2
    Metal bindingi290 – 2901Calcium 3
    Sitei702 – 7032Cleavage; by a metalloproteinaseBy similarity
    Sitei733 – 7342Cleavage; by gamma-secretase/PS1By similarity
    Sitei752 – 7532Cleavage; by caspase-3By similarity

    GO - Molecular functioni

    1. beta-catenin binding Source: MGI
    2. calcium ion binding Source: MGI
    3. protein binding Source: UniProtKB
    4. protein domain specific binding Source: MGI
    5. protein phosphatase binding Source: UniProtKB

    GO - Biological processi

    1. calcium-dependent cell-cell adhesion Source: MGI
    2. cellular response to amino acid stimulus Source: MGI
    3. cellular response to indole-3-methanol Source: Ensembl
    4. cellular response to lithium ion Source: Ensembl
    5. cochlea development Source: MGI
    6. epithelial cell morphogenesis Source: MGI
    7. establishment of protein localization to plasma membrane Source: BHF-UCL
    8. homophilic cell adhesion Source: InterPro
    9. intestinal epithelial cell development Source: MGI
    10. in utero embryonic development Source: MGI
    11. negative regulation of canonical Wnt signaling pathway Source: MGI
    12. negative regulation of cell-cell adhesion Source: Ensembl
    13. negative regulation of epithelial cell proliferation Source: MGI
    14. neuron projection development Source: Ensembl
    15. pituitary gland development Source: Ensembl
    16. positive regulation of transcription, DNA-templated Source: Ensembl
    17. positive regulation of transcription factor import into nucleus Source: Ensembl
    18. protein homooligomerization Source: MGI
    19. protein metabolic process Source: MGI
    20. regulation of branching involved in salivary gland morphogenesis Source: MGI
    21. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
    22. regulation of neuron migration Source: MGI
    23. regulation of protein localization Source: MGI
    24. regulation of protein localization to cell surface Source: MGI
    25. regulation of water loss via skin Source: MGI
    26. response to drug Source: Ensembl
    27. response to toxic substance Source: Ensembl
    28. salivary gland cavitation Source: MGI
    29. sensory perception of sound Source: MGI
    30. single organismal cell-cell adhesion Source: MGI
    31. synapse assembly Source: Ensembl
    32. tight junction assembly Source: MGI
    33. trophectodermal cell differentiation Source: MGI

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_199052. Degradation of the extracellular matrix.
    REACT_202937. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_212869. Apoptotic cleavage of cell adhesion proteins.
    REACT_216309. Integrin cell surface interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cadherin-1
    Alternative name(s):
    ARC-1
    Epithelial cadherin
    Short name:
    E-cadherin
    Uvomorulin
    CD_antigen: CD324
    Cleaved into the following 3 chains:
    Gene namesi
    Name:Cdh1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:88354. Cdh1.

    Subcellular locationi

    Cell junction. Cell membrane; Single-pass type I membrane protein. Endosome By similarity. Golgi apparatustrans-Golgi network By similarity
    Note: Colocalizes with DLGAP5 at sites of cell-cell contact in intestinal epithelial cells. Anchored to actin microfilaments through association with alpha-, beta- and gamma-catenin. Sequential proteolysis induced by apoptosis or calcium influx, results in translocation from sites of cell-cell contact to the cytoplasm. Colocalizes with RAB11A endosomes during its transport from the Golgi apparatus to the plasma membrane By similarity.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: Ensembl
    2. adherens junction Source: UniProtKB
    3. aggresome Source: Ensembl
    4. apical junction complex Source: MGI
    5. apical part of cell Source: MGI
    6. axon Source: MGI
    7. axon terminus Source: MGI
    8. basolateral plasma membrane Source: MGI
    9. catenin complex Source: Ensembl
    10. cell-cell adherens junction Source: MGI
    11. cell-cell junction Source: MGI
    12. cell periphery Source: MGI
    13. cell surface Source: MGI
    14. cytoplasm Source: MGI
    15. cytoplasmic side of plasma membrane Source: Ensembl
    16. endosome Source: UniProtKB-SubCell
    17. focal adhesion Source: Ensembl
    18. integral component of membrane Source: UniProtKB-KW
    19. lateral loop Source: BHF-UCL
    20. lateral plasma membrane Source: Ensembl
    21. node of Ranvier Source: BHF-UCL
    22. perinuclear region of cytoplasm Source: Ensembl
    23. plasma membrane Source: MGI
    24. Schmidt-Lanterman incisure Source: BHF-UCL
    25. trans-Golgi network Source: Ensembl

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Endosome, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Propeptidei24 – 156133Sequence AnalysisPRO_0000003717Add
    BLAST
    Chaini157 – 884728Cadherin-1PRO_0000003718Add
    BLAST
    Chaini703 – 884182E-Cad/CTF1Sequence AnalysisPRO_0000236070Add
    BLAST
    Chaini734 – 884151E-Cad/CTF2Sequence AnalysisPRO_0000236071Add
    BLAST
    Chaini753 – 884132E-Cad/CTF3Sequence AnalysisPRO_0000236072Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi560 – 5601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi639 – 6391N-linked (GlcNAc...)Sequence Analysis
    Modified residuei755 – 7551Phosphotyrosine; by SRCBy similarity
    Modified residuei756 – 7561Phosphotyrosine; by SRCBy similarity
    Modified residuei757 – 7571Phosphotyrosine; by SRCBy similarity
    Modified residuei840 – 8401Phosphoserine2 Publications
    Modified residuei842 – 8421Phosphoserine2 Publications
    Modified residuei848 – 8481Phosphoserine2 Publications

    Post-translational modificationi

    N-glycosylation at Asn-639 is essential for expression, folding and trafficking.By similarity
    Ubiquitinated by a SCF complex containing SKP2, which requires prior phosphorylation by CK1/CSNK1A1. Ubiquitinated by CBLL1/HAKAI, requires prior phosphorylation at Tyr-756 By similarity.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP09803.
    PaxDbiP09803.
    PRIDEiP09803.

    PTM databases

    PhosphoSiteiP09803.

    Expressioni

    Tissue specificityi

    Non-neural epithelial tissues.

    Developmental stagei

    In the testis, expression is highest in fetal gonad, then decreases 5-fold in newborn. Detectable in 7-day-old but not in 21-day-old or adult.1 Publication

    Gene expression databases

    BgeeiP09803.
    CleanExiMM_CDH1.
    GenevestigatoriP09803.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1, beta-catenin/CTNNB1 or gamma-catenin/JUP, and potentially alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Interaction with PSEN1, cleaves CDH1 resulting in the disassociation of cadherin-based adherens junctions (CAJs). Interacts with AJAP1, CTNND1 and DLGAP5 By similarity. Interacts with TBC1D2. Interacts with LIMA1. Interacts with CAV1 By similarity. Interacts with the TRPV4 and CTNNB1 complex. Interacts with PIP5K1C By similarity. Interacts with RAB8B. Interacts with DDR1; this stabilizes CDH1 at the cell surface and inhibits its internalization By similarity. Interacts with RAPGEF2 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Cdk5r1P618092EBI-984420,EBI-7840438
    Ctnnb1Q0224813EBI-984420,EBI-397872
    CTNND1O60716-293EBI-984420,EBI-702059From a different organism.
    PTPRMP288273EBI-984420,EBI-2257317From a different organism.
    SKP2Q133092EBI-984420,EBI-456291From a different organism.

    Protein-protein interaction databases

    BioGridi198631. 13 interactions.
    DIPiDIP-29635N.
    IntActiP09803. 12 interactions.
    MINTiMINT-121804.

    Structurei

    Secondary structure

    1
    884
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi160 – 1667
    Beta strandi171 – 1799
    Helixi183 – 1864
    Beta strandi190 – 1978
    Turni198 – 2003
    Beta strandi201 – 2033
    Beta strandi206 – 2094
    Turni211 – 2133
    Beta strandi215 – 2184
    Turni224 – 2263
    Beta strandi228 – 23811
    Turni239 – 2413
    Beta strandi243 – 2453
    Beta strandi248 – 2558
    Beta strandi263 – 2653
    Beta strandi267 – 2748
    Beta strandi282 – 2854
    Turni294 – 2963
    Helixi298 – 3003
    Beta strandi303 – 3119
    Beta strandi314 – 3163
    Beta strandi318 – 3214
    Turni323 – 3253
    Beta strandi327 – 3304
    Turni337 – 3393
    Beta strandi342 – 3509
    Helixi352 – 3543
    Beta strandi358 – 36811
    Beta strandi376 – 38914
    Beta strandi396 – 3983
    Turni409 – 4113
    Beta strandi413 – 4197
    Beta strandi425 – 4295
    Turni431 – 4333
    Beta strandi436 – 4427
    Turni446 – 4483
    Beta strandi450 – 46213
    Beta strandi471 – 48010
    Beta strandi487 – 4926
    Beta strandi494 – 4985
    Beta strandi506 – 5094
    Beta strandi524 – 5296
    Beta strandi535 – 5373
    Turni539 – 5413
    Beta strandi543 – 5464
    Turni555 – 5573
    Beta strandi560 – 57011
    Beta strandi573 – 5753
    Beta strandi579 – 58810
    Beta strandi596 – 5983
    Beta strandi603 – 6086
    Beta strandi612 – 6176
    Beta strandi624 – 6274
    Beta strandi631 – 6344
    Beta strandi637 – 6393
    Beta strandi641 – 6433
    Beta strandi649 – 6557
    Beta strandi668 – 6703
    Beta strandi673 – 6753
    Beta strandi684 – 6885
    Beta strandi785 – 7895
    Turni806 – 8083
    Helixi818 – 8225
    Beta strandi824 – 8274
    Beta strandi830 – 8345
    Turni864 – 8663
    Helixi869 – 8713
    Helixi872 – 8776

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EDHX-ray2.00A/B156-380[»]
    1FF5X-ray2.93A/B157-374[»]
    1I7WX-ray2.00B/D734-884[»]
    1I7XX-ray3.00B/D734-884[»]
    1Q1PX-ray3.20A158-369[»]
    1SUHNMR-A156-300[»]
    2OMWX-ray1.85B158-256[»]
    2QVFX-ray2.40B157-369[»]
    3IFQX-ray2.80C/D778-884[»]
    3LNEX-ray2.00A157-369[»]
    3LNFX-ray2.50A/B157-369[»]
    3LNGX-ray2.70A/B157-369[»]
    3LNHX-ray2.60A/B157-369[»]
    3LNIX-ray2.30A/B157-369[»]
    3Q2LX-ray2.70A/B157-369[»]
    3Q2NX-ray2.73A/B157-369[»]
    3Q2VX-ray3.40A/B157-700[»]
    3QRBX-ray1.80A/B157-369[»]
    DisProtiDP00159.
    ProteinModelPortaliP09803.
    SMRiP09803. Positions 157-692, 784-877.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09803.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini157 – 709553ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini734 – 884151CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei710 – 73324HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini157 – 264108Cadherin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini265 – 377113Cadherin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini378 – 488111Cadherin 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini489 – 595107Cadherin 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini596 – 699104Cadherin 5PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni760 – 77112Required for binding CTNND1 and PSEN1By similarityAdd
    BLAST
    Regioni813 – 88472Required for binding alpha, beta and gamma cateninsBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi840 – 85516Ser-richAdd
    BLAST

    Domaini

    Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.

    Sequence similaritiesi

    Contains 5 cadherin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG328838.
    GeneTreeiENSGT00740000115112.
    HOGENOMiHOG000231254.
    HOVERGENiHBG106438.
    InParanoidiP09803.
    KOiK05689.
    OrthoDBiEOG7PS1DS.
    PhylomeDBiP09803.
    TreeFamiTF316817.

    Family and domain databases

    Gene3Di2.60.40.60. 6 hits.
    4.10.900.10. 1 hit.
    InterProiIPR002126. Cadherin.
    IPR015919. Cadherin-like.
    IPR020894. Cadherin_CS.
    IPR000233. Cadherin_cytoplasmic-dom.
    IPR014868. Cadherin_pro_dom.
    IPR027397. Catenin_binding_dom.
    [Graphical view]
    PfamiPF00028. Cadherin. 5 hits.
    PF01049. Cadherin_C. 1 hit.
    PF08758. Cadherin_pro. 1 hit.
    [Graphical view]
    PRINTSiPR00205. CADHERIN.
    SMARTiSM00112. CA. 4 hits.
    SM01055. Cadherin_pro. 1 hit.
    [Graphical view]
    SUPFAMiSSF49313. SSF49313. 6 hits.
    PROSITEiPS00232. CADHERIN_1. 3 hits.
    PS50268. CADHERIN_2. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P09803-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGARCRSFSA LLLLLQVSSW LCQELEPESC SPGFSSEVYT FPVPERHLER    50
    GHVLGRVRFE GCTGRPRTAF FSEDSRFKVA TDGTITVKRH LKLHKLETSF 100
    LVRARDSSHR ELSTKVTLKS MGHHHHRHHH RDPASESNPE LLMFPSVYPG 150
    LRRQKRDWVI PPISCPENEK GEFPKNLVQI KSNRDKETKV FYSITGQGAD 200
    KPPVGVFIIE RETGWLKVTQ PLDREAIAKY ILYSHAVSSN GEAVEDPMEI 250
    VITVTDQNDN RPEFTQEVFE GSVAEGAVPG TSVMKVSATD ADDDVNTYNA 300
    AIAYTIVSQD PELPHKNMFT VNRDTGVISV LTSGLDRESY PTYTLVVQAA 350
    DLQGEGLSTT AKAVITVKDI NDNAPVFNPS TYQGQVPENE VNARIATLKV 400
    TDDDAPNTPA WKAVYTVVND PDQQFVVVTD PTTNDGILKT AKGLDFEAKQ 450
    QYILHVRVEN EEPFEGSLVP STATVTVDVV DVNEAPIFMP AERRVEVPED 500
    FGVGQEITSY TAREPDTFMD QKITYRIWRD TANWLEINPE TGAIFTRAEM 550
    DREDAEHVKN STYVALIIAT DDGSPIATGT GTLLLVLLDV NDNAPIPEPR 600
    NMQFCQRNPQ PHIITILDPD LPPNTSPFTA ELTHGASVNW TIEYNDAAQE 650
    SLILQPRKDL EIGEYKIHLK LADNQNKDQV TTLDVHVCDC EGTVNNCMKA 700
    GIVAAGLQVP AILGILGGIL ALLILILLLL LFLRRRTVVK EPLLPPDDDT 750
    RDNVYYYDEE GGGEEDQDFD LSQLHRGLDA RPEVTRNDVA PTLMSVPQYR 800
    PRPANPDEIG NFIDENLKAA DSDPTAPPYD SLLVFDYEGS GSEAASLSSL 850
    NSSESDQDQD YDYLNEWGNR FKKLADMYGG GEDD 884
    Length:884
    Mass (Da):98,256
    Last modified:July 1, 1989 - v1
    Checksum:i7A6444148D3D5983
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti267 – 2671E → P in CAA43292. (PubMed:1754391)Curated
    Sequence conflicti272 – 2721S → F in CAA43292. (PubMed:1754391)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06115 mRNA. Translation: CAA29488.1.
    X60961
    , X60962, X60963, X60964, X60965, X60966, X60967, X60968, X60969, X60970, X60971, X60972, X60973, X60974, X60975 Genomic DNA. Translation: CAA43292.1.
    X06339 mRNA. Translation: CAA29645.1.
    M81449 Genomic DNA. Translation: AAA37352.1.
    CCDSiCCDS22638.1.
    PIRiS04528. IJMSCE.
    S34438.
    RefSeqiNP_033994.1. NM_009864.2.
    UniGeneiMm.35605.

    Genome annotation databases

    EnsembliENSMUST00000000312; ENSMUSP00000000312; ENSMUSG00000000303.
    ENSMUST00000167688; ENSMUSP00000132112; ENSMUSG00000000303.
    GeneIDi12550.
    KEGGimmu:12550.
    UCSCiuc009ngi.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06115 mRNA. Translation: CAA29488.1 .
    X60961
    , X60962 , X60963 , X60964 , X60965 , X60966 , X60967 , X60968 , X60969 , X60970 , X60971 , X60972 , X60973 , X60974 , X60975 Genomic DNA. Translation: CAA43292.1 .
    X06339 mRNA. Translation: CAA29645.1 .
    M81449 Genomic DNA. Translation: AAA37352.1 .
    CCDSi CCDS22638.1.
    PIRi S04528. IJMSCE.
    S34438.
    RefSeqi NP_033994.1. NM_009864.2.
    UniGenei Mm.35605.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EDH X-ray 2.00 A/B 156-380 [» ]
    1FF5 X-ray 2.93 A/B 157-374 [» ]
    1I7W X-ray 2.00 B/D 734-884 [» ]
    1I7X X-ray 3.00 B/D 734-884 [» ]
    1Q1P X-ray 3.20 A 158-369 [» ]
    1SUH NMR - A 156-300 [» ]
    2OMW X-ray 1.85 B 158-256 [» ]
    2QVF X-ray 2.40 B 157-369 [» ]
    3IFQ X-ray 2.80 C/D 778-884 [» ]
    3LNE X-ray 2.00 A 157-369 [» ]
    3LNF X-ray 2.50 A/B 157-369 [» ]
    3LNG X-ray 2.70 A/B 157-369 [» ]
    3LNH X-ray 2.60 A/B 157-369 [» ]
    3LNI X-ray 2.30 A/B 157-369 [» ]
    3Q2L X-ray 2.70 A/B 157-369 [» ]
    3Q2N X-ray 2.73 A/B 157-369 [» ]
    3Q2V X-ray 3.40 A/B 157-700 [» ]
    3QRB X-ray 1.80 A/B 157-369 [» ]
    DisProti DP00159.
    ProteinModelPortali P09803.
    SMRi P09803. Positions 157-692, 784-877.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198631. 13 interactions.
    DIPi DIP-29635N.
    IntActi P09803. 12 interactions.
    MINTi MINT-121804.

    PTM databases

    PhosphoSitei P09803.

    Proteomic databases

    MaxQBi P09803.
    PaxDbi P09803.
    PRIDEi P09803.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000000312 ; ENSMUSP00000000312 ; ENSMUSG00000000303 .
    ENSMUST00000167688 ; ENSMUSP00000132112 ; ENSMUSG00000000303 .
    GeneIDi 12550.
    KEGGi mmu:12550.
    UCSCi uc009ngi.1. mouse.

    Organism-specific databases

    CTDi 999.
    MGIi MGI:88354. Cdh1.

    Phylogenomic databases

    eggNOGi NOG328838.
    GeneTreei ENSGT00740000115112.
    HOGENOMi HOG000231254.
    HOVERGENi HBG106438.
    InParanoidi P09803.
    KOi K05689.
    OrthoDBi EOG7PS1DS.
    PhylomeDBi P09803.
    TreeFami TF316817.

    Enzyme and pathway databases

    Reactomei REACT_199052. Degradation of the extracellular matrix.
    REACT_202937. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_212869. Apoptotic cleavage of cell adhesion proteins.
    REACT_216309. Integrin cell surface interactions.

    Miscellaneous databases

    ChiTaRSi CDH1. mouse.
    EvolutionaryTracei P09803.
    NextBioi 281598.
    PROi P09803.
    SOURCEi Search...

    Gene expression databases

    Bgeei P09803.
    CleanExi MM_CDH1.
    Genevestigatori P09803.

    Family and domain databases

    Gene3Di 2.60.40.60. 6 hits.
    4.10.900.10. 1 hit.
    InterProi IPR002126. Cadherin.
    IPR015919. Cadherin-like.
    IPR020894. Cadherin_CS.
    IPR000233. Cadherin_cytoplasmic-dom.
    IPR014868. Cadherin_pro_dom.
    IPR027397. Catenin_binding_dom.
    [Graphical view ]
    Pfami PF00028. Cadherin. 5 hits.
    PF01049. Cadherin_C. 1 hit.
    PF08758. Cadherin_pro. 1 hit.
    [Graphical view ]
    PRINTSi PR00205. CADHERIN.
    SMARTi SM00112. CA. 4 hits.
    SM01055. Cadherin_pro. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49313. SSF49313. 6 hits.
    PROSITEi PS00232. CADHERIN_1. 3 hits.
    PS50268. CADHERIN_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Transformation of cell adhesion properties by exogenously introduced E-cadherin cDNA."
      Nagafuchi A., Shirayoshi Y., Okazari K., Yasuda K., Takeichi M.
      Nature 329:341-343(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: ICR.
    2. "The structure of the gene coding for the mouse cell adhesion molecule uvomorulin."
      Ringwald M., Baribault H., Schmidt C., Kemler R.
      Nucleic Acids Res. 19:6533-6539(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/Sv.
    3. "The structure of cell adhesion molecule uvomorulin. Insights into the molecular mechanism of Ca2+-dependent cell adhesion."
      Ringwald M., Schuh R., Vestweber D., Eistetter H., Lottspeich F., Engel J., Doelz R., Jaehnig F., Epplen J., Mayer S., Mueller C., Kemler R.
      EMBO J. 6:3647-3653(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 174-884, PROTEIN SEQUENCE OF 157-181.
    4. "The E-cadherin promoter: functional analysis of a G.C-rich region and an epithelial cell-specific palindromic regulatory element."
      Behrens J., Loewrick O., Klein-Hitpass L., Birchmeier W.
      Proc. Natl. Acad. Sci. U.S.A. 88:11495-11499(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
    5. "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion."
      Butz S., Kemler R.
      FEBS Lett. 355:195-200(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
    6. "A comprehensive survey of the cadherins expressed in the testes of fetal, immature, and adult mice utilizing the polymerase chain reaction."
      Munro S.B., Blaschuk O.W.
      Biol. Reprod. 55:822-827(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
      Strain: C57BL/6.
      Tissue: Testis.
    7. "Deconstructing the cadherin-catenin-actin complex."
      Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.
      Cell 123:889-901(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
    8. "EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt."
      Abe K., Takeichi M.
      Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
    9. "The TRPV4 channel contributes to intercellular junction formation in keratinocytes."
      Sokabe T., Fukumi-Tominaga T., Yonemura S., Mizuno A., Tominaga M.
      J. Biol. Chem. 285:18749-18758(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRPV4 AND CTNNB1.
    10. "Structural basis of calcium-induced E-cadherin rigidification and dimerization."
      Nagar B., Overduin M., Ikura M., Rini J.M.
      Nature 380:360-364(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 157-370, CALCIUM-BINDING SITES.
    11. "1H, 15N and 13C resonance assignments and monomeric structure of the amino-terminal extracellular domain of epithelial cadherin."
      Overduin M., Tong K.I., Kay C.M., Ikura M.
      J. Biomol. NMR 7:173-189(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 157-260.
    12. "The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin."
      Huber A.H., Weis W.I.
      Cell 105:391-402(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 577-728 IN COMPLEX WITH CTNNB1, PHOSPHORYLATION.
    13. "Interactions of plakoglobin and beta-catenin with desmosomal cadherins: basis of selective exclusion of alpha- and beta-catenin from desmosomes."
      Choi H.J., Gross J.C., Pokutta S., Weis W.I.
      J. Biol. Chem. 284:31776-31788(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 778-884 IN COMPLEX WITH HUMAN JUP, PHOSPHORYLATION AT SER-840; SER-842 AND SER-848.

    Entry informationi

    Entry nameiCADH1_MOUSE
    AccessioniPrimary (citable) accession number: P09803
    Secondary accession number(s): Q61377
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 165 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

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