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P09803

- CADH1_MOUSE

UniProt

P09803 - CADH1_MOUSE

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Protein
Cadherin-1
Gene
Cdh1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.
E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production 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 metalloproteinase By similarity
Sitei733 – 7342Cleavage; by gamma-secretase/PS1 By similarity
Sitei752 – 7532Cleavage; by caspase-3 By 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. in utero embryonic development Source: MGI
  10. intestinal epithelial cell 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 factor import into nucleus Source: Ensembl
  17. positive regulation of transcription, DNA-templated 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
Complete GO annotation...

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini157 – 709553Extracellular Reviewed prediction
Add
BLAST
Transmembranei710 – 73324Helical; Reviewed prediction
Add
BLAST
Topological domaini734 – 884151Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed prediction
Add
BLAST
Propeptidei24 – 156133 Reviewed prediction
PRO_0000003717Add
BLAST
Chaini157 – 884728Cadherin-1
PRO_0000003718Add
BLAST
Chaini703 – 884182E-Cad/CTF1 Reviewed prediction
PRO_0000236070Add
BLAST
Chaini734 – 884151E-Cad/CTF2 Reviewed prediction
PRO_0000236071Add
BLAST
Chaini753 – 884132E-Cad/CTF3 Reviewed prediction
PRO_0000236072Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi560 – 5601N-linked (GlcNAc...) Reviewed prediction
Glycosylationi639 – 6391N-linked (GlcNAc...) Reviewed prediction
Modified residuei755 – 7551Phosphotyrosine; by SRC By similarity
Modified residuei756 – 7561Phosphotyrosine; by SRC By similarity
Modified residuei757 – 7571Phosphotyrosine; by SRC By similarity
Modified residuei840 – 8401Phosphoserine1 Publication
Modified residuei842 – 8421Phosphoserine1 Publication
Modified residuei848 – 8481Phosphoserine1 Publication

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.

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.2 Publications

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

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.

Miscellaneous databases

EvolutionaryTraceiP09803.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni760 – 77112Required for binding CTNND1 and PSEN1 By similarity
Add
BLAST
Regioni813 – 88472Required for binding alpha, beta and gamma catenins By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi840 – 85516Ser-rich
Add
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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti267 – 2671E → P in CAA43292. 1 Publication
Sequence conflicti272 – 2721S → F in CAA43292. 1 Publication

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: September 3, 2014
This is version 164 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

Dasty 3

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