| General information | | DisProt: | DP00159 | | Name: | Cadherin-1 | | Synonym(s): | CADH1_MOUSE
Epithelial cadherin
E-cadherin
Uvomorulin
ARC-1
Antigen CD324
E-Cad/CTF1 [cleavage product 1]
E-Cad/CTF2 [cleavage product 2]
E-Cad/CTF3 [cleavage product 3]
| | First appeared in release: | Release 1.1 (12/01/2003) | | UniProt: | P09803 | | UniGene: | Mm.35605 | | SwissProt: | CADH1_MOUSE | | TrEMBL: | | | NCBI (GI): | 115419 | | Source organism: | Mus musculus (Mouse) | | Sequence length: | 884 | | Percent disordered: | 17% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MGARCRSFSA LLLLLQVSSW LCQELEPESC SPGFSSEVYT FPVPERHLER GHVLGRVRFE - 60
GCTGRPRTAF FSEDSRFKVA TDGTITVKRH LKLHKLETSF LVRARDSSHR ELSTKVTLKS - 120
MGHHHHRHHH RDPASESNPE LLMFPSVYPG LRRQKRDWVI PPISCPENEK GEFPKNLVQI - 180
KSNRDKETKV FYSITGQGAD KPPVGVFIIE RETGWLKVTQ PLDREAIAKY ILYSHAVSSN - 240
GEAVEDPMEI VITVTDQNDN RPEFTQEVFE GSVAEGAVPG TSVMKVSATD ADDDVNTYNA - 300
AIAYTIVSQD PELPHKNMFT VNRDTGVISV LTSGLDRESY PTYTLVVQAA DLQGEGLSTT - 360
AKAVITVKDI NDNAPVFNPS TYQGQVPENE VNARIATLKV TDDDAPNTPA WKAVYTVVND - 420
PDQQFVVVTD PTTNDGILKT AKGLDFEAKQ QYILHVRVEN EEPFEGSLVP STATVTVDVV - 480
DVNEAPIFMP AERRVEVPED FGVGQEITSY TAREPDTFMD QKITYRIWRD TANWLEINPE - 540
TGAIFTRAEM DREDAEHVKN STYVALIIAT DDGSPIATGT GTLLLVLLDV NDNAPIPEPR - 600
NMQFCQRNPQ PHIITILDPD LPPNTSPFTA ELTHGASVNW TIEYNDAAQE SLILQPRKDL - 660
EIGEYKIHLK LADNQNKDQV TTLDVHVCDC EGTVNNCMKA GIVAAGLQVP AILGILGGIL - 720
ALLILILLLL LFLRRRTVVK EPLLPPDDDT RDNVYYYDEE GGGEEDQDFD LSQLHRGLDA - 780
RPEVTRNDVA PTLMSVPQYR PRPANPDEIG NFIDENLKAA DSDPTAPPYD SLLVFDYEGS - 840
GSEAASLSSL NSSESDQDQD YDYLNEWGNR FKKLADMYGG GEDD
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| Functional narrative |
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. E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 736 - 884 | | Length: | 149 | | Region sequence: |
RTVVKEPLLPPDDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMS
VPQYRPRPANPDEIGNFIDENLKAADSDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSES
DQDQDYDYLNEWGNRFKKLADMYGGGEDD | | Modification type: | Engineered
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (273 K; pH: 7; phosphate 10 mM)
- Fluorescence polarization/anisotropy (DTT 1 mM; NaCl (buffer) 20 mM; protein 12 mM; Tris-HCl or HEPES (pH 7.0 to 8.5 (10 to 100 mM)))
- Fluorescence polarization/anisotropy (B-mercaptoethanol 10 mM; NaCl (buffer) 20 mM; protein 12 mM; Tris-HCl or HEPES (pH 7.0 to 8.5 (10 to 100 mM)))
- Fluorescence polarization/anisotropy (pH: 7; guanidine HCl 6 M; protein 12 mM; Tris-HCl 100 mM)
- Nuclear magnetic resonance (NMR) (323 K; pH: 8; D2O 50 %; NaCl 10 mM; trimethyl silyl propionate 0.35 mM; Tris-HCl 5 mM)
- Nuclear magnetic resonance (NMR) (298 K; pH: 8; D2O 50 %; NaCl 10 mM; trimethyl silyl propionate 0.35 mM; Tris-HCl 5 mM)
- Nuclear magnetic resonance (NMR) (276 K; pH: 8; D2O 50 %; NaCl 10 mM; trimethyl silyl propionate 0.35 mM; Tris-HCl 5 mM)
- Sensitivity to proteolysis (298 K; CaCl2 2 mM; CHES (pH 9.2) 100 mM; DTT 5 mM)
| References:
- Huber AH, Stewart DB, Laurents DV, Nelson WJ, Weis WI. "The cadherin cytoplasmic domain is unstructured in the absence of beta-catenin. A possible mechanism for regulating cadherin turnover." J Biol Chem. 2001; 276(15): 12301-12309. PubMed: 11121423
| Comments:
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| Comments |
Disordered residues lie within the regions corresponding to cleavage products 1 - 3, however, there is no experimental evidence to confirm that these products are disordered.
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