Structure
atLeast majority ProS Experiment
:order disorder conflict PDB cluster ProS Pfam Domain SEG
884
order/disorder by at least rule
disorder by at least rule
order/disorder by majority rule
Region 1suh A 156-156 disorder
Region 1suh A 157-260 order
Region 1suh A 258-260 high_rmsd
Region 1suh A 261-300 disorder
Region 2qvf B 157-369 order
Region 3qrb B 157-369 order
Region 3qrb A 157-369 order
Region 3q2n B 157-369 order
Region 3q2n A 157-369 order
Region 3q2l B 157-369 order
Region 3q2l A 157-369 order
Region 3lni B 157-157 disorder
Region 3lni B 158-182 order
Region 3lni B 183-187 disorder
Region 3lni B 188-369 order
Region 3lni A 157-184 order
Region 3lni A 185-186 disorder
Region 3lni A 187-369 order
Region 3lnh B 157-160 disorder
Region 3lnh B 161-369 order
Region 3lnh A 157-160 disorder
Region 3lnh A 161-369 order
Region 3lng B 157-157 disorder
Region 3lng B 158-369 order
Region 3lng A 157-157 disorder
Region 3lng A 158-369 order
Region 3lne A 157-369 order
Region 1ff5 B 157-374 order
Region 1ff5 A 157-374 order
Region 1edh B 156-158 disorder
Region 1edh B 159-369 order
Region 1edh B 370-380 disorder
Region 1edh A 156-158 disorder
Region 1edh A 159-369 order
Region 1edh A 370-380 disorder
Region 1q1p A 158-369 order
Region 3lnf B 157-160 disorder
Region 3lnf B 161-183 order
Region 3lnf B 184-187 disorder
Region 3lnf B 188-369 order
Region 3lnf A 157-158 disorder
Region 3lnf A 159-369 order
Region 4qd2 J 157-157 disorder
Region 4qd2 J 158-369 order
Region 4qd2 E 157-157 disorder
Region 4qd2 E 158-369 order
Region 3q2v B 157-590 order
Region 3q2v B 591-617 disorder
Region 3q2v B 618-623 order
Region 3q2v B 624-700 disorder
Region 3q2v A 157-659 order
Region 3q2v A 660-663 disorder
Region 3q2v A 664-692 order
Region 3q2v A 693-700 disorder
Seq 158-256 Hetero dimer : P0DJM0
Region 2omw B 158-256 order
Seq 734-884 Hetero trimer : IID50011 Complex
Region 1i7x D 734-785 disorder
Region 1i7x D 786-791 order
Region 1i7x D 792-809 disorder
Region 1i7x D 810-840 order
Region 1i7x D 841-853 disorder
Region 1i7x D 854-879 order
Region 1i7x D 880-884 disorder
Region 1i7x B 734-783 disorder
Region 1i7x B 784-840 order
Region 1i7x B 841-884 disorder
Seq 734-884 Hetero tetramer : IID50011 Complex
Region 1i7w D 734-787 disorder
Region 1i7w D 788-791 order
Region 1i7w D 792-812 disorder
Region 1i7w D 813-850 order
Region 1i7w D 851-860 disorder
Region 1i7w D 861-878 order
Region 1i7w D 879-884 disorder
Region 1i7w B 734-816 disorder
Region 1i7w B 817-850 order
Region 1i7w B 851-861 disorder
Region 1i7w B 862-878 order
Region 1i7w B 879-884 disorder
Seq 778-884 Hetero tetramer : IID00298 Complex
Region 3ifq D 778-783 disorder
Region 3ifq D 784-851 order
Region 3ifq D 852-854 disorder
Region 3ifq D 855-877 order
Region 3ifq D 878-884 disorder
Region 3ifq C 778-783 disorder
Region 3ifq C 784-852 order
Region 3ifq C 853-857 disorder
Region 3ifq C 858-881 order
Region 3ifq C 882-884 disorder
Seq ProS verified 784-881 Hetero tetramer : IID50011 Complex
Region 1i7w B 817-850 order
Region 1i7w B 862-878 order
Region 1i7w D 788-791 order
Region 1i7w D 813-850 order
Region 1i7w D 861-878 order
Seq ProS verified 784-881 Hetero tetramer : IID00298 Complex
Region 3ifq C 784-852 order
Region 3ifq C 858-881 order
Region 3ifq D 784-851 order
Region 3ifq D 855-877 order
Seq ProS verified 784-881 Hetero trimer : IID50011 Complex
Region 1i7x B 784-840 order
Region 1i7x D 786-791 order
Region 1i7x D 810-840 order
Region 1i7x D 854-879 order
757-757 Phosphotyrosine; by SRC
756-756 Phosphotyrosine; by SRC
755-755 Phosphotyrosine; by SRC
Prediction
Disorder 1-24,121-147,734-802,841-858,881-884
Order 25-120,148-733,803-840,859-880
ProS 4-24,141-147,734-739,747-795,841-851
Disorder 1-30,63-67,121-159,694-712,733-798,824-862,878-884
Order 31-62,68-120,160-693,713-732,799-823,863-877
SEG 11-15
,123-131
,474-482
,579-593
,711-731
,755-768
,839-863
Function
Function in SwissProt
Cadherins are calcium-dependent cell adhesion proteins (PubMed:11976333). 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 (PubMed:11976333). 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).
(Microbial infection) Does not function as a receptor for L.monocytogenes internalin A (InlA); mutating a single surface-exposed residue confers receptor activity to this protein and promotes uptake of the bacteria.
Biological Process
Diagram with PDB data
Cdh1/Ctnnb1 BETA-CATENIN/E-CADHERIN COMPLEX