Cdh1
entrez
83502
canonical
uniprot
Q9R0T4
canonical
ensembl
ENSRNOG00000020151
resolver
ensembl
ENSRNOG00055018591
resolver
ensembl
ENSRNOG00060012890
resolver
ensembl
ENSRNOG00065012250
resolver
ensp
ENSRNOP00000027346
resolver
ensp
ENSRNOP00055025558
resolver
ensp
ENSRNOP00060017349
resolver
ensp
ENSRNOP00065015259
resolver
enst
ENSRNOT00000027346
resolver
enst
ENSRNOT00055031626
resolver
enst
ENSRNOT00060021932
resolver
enst
ENSRNOT00065019909
resolver
genesymbol
Cdh1
resolver
uniprot
O35794
resolver
uniprot
Q9JIV9
resolver
uniprot_entry
CADH1_RAT
resolver
uniprot_sec
O35794
resolver
uniprot_sec
Q9JIV9
resolver
amino_acid_sequence
MGARCRSFSALLLLLQVSSWLCQQPESESDSCRPGFSSEVYTFLVPERHLERGHILGRVKFEGCTGRPRTAFFSEDSRFKVSTDGVITVKRHLKLHKLETSFLVHAWDSSYRKLSTKVTLKSLGHHHHRHHHRDPVSESNPELLTFPSFHQGLRRQKRDWVIPPINCPENQKGEFPQRLVQIKSNRDKETTVFYSITGPGADKPPVGVFIIERETGWLKVTQPLDREAIDKYLLYSHAVSSNGEAVEDPMEIVVTVTDQNDNRPEFIQEVFEGSVAEGALPGTSVMQVSATDADDDINTYNAAIAYTILSQDPELPHKNMFTVNRDTGVISVVTSGLDRESYPTYTLVVQAADLQGEGLSTTAKAVITVKDINDNAPIFNPSTYQGQVLENEVGARIATLKVTDDDAPNTPAWNAVYTVVNDPDHQFTVITDPKTNEGILKTAKGLDFEAKQQYILHVTVENEEPFEGSLVPSTATVTVDVVDVNEAPIFVPAEKRVEVPEDFGVGLEIASYTAREPDTFMEQKITYRIWRDTANWLEINPETGVISTRAEMDREDSEHVKNSTYTALIIATDDGSPIATGTGTLLLVLSDVNDNAPIPEPRNMQFCQRNPKPHVITILDPDLPPNTSPFTAELTHGASVNWTIEYNDAEQESLILQPRKDLEIGEYKINLKLSDNQNKDQVTTLEVHVCDCEGTVNNCMKAISLEAGLQVPAILGILGGILALLILILLLLLFLRRRTVVKEPLLPPDDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVIRNDVAPTLMSMPQYRPRPANPDEIGNFIDENLKAADSDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDQDQDYDYLNEWGNRFKKLADMYGGGEED
uniprot
proteins
function
FUNCTION: 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. Promotes organization of radial actin fiber structure and cellular response to contractile forces, via its interaction with AMOTL2 which facilitates anchoring of radial actin fibers to CDH1 junction complexes at the cell membrane (By similarity). Plays a role in the early stages of desmosome cell-cell junction formation via facilitating the recruitment of DSG2 and DSP to desmosome plaques (By similarity). Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7. {ECO:0000250|UniProtKB:F1PAA9, ECO:0000250|UniProtKB:P12830}.; FUNCTION: E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production (By similarity). {ECO:0000250|UniProtKB:P12830}.
uniprot
proteins
mass_dalton
98715
uniprot
proteins
post_translational_modification
PTM: During apoptosis or with calcium influx, cleaved by a membrane-bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3 (By similarity). Processing by the metalloproteinase, induced by calcium influx, causes disruption of cell-cell adhesion and the subsequent release of beta-catenin into the cytoplasm (By similarity). The residual membrane-tethered cleavage product is rapidly degraded via an intracellular proteolytic pathway (By similarity). Cleavage by caspase-3 releases the cytoplasmic tail resulting in disintegration of the actin microfilament system (By similarity). The gamma-secretase-mediated cleavage promotes disassembly of adherens junctions (By similarity). During development of the cochlear organ of Corti, cleavage by ADAM10 at adherens junctions promotes pillar cell separation (By similarity). {ECO:0000250|UniProtKB:P09803, ECO:0000250|UniProtKB:P12830}.; PTM: N-glycosylation at Asn-641 is essential for expression, folding and trafficking. Addition of bisecting N-acetylglucosamine by MGAT3 modulates its cell membrane location (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P12830}.; PTM: Ubiquitinated by a SCF complex containing SKP2, which requires prior phosphorylation by CK1/CSNK1A1. Ubiquitinated by CBLL1/HAKAI, requires prior phosphorylation at Tyr-758 (By similarity). {ECO:0000250}.; PTM: O-glycosylated. O-manosylated by TMTC1, TMTC2, TMTC3 or TMTC4. Ser-289 and Thr-513 are O-manosylated by TMTC2 or TMTC4 but not TMTC1 or TMTC3. {ECO:0000250|UniProtKB:P09803}.
uniprot
proteins
pubmed
10650949
uniprot
proteins
pubmed
12639940
uniprot
proteins
sequence_length
886
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250|UniProtKB:P12830}. Cell membrane {ECO:0000250|UniProtKB:P12830}; Single-pass type I membrane protein. Endosome {ECO:0000250|UniProtKB:P12830}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P12830}. Cytoplasm {ECO:0000250|UniProtKB:P09803}. Cell junction, desmosome {ECO:0000250|UniProtKB:P12830}. 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). Recruited to desmosomes at the initial assembly phase and also accumulates progressively at mature desmosome cell-cell junctions (By similarity). Localizes to cell-cell contacts as keratinocyte differentiation progresses (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P09803, ECO:0000250|UniProtKB:P12830}.
uniprot
proteins
transmembrane_region
TRANSMEM 714..734; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins