P12830 · CADH1_HUMAN
- ProteinCadherin-1
- GeneCDH1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids882 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
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).
Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 257 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 257 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 288 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 364-365 | Cleavage; by S.pyogenes SpeB | ||||
Sequence: TV | ||||||
Site | 700-701 | Cleavage; by a metalloproteinase | ||||
Sequence: PV | ||||||
Site | 731-732 | Cleavage; by gamma-secretase/PS1 | ||||
Sequence: LR | ||||||
Site | 750-751 | Cleavage; by caspase-3 | ||||
Sequence: DN |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCadherin-1
- Alternative names
- Cleaved into 3 chains
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP12830
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 155-709 | Extracellular | ||||
Sequence: DWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTINRNTGVISVVTTGLDRESFPTYTLVVQAADLQGEGLSTTATAVITVTDTNDNPPIFNPTTYKGQVPENEANVVITTLKVTDADAPNTPAWEAVYTILNDDGGQFVVTTNPVNNDGILKTAKGLDFEAKQQYILHVAVTNVVPFEVSLTTSTATVTVDVLDVNEAPIFVPPEKRVEVSEDFGVGQEITSYTAQEPDTFMEQKITYRIWRDTANWLEINPDTGAISTRAELDREDFEHVKNSTYTALIIATDNGSPVATGTGTLLLILSDVNDNAPIPEPRTIFFCERNPKPQVINIIDADLPPNTSPFTAELTHGASANWTIQYNDPTQESIILKPKMALEVGDYKINLKLMDNQNKDQVTTLEVSVCDCEGAAGVCRKAQPVEAGLQIPA | ||||||
Transmembrane | 710-730 | Helical | ||||
Sequence: ILGILGGILALLILILLLLLF | ||||||
Topological domain | 731-882 | Cytoplasmic | ||||
Sequence: LRRRAVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Diffuse gastric and lobular breast cancer syndrome (DGLBC)
- Note
- DescriptionA cancer predisposition syndrome with increased susceptibility to diffuse gastric cancer. Diffuse gastric cancer is a malignant disease characterized by poorly differentiated infiltrating lesions resulting in thickening of the stomach. Malignant tumors start in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. In addition to gastric cancer, most female mutation carriers develop lobular carcinoma of the breast.
- See alsoMIM:137215
Natural variants in DGLBC
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_008712 | 244 | D>G | in DGLBC; dbSNP:rs1064794231 | |
VAR_008713 | 487 | V>A | in DGLBC; dbSNP:rs1960965342 | |
VAR_023358 | 832 | V>M | in DGLBC; dbSNP:rs35572355 |
Endometrial cancer (ENDMC)
- Note
- DescriptionA malignancy of endometrium, the mucous lining of the uterus. Most endometrial cancers are adenocarcinomas, cancers that begin in cells that make and release mucus and other fluids.
- See alsoMIM:608089
Ovarian cancer (OC)
- Note
- DescriptionThe term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease.
- See alsoMIM:167000
Breast cancer, lobular (LBC)
- Note
- DescriptionA type of breast cancer that begins in the milk-producing glands (lobules) of the breast.
- See alsoMIM:137215
Blepharocheilodontic syndrome 1 (BCDS1)
- Note
- DescriptionA form of blepharocheilodontic syndrome, a rare autosomal dominant disorder. It is characterized by lower eyelid ectropion, upper eyelid distichiasis, euryblepharon, bilateral cleft lip and palate, and features of ectodermal dysplasia, including hair anomalies, conical teeth and tooth agenesis. An additional rare manifestation is imperforate anus. There is considerable phenotypic variability among affected individuals.
- See alsoMIM:119580
Natural variants in BCDS1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_079392 | 254 | D>Y | in BCDS1; abolishes protein abundance; loss of cell membrane localization; dbSNP:rs1555515445 | |
VAR_079393 | 257 | D>V | in BCDS1; slightly decreases protein abundance; loss of cell membrane localization; dbSNP:rs1555515446 | |
VAR_079394 | 454 | missing | in BCDS1; decreases protein abundance; loss of cell membrane localization |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_048500 | 72 | in dbSNP:rs35606263 | |||
Sequence: D → N | ||||||
Natural variant | VAR_001306 | 123 | in a gastric cancer sample; dbSNP:rs1555514482 | |||
Sequence: H → Y | ||||||
Mutagenesis | 156 | No longer binds L.monocytogenes InlA. | ||||
Sequence: W → A or S | ||||||
Mutagenesis | 156 | Protein is partially unfolded, no longer binds L.monocytogenes InlA. | ||||
Sequence: W → D | ||||||
Mutagenesis | 170 | No longer binds L.monocytogenes InlA. | ||||
Sequence: P → A, E, or V | ||||||
Mutagenesis | 170 | No longer adheres to L.monocytogenes InlA coated beads, nor do cells take up InlA coated beads. | ||||
Sequence: P → E | ||||||
Natural variant | VAR_001307 | 193 | in a diffuse gastric cancer sample; dbSNP:rs1597891014 | |||
Sequence: T → P | ||||||
Natural variant | VAR_008712 | 244 | in DGLBC; dbSNP:rs1064794231 | |||
Sequence: D → G | ||||||
Natural variant | VAR_079392 | 254 | in BCDS1; abolishes protein abundance; loss of cell membrane localization; dbSNP:rs1555515445 | |||
Sequence: D → Y | ||||||
Natural variant | VAR_079393 | 257 | in BCDS1; slightly decreases protein abundance; loss of cell membrane localization; dbSNP:rs1555515446 | |||
Sequence: D → V | ||||||
Natural variant | VAR_013970 | 270 | may contribute to prostate cancer; dbSNP:rs587776399 | |||
Sequence: S → A | ||||||
Natural variant | VAR_001308 | 274-277 | found in gastric carcinoma cell lines | |||
Sequence: Missing | ||||||
Natural variant | VAR_033026 | 282 | in a breast cancer sample; somatic mutation; dbSNP:rs200932258 | |||
Sequence: M → I | ||||||
Natural variant | VAR_001309 | 315 | in lobular breast carcinoma | |||
Sequence: N → S | ||||||
Natural variant | VAR_001310 | 336 | in dbSNP:rs267606712 | |||
Sequence: E → D | ||||||
Natural variant | VAR_013971 | 340 | found in gastric and colorectal cancer samples; cells exhibited decreased aggregation increased invasiveness and non-uniform migration in vitro compared to cells transfected with wild-type sequence; dbSNP:rs116093741 | |||
Sequence: T → A | ||||||
Natural variant | VAR_001311 | 370 | in a diffuse gastric cancer sample; dbSNP:rs2152132676 | |||
Sequence: D → A | ||||||
Natural variant | VAR_048501 | 393 | in dbSNP:rs34466743 | |||
Sequence: I → N | ||||||
Natural variant | VAR_001312 | 400 | in a gastric carcinoma sample; loss of heterozygosity | |||
Sequence: Missing | ||||||
Natural variant | VAR_001313 | 418-423 | in a gastric carcinoma sample | |||
Sequence: Missing | ||||||
Natural variant | VAR_079394 | 454 | in BCDS1; decreases protein abundance; loss of cell membrane localization | |||
Sequence: Missing | ||||||
Natural variant | VAR_001314 | 463 | in a gastric carcinoma sample; dbSNP:rs1960961009 | |||
Sequence: E → Q | ||||||
Natural variant | VAR_001315 | 470 | in dbSNP:rs370864592 | |||
Sequence: T → I | ||||||
Natural variant | VAR_001317 | 473 | in a diffuse gastric cancer sample; dbSNP:rs2152134881 | |||
Sequence: V → D | ||||||
Natural variant | VAR_048502 | 473 | in dbSNP:rs36087757 | |||
Sequence: V → I | ||||||
Natural variant | VAR_023357 | 478 | in dbSNP:rs35520415 | |||
Sequence: L → P | ||||||
Natural variant | VAR_008713 | 487 | in DGLBC; dbSNP:rs1960965342 | |||
Sequence: V → A | ||||||
Natural variant | VAR_001318 | 592 | in a thyroid cancer sample; may play a role in colorectal carcinogenesis; dbSNP:rs35187787 | |||
Sequence: A → T | ||||||
Natural variant | VAR_001319 | 598 | in a gastric cancer sample; dbSNP:rs780759537 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_001320 | 617 | detected in an endometrial cancer sample; loss of heterozygosity; cells exhibited an intermediate phenotype concerning aggregation invasiveness and migration in vitro compared to cells transfected with wild-type sequence; dbSNP:rs33935154 | |||
Sequence: A → T | ||||||
Natural variant | VAR_021868 | 630 | in dbSNP:rs2276331 | |||
Sequence: L → V | ||||||
Natural variant | VAR_055431 | 634 | found in a gastric cancer sample; cells exhibited decreased aggregation increased invasiveness and non-uniform migration in vitro compared to cells transfected with wild-type sequence; dbSNP:rs121964878 | |||
Sequence: A → V | ||||||
Mutagenesis | 637 | CDH1 becomes a substrate for ERAD and is retro-translocated from ER to cytoplasm. | ||||
Sequence: N → Q | ||||||
Natural variant | VAR_021869 | 695 | in dbSNP:rs9282655 | |||
Sequence: C → R | ||||||
Natural variant | VAR_001321 | 711 | detected in an endometrial cancer sample; dbSNP:rs121964871 | |||
Sequence: L → V | ||||||
Mutagenesis | 754 | Abolishes binding to CBLL1. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 759-761 | Binds to CTNNB1 but abolishes interaction of CTNNB1 with PSEN1. Abolishes gamma-secretase cleavage. | ||||
Sequence: GGG → AAA | ||||||
Natural variant | VAR_033027 | 777 | in a breast cancer sample; somatic mutation; dbSNP:rs372989292 | |||
Sequence: D → N | ||||||
Natural variant | VAR_023358 | 832 | in DGLBC; dbSNP:rs35572355 | |||
Sequence: V → M | ||||||
Natural variant | VAR_001322 | 838 | in an ovarian carcinoma sample; somatic mutation; loss of heterozygosity; dbSNP:rs121964872 | |||
Sequence: S → G | ||||||
Natural variant | VAR_023359 | 880 | in dbSNP:rs34507583 | |||
Sequence: E → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 4,375 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond, glycosylation, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-22 | UniProt | |||||
Sequence: MGPWSRSLSALLLLLQVSSWLC | |||||||
Propeptide | PRO_0000003715 | 23-154 | UniProt | ||||
Sequence: QEPEPCHPGFDAESYTFTVPRRHLERGRVLGRVNFEDCTGRQRTAYFSLDTRFKVGTDGVITVKRPLRFHNPQIHFLVYAWDSTYRKFSTKVTLNTVGHHHRPPPHQASVSGIQAELLTFPNSSPGLRRQKR | |||||||
Chain | PRO_0000003716 | 155-882 | UniProt | Cadherin-1 | |||
Sequence: DWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTINRNTGVISVVTTGLDRESFPTYTLVVQAADLQGEGLSTTATAVITVTDTNDNPPIFNPTTYKGQVPENEANVVITTLKVTDADAPNTPAWEAVYTILNDDGGQFVVTTNPVNNDGILKTAKGLDFEAKQQYILHVAVTNVVPFEVSLTTSTATVTVDVLDVNEAPIFVPPEKRVEVSEDFGVGQEITSYTAQEPDTFMEQKITYRIWRDTANWLEINPDTGAISTRAELDREDFEHVKNSTYTALIIATDNGSPVATGTGTLLLILSDVNDNAPIPEPRTIFFCERNPKPQVINIIDADLPPNTSPFTAELTHGASANWTIQYNDPTQESIILKPKMALEVGDYKINLKLMDNQNKDQVTTLEVSVCDCEGAAGVCRKAQPVEAGLQIPAILGILGGILALLILILLLLLFLRRRAVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD | |||||||
Disulfide bond | 163 | UniProt | Interchain | ||||
Sequence: C | |||||||
Glycosylation | 280 | UniProt | O-linked (Man...) serine | ||||
Sequence: S | |||||||
Glycosylation | 285 | UniProt | O-linked (Man...) threonine | ||||
Sequence: T | |||||||
Glycosylation | 358 | UniProt | O-linked (Man...) threonine | ||||
Sequence: T | |||||||
Glycosylation | 470 | UniProt | O-linked (Man...) threonine | ||||
Sequence: T | |||||||
Glycosylation | 472 | UniProt | O-linked (Man...) threonine | ||||
Sequence: T | |||||||
Glycosylation | 509 | UniProt | O-linked (Man...) threonine | ||||
Sequence: T | |||||||
Glycosylation | 558 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 570 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 576 | UniProt | O-linked (Man...) threonine | ||||
Sequence: T | |||||||
Glycosylation | 578 | UniProt | O-linked (Man...) threonine | ||||
Sequence: T | |||||||
Glycosylation | 580 | UniProt | O-linked (Man...) threonine | ||||
Sequence: T | |||||||
Glycosylation | 622 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 637 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Chain | PRO_0000236067 | 701-882 | UniProt | E-Cad/CTF1 | |||
Sequence: VEAGLQIPAILGILGGILALLILILLLLLFLRRRAVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD | |||||||
Chain | PRO_0000236068 | 732-882 | UniProt | E-Cad/CTF2 | |||
Sequence: RRRAVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD | |||||||
Modified residue (large scale data) | 748 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Chain | PRO_0000236069 | 751-882 | UniProt | E-Cad/CTF3 | |||
Sequence: NVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD | |||||||
Modified residue | 753 | UniProt | Phosphotyrosine; by SRC | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 753 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 754 | UniProt | Phosphotyrosine; by SRC | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 754 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 755 | UniProt | Phosphotyrosine; by SRC | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 755 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 770 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 770 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 790 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 793 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 793 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 797 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 838 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 840 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 846 | UniProt | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Processing by the metalloproteinase, induced by calcium influx, causes disruption of cell-cell adhesion and the subsequent release of beta-catenin into the cytoplasm (PubMed:10597309).
The residual membrane-tethered cleavage product is rapidly degraded via an intracellular proteolytic pathway (PubMed:10597309).
Cleavage by caspase-3 releases the cytoplasmic tail resulting in disintegration of the actin microfilament system (PubMed:11076937).
The gamma-secretase-mediated cleavage promotes disassembly of adherens junctions (PubMed:11953314).
During development of the cochlear organ of Corti, cleavage by ADAM10 at adherens junctions promotes pillar cell separation (By similarity).
Degradation by SpeB promotes bacterial translocation across the host epithelial barrier (PubMed:23532847).
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
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 (PubMed:16126725, PubMed:7982500).
Found in a complex composed of CDH1, RAP1A and PKP3; PKP3 acts as a scaffold protein within the complex, the complex is required for CDH1 localization to mature desmosome cell junctions (PubMed:25208567).
Interacts with the TRPV4 and CTNNB1 complex (By similarity).
Interacts with CTNND1 (PubMed:15240885).
The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex (By similarity).
Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1 (By similarity).
Interaction with PSEN1, cleaves CDH1 resulting in the disassociation of cadherin-based adherens junctions (CAJs) (PubMed:11226248, PubMed:16126725).
Interacts with AJAP1 and DLGAP5 (PubMed:14595118, PubMed:14699157).
Interacts with TBC1D2 (PubMed:20116244).
Interacts with LIMA1 (PubMed:18093941).
Interacts with CAV1. Interacts with PIP5K1C (PubMed:17261850).
Interacts with RAB8B (By similarity).
Interacts with RAPGEF2 (By similarity).
Interacts with DDR1; this stabilizes CDH1 at the cell surface and inhibits its internalization (PubMed:20432435).
Interacts with KLRG1 (PubMed:19604491).
Forms a ternary complex composed of ADAM10, CADH1 and EPHA4; within the complex, CADH1 is cleaved by ADAM10 which disrupts adherens junctions (By similarity).
Interacts with SPEF1 (PubMed:31473225).
Interacts with CTNNB1 and PKP2 (PubMed:11790773).
Interacts with AMOTL2; the interaction may facilitate binding of radial actin fibers to cell junction complexes (By similarity).
The formation of the complex between InlA and cadherin-1 is calcium-dependent (PubMed:12526809).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 155-262 | Cadherin 1 | ||||
Sequence: DWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEF | ||||||
Domain | 263-375 | Cadherin 2 | ||||
Sequence: TQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTINRNTGVISVVTTGLDRESFPTYTLVVQAADLQGEGLSTTATAVITVTDTNDNPPIF | ||||||
Domain | 376-486 | Cadherin 3 | ||||
Sequence: NPTTYKGQVPENEANVVITTLKVTDADAPNTPAWEAVYTILNDDGGQFVVTTNPVNNDGILKTAKGLDFEAKQQYILHVAVTNVVPFEVSLTTSTATVTVDVLDVNEAPIF | ||||||
Domain | 487-593 | Cadherin 4 | ||||
Sequence: VPPEKRVEVSEDFGVGQEITSYTAQEPDTFMEQKITYRIWRDTANWLEINPDTGAISTRAELDREDFEHVKNSTYTALIIATDNGSPVATGTGTLLLILSDVNDNAP | ||||||
Domain | 594-697 | Cadherin 5 | ||||
Sequence: IPEPRTIFFCERNPKPQVINIIDADLPPNTSPFTAELTHGASANWTIQYNDPTQESIILKPKMALEVGDYKINLKLMDNQNKDQVTTLEVSVCDCEGAAGVCRK | ||||||
Region | 747-767 | Disordered | ||||
Sequence: DTRDNVYYYDEEGGGEEDQDF | ||||||
Region | 758-769 | Required for binding CTNND1 and PSEN1 | ||||
Sequence: EGGGEEDQDFDL | ||||||
Region | 811-882 | Required for binding alpha, beta and gamma catenins | ||||
Sequence: IDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P12830-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length882
- Mass (Da)97,456
- Last updated1993-07-01 v3
- ChecksumE427118043A13C67
P12830-2
- Name2
- Differences from canonical
- 380-440: Missing
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 10 | in Ref. 3; AAA61259 | ||||
Sequence: A → G | ||||||
Sequence conflict | 29 | in Ref. 3; AAA61259 | ||||
Sequence: H → L | ||||||
Sequence conflict | 47 | in Ref. 3; AAA61259 | ||||
Sequence: E → R | ||||||
Sequence conflict | 70-71 | in Ref. 3; AAA61259 | ||||
Sequence: SL → P | ||||||
Alternative sequence | VSP_055586 | 380-440 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 483 | in Ref. 3; AAA61259 | ||||
Sequence: A → G | ||||||
Sequence conflict | 530 | in Ref. 3; AAA61259 | ||||
Sequence: A → R | ||||||
Sequence conflict | 543 | in Ref. 2; CAA79356 | ||||
Sequence: S → F | ||||||
Sequence conflict | 615 | in Ref. 3; AAA61259 | ||||
Sequence: I → H | ||||||
Sequence conflict | 634-636 | in Ref. 3; AAA61259 | ||||
Sequence: ASA → RVP | ||||||
Sequence conflict | 868 | in Ref. 3; AAA61259 | ||||
Sequence: R → P | ||||||
Sequence conflict | 882 | in Ref. 3; AAA61259 | ||||
Sequence: D → H |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z13009 EMBL· GenBank· DDBJ | CAA78353.1 EMBL· GenBank· DDBJ | mRNA | ||
Z18923 EMBL· GenBank· DDBJ | CAA79356.1 EMBL· GenBank· DDBJ | mRNA | ||
L08599 EMBL· GenBank· DDBJ | AAA61259.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AB025105 EMBL· GenBank· DDBJ | BAA88956.1 EMBL· GenBank· DDBJ | mRNA | ||
AK290012 EMBL· GenBank· DDBJ | BAF82701.1 EMBL· GenBank· DDBJ | mRNA | ||
AK312551 EMBL· GenBank· DDBJ | BAG35448.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ090940 EMBL· GenBank· DDBJ | AAY68225.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC099314 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471092 EMBL· GenBank· DDBJ | EAW83243.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471092 EMBL· GenBank· DDBJ | EAW83244.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L34545 EMBL· GenBank· DDBJ | AAA21764.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D49685 EMBL· GenBank· DDBJ | BAA08537.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35402 EMBL· GenBank· DDBJ | CAA84586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35403 EMBL· GenBank· DDBJ | CAA84586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35404 EMBL· GenBank· DDBJ | CAA84586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35405 EMBL· GenBank· DDBJ | CAA84586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35406 EMBL· GenBank· DDBJ | CAA84586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35407 EMBL· GenBank· DDBJ | CAA84586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35408 EMBL· GenBank· DDBJ | CAA84586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35409 EMBL· GenBank· DDBJ | CAA84586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35410 EMBL· GenBank· DDBJ | CAA84586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35411 EMBL· GenBank· DDBJ | CAA84586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35412 EMBL· GenBank· DDBJ | CAA84586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35413 EMBL· GenBank· DDBJ | CAA84586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35414 EMBL· GenBank· DDBJ | CAA84586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z35415 EMBL· GenBank· DDBJ | CAA84586.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X12790 EMBL· GenBank· DDBJ | CAA31279.1 EMBL· GenBank· DDBJ | mRNA | ||
X52279 EMBL· GenBank· DDBJ | CAA36522.1 EMBL· GenBank· DDBJ | mRNA | ||
S72492 EMBL· GenBank· DDBJ | AAD14108.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
S72397 EMBL· GenBank· DDBJ | AAD14108.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
S72491 EMBL· GenBank· DDBJ | AAD14108.1 EMBL· GenBank· DDBJ | Genomic DNA |