CDH1
Cadherin-1. UniProt annotates extracellular residues 155–709.
Predicted protein structure
A downloaded AlphaFold model connects the CDH1 sequence to its predicted three-dimensional structure.
Open this viewRNA expression by cell type
Percentage of cells with detected CDH1 RNA in the public colon adenocarcinoma cell groups.
Tumor cells34.2%
Dendritic cells3.9%
Fibroblasts2.7%
Macrophages (group B)2.6%
Endothelial cells2.0%
Regulatory T cells2.0%
CD4 T cells1.8%
Macrophages (group A)1.7%
Natural killer cells1.7%
B cells1.4%
Adipocytes1.4%
CD8 T cells1.2%
Granulocytes0.9%
Sequence & binding sites
Choose a protein region, search amino-acid letters, or inspect a recorded binding site.
Loading sequence…
Open the sequence explorerSequence annotations and source records
Canonical sequence and topology
- Target ID
- T-ENSG00000039068
- UniProt accession
- P12830
- Sequence state
- available
- Canonical sequence
- Yes
- Length in amino acids
- 882
- Sequence SHA-256
- 6c2a333136e50ec3440f42cf6abea8d429a38b758d97b3f3610f96b0e25a1d9d
View and select the full canonical sequence
Gray shows the full canonical sequence. Colored spans mark the listed intervals.
Signal peptide
1–22
Membrane-spanning segments
710–730 (Helical)
Source-annotated domains
155–709 (Extracellular); 731–882 (Cytoplasmic)
Source-annotated extracellular intervals
155–709
UniProt annotates the following extracellular intervals.
| Start | End | Length | Sequence and source |
|---|---|---|---|
| 155 | 709 | 555 | Sequence and source
|
Sequence and topology sources
- Source role
- canonical-sequence
- Source
- alphafold-db-canonical-uniprot-field
- Extracted field
- uniprotSequence
- Source row accession
- Not recorded
- Source role
- reviewed-topology
- Source
- UniProt reviewed human surface-field snapshot
- Extracted field
- Not recorded
- Source row accession
- P12830
Download source snapshot (gzip)
- subcellular_location
- SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:18343367, ECO:0000269|PubMed:22294297, ECO:0000269|PubMed:27760340, ECO:0000269|PubMed:28169360}. Cell membrane {ECO:0000269|PubMed:19403558, ECO:0000269|PubMed:20859650, ECO:0000269|PubMed:28301459, ECO:0000269|PubMed:36309486}; Single-pass type I membrane protein. Endosome {ECO:0000269|PubMed:15689490}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:15689490}. Cytoplasm {ECO:0000269|PubMed:22294297}. Cell junction, desmosome {ECO:0000269|PubMed:25208567, ECO:0000269|PubMed:29999492, ECO:0000269|PubMed:33596089}. 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. Recruited to desmosomes at the initial assembly phase and also accumulates progressively at mature desmosome cell-cell junctions (PubMed:25208567, PubMed:29999492). Localizes to cell-cell contacts as keratinocyte differentiation progresses (By similarity). {ECO:0000250|UniProtKB:P09803, ECO:0000269|PubMed:25208567, ECO:0000269|PubMed:29999492}.; SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:34742300}. Note=(Microbial infection) Proteolytically cleaved at the cell membrane upon H.pylori infection. {ECO:0000269|PubMed:34742300}.
- transmembrane
- TRANSMEM 710..730; /note="Helical"; /evidence="ECO:0000255"
- topological_domain
- TOPO_DOM 155..709; /note="Extracellular"; /evidence="ECO:0000255"; TOPO_DOM 731..882; /note="Cytoplasmic"; /evidence="ECO:0000255"
- signal_peptide
- SIGNAL 1..22; /evidence="ECO:0000255"
- lipidation
- Not recorded
Protein identity and location
- Protein
- Cadherin-1
- Protein location
- Transmembrane protein
- Canonical sequence
- P12830 · 882 amino acids
- Extracellular region
- UniProt annotates extracellular residues 155–709.
Expression in normal tissues
- RNA specificity
- Tissue enhanced
- RNA distribution
- Detected in many
- RNA tissue-specific nTPM
- parathyroid gland: 186.0
- Protein specificity
- Low tissue specificity
- Protein distribution
- Detected in all
- Immunohistochemistry reliability
- Enhanced
- Immunofluorescence reliability
- Supported
- Tissue cell-type enrichment
- Adipose visceral - Mesothelial cells, Colon - Colon enterocytes, Liver - Hepatocytes, Lung - Alveolar cells type 2, Prostate - Prostate glandular cells, Thyroid gland - Thyroid glandular cells
- Subcellular location
- Plasma membrane, Cell Junctions
Structures
A predicted target model is available.
Browse related molecular viewsSources and downloads
CDH1 · ENSG00000039068 · P12830