P33148 · CADHF_XENLA
- ProteinEP-cadherin
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids880 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
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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Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | calcium ion binding | |
Biological Process | homophilic cell adhesion via plasma membrane adhesion molecules |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameEP-cadherin
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus
Accessions
- Primary accessionP33148
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 156-703 | Extracellular | ||||
Sequence: DWVIPPIKVSENERGPFPKRLVQIKSNKDRFNKVYYSITGQGADNPPQGVFRIEWETGWMLVTRPLDREEYDKYVLSSHAVSENGSPVEEPMEITINVIDQNDNRPKFTQDVFRGSVREGVQPGTQVMAVSATDEDDNIDSLNGVLSYSILKQDPEEPIPNLFTINRETGVISLIGTGLDREKFPEYTLTVQATDLEGAGLSVEGKAIIQITDANDNAPIFDPKTYTALVPENEIGFEVQRLSVTDLDMPGTPAWQAVYKIRVNEGGFFNITTDPESNQGILTTAKGLDFELRKQYVLQITVENAEPFSVPLPTSTATVTVTVEDVNEAPFFVPAVSRVDVSEDLSRGEKIISLVAQDPDKQQIQKLSYFIGNDPARWLTVNKDNGIVTGNGNLDRESEYVKNNTYTVIMLVTDDGVSVGTGTGTLILHVLDVNDNGPVPSPRVFTMCDQNPEPQVLTISDADIPPNTYPYKVSLSHGSDLTWKAELDSKGTSMLLSPTQQLKKGDYSIYVLLSDAQNNPQLTVVNATVCSCEGKAIKCQEKLVGGFD | ||||||
Transmembrane | 704-728 | Helical | ||||
Sequence: LPIILVILGSVLALLILFLLLLLFL | ||||||
Topological domain | 729-880 | Cytoplasmic | ||||
Sequence: KRKKVVKEPLLLPEDDTRDNIFYYGEEGGGEEDQDYDLSQLHRGLDSRPDIMRNDVVPTLMPAPHYRPRPSNPDEIGNFIDENLDAADNDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSNSNDEHDYNYLSDWGSRFRKLADMYGGDDDEE |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, propeptide, glycosylation, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-28 | |||||
Sequence: MGSTRLRNASVWLCGLLCLLQVVPSINA | ||||||
Propeptide | PRO_0000003725 | 29-155 | ||||
Sequence: DVSGCKPGFSSAEYIFSVNRRELERGRKLGKVNFSDCTTRKHGLYDVGDSRFRVLPDGTVLVKRHVKLHKDTKFTISTWDARGIKHSTNIAVASKRHRSGEEAHSRSSKLPVLTFPETHTGLKRKKR | ||||||
Glycosylation | 61 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000003726 | 156-880 | EP-cadherin | |||
Sequence: DWVIPPIKVSENERGPFPKRLVQIKSNKDRFNKVYYSITGQGADNPPQGVFRIEWETGWMLVTRPLDREEYDKYVLSSHAVSENGSPVEEPMEITINVIDQNDNRPKFTQDVFRGSVREGVQPGTQVMAVSATDEDDNIDSLNGVLSYSILKQDPEEPIPNLFTINRETGVISLIGTGLDREKFPEYTLTVQATDLEGAGLSVEGKAIIQITDANDNAPIFDPKTYTALVPENEIGFEVQRLSVTDLDMPGTPAWQAVYKIRVNEGGFFNITTDPESNQGILTTAKGLDFELRKQYVLQITVENAEPFSVPLPTSTATVTVTVEDVNEAPFFVPAVSRVDVSEDLSRGEKIISLVAQDPDKQQIQKLSYFIGNDPARWLTVNKDNGIVTGNGNLDRESEYVKNNTYTVIMLVTDDGVSVGTGTGTLILHVLDVNDNGPVPSPRVFTMCDQNPEPQVLTISDADIPPNTYPYKVSLSHGSDLTWKAELDSKGTSMLLSPTQQLKKGDYSIYVLLSDAQNNPQLTVVNATVCSCEGKAIKCQEKLVGGFDLPIILVILGSVLALLILFLLLLLFLKRKKVVKEPLLLPEDDTRDNIFYYGEEGGGEEDQDYDLSQLHRGLDSRPDIMRNDVVPTLMPAPHYRPRPSNPDEIGNFIDENLDAADNDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSNSNDEHDYNYLSDWGSRFRKLADMYGGDDDEE | ||||||
Glycosylation | 343 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 382 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 400 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 425 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 428 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 469 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 471 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 473 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 475 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 558 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 562 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 576 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 578 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 580 | O-linked (GalNAc...) threonine | ||||
Sequence: T | ||||||
Disulfide bond | 603↔687 | |||||
Sequence: CDQNPEPQVLTISDADIPPNTYPYKVSLSHGSDLTWKAELDSKGTSMLLSPTQQLKKGDYSIYVLLSDAQNNPQLTVVNATVCSC | ||||||
Glycosylation | 681 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 685↔694 | |||||
Sequence: CSCEGKAIKC |
Keywords
- PTM
PTM databases
Expression
Interaction
Subunit
Interacts with CTNNB1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P33148 | Ctnnb1 Q02248 | 4 | EBI-15603953, EBI-397872 | |
XENO | P33148 | nmo Q23993 | 4 | EBI-15603953, EBI-876224 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 156-263 | Cadherin 1 | ||||
Sequence: DWVIPPIKVSENERGPFPKRLVQIKSNKDRFNKVYYSITGQGADNPPQGVFRIEWETGWMLVTRPLDREEYDKYVLSSHAVSENGSPVEEPMEITINVIDQNDNRPKF | ||||||
Domain | 264-376 | Cadherin 2 | ||||
Sequence: TQDVFRGSVREGVQPGTQVMAVSATDEDDNIDSLNGVLSYSILKQDPEEPIPNLFTINRETGVISLIGTGLDREKFPEYTLTVQATDLEGAGLSVEGKAIIQITDANDNAPIF | ||||||
Domain | 377-487 | Cadherin 3 | ||||
Sequence: DPKTYTALVPENEIGFEVQRLSVTDLDMPGTPAWQAVYKIRVNEGGFFNITTDPESNQGILTTAKGLDFELRKQYVLQITVENAEPFSVPLPTSTATVTVTVEDVNEAPFF | ||||||
Domain | 488-593 | Cadherin 4 | ||||
Sequence: VPAVSRVDVSEDLSRGEKIISLVAQDPDKQQIQKLSYFIGNDPARWLTVNKDNGIVTGNGNLDRESEYVKNNTYTVIMLVTDDGVSVGTGTGTLILHVLDVNDNGP | ||||||
Domain | 594-704 | Cadherin 5 | ||||
Sequence: VPSPRVFTMCDQNPEPQVLTISDADIPPNTYPYKVSLSHGSDLTWKAELDSKGTSMLLSPTQQLKKGDYSIYVLLSDAQNNPQLTVVNATVCSCEGKAIKCQEKLVGGFDL | ||||||
Region | 790-826 | Disordered | ||||
Sequence: PAPHYRPRPSNPDEIGNFIDENLDAADNDPTAPPYDS |
Domain
Three calcium ions are usually bound at the interface of each cadherin domain.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length880
- Mass (Da)97,651
- Last updated2001-04-27 v2
- ChecksumC6CCD91566427D86
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 3 | in Ref. 2; AAC16910 | ||||
Sequence: S → G | ||||||
Sequence conflict | 112 | in Ref. 2; AAC16910 | ||||
Sequence: I → N | ||||||
Sequence conflict | 163 | in Ref. 4; AA sequence | ||||
Sequence: K → I | ||||||
Sequence conflict | 169 | in Ref. 4; AA sequence | ||||
Sequence: R → K | ||||||
Sequence conflict | 176 | in Ref. 4; AA sequence | ||||
Sequence: L → I | ||||||
Sequence conflict | 573 | in Ref. 2; AAC16910 | ||||
Sequence: S → P | ||||||
Sequence conflict | 864 | in Ref. 2; AAC16910 | ||||
Sequence: S → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X63720 EMBL· GenBank· DDBJ | CAA45252.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
U04707 EMBL· GenBank· DDBJ | AAC16910.1 EMBL· GenBank· DDBJ | mRNA |