P97291 · CADH8_MOUSE
- ProteinCadherin-8
- GeneCdh8
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids799 (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 | adherens junction | |
Cellular Component | axon terminus | |
Cellular Component | catenin complex | |
Cellular Component | glutamatergic synapse | |
Cellular Component | plasma membrane | |
Cellular Component | synaptic cleft | |
Cellular Component | synaptic membrane | |
Molecular Function | beta-catenin binding | |
Molecular Function | cadherin binding | |
Molecular Function | calcium ion binding | |
Molecular Function | identical protein binding | |
Biological Process | adherens junction organization | |
Biological Process | calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules | |
Biological Process | cell migration | |
Biological Process | cell morphogenesis | |
Biological Process | cell-cell adhesion mediated by cadherin | |
Biological Process | cell-cell junction assembly | |
Biological Process | chemical synaptic transmission | |
Biological Process | homophilic cell adhesion via plasma membrane adhesion molecules | |
Biological Process | regulation of synapse organization | |
Biological Process | response to cold | |
Biological Process | synaptic transmission, glutamatergic |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCadherin-8
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP97291
- 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 | 62-621 | Extracellular | ||||
Sequence: GWVWNQMFVLEEFSGPEPILVGRLHTDLDPGSKKIKYILSGDGAGTIFQINDITGDIHAIKRLDREEKAEYTLTAQAVDFETNKPLEPPSEFIIKVQDINDNAPEFLNGPYHATVPEMSILGTSVTNVTATDADDPVYGNSAKLVYSILEGQPYFSIEPETAIIKTALPNMDREAKEEYLVVIQAKDMGGHSGGLSGTTTLTVTLTDVNDNPPKFAQSLYHFSVPEDVVLGTAIGRVKANDQDIGENAQSSYDIIDGDGTALFEITSDAQAQDGVIRLRKPLDFETKKSYTLKVEAANIHIDPRFSSRGPFKDTATVKIVVEDADEPPVFSSPTYLLEVHENAALNSVIGQVTARDPDITSSPIRFSIDRHTDLERQFNINADDGKITLATPLDRELSVWHNITIIATEIRNHSQISRVPVAIKVLDVNDNAPEFASEYEAFLCENGKPGQVIQTVSAMDKDDPKNGHFFLYSLLPEMVNNPNFTIKKNEDNSLSILAKHNGFNRQKQEVYLLPIVISDSGNPPLSSTSTLTIRVCGCSNDGVVQSCNVEAYVLPIGLSM | ||||||
Transmembrane | 622-642 | Helical | ||||
Sequence: GALIAILACIILLLVIVVLFV | ||||||
Topological domain | 643-799 | Cytoplasmic | ||||
Sequence: TLRRHKNEPLIIKDDEDVRENIIRYDDEGGGEEDTEAFDIATLQNPDGINGFLPRKDIKPDLQFMPRQGLAPVPNGVDVDEFINVRLHEADNDPTAPPYDSIQIYGYEGRGSVAGSLSSLESTTSDSDQNFDYLSDWGPRFKRLGELYSVGESDKET |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, propeptide, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-29 | |||||
Sequence: MPERLAETLMDLWTPLIILWITLPSCVYT | ||||||
Propeptide | PRO_0000003775 | 30-61 | ||||
Sequence: APMNQAHVLTTGSPLELSRQSEDMRILSRSKR | ||||||
Chain | PRO_0000003776 | 62-799 | Cadherin-8 | |||
Sequence: GWVWNQMFVLEEFSGPEPILVGRLHTDLDPGSKKIKYILSGDGAGTIFQINDITGDIHAIKRLDREEKAEYTLTAQAVDFETNKPLEPPSEFIIKVQDINDNAPEFLNGPYHATVPEMSILGTSVTNVTATDADDPVYGNSAKLVYSILEGQPYFSIEPETAIIKTALPNMDREAKEEYLVVIQAKDMGGHSGGLSGTTTLTVTLTDVNDNPPKFAQSLYHFSVPEDVVLGTAIGRVKANDQDIGENAQSSYDIIDGDGTALFEITSDAQAQDGVIRLRKPLDFETKKSYTLKVEAANIHIDPRFSSRGPFKDTATVKIVVEDADEPPVFSSPTYLLEVHENAALNSVIGQVTARDPDITSSPIRFSIDRHTDLERQFNINADDGKITLATPLDRELSVWHNITIIATEIRNHSQISRVPVAIKVLDVNDNAPEFASEYEAFLCENGKPGQVIQTVSAMDKDDPKNGHFFLYSLLPEMVNNPNFTIKKNEDNSLSILAKHNGFNRQKQEVYLLPIVISDSGNPPLSSTSTLTIRVCGCSNDGVVQSCNVEAYVLPIGLSMGALIAILACIILLLVIVVLFVTLRRHKNEPLIIKDDEDVRENIIRYDDEGGGEEDTEAFDIATLQNPDGINGFLPRKDIKPDLQFMPRQGLAPVPNGVDVDEFINVRLHEADNDPTAPPYDSIQIYGYEGRGSVAGSLSSLESTTSDSDQNFDYLSDWGPRFKRLGELYSVGESDKET | ||||||
Glycosylation | 188 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 463 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 473 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 544 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 795 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P97291 | Cdh8 P97291 | 2 | EBI-15719457, EBI-15719457 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 62-167 | Cadherin 1 | ||||
Sequence: GWVWNQMFVLEEFSGPEPILVGRLHTDLDPGSKKIKYILSGDGAGTIFQINDITGDIHAIKRLDREEKAEYTLTAQAVDFETNKPLEPPSEFIIKVQDINDNAPEF | ||||||
Domain | 168-276 | Cadherin 2 | ||||
Sequence: LNGPYHATVPEMSILGTSVTNVTATDADDPVYGNSAKLVYSILEGQPYFSIEPETAIIKTALPNMDREAKEEYLVVIQAKDMGGHSGGLSGTTTLTVTLTDVNDNPPKF | ||||||
Domain | 277-391 | Cadherin 3 | ||||
Sequence: AQSLYHFSVPEDVVLGTAIGRVKANDQDIGENAQSSYDIIDGDGTALFEITSDAQAQDGVIRLRKPLDFETKKSYTLKVEAANIHIDPRFSSRGPFKDTATVKIVVEDADEPPVF | ||||||
Domain | 392-494 | Cadherin 4 | ||||
Sequence: SSPTYLLEVHENAALNSVIGQVTARDPDITSSPIRFSIDRHTDLERQFNINADDGKITLATPLDRELSVWHNITIIATEIRNHSQISRVPVAIKVLDVNDNAP | ||||||
Domain | 495-616 | Cadherin 5 | ||||
Sequence: EFASEYEAFLCENGKPGQVIQTVSAMDKDDPKNGHFFLYSLLPEMVNNPNFTIKKNEDNSLSILAKHNGFNRQKQEVYLLPIVISDSGNPPLSSTSTLTIRVCGCSNDGVVQSCNVEAYVLP |
Domain
Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length799
- Mass (Da)88,215
- Last updated2012-10-03 v2
- Checksum0EF1285E5DD67F76
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 247 | in Ref. 1; CAA64857 | ||||
Sequence: K → I |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X95600 EMBL· GenBank· DDBJ | CAA64857.1 EMBL· GenBank· DDBJ | mRNA | ||
AC102643 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC103397 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC162519 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC162867 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466525 EMBL· GenBank· DDBJ | EDL11191.1 EMBL· GenBank· DDBJ | Genomic DNA |