P70408 · CAD10_MOUSE
- ProteinCadherin-10
- GeneCdh10
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids788 (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 | catenin complex | |
Cellular Component | GABA-ergic synapse | |
Cellular Component | glutamatergic synapse | |
Cellular Component | postsynaptic specialization membrane | |
Cellular Component | presynaptic active zone membrane | |
Cellular Component | synapse | |
Molecular Function | beta-catenin binding | |
Molecular Function | cadherin binding | |
Molecular Function | calcium ion 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 | homophilic cell adhesion via plasma membrane adhesion molecules | |
Biological Process | synaptic membrane adhesion |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCadherin-10
- Alternative names
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 accessionP70408
- 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 | 23-613 | Extracellular | ||||
Sequence: ELTFRRTPGIQQMTAESRAPRSDGKILHRQKRGWMWNQFFLLEEYTGSDYQYVGKLHSDQDKGDGSLKYILSGDGAGTLFIIDEKTGDIHATRRIDREEKAFYTLRAQAINRRTLRPVEPESEFVIKIHDINDNEPTFPEEIYTASVPEMSVVGTSVVQVTATDADDPSYGNSARVIYSILQGQPYFSVEPETGIIRTALPNMNRENKEQYQVVIQAKDMGGQMGGLSGTTTVNITLTDVNDNPPRFPQNTIHLRVLESSPVGTAVGSVKATDADTGKNAEVDYRIIDGDGTDMFDIITEKDTQEGIITVKKPLDYENRRLYTLKVEAENTHVDPRFYYLGPFKDTTIVKISIEDVDEPPVFSRSSYLFEVHEDIEVGTIIGTVMARDPDSTSSPIRFTLDRHTDLDRIFNIHSGNGSLYTSKPLDRELSQWHNLTVIAAEINNPKETTRVSVFVRILDVNDNAPQFAVFYDTFVCENARPGQLIQTISAVDKDDPLGGQKFFFSLAAVNPNFTVQDNEDNTARILTRKNGFNRHEISTYLLPVVISDNDYPIQSSTGTLTIRVCACDSQGNMQSCSAEALLLPAGLSTGA | ||||||
Transmembrane | 614-634 | Helical | ||||
Sequence: LIAILLCIIILLVIVVLFAAL | ||||||
Topological domain | 635-788 | Cytoplasmic | ||||
Sequence: KRQRKKEPLILSKEDIRDNIVSYNDEGGGEEDTQAFDIGTLRNPAAIEEKKLRRDIIPETLFIPRRTPTAPDNTDVRDFINERLKEHDLDPTAPPYDSLATYAYEGNDSVAESLSSLESGTTEGDQNYDYLREWGPRFNKLAEMYGGGESDKDA |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, propeptide, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MTIYQFLRLFVLWACLPHFCCP | ||||||
Propeptide | PRO_0000269662 | 23-54 | ||||
Sequence: ELTFRRTPGIQQMTAESRAPRSDGKILHRQKR | ||||||
Chain | PRO_0000126646 | 55-788 | Cadherin-10 | |||
Sequence: GWMWNQFFLLEEYTGSDYQYVGKLHSDQDKGDGSLKYILSGDGAGTLFIIDEKTGDIHATRRIDREEKAFYTLRAQAINRRTLRPVEPESEFVIKIHDINDNEPTFPEEIYTASVPEMSVVGTSVVQVTATDADDPSYGNSARVIYSILQGQPYFSVEPETGIIRTALPNMNRENKEQYQVVIQAKDMGGQMGGLSGTTTVNITLTDVNDNPPRFPQNTIHLRVLESSPVGTAVGSVKATDADTGKNAEVDYRIIDGDGTDMFDIITEKDTQEGIITVKKPLDYENRRLYTLKVEAENTHVDPRFYYLGPFKDTTIVKISIEDVDEPPVFSRSSYLFEVHEDIEVGTIIGTVMARDPDSTSSPIRFTLDRHTDLDRIFNIHSGNGSLYTSKPLDRELSQWHNLTVIAAEINNPKETTRVSVFVRILDVNDNAPQFAVFYDTFVCENARPGQLIQTISAVDKDDPLGGQKFFFSLAAVNPNFTVQDNEDNTARILTRKNGFNRHEISTYLLPVVISDNDYPIQSSTGTLTIRVCACDSQGNMQSCSAEALLLPAGLSTGALIAILLCIIILLVIVVLFAALKRQRKKEPLILSKEDIRDNIVSYNDEGGGEEDTQAFDIGTLRNPAAIEEKKLRRDIIPETLFIPRRTPTAPDNTDVRDFINERLKEHDLDPTAPPYDSLATYAYEGNDSVAESLSSLESGTTEGDQNYDYLREWGPRFNKLAEMYGGGESDKDA | ||||||
Glycosylation | 256 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 456 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 534 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 784 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Expressed at all stages of testicular development with highest levels found in fetal gonad.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 56-160 | Cadherin 1 | ||||
Sequence: WMWNQFFLLEEYTGSDYQYVGKLHSDQDKGDGSLKYILSGDGAGTLFIIDEKTGDIHATRRIDREEKAFYTLRAQAINRRTLRPVEPESEFVIKIHDINDNEPTF | ||||||
Domain | 161-269 | Cadherin 2 | ||||
Sequence: PEEIYTASVPEMSVVGTSVVQVTATDADDPSYGNSARVIYSILQGQPYFSVEPETGIIRTALPNMNRENKEQYQVVIQAKDMGGQMGGLSGTTTVNITLTDVNDNPPRF | ||||||
Domain | 270-384 | Cadherin 3 | ||||
Sequence: PQNTIHLRVLESSPVGTAVGSVKATDADTGKNAEVDYRIIDGDGTDMFDIITEKDTQEGIITVKKPLDYENRRLYTLKVEAENTHVDPRFYYLGPFKDTTIVKISIEDVDEPPVF | ||||||
Domain | 385-489 | Cadherin 4 | ||||
Sequence: SRSSYLFEVHEDIEVGTIIGTVMARDPDSTSSPIRFTLDRHTDLDRIFNIHSGNGSLYTSKPLDRELSQWHNLTVIAAEINNPKETTRVSVFVRILDVNDNAPQF | ||||||
Domain | 489-603 | Cadherin 5 | ||||
Sequence: FAVFYDTFVCENARPGQLIQTISAVDKDDPLGGQKFFFSLAAVNPNFTVQDNEDNTARILTRKNGFNRHEISTYLLPVVISDNDYPIQSSTGTLTIRVCACDSQGNMQSCSAEAL |
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.
- Length788
- Mass (Da)88,312
- Last updated2011-07-27 v3
- Checksum4066D21DBB038AE1
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H3BKV8 | H3BKV8_MOUSE | Cdh10 | 419 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 142 | in Ref. 2; AAH52056/AAH62962 | ||||
Sequence: P → S | ||||||
Sequence conflict | 518-525 | in Ref. 3; AAB87708 | ||||
Sequence: PLGGQKFF → VDRRSFS | ||||||
Sequence conflict | 549 | in Ref. 3; AAB87708 | ||||
Sequence: T → A | ||||||
Sequence conflict | 607-610 | in Ref. 3; AAB87708 | ||||
Sequence: AGLS → WPH | ||||||
Sequence conflict | 635-639 | in Ref. 3; AAB87708 | ||||
Sequence: Missing | ||||||
Sequence conflict | 699 | in Ref. 3; AAB87708 | ||||
Sequence: Missing | ||||||
Sequence conflict | 706 | in Ref. 3; AAB87708 | ||||
Sequence: D → G | ||||||
Sequence conflict | 773 | in Ref. 3; AAB87708 | ||||
Sequence: N → K | ||||||
Sequence conflict | 788 | in Ref. 3; AAB87708 | ||||
Sequence: A → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK138606 EMBL· GenBank· DDBJ | BAE23714.1 EMBL· GenBank· DDBJ | mRNA | ||
BC052056 EMBL· GenBank· DDBJ | AAH52056.1 EMBL· GenBank· DDBJ | mRNA | ||
BC062962 EMBL· GenBank· DDBJ | AAH62962.1 EMBL· GenBank· DDBJ | mRNA | ||
U69137 EMBL· GenBank· DDBJ | AAB87708.1 EMBL· GenBank· DDBJ | mRNA |