P55289 · CAD12_HUMAN
- ProteinCadherin-12
- GeneCDH12
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids794 (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 | plasma membrane | |
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 |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCadherin-12
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP55289
- 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 | 55-609 | Extracellular | ||||
Sequence: GWVWNQFFVLEEYVGSEPQYVGKLHSDLDKGEGTVKYTLSGDGAGTVFTIDETTGDIHAIRSLDREEKPFYTLRAQAVDIETRKPLEPESEFIIKVQDINDNEPKFLDGPYVATVPEMSPVGAYVLQVKATDADDPTYGNSARVVYSILQGQPYFSIDPKTGVIRTALPNMDREVKEQYQVLIQAKDMGGQLGGLAGTTIVNITLTDVNDNPPRFPKSIFHLKVPESSPIGSAIGRIRAVDPDFGQNAEIEYNIVPGDGGNLFDIVTDEDTQEGVIKLKKPLDFETKKAYTFKVEASNLHLDHRFHSAGPFKDTATVKISVLDVDEPPVFSKPLYTMEVYEDTPVGTIIGAVTAQDLDVGSSAVRYFIDWKSDGDSYFTIDGNEGTIATNELLDRESTAQYNFSIIASKVSNPLLTSKVNILINVLDVNEFPPEISVPYETAVCENAKPGQIIQIVSAADRDLSPAGQQFSFRLSPEAAIKPNFTVRDFRNNTAGIETRRNGYSRRQQELYFLPVVIEDSSYPVQSSTNTMTIRVCRCDSDGTILSCNVEAIFLP | ||||||
Transmembrane | 610-637 | Helical | ||||
Sequence: VGLSTGALIAILLCIVILLAIVVLYVAL | ||||||
Topological domain | 638-794 | Cytoplasmic | ||||
Sequence: RRQKKKDTLMTSKEDIRDNVIHYDDEGGGEEDTQAFDIGALRNPKVIEENKIRRDIKPDSLCLPRQRPPMEDNTDIRDFIHQRLQENDVDPTAPPYDSLATYAYEGSGSVAESLSSIDSLTTEADQDYDYLTDWGPRFKVLADMFGEEESYNPDKVT |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_048505 | 68 | in dbSNP:rs4371716 | |||
Sequence: V → M | ||||||
Natural variant | VAR_048506 | 284 | in dbSNP:rs17328673 | |||
Sequence: I → V | ||||||
Natural variant | VAR_048507 | 475 | in dbSNP:rs12108814 | |||
Sequence: I → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,381 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, propeptide, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MLTRNCLSLLLWVLFDGGLLTPL | ||||||
Propeptide | PRO_0000003791 | 24-54 | ||||
Sequence: QPQPQQTLATEPRENVIHLPGQRSHFQRVKR | ||||||
Chain | PRO_0000003792 | 55-794 | Cadherin-12 | |||
Sequence: GWVWNQFFVLEEYVGSEPQYVGKLHSDLDKGEGTVKYTLSGDGAGTVFTIDETTGDIHAIRSLDREEKPFYTLRAQAVDIETRKPLEPESEFIIKVQDINDNEPKFLDGPYVATVPEMSPVGAYVLQVKATDADDPTYGNSARVVYSILQGQPYFSIDPKTGVIRTALPNMDREVKEQYQVLIQAKDMGGQLGGLAGTTIVNITLTDVNDNPPRFPKSIFHLKVPESSPIGSAIGRIRAVDPDFGQNAEIEYNIVPGDGGNLFDIVTDEDTQEGVIKLKKPLDFETKKAYTFKVEASNLHLDHRFHSAGPFKDTATVKISVLDVDEPPVFSKPLYTMEVYEDTPVGTIIGAVTAQDLDVGSSAVRYFIDWKSDGDSYFTIDGNEGTIATNELLDRESTAQYNFSIIASKVSNPLLTSKVNILINVLDVNEFPPEISVPYETAVCENAKPGQIIQIVSAADRDLSPAGQQFSFRLSPEAAIKPNFTVRDFRNNTAGIETRRNGYSRRQQELYFLPVVIEDSSYPVQSSTNTMTIRVCRCDSDGTILSCNVEAIFLPVGLSTGALIAILLCIVILLAIVVLYVALRRQKKKDTLMTSKEDIRDNVIHYDDEGGGEEDTQAFDIGALRNPKVIEENKIRRDIKPDSLCLPRQRPPMEDNTDIRDFIHQRLQENDVDPTAPPYDSLATYAYEGSGSVAESLSSIDSLTTEADQDYDYLTDWGPRFKVLADMFGEEESYNPDKVT | ||||||
Glycosylation | 256 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 456 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 537 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 545 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 787 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 55-160 | Cadherin 1 | ||||
Sequence: GWVWNQFFVLEEYVGSEPQYVGKLHSDLDKGEGTVKYTLSGDGAGTVFTIDETTGDIHAIRSLDREEKPFYTLRAQAVDIETRKPLEPESEFIIKVQDINDNEPKF | ||||||
Domain | 161-269 | Cadherin 2 | ||||
Sequence: LDGPYVATVPEMSPVGAYVLQVKATDADDPTYGNSARVVYSILQGQPYFSIDPKTGVIRTALPNMDREVKEQYQVLIQAKDMGGQLGGLAGTTIVNITLTDVNDNPPRF | ||||||
Domain | 270-384 | Cadherin 3 | ||||
Sequence: PKSIFHLKVPESSPIGSAIGRIRAVDPDFGQNAEIEYNIVPGDGGNLFDIVTDEDTQEGVIKLKKPLDFETKKAYTFKVEASNLHLDHRFHSAGPFKDTATVKISVLDVDEPPVF | ||||||
Domain | 385-487 | Cadherin 4 | ||||
Sequence: SKPLYTMEVYEDTPVGTIIGAVTAQDLDVGSSAVRYFIDWKSDGDSYFTIDGNEGTIATNELLDRESTAQYNFSIIASKVSNPLLTSKVNILINVLDVNEFPP | ||||||
Domain | 488-609 | Cadherin 5 | ||||
Sequence: EISVPYETAVCENAKPGQIIQIVSAADRDLSPAGQQFSFRLSPEAAIKPNFTVRDFRNNTAGIETRRNGYSRRQQELYFLPVVIEDSSYPVQSSTNTMTIRVCRCDSDGTILSCNVEAIFLP |
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 & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P55289-1
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
- Length794
- Mass (Da)88,332
- Last updated2007-08-21 v2
- Checksum76DF39AB56E7BC2D
P55289-2
- Name2
- Differences from canonical
- 176-215: Missing
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_056449 | 176-215 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 349 | in Ref. 2; AAB48539 | ||||
Sequence: E → D | ||||||
Sequence conflict | 416 | in Ref. 1; AAA35623 | ||||
Sequence: S → G | ||||||
Sequence conflict | 644 | in Ref. 1; AAA35623 | ||||
Sequence: D → H | ||||||
Sequence conflict | 733 | in Ref. 1; AAA35623 | ||||
Sequence: Y → I | ||||||
Sequence conflict | 761 | in Ref. 2; AAB48539 | ||||
Sequence: A → T |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L34057 EMBL· GenBank· DDBJ | AAA35623.1 EMBL· GenBank· DDBJ | mRNA | ||
L33477 EMBL· GenBank· DDBJ | AAB48539.1 EMBL· GenBank· DDBJ | mRNA | ||
AK295123 EMBL· GenBank· DDBJ | BAH11982.1 EMBL· GenBank· DDBJ | mRNA | ||
AK314800 EMBL· GenBank· DDBJ | BAG37328.1 EMBL· GenBank· DDBJ | mRNA | ||
AC022139 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC026716 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC034239 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC091938 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC093263 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC108089 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC109455 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC138854 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC138940 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC139497 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC140132 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC140171 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471118 EMBL· GenBank· DDBJ | EAX10736.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC047608 EMBL· GenBank· DDBJ | AAH47608.1 EMBL· GenBank· DDBJ | mRNA |