P58365 (CAD23_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 84.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cadherin-23 Alternative name(s): Otocadherin | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 3317 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells. CDH23 is required for establishing and/or maintaining the proper organization of the stereocilia bundle of hair cells in the cochlea and the vestibule during late embryonic/early postnatal development. It is part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal hearing By similarity. |
| Subunit structure | Interacts with USH1C and USH1G. Interacts with PCDH15 By similarity. |
| Subcellular location | Cell membrane; Single-pass type I membrane protein By similarity. |
| 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 By similarity. |
| Sequence similarities | Contains 27 cadherin domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell adhesion Hearing |
| Cellular component | Cell membrane Membrane |
| Domain | Repeat Signal Transmembrane Transmembrane helix |
| Ligand | Calcium Metal-binding |
| PTM | Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | detection of mechanical stimulus involved in sensory perception of sound Traceable author statement PubMed 15882573. Source: RGD homophilic cell adhesionInferred from electronic annotation. Source: InterPro |
| Cellular_component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | calcium ion binding Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 23 | 23 | Potential | ||||||
| Chain | 24 – 3317 | 3294 | Cadherin-23 | PRO_0000003826 | |||||
Regions | |||||||||
| Topological domain | 24 – 3062 | 3039 | Extracellular Potential | ||||||
| Transmembrane | 3063 – 3083 | 21 | Helical; Potential | ||||||
| Topological domain | 3084 – 3317 | 234 | Cytoplasmic Potential | ||||||
| Domain | 34 – 132 | 99 | Cadherin 1 | ||||||
| Domain | 133 – 236 | 104 | Cadherin 2 | ||||||
| Domain | 237 – 348 | 112 | Cadherin 3 | ||||||
| Domain | 349 – 458 | 110 | Cadherin 4 | ||||||
| Domain | 459 – 559 | 101 | Cadherin 5 | ||||||
| Domain | 560 – 669 | 110 | Cadherin 6 | ||||||
| Domain | 670 – 782 | 113 | Cadherin 7 | ||||||
| Domain | 777 – 888 | 112 | Cadherin 8 | ||||||
| Domain | 889 – 993 | 105 | Cadherin 9 | ||||||
| Domain | 994 – 1100 | 107 | Cadherin 10 | ||||||
| Domain | 1101 – 1206 | 106 | Cadherin 11 | ||||||
| Domain | 1208 – 1311 | 104 | Cadherin 12 | ||||||
| Domain | 1312 – 1416 | 105 | Cadherin 13 | ||||||
| Domain | 1418 – 1525 | 108 | Cadherin 14 | ||||||
| Domain | 1527 – 1632 | 106 | Cadherin 15 | ||||||
| Domain | 1633 – 1742 | 110 | Cadherin 16 | ||||||
| Domain | 1743 – 1849 | 107 | Cadherin 17 | ||||||
| Domain | 1850 – 1957 | 108 | Cadherin 18 | ||||||
| Domain | 1958 – 2067 | 110 | Cadherin 19 | ||||||
| Domain | 2068 – 2172 | 105 | Cadherin 20 | ||||||
| Domain | 2173 – 2291 | 119 | Cadherin 21 | ||||||
| Domain | 2295 – 2400 | 106 | Cadherin 22 | ||||||
| Domain | 2401 – 2507 | 107 | Cadherin 23 | ||||||
| Domain | 2508 – 2609 | 102 | Cadherin 24 | ||||||
| Domain | 2612 – 2720 | 109 | Cadherin 25 | ||||||
| Domain | 2727 – 2844 | 118 | Cadherin 26 | ||||||
| Domain | 2845 – 2973 | 129 | Cadherin 27 | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 155 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 206 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 349 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 391 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 432 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 464 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 470 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 600 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 692 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 763 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 808 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 825 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 939 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 999 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1016 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1169 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1280 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1313 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1471 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1532 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1649 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1665 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1816 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1855 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1887 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1900 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2012 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2048 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2127 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2166 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2193 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2261 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2355 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2367 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2576 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2614 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2747 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2806 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2875 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2894 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2939 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2979 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Identification of three novel non-classical cadherin genes through comprehensive analysis of large cDNAs." Nakajima D., Nakayama M., Kikuno R., Hirosawa M., Nagase T., Ohara O. Brain Res. Mol. Brain Res. 94:85-95(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Testis. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB053447 mRNA. Translation: BAB61904.1. |
| IPI | IPI00480591. |
| RefSeq | NP_446096.1. NM_053644.1. |
| UniGene | Rn.208796. |
3D structure databases | |
| ProteinModelPortal | P58365. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10116.ENSRNOP00000049630. |
PTM databases | |
| PhosphoSite | P58365. |
Proteomic databases | |
| PaxDb | P58365. |
| PRIDE | P58365. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 114102. |
| KEGG | rno:114102. |
| UCSC | RGD:619760. rat. |
Organism-specific databases | |
| CTD | 64072. |
| RGD | 619760. Cdh23. |
Phylogenomic databases | |
| eggNOG | NOG12793. |
| HOGENOM | HOG000139588. |
| HOVERGEN | HBG050768. |
| KO | K06813. |
Gene expression databases | |
| ArrayExpress | P58365. |
| Genevestigator | P58365. |
Family and domain databases | |
| Gene3D | 2.60.40.60. 27 hits. |
| InterPro | IPR002126. Cadherin. IPR015919. Cadherin-like. IPR020894. Cadherin_CS. [Graphical view] |
| Pfam | PF00028. Cadherin. 25 hits. [Graphical view] |
| PRINTS | PR00205. CADHERIN. |
| SMART | SM00112. CA. 26 hits. [Graphical view] |
| SUPFAM | SSF49313. Cadherin. 27 hits. |
| PROSITE | PS00232. CADHERIN_1. 17 hits. PS50268. CADHERIN_2. 27 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 618265. |
Entry information
| Entry name | CAD23_RAT | ||||||||
| Accession | Primary (citable) accession number: P58365 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
