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Q99PF4

- CAD23_MOUSE

UniProt

Q99PF4 - CAD23_MOUSE

Protein

Cadherin-23

Gene

Cdh23

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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.1 Publication

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. protein binding Source: IntAct

    GO - Biological processi

    1. auditory receptor cell differentiation Source: MGI
    2. auditory receptor cell stereocilium organization Source: MGI
    3. calcium-dependent cell-cell adhesion Source: MGI
    4. cell adhesion Source: MGI
    5. homophilic cell adhesion Source: InterPro
    6. inner ear development Source: MGI
    7. inner ear morphogenesis Source: MGI
    8. locomotory behavior Source: MGI
    9. post-embryonic organ morphogenesis Source: MGI
    10. sensory perception of light stimulus Source: MGI
    11. sensory perception of sound Source: MGI

    Keywords - Biological processi

    Cell adhesion, Hearing

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cadherin-23
    Alternative name(s):
    Otocadherin
    Gene namesi
    Name:Cdh23
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1890219. Cdh23.

    Subcellular locationi

    GO - Cellular componenti

    1. centrosome Source: MGI
    2. integral component of membrane Source: UniProtKB-KW
    3. kinocilium Source: MGI
    4. photoreceptor inner segment Source: MGI
    5. plasma membrane Source: UniProtKB-SubCell
    6. stereocilium Source: HGNC
    7. stereocilium bundle tip Source: MGI
    8. synapse Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Defects in Cdh23 are the cause of waltzer (v) phenotype. Waltzer mice are characterized by deafness and vestibular dysfunction due to degeneration of the neuroepithelium within the inner ear.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi26 – 261N → I: Strongly reduced affinity for PCDH15. 1 Publication
    Mutagenesisi27 – 271R → I: Strongly reduced affinity for PCDH15. 1 Publication
    Mutagenesisi168 – 1681L → G: Strongly reduced interaction with PCDH15. 1 Publication

    Keywords - Diseasei

    Deafness, Disease mutation, Non-syndromic deafness

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 33543331Cadherin-23PRO_0000003825Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi349 – 3491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi393 – 3931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi434 – 4341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi466 – 4661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi472 – 4721N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi602 – 6021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi694 – 6941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi765 – 7651N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi810 – 8101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi827 – 8271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi941 – 9411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1001 – 10011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1018 – 10181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1171 – 11711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1282 – 12821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1315 – 13151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1473 – 14731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1534 – 15341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1651 – 16511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1667 – 16671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1818 – 18181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1857 – 18571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1889 – 18891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1902 – 19021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2014 – 20141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2050 – 20501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2129 – 21291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2168 – 21681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2195 – 21951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2263 – 22631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2357 – 23571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2369 – 23691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2578 – 25781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2616 – 26161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2749 – 27491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2808 – 28081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2877 – 28771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2896 – 28961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2941 – 29411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2981 – 29811N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ99PF4.
    PRIDEiQ99PF4.

    PTM databases

    PhosphoSiteiQ99PF4.

    Expressioni

    Tissue specificityi

    In adult animals relatively high levels of expression are found in testis, skeletal muscle, heart, eye and thymus, and lower expression in kidney, lung and brain. Found in the sensory hair cells of the inner ear.1 Publication

    Gene expression databases

    BgeeiQ99PF4.
    GenevestigatoriQ99PF4.

    Interactioni

    Subunit structurei

    Interacts with USH1C and USH1G By similarity. antiparallel heterodimer with PCDH15.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ush1cQ9ES64-32EBI-7419021,EBI-7418919

    Protein-protein interaction databases

    BioGridi204475. 1 interaction.
    DIPiDIP-42152N.
    IntActiQ99PF4. 1 interaction.
    MINTiMINT-1895823.

    Structurei

    Secondary structure

    1
    3354
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi34 – 363
    Beta strandi40 – 434
    Beta strandi51 – 544
    Beta strandi66 – 716
    Helixi72 – 776
    Beta strandi78 – 803
    Turni82 – 843
    Beta strandi86 – 916
    Turni95 – 973
    Beta strandi100 – 1089
    Beta strandi113 – 12311
    Beta strandi131 – 1344
    Beta strandi136 – 1427
    Beta strandi150 – 1534
    Helixi162 – 1654
    Beta strandi167 – 1737
    Beta strandi176 – 1805
    Turni182 – 1843
    Beta strandi186 – 1894
    Turni195 – 1973
    Beta strandi199 – 20911
    Beta strandi212 – 2143
    Beta strandi217 – 22711

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WBXX-ray1.50A24-124[»]
    2WCPX-ray1.98A24-228[»]
    2WD0X-ray2.74A/C24-228[»]
    2WHVX-ray2.36A24-228[»]
    3MVSX-ray1.10A24-233[»]
    4APXX-ray1.65A24-228[»]
    4AQ8X-ray2.63A/B24-228[»]
    4AQAX-ray1.96A24-228[»]
    4AQEX-ray2.27A24-228[»]
    4AXWX-ray2.23A24-228[»]
    ProteinModelPortaliQ99PF4.
    SMRiQ99PF4. Positions 24-233.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ99PF4.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 30643041ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini3086 – 3354269CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei3065 – 308521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini34 – 13299Cadherin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini133 – 236104Cadherin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini237 – 348112Cadherin 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini349 – 460112Cadherin 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini461 – 561101Cadherin 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini562 – 671110Cadherin 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini672 – 784113Cadherin 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini779 – 890112Cadherin 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini891 – 995105Cadherin 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini996 – 1102107Cadherin 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1103 – 1208106Cadherin 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1210 – 1313104Cadherin 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1314 – 1418105Cadherin 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1420 – 1527108Cadherin 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini1529 – 1634106Cadherin 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini1635 – 1744110Cadherin 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini1745 – 1851107Cadherin 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini1852 – 1959108Cadherin 18PROSITE-ProRule annotationAdd
    BLAST
    Domaini1960 – 2069110Cadherin 19PROSITE-ProRule annotationAdd
    BLAST
    Domaini2070 – 2174105Cadherin 20PROSITE-ProRule annotationAdd
    BLAST
    Domaini2175 – 2293119Cadherin 21PROSITE-ProRule annotationAdd
    BLAST
    Domaini2297 – 2402106Cadherin 22PROSITE-ProRule annotationAdd
    BLAST
    Domaini2403 – 2509107Cadherin 23PROSITE-ProRule annotationAdd
    BLAST
    Domaini2510 – 2611102Cadherin 24PROSITE-ProRule annotationAdd
    BLAST
    Domaini2614 – 2722109Cadherin 25PROSITE-ProRule annotationAdd
    BLAST
    Domaini2729 – 2846118Cadherin 26PROSITE-ProRule annotationAdd
    BLAST
    Domaini2847 – 2975129Cadherin 27PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    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
    Cadherin repeats 1 and 2 mediate calcium-dependent heterophilic interaction with PCDH15.1 Publication

    Sequence similaritiesi

    Contains 27 cadherin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG12793.
    GeneTreeiENSGT00750000117340.
    HOGENOMiHOG000139588.
    HOVERGENiHBG050768.
    InParanoidiQ99PF4.
    KOiK06813.
    OMAiDVTEGQP.
    TreeFamiTF316403.

    Family and domain databases

    Gene3Di2.60.40.60. 27 hits.
    InterProiIPR002126. Cadherin.
    IPR015919. Cadherin-like.
    IPR020894. Cadherin_CS.
    [Graphical view]
    PfamiPF00028. Cadherin. 24 hits.
    [Graphical view]
    PRINTSiPR00205. CADHERIN.
    SMARTiSM00112. CA. 26 hits.
    [Graphical view]
    SUPFAMiSSF49313. SSF49313. 27 hits.
    PROSITEiPS00232. CADHERIN_1. 17 hits.
    PS50268. CADHERIN_2. 27 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99PF4-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MRYSLVTCYA VLWLLMLVPG SWGQVNRLPF FTNHFFDTYL LISEDTPVGS     50
    SVTQLLARDM DNDPLVFGVS GEEASRFFAV EPDTGVVWLR QPLDRETKSE 100
    FTVEFSVSDH QGVITRKVNI QVGDVNDNAP TFHNQPYSVR IPENTPVGTP 150
    IFIVNATDPD LGAGGSVLYS FQPPSPFFAI DSARGIVTVI QELDYEVTQA 200
    YQLTVNATDQ DKTRPLSTLA NLAIIITDMQ DMDPIFINLP YSTNIYEHSP 250
    PGTTVRVITA VDQDKGRPRG IGYTIVSGNT NSIFALDYIS GALTLNGLLD 300
    RENPLYSHGF ILTVKGTELN DDRTPSDATV TTTFNILVID INDNAPEFNS 350
    SEYSVAITEL AQVGFALPLF IQVVDKDEDL GLNSMFEVYL VGNNSHHFII 400
    SPTSVQGKAD IRIRVAIPLD YETVDRYDFD LFANESVPDH VGYAKVKITL 450
    INENDNRPIF SQPLYNVSLY ENITVGTSVL TVLATDNDVG TFGEVNYFFS 500
    DDPDRFSLDK DTGLIMLIAR LDYELIQRFT LTVIARDGGG EETTGRVRIN 550
    VLDVNDNVPT FQKDAYVGAL RENEPSVTQL VRLRATDEDS PPNNLITYSI 600
    VNASAFGSYF DISIYEGYGV ISVSRPLDYE QIPNGLIYLT VMAKDAGNPP 650
    LYSTVPVTIE VFDENDNPPT FSKPAYFVSV LENIMAGATV LFLNATDLDR 700
    SREYGQESII YSLEGSSQFR INARSGEITT TSLLDRETKS EYILIVRAVD 750
    GGVGHNQKTG IATVNVTLLD INDNHPTWKD APYYINLVEM TPPDSDVTTV 800
    VAVDPDLGEN GTLVYSIHPP NKFYSLNSTT GKIRTTHVML DRENPDPVEA 850
    ELMRKIIVSV TDCGRPPLKA TSSATVFVNL LDLNDNDPTF RNLPFVAEIL 900
    EGTPAGVSVY QVVAIDLDEG LNGLVSYRMQ VGMPRMDFVI NSTSGVVTTT 950
    AELDRERIAE YQLRVVASDA GTPTKSSTST LTVRVLDVND ETPTFFPAVY 1000
    NVSVSEDVPR EFRVVWLNCT DNDVGLNAEL SYFITAGNVD GKFSVGYRDA 1050
    VVRTVVGLDR ETTAAYTLVL EAIDNGPVGK RRTGTATVFV TVLDVNDNRP 1100
    IFLQSSYEAS VPEDIPEGHS IVQLKATDAD EGEFGRVWYR ILHGNHGNNF 1150
    RIHVGSGLLM RGPRPLDRER NSSHVLMVEA YNHDLGPMRS SVRVIVYVED 1200
    VNDEAPVFTQ QQYNRLGLRE TAGIGTSVIV VRATDKDTGD GGLVNYRILS 1250
    GAEGKFEIDE STGLIVTVDY LDYETKTSYL MNVSATDGAP PFNQGFCSVY 1300
    VTLLNELDEA VQFSNASYEA VIMENLALGT EIVRVQAYSI DNLNQITYRF 1350
    DAYTSAQAKA LFKIDAITGV ITVKGLVDRE KGDFYTLTVV ADDGGPKVDS 1400
    TVKVYITVLD ENDNSPRFDF TSDSAISVPE DCPVGQRVAT VKARDPDAGS 1450
    NGQVVFSLAS GNIAGAFEII TSNDSIGEVF VAKPLDREEL DHYILKVVAS 1500
    DRGTPPRKKD HILQVTILDV NDNPPVIESP FGYNVSVNEN VGGGTSVVQV 1550
    RATDRDIGIN SVLSYYITEG NEDMTFRMDR ISGEIATRPA PPDRERQNFY 1600
    HLVVTVEDEG TPTLSATTHV YVTIVDENDN APVFQQPHYE VVLDEGPDTI 1650
    NTSLITVQAL DLDEGPNGTV TYAIVAGNII NTFRINKHTG VITAAKELDY 1700
    EISHGRYTLI VTATDQCPIL SHRLTSTTTV LVNVNDINDN VPTFPRDYEG 1750
    PFDVTEGQPG PRVWTFLAHD RDSGPNGQVE YSVVDGDPLG EFVISPVEGV 1800
    LRVRKDVELD RETIAFYNLT ICARDRGVPP LSSTMLVGIR VLDINDNDPV 1850
    LLNLPMNVTI SENSPVSSFV AHVLASDADS GCNALLTFNI TAGNRERAFF 1900
    INATTGIVTV NRPLDRERIP EYRLTVSVKD NPENPRIARK DFDLLLVSLA 1950
    DENDNHPLFT EGTYQAEVME NSPAGTPLTV LNGPILALDA DEDVYAVVTY 2000
    QLLGTHSDLF VIDNSTGVVT VRSGIIIDRE AFSPPFLELL LLAEDIGQLN 2050
    GTAHLFITIL DDNDNWPTFS PPTYTVHLLE NCPPGFSVLQ VTATDEDSGL 2100
    NGELVYRIEA GAQDRFLIHP VTGVIRVGNA TIDREEQESY RLTVVATDRG 2150
    TVPLSGTAIV TILIDDINDS RPEFLNPIQT VSVLESAEPG TIIANVTAID 2200
    LDLNPKLEYH IISIVAKDDT DRLVPDQEDA FAVNINTGSV MVKSPLNREL 2250
    VATYEVTLSV IDNASDLPEH SVSVPNAKLT VNILDVNDNT PQFKPFGITY 2300
    YTERVLEGAT PGTTLIAVAA VDPDKGLNGL ITYTLLDLTP PGYVQLEDSS 2350
    AGKVIANRTV DYEEVHWLNF TVRASDNGSP PRAAEIPVYL EIVDINDNNP 2400
    IFDQPSYQEA VFEDIAVGTV ILRVTATDAD SGNFALIEYS LVDGEGKFAI 2450
    NPNTGDISVL SSLDREKKDH YILTALAKDN PGDVASNRRE NSVQVVIRVL 2500
    DVNDCRPQFS KPQFSTSVYE NEPAGTSVIT MLATDQDEGS NSQLTYSLEG 2550
    PGMEAFSVDM DSGLVTTQRP LQSYERFNLT VVATDGGEPP LWGTTMLLVE 2600
    VIDVNDNRPV FVRPPNGTIL HIKEEIPLRS NVYEVYATDN DEGLNGAVRY 2650
    SFLKTTGNRD WEYFTIDPIS GLIQTAQRLD REKQAVYSLI LVASDLGQPV 2700
    PYETMQPLQV ALEDIDDNEP LFVRPPKGSP QYQLLTVPEH SPRGTLVGNV 2750
    TGAVDADEGP NAIVYYFIAA GDEDKNFHLQ PDGRLLVLRD LDRETEATFS 2800
    FIVKASSNRS WTPPRGPSPA LDLLTDLTLQ EVRVVLEDIN DQPPRFTKAE 2850
    YTAGVATDAK VGSELIQVLA LDADIGNNSL VFYGILAIHY FRALANDSED 2900
    VGQVFTMGSV DGILRTFDLF MAYSPGYFVV DIVARDLAGH NDTAIIGIYI 2950
    LRDDQRVKIV INEIPDRVRG FEEEFIRLLS NITGAIVNTD DVQFHVDMKG 3000
    RVNFAQTELL IHVVNRDTNR ILDVDRVIQM IDENKEQLRN LFRNYNVLDV 3050
    QPAISVQLPD DMSALQMAII VLAILLFLAA MLFVLMNWYY RTIHKRKLKA 3100
    IVAGSAGNRG FIDIMDMPNT NKYSFDGSNP VWLDPFCRNL ELAAQAEHED 3150
    DLPENLSEIA DLWNSPTRTH GTFGREPAAV KPDDDRYLRA AIQEYDNIAK 3200
    LGQIIREGPI KGSLLKVVLE DYLRLKKLFA QRMVQKASSC HSSISELIHT 3250
    DLEEEPGDHS PGQGSLRFRH KPPMELKGQD GIHMVHGSTG TLLATDLNSL 3300
    PEDDQKGLDR SLETLTASEA TAFERNARTE SAKSTPLHKL RDVIMESPLE 3350
    ITEL 3354
    Length:3,354
    Mass (Da):369,623
    Last modified:July 27, 2011 - v2
    Checksum:i6ADFABF6A5001DC0
    GO
    Isoform 2 (identifier: Q99PF4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         3212-3246: Missing.

    Show »
    Length:3,319
    Mass (Da):365,675
    Checksum:i9ECA04DF22B1943F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941D → G in AAK07670. (PubMed:11386759)Curated
    Sequence conflicti142 – 1432PE → TQ in AAK07670. (PubMed:11386759)Curated
    Sequence conflicti248 – 2514HSPP → QLTVNAT in AAK07670. (PubMed:11386759)Curated
    Sequence conflicti379 – 3791D → N in AAG52817. (PubMed:11138008)Curated
    Sequence conflicti379 – 3791D → N in AAK07670. (PubMed:11386759)Curated
    Sequence conflicti3128 – 31281S → A in AAG52817. (PubMed:11138008)Curated
    Sequence conflicti3128 – 31281S → A in AAK07670. (PubMed:11386759)Curated
    Sequence conflicti3262 – 32621G → S in AAG52817. (PubMed:11138008)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51L → P in strain: CAST/Ei. 1 Publication
    Natural varianti229 – 2291M → V in strain: CAST/Ei. 1 Publication
    Natural varianti891 – 8911R → K in strain: CAST/Ei. 1 Publication
    Natural varianti1137 – 11371V → I in strain: CAST/Ei. 1 Publication
    Natural varianti1236 – 12361K → R in strain: CAST/Ei. 1 Publication
    Natural varianti2025 – 20251I → V in strain: CAST/Ei. 1 Publication
    Natural varianti2026 – 20261I → V in strain: CAST/Ei. 1 Publication
    Natural varianti2217 – 22171K → T in strain: CAST/Ei. 1 Publication
    Natural varianti2222 – 22221R → H in strain: CAST/Ei. 1 Publication
    Natural varianti2270 – 22701H → R in strain: CAST/Ei. 1 Publication
    Natural varianti2617 – 26171G → A in strain: CAST/Ei. 1 Publication
    Natural varianti2718 – 27203Missing in waltzer. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei3212 – 324635Missing in isoform 2. 1 PublicationVSP_000648Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF308939 mRNA. Translation: AAG52817.1.
    AY026062 mRNA. Translation: AAK07670.1.
    AK016365 mRNA. No translation available.
    AC079082 Genomic DNA. No translation available.
    AC079818 Genomic DNA. No translation available.
    AC079819 Genomic DNA. No translation available.
    AC153517 Genomic DNA. No translation available.
    RefSeqiNP_075859.2. NM_023370.3.
    UniGeneiMm.440327.

    Genome annotation databases

    EnsembliENSMUST00000105461; ENSMUSP00000101101; ENSMUSG00000012819. [Q99PF4-1]
    ENSMUST00000105463; ENSMUSP00000101103; ENSMUSG00000012819. [Q99PF4-2]
    GeneIDi22295.
    KEGGimmu:22295.
    UCSCiuc007fev.2. mouse. [Q99PF4-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF308939 mRNA. Translation: AAG52817.1 .
    AY026062 mRNA. Translation: AAK07670.1 .
    AK016365 mRNA. No translation available.
    AC079082 Genomic DNA. No translation available.
    AC079818 Genomic DNA. No translation available.
    AC079819 Genomic DNA. No translation available.
    AC153517 Genomic DNA. No translation available.
    RefSeqi NP_075859.2. NM_023370.3.
    UniGenei Mm.440327.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WBX X-ray 1.50 A 24-124 [» ]
    2WCP X-ray 1.98 A 24-228 [» ]
    2WD0 X-ray 2.74 A/C 24-228 [» ]
    2WHV X-ray 2.36 A 24-228 [» ]
    3MVS X-ray 1.10 A 24-233 [» ]
    4APX X-ray 1.65 A 24-228 [» ]
    4AQ8 X-ray 2.63 A/B 24-228 [» ]
    4AQA X-ray 1.96 A 24-228 [» ]
    4AQE X-ray 2.27 A 24-228 [» ]
    4AXW X-ray 2.23 A 24-228 [» ]
    ProteinModelPortali Q99PF4.
    SMRi Q99PF4. Positions 24-233.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204475. 1 interaction.
    DIPi DIP-42152N.
    IntActi Q99PF4. 1 interaction.
    MINTi MINT-1895823.

    PTM databases

    PhosphoSitei Q99PF4.

    Proteomic databases

    PaxDbi Q99PF4.
    PRIDEi Q99PF4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000105461 ; ENSMUSP00000101101 ; ENSMUSG00000012819 . [Q99PF4-1 ]
    ENSMUST00000105463 ; ENSMUSP00000101103 ; ENSMUSG00000012819 . [Q99PF4-2 ]
    GeneIDi 22295.
    KEGGi mmu:22295.
    UCSCi uc007fev.2. mouse. [Q99PF4-1 ]

    Organism-specific databases

    CTDi 64072.
    MGIi MGI:1890219. Cdh23.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00750000117340.
    HOGENOMi HOG000139588.
    HOVERGENi HBG050768.
    InParanoidi Q99PF4.
    KOi K06813.
    OMAi DVTEGQP.
    TreeFami TF316403.

    Miscellaneous databases

    EvolutionaryTracei Q99PF4.
    NextBioi 302447.
    PROi Q99PF4.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99PF4.
    Genevestigatori Q99PF4.

    Family and domain databases

    Gene3Di 2.60.40.60. 27 hits.
    InterProi IPR002126. Cadherin.
    IPR015919. Cadherin-like.
    IPR020894. Cadherin_CS.
    [Graphical view ]
    Pfami PF00028. Cadherin. 24 hits.
    [Graphical view ]
    PRINTSi PR00205. CADHERIN.
    SMARTi SM00112. CA. 26 hits.
    [Graphical view ]
    SUPFAMi SSF49313. SSF49313. 27 hits.
    PROSITEi PS00232. CADHERIN_1. 17 hits.
    PS50268. CADHERIN_2. 27 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mutations in Cdh23, encoding a new type of cadherin, cause stereocilia disorganization in waltzer, the mouse model for Usher syndrome type 1D."
      Di Palma F., Holme R.H., Bryda E.C., Belyantseva I.A., Pellegrino R., Kachar B., Steel K.P., Noben-Trauth K.
      Nat. Genet. 27:103-107(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION.
      Strain: C57BL/6J.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Testis.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "Genomic structure, alternative splice forms and normal and mutant alleles of cadherin 23 (Cdh23)."
      Di Palma F., Pellegrino R., Noben-Trauth K.
      Gene 281:31-41(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOMIC ORGANIZATION, ALTERNATIVE SPLICING, VARIANT WALTZER 2718-ASN--PRO-2720 DEL, VARIANTS PRO-5; VAL-229; LYS-891; ILE-1137; ARG-1236; VAL-2025; VAL-2026; THR-2217; HIS-2222; ARG-2270 AND ALA-2617.
      Strain: C57BL/6J and CAST/Ei.
    6. "Cadherin 23 and protocadherin 15 interact to form tip-link filaments in sensory hair cells."
      Kazmierczak P., Sakaguchi H., Tokita J., Wilson-Kubalek E.M., Milligan R.A., Muller U., Kachar B.
      Nature 449:87-91(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PCDH15.
    7. "Structural determinants of cadherin-23 function in hearing and deafness."
      Sotomayor M., Weihofen W.A., Gaudet R., Corey D.P.
      Neuron 66:85-100(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 24-228 IN COMPLEX WITH CALCIUM.
    8. "Structure of the N terminus of cadherin 23 reveals a new adhesion mechanism for a subset of cadherin superfamily members."
      Elledge H.M., Kazmierczak P., Clark P., Joseph J.S., Kolatkar A., Kuhn P., Muller U.
      Proc. Natl. Acad. Sci. U.S.A. 107:10708-10712(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 24-233 IN COMPLEX WITH CALCIUM, MUTAGENESIS OF ASN-26 AND ARG-27, INTERACTION WITH PCDH15.
    9. "Structure of a force-conveying cadherin bond essential for inner-ear mechanotransduction."
      Sotomayor M., Weihofen W.A., Gaudet R., Corey D.P.
      Nature 492:128-132(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 24-228 IN COMPLEX WITH CALCIUM IONS AND PCDH15, SUBUNIT, MUTAGENESIS OF LEU-168.

    Entry informationi

    Entry nameiCAD23_MOUSE
    AccessioniPrimary (citable) accession number: Q99PF4
    Secondary accession number(s): E9QP63, Q99NH1, Q9D4N9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 111 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3