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Q99PF4 (CAD23_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cadherin-23
Alternative name(s):
Otocadherin
Gene names
Name:Cdh23
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length3354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.1

Subunit structure

Interacts with USH1C and USH1G By similarity. antiparallel heterodimer with PCDH15. Ref.6 Ref.8 Ref.9

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Tissue specificity

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. Ref.1

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.

Cadherin repeats 1 and 2 mediate calcium-dependent heterophilic interaction with PCDH15 (Ref.9).

Involvement in disease

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.

Sequence similarities

Contains 27 cadherin domains.

Ontologies

Keywords
   Biological processCell adhesion
Hearing
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDeafness
Disease mutation
Non-syndromic deafness
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processauditory receptor cell differentiation

Inferred from mutant phenotype PubMed 12121736. Source: MGI

auditory receptor cell stereocilium organization

Inferred from mutant phenotype Ref.1PubMed 11322776PubMed 12121736PubMed 17050716PubMed 23217710PubMed 7610888PubMed 8790740PubMed 9039475. Source: MGI

calcium-dependent cell-cell adhesion

Inferred from sequence or structural similarity PubMed 11138009. Source: MGI

cell adhesion

Traceable author statement PubMed 11138009. Source: MGI

homophilic cell adhesion

Inferred from electronic annotation. Source: InterPro

inner ear development

Inferred from mutant phenotype PubMed 13336002PubMed 14759567PubMed 8790740. Source: MGI

inner ear morphogenesis

Inferred from mutant phenotype PubMed 15925194PubMed 7610888. Source: MGI

locomotory behavior

Inferred from mutant phenotype PubMed 10452381Ref.2PubMed 16962269. Source: MGI

post-embryonic organ morphogenesis

Inferred from mutant phenotype PubMed 13336002. Source: MGI

sensory perception of light stimulus

Inferred from mutant phenotype PubMed 14609561. Source: MGI

sensory perception of sound

Inferred from mutant phenotype PubMed 10452381Ref.1PubMed 11322776PubMed 12121736PubMed 13336002PubMed 14759567PubMed 15820310PubMed 15925194PubMed 17329413PubMed 9447922. Source: MGI

   Cellular_componentcentrosome

Inferred from direct assay PubMed 15882574. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

kinocilium

Inferred from direct assay PubMed 15882574. Source: MGI

photoreceptor inner segment

Inferred from direct assay PubMed 14578428. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

stereocilium

Inferred from direct assay PubMed 12485990. Source: HGNC

stereocilium bundle tip

Inferred from direct assay PubMed 12485990PubMed 17050716. Source: MGI

synapse

Inferred from direct assay PubMed 14578428. Source: MGI

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 15590703PubMed 15928608. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ush1cQ9ES64-32EBI-7419021,EBI-7418919

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99PF4-1)

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.
Isoform 2 (identifier: Q99PF4-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 33543331Cadherin-23
PRO_0000003825

Regions

Topological domain24 – 30643041Extracellular Potential
Transmembrane3065 – 308521Helical; Potential
Topological domain3086 – 3354269Cytoplasmic Potential
Domain34 – 13299Cadherin 1
Domain133 – 236104Cadherin 2
Domain237 – 348112Cadherin 3
Domain349 – 460112Cadherin 4
Domain461 – 561101Cadherin 5
Domain562 – 671110Cadherin 6
Domain672 – 784113Cadherin 7
Domain779 – 890112Cadherin 8
Domain891 – 995105Cadherin 9
Domain996 – 1102107Cadherin 10
Domain1103 – 1208106Cadherin 11
Domain1210 – 1313104Cadherin 12
Domain1314 – 1418105Cadherin 13
Domain1420 – 1527108Cadherin 14
Domain1529 – 1634106Cadherin 15
Domain1635 – 1744110Cadherin 16
Domain1745 – 1851107Cadherin 17
Domain1852 – 1959108Cadherin 18
Domain1960 – 2069110Cadherin 19
Domain2070 – 2174105Cadherin 20
Domain2175 – 2293119Cadherin 21
Domain2297 – 2402106Cadherin 22
Domain2403 – 2509107Cadherin 23
Domain2510 – 2611102Cadherin 24
Domain2614 – 2722109Cadherin 25
Domain2729 – 2846118Cadherin 26
Domain2847 – 2975129Cadherin 27

Amino acid modifications

Glycosylation1551N-linked (GlcNAc...) Potential
Glycosylation2061N-linked (GlcNAc...) Potential
Glycosylation3491N-linked (GlcNAc...) Potential
Glycosylation3931N-linked (GlcNAc...) Potential
Glycosylation4341N-linked (GlcNAc...) Potential
Glycosylation4661N-linked (GlcNAc...) Potential
Glycosylation4721N-linked (GlcNAc...) Potential
Glycosylation6021N-linked (GlcNAc...) Potential
Glycosylation6941N-linked (GlcNAc...) Potential
Glycosylation7651N-linked (GlcNAc...) Potential
Glycosylation8101N-linked (GlcNAc...) Potential
Glycosylation8271N-linked (GlcNAc...) Potential
Glycosylation9411N-linked (GlcNAc...) Potential
Glycosylation10011N-linked (GlcNAc...) Potential
Glycosylation10181N-linked (GlcNAc...) Potential
Glycosylation11711N-linked (GlcNAc...) Potential
Glycosylation12821N-linked (GlcNAc...) Potential
Glycosylation13151N-linked (GlcNAc...) Potential
Glycosylation14731N-linked (GlcNAc...) Potential
Glycosylation15341N-linked (GlcNAc...) Potential
Glycosylation16511N-linked (GlcNAc...) Potential
Glycosylation16671N-linked (GlcNAc...) Potential
Glycosylation18181N-linked (GlcNAc...) Potential
Glycosylation18571N-linked (GlcNAc...) Potential
Glycosylation18891N-linked (GlcNAc...) Potential
Glycosylation19021N-linked (GlcNAc...) Potential
Glycosylation20141N-linked (GlcNAc...) Potential
Glycosylation20501N-linked (GlcNAc...) Potential
Glycosylation21291N-linked (GlcNAc...) Potential
Glycosylation21681N-linked (GlcNAc...) Potential
Glycosylation21951N-linked (GlcNAc...) Potential
Glycosylation22631N-linked (GlcNAc...) Potential
Glycosylation23571N-linked (GlcNAc...) Potential
Glycosylation23691N-linked (GlcNAc...) Potential
Glycosylation25781N-linked (GlcNAc...) Potential
Glycosylation26161N-linked (GlcNAc...) Potential
Glycosylation27491N-linked (GlcNAc...) Potential
Glycosylation28081N-linked (GlcNAc...) Potential
Glycosylation28771N-linked (GlcNAc...) Potential
Glycosylation28961N-linked (GlcNAc...) Potential
Glycosylation29411N-linked (GlcNAc...) Potential
Glycosylation29811N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence3212 – 324635Missing in isoform 2.
VSP_000648
Natural variant51L → P in strain: CAST/Ei. Ref.5
Natural variant2291M → V in strain: CAST/Ei. Ref.5
Natural variant8911R → K in strain: CAST/Ei. Ref.5
Natural variant11371V → I in strain: CAST/Ei. Ref.5
Natural variant12361K → R in strain: CAST/Ei. Ref.5
Natural variant20251I → V in strain: CAST/Ei. Ref.5
Natural variant20261I → V in strain: CAST/Ei. Ref.5
Natural variant22171K → T in strain: CAST/Ei. Ref.5
Natural variant22221R → H in strain: CAST/Ei. Ref.5
Natural variant22701H → R in strain: CAST/Ei. Ref.5
Natural variant26171G → A in strain: CAST/Ei. Ref.5
Natural variant2718 – 27203Missing in waltzer.

Experimental info

Mutagenesis261N → I: Strongly reduced affinity for PCDH15. Ref.8
Mutagenesis271R → I: Strongly reduced affinity for PCDH15. Ref.8
Mutagenesis1681L → G: Strongly reduced interaction with PCDH15. Ref.9
Sequence conflict941D → G in AAK07670. Ref.2
Sequence conflict142 – 1432PE → TQ in AAK07670. Ref.2
Sequence conflict248 – 2514HSPP → QLTVNAT in AAK07670. Ref.2
Sequence conflict3791D → N in AAG52817. Ref.1
Sequence conflict3791D → N in AAK07670. Ref.2
Sequence conflict31281S → A in AAG52817. Ref.1
Sequence conflict31281S → A in AAK07670. Ref.2
Sequence conflict32621G → S in AAG52817. Ref.1

Secondary structure

............................................. 3354
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 6ADFABF6A5001DC0

FASTA3,354369,623
        10         20         30         40         50         60 
MRYSLVTCYA VLWLLMLVPG SWGQVNRLPF FTNHFFDTYL LISEDTPVGS SVTQLLARDM 

        70         80         90        100        110        120 
DNDPLVFGVS GEEASRFFAV EPDTGVVWLR QPLDRETKSE FTVEFSVSDH QGVITRKVNI 

       130        140        150        160        170        180 
QVGDVNDNAP TFHNQPYSVR IPENTPVGTP IFIVNATDPD LGAGGSVLYS FQPPSPFFAI 

       190        200        210        220        230        240 
DSARGIVTVI QELDYEVTQA YQLTVNATDQ DKTRPLSTLA NLAIIITDMQ DMDPIFINLP 

       250        260        270        280        290        300 
YSTNIYEHSP PGTTVRVITA VDQDKGRPRG IGYTIVSGNT NSIFALDYIS GALTLNGLLD 

       310        320        330        340        350        360 
RENPLYSHGF ILTVKGTELN DDRTPSDATV TTTFNILVID INDNAPEFNS SEYSVAITEL 

       370        380        390        400        410        420 
AQVGFALPLF IQVVDKDEDL GLNSMFEVYL VGNNSHHFII SPTSVQGKAD IRIRVAIPLD 

       430        440        450        460        470        480 
YETVDRYDFD LFANESVPDH VGYAKVKITL INENDNRPIF SQPLYNVSLY ENITVGTSVL 

       490        500        510        520        530        540 
TVLATDNDVG TFGEVNYFFS DDPDRFSLDK DTGLIMLIAR LDYELIQRFT LTVIARDGGG 

       550        560        570        580        590        600 
EETTGRVRIN VLDVNDNVPT FQKDAYVGAL RENEPSVTQL VRLRATDEDS PPNNLITYSI 

       610        620        630        640        650        660 
VNASAFGSYF DISIYEGYGV ISVSRPLDYE QIPNGLIYLT VMAKDAGNPP LYSTVPVTIE 

       670        680        690        700        710        720 
VFDENDNPPT FSKPAYFVSV LENIMAGATV LFLNATDLDR SREYGQESII YSLEGSSQFR 

       730        740        750        760        770        780 
INARSGEITT TSLLDRETKS EYILIVRAVD GGVGHNQKTG IATVNVTLLD INDNHPTWKD 

       790        800        810        820        830        840 
APYYINLVEM TPPDSDVTTV VAVDPDLGEN GTLVYSIHPP NKFYSLNSTT GKIRTTHVML 

       850        860        870        880        890        900 
DRENPDPVEA ELMRKIIVSV TDCGRPPLKA TSSATVFVNL LDLNDNDPTF RNLPFVAEIL 

       910        920        930        940        950        960 
EGTPAGVSVY QVVAIDLDEG LNGLVSYRMQ VGMPRMDFVI NSTSGVVTTT AELDRERIAE 

       970        980        990       1000       1010       1020 
YQLRVVASDA GTPTKSSTST LTVRVLDVND ETPTFFPAVY NVSVSEDVPR EFRVVWLNCT 

      1030       1040       1050       1060       1070       1080 
DNDVGLNAEL SYFITAGNVD GKFSVGYRDA VVRTVVGLDR ETTAAYTLVL EAIDNGPVGK 

      1090       1100       1110       1120       1130       1140 
RRTGTATVFV TVLDVNDNRP IFLQSSYEAS VPEDIPEGHS IVQLKATDAD EGEFGRVWYR 

      1150       1160       1170       1180       1190       1200 
ILHGNHGNNF RIHVGSGLLM RGPRPLDRER NSSHVLMVEA YNHDLGPMRS SVRVIVYVED 

      1210       1220       1230       1240       1250       1260 
VNDEAPVFTQ QQYNRLGLRE TAGIGTSVIV VRATDKDTGD GGLVNYRILS GAEGKFEIDE 

      1270       1280       1290       1300       1310       1320 
STGLIVTVDY LDYETKTSYL MNVSATDGAP PFNQGFCSVY VTLLNELDEA VQFSNASYEA 

      1330       1340       1350       1360       1370       1380 
VIMENLALGT EIVRVQAYSI DNLNQITYRF DAYTSAQAKA LFKIDAITGV ITVKGLVDRE 

      1390       1400       1410       1420       1430       1440 
KGDFYTLTVV ADDGGPKVDS TVKVYITVLD ENDNSPRFDF TSDSAISVPE DCPVGQRVAT 

      1450       1460       1470       1480       1490       1500 
VKARDPDAGS NGQVVFSLAS GNIAGAFEII TSNDSIGEVF VAKPLDREEL DHYILKVVAS 

      1510       1520       1530       1540       1550       1560 
DRGTPPRKKD HILQVTILDV NDNPPVIESP FGYNVSVNEN VGGGTSVVQV RATDRDIGIN 

      1570       1580       1590       1600       1610       1620 
SVLSYYITEG NEDMTFRMDR ISGEIATRPA PPDRERQNFY HLVVTVEDEG TPTLSATTHV 

      1630       1640       1650       1660       1670       1680 
YVTIVDENDN APVFQQPHYE VVLDEGPDTI NTSLITVQAL DLDEGPNGTV TYAIVAGNII 

      1690       1700       1710       1720       1730       1740 
NTFRINKHTG VITAAKELDY EISHGRYTLI VTATDQCPIL SHRLTSTTTV LVNVNDINDN 

      1750       1760       1770       1780       1790       1800 
VPTFPRDYEG PFDVTEGQPG PRVWTFLAHD RDSGPNGQVE YSVVDGDPLG EFVISPVEGV 

      1810       1820       1830       1840       1850       1860 
LRVRKDVELD RETIAFYNLT ICARDRGVPP LSSTMLVGIR VLDINDNDPV LLNLPMNVTI 

      1870       1880       1890       1900       1910       1920 
SENSPVSSFV AHVLASDADS GCNALLTFNI TAGNRERAFF INATTGIVTV NRPLDRERIP 

      1930       1940       1950       1960       1970       1980 
EYRLTVSVKD NPENPRIARK DFDLLLVSLA DENDNHPLFT EGTYQAEVME NSPAGTPLTV 

      1990       2000       2010       2020       2030       2040 
LNGPILALDA DEDVYAVVTY QLLGTHSDLF VIDNSTGVVT VRSGIIIDRE AFSPPFLELL 

      2050       2060       2070       2080       2090       2100 
LLAEDIGQLN GTAHLFITIL DDNDNWPTFS PPTYTVHLLE NCPPGFSVLQ VTATDEDSGL 

      2110       2120       2130       2140       2150       2160 
NGELVYRIEA GAQDRFLIHP VTGVIRVGNA TIDREEQESY RLTVVATDRG TVPLSGTAIV 

      2170       2180       2190       2200       2210       2220 
TILIDDINDS RPEFLNPIQT VSVLESAEPG TIIANVTAID LDLNPKLEYH IISIVAKDDT 

      2230       2240       2250       2260       2270       2280 
DRLVPDQEDA FAVNINTGSV MVKSPLNREL VATYEVTLSV IDNASDLPEH SVSVPNAKLT 

      2290       2300       2310       2320       2330       2340 
VNILDVNDNT PQFKPFGITY YTERVLEGAT PGTTLIAVAA VDPDKGLNGL ITYTLLDLTP 

      2350       2360       2370       2380       2390       2400 
PGYVQLEDSS AGKVIANRTV DYEEVHWLNF TVRASDNGSP PRAAEIPVYL EIVDINDNNP 

      2410       2420       2430       2440       2450       2460 
IFDQPSYQEA VFEDIAVGTV ILRVTATDAD SGNFALIEYS LVDGEGKFAI NPNTGDISVL 

      2470       2480       2490       2500       2510       2520 
SSLDREKKDH YILTALAKDN PGDVASNRRE NSVQVVIRVL DVNDCRPQFS KPQFSTSVYE 

      2530       2540       2550       2560       2570       2580 
NEPAGTSVIT MLATDQDEGS NSQLTYSLEG PGMEAFSVDM DSGLVTTQRP LQSYERFNLT 

      2590       2600       2610       2620       2630       2640 
VVATDGGEPP LWGTTMLLVE VIDVNDNRPV FVRPPNGTIL HIKEEIPLRS NVYEVYATDN 

      2650       2660       2670       2680       2690       2700 
DEGLNGAVRY SFLKTTGNRD WEYFTIDPIS GLIQTAQRLD REKQAVYSLI LVASDLGQPV 

      2710       2720       2730       2740       2750       2760 
PYETMQPLQV ALEDIDDNEP LFVRPPKGSP QYQLLTVPEH SPRGTLVGNV TGAVDADEGP 

      2770       2780       2790       2800       2810       2820 
NAIVYYFIAA GDEDKNFHLQ PDGRLLVLRD LDRETEATFS FIVKASSNRS WTPPRGPSPA 

      2830       2840       2850       2860       2870       2880 
LDLLTDLTLQ EVRVVLEDIN DQPPRFTKAE YTAGVATDAK VGSELIQVLA LDADIGNNSL 

      2890       2900       2910       2920       2930       2940 
VFYGILAIHY FRALANDSED VGQVFTMGSV DGILRTFDLF MAYSPGYFVV DIVARDLAGH 

      2950       2960       2970       2980       2990       3000 
NDTAIIGIYI LRDDQRVKIV INEIPDRVRG FEEEFIRLLS NITGAIVNTD DVQFHVDMKG 

      3010       3020       3030       3040       3050       3060 
RVNFAQTELL IHVVNRDTNR ILDVDRVIQM IDENKEQLRN LFRNYNVLDV QPAISVQLPD 

      3070       3080       3090       3100       3110       3120 
DMSALQMAII VLAILLFLAA MLFVLMNWYY RTIHKRKLKA IVAGSAGNRG FIDIMDMPNT 

      3130       3140       3150       3160       3170       3180 
NKYSFDGSNP VWLDPFCRNL ELAAQAEHED DLPENLSEIA DLWNSPTRTH GTFGREPAAV 

      3190       3200       3210       3220       3230       3240 
KPDDDRYLRA AIQEYDNIAK LGQIIREGPI KGSLLKVVLE DYLRLKKLFA QRMVQKASSC 

      3250       3260       3270       3280       3290       3300 
HSSISELIHT DLEEEPGDHS PGQGSLRFRH KPPMELKGQD GIHMVHGSTG TLLATDLNSL 

      3310       3320       3330       3340       3350 
PEDDQKGLDR SLETLTASEA TAFERNARTE SAKSTPLHKL RDVIMESPLE ITEL 

« Hide

Isoform 2 [UniParc].

Checksum: 9ECA04DF22B1943F
Show »

FASTA3,319365,675

References

« Hide 'large scale' references
[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]"Mutations in Cdh23 cause nonsyndromic hearing loss in waltzer mice."
Wilson S.M., Householder D.B., Coppola V., Tessarollo L., Fritzsch B., Lee E.-C., Goss D., Carlson G.A., Copeland N.G., Jenkins N.A.
Genomics 74:228-233(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_075859.2. NM_023370.3.
UniGeneMm.440327.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ99PF4.
SMRQ99PF4. Positions 24-233.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204475. 1 interaction.
DIPDIP-42152N.
IntActQ99PF4. 1 interaction.
MINTMINT-1895823.

PTM databases

PhosphoSiteQ99PF4.

Proteomic databases

PaxDbQ99PF4.
PRIDEQ99PF4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000105461; ENSMUSP00000101101; ENSMUSG00000012819. [Q99PF4-1]
ENSMUST00000105463; ENSMUSP00000101103; ENSMUSG00000012819. [Q99PF4-2]
GeneID22295.
KEGGmmu:22295.
UCSCuc007fev.2. mouse. [Q99PF4-1]

Organism-specific databases

CTD64072.
MGIMGI:1890219. Cdh23.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00750000117340.
HOGENOMHOG000139588.
HOVERGENHBG050768.
InParanoidQ99PF4.
KOK06813.
OMADVTEGQP.
TreeFamTF316403.

Gene expression databases

BgeeQ99PF4.
GenevestigatorQ99PF4.

Family and domain databases

Gene3D2.60.40.60. 27 hits.
InterProIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
[Graphical view]
PfamPF00028. Cadherin. 24 hits.
[Graphical view]
PRINTSPR00205. CADHERIN.
SMARTSM00112. CA. 26 hits.
[Graphical view]
SUPFAMSSF49313. SSF49313. 27 hits.
PROSITEPS00232. CADHERIN_1. 17 hits.
PS50268. CADHERIN_2. 27 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ99PF4.
NextBio302447.
PROQ99PF4.
SOURCESearch...

Entry information

Entry nameCAD23_MOUSE
AccessionPrimary (citable) accession number: Q99PF4
Secondary accession number(s): E9QP63, Q99NH1, Q9D4N9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: July 27, 2011
Last modified: June 11, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot