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Q99PF4

- CAD23_MOUSE

UniProt

Q99PF4 - CAD23_MOUSE

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Protein

Cadherin-23

Gene
Cdh23
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 30643041Extracellular Reviewed predictionAdd
BLAST
Transmembranei3065 – 308521Helical; Reviewed predictionAdd
BLAST
Topological domaini3086 – 3354269Cytoplasmic Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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 – 2323 Reviewed predictionAdd
BLAST
Chaini24 – 33543331Cadherin-23PRO_0000003825Add
BLAST

Amino acid modifications

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

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 PCDH15.3 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.

Miscellaneous databases

EvolutionaryTraceiQ99PF4.

Family & Domainsi

Domains and Repeats

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

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

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei3212 – 324635Missing in isoform 2. VSP_000648Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941D → G in AAK07670. 1 Publication
Sequence conflicti142 – 1432PE → TQ in AAK07670. 1 Publication
Sequence conflicti248 – 2514HSPP → QLTVNAT in AAK07670. 1 Publication
Sequence conflicti379 – 3791D → N in AAG52817. 1 Publication
Sequence conflicti379 – 3791D → N in AAK07670. 1 Publication
Sequence conflicti3128 – 31281S → A in AAG52817. 1 Publication
Sequence conflicti3128 – 31281S → A in AAK07670. 1 Publication
Sequence conflicti3262 – 32621G → S in AAG52817. 1 Publication

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 110 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

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