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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

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

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-KW
  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 – 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.
ExpressionAtlasiQ99PF4. baseline and differential.
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.
GeneTreeiENSGT00760000118805.
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

        10         20         30         40         50
MRYSLVTCYA VLWLLMLVPG SWGQVNRLPF FTNHFFDTYL LISEDTPVGS
60 70 80 90 100
SVTQLLARDM DNDPLVFGVS GEEASRFFAV EPDTGVVWLR QPLDRETKSE
110 120 130 140 150
FTVEFSVSDH QGVITRKVNI QVGDVNDNAP TFHNQPYSVR IPENTPVGTP
160 170 180 190 200
IFIVNATDPD LGAGGSVLYS FQPPSPFFAI DSARGIVTVI QELDYEVTQA
210 220 230 240 250
YQLTVNATDQ DKTRPLSTLA NLAIIITDMQ DMDPIFINLP YSTNIYEHSP
260 270 280 290 300
PGTTVRVITA VDQDKGRPRG IGYTIVSGNT NSIFALDYIS GALTLNGLLD
310 320 330 340 350
RENPLYSHGF ILTVKGTELN DDRTPSDATV TTTFNILVID INDNAPEFNS
360 370 380 390 400
SEYSVAITEL AQVGFALPLF IQVVDKDEDL GLNSMFEVYL VGNNSHHFII
410 420 430 440 450
SPTSVQGKAD IRIRVAIPLD YETVDRYDFD LFANESVPDH VGYAKVKITL
460 470 480 490 500
INENDNRPIF SQPLYNVSLY ENITVGTSVL TVLATDNDVG TFGEVNYFFS
510 520 530 540 550
DDPDRFSLDK DTGLIMLIAR LDYELIQRFT LTVIARDGGG EETTGRVRIN
560 570 580 590 600
VLDVNDNVPT FQKDAYVGAL RENEPSVTQL VRLRATDEDS PPNNLITYSI
610 620 630 640 650
VNASAFGSYF DISIYEGYGV ISVSRPLDYE QIPNGLIYLT VMAKDAGNPP
660 670 680 690 700
LYSTVPVTIE VFDENDNPPT FSKPAYFVSV LENIMAGATV LFLNATDLDR
710 720 730 740 750
SREYGQESII YSLEGSSQFR INARSGEITT TSLLDRETKS EYILIVRAVD
760 770 780 790 800
GGVGHNQKTG IATVNVTLLD INDNHPTWKD APYYINLVEM TPPDSDVTTV
810 820 830 840 850
VAVDPDLGEN GTLVYSIHPP NKFYSLNSTT GKIRTTHVML DRENPDPVEA
860 870 880 890 900
ELMRKIIVSV TDCGRPPLKA TSSATVFVNL LDLNDNDPTF RNLPFVAEIL
910 920 930 940 950
EGTPAGVSVY QVVAIDLDEG LNGLVSYRMQ VGMPRMDFVI NSTSGVVTTT
960 970 980 990 1000
AELDRERIAE YQLRVVASDA GTPTKSSTST LTVRVLDVND ETPTFFPAVY
1010 1020 1030 1040 1050
NVSVSEDVPR EFRVVWLNCT DNDVGLNAEL SYFITAGNVD GKFSVGYRDA
1060 1070 1080 1090 1100
VVRTVVGLDR ETTAAYTLVL EAIDNGPVGK RRTGTATVFV TVLDVNDNRP
1110 1120 1130 1140 1150
IFLQSSYEAS VPEDIPEGHS IVQLKATDAD EGEFGRVWYR ILHGNHGNNF
1160 1170 1180 1190 1200
RIHVGSGLLM RGPRPLDRER NSSHVLMVEA YNHDLGPMRS SVRVIVYVED
1210 1220 1230 1240 1250
VNDEAPVFTQ QQYNRLGLRE TAGIGTSVIV VRATDKDTGD GGLVNYRILS
1260 1270 1280 1290 1300
GAEGKFEIDE STGLIVTVDY LDYETKTSYL MNVSATDGAP PFNQGFCSVY
1310 1320 1330 1340 1350
VTLLNELDEA VQFSNASYEA VIMENLALGT EIVRVQAYSI DNLNQITYRF
1360 1370 1380 1390 1400
DAYTSAQAKA LFKIDAITGV ITVKGLVDRE KGDFYTLTVV ADDGGPKVDS
1410 1420 1430 1440 1450
TVKVYITVLD ENDNSPRFDF TSDSAISVPE DCPVGQRVAT VKARDPDAGS
1460 1470 1480 1490 1500
NGQVVFSLAS GNIAGAFEII TSNDSIGEVF VAKPLDREEL DHYILKVVAS
1510 1520 1530 1540 1550
DRGTPPRKKD HILQVTILDV NDNPPVIESP FGYNVSVNEN VGGGTSVVQV
1560 1570 1580 1590 1600
RATDRDIGIN SVLSYYITEG NEDMTFRMDR ISGEIATRPA PPDRERQNFY
1610 1620 1630 1640 1650
HLVVTVEDEG TPTLSATTHV YVTIVDENDN APVFQQPHYE VVLDEGPDTI
1660 1670 1680 1690 1700
NTSLITVQAL DLDEGPNGTV TYAIVAGNII NTFRINKHTG VITAAKELDY
1710 1720 1730 1740 1750
EISHGRYTLI VTATDQCPIL SHRLTSTTTV LVNVNDINDN VPTFPRDYEG
1760 1770 1780 1790 1800
PFDVTEGQPG PRVWTFLAHD RDSGPNGQVE YSVVDGDPLG EFVISPVEGV
1810 1820 1830 1840 1850
LRVRKDVELD RETIAFYNLT ICARDRGVPP LSSTMLVGIR VLDINDNDPV
1860 1870 1880 1890 1900
LLNLPMNVTI SENSPVSSFV AHVLASDADS GCNALLTFNI TAGNRERAFF
1910 1920 1930 1940 1950
INATTGIVTV NRPLDRERIP EYRLTVSVKD NPENPRIARK DFDLLLVSLA
1960 1970 1980 1990 2000
DENDNHPLFT EGTYQAEVME NSPAGTPLTV LNGPILALDA DEDVYAVVTY
2010 2020 2030 2040 2050
QLLGTHSDLF VIDNSTGVVT VRSGIIIDRE AFSPPFLELL LLAEDIGQLN
2060 2070 2080 2090 2100
GTAHLFITIL DDNDNWPTFS PPTYTVHLLE NCPPGFSVLQ VTATDEDSGL
2110 2120 2130 2140 2150
NGELVYRIEA GAQDRFLIHP VTGVIRVGNA TIDREEQESY RLTVVATDRG
2160 2170 2180 2190 2200
TVPLSGTAIV TILIDDINDS RPEFLNPIQT VSVLESAEPG TIIANVTAID
2210 2220 2230 2240 2250
LDLNPKLEYH IISIVAKDDT DRLVPDQEDA FAVNINTGSV MVKSPLNREL
2260 2270 2280 2290 2300
VATYEVTLSV IDNASDLPEH SVSVPNAKLT VNILDVNDNT PQFKPFGITY
2310 2320 2330 2340 2350
YTERVLEGAT PGTTLIAVAA VDPDKGLNGL ITYTLLDLTP PGYVQLEDSS
2360 2370 2380 2390 2400
AGKVIANRTV DYEEVHWLNF TVRASDNGSP PRAAEIPVYL EIVDINDNNP
2410 2420 2430 2440 2450
IFDQPSYQEA VFEDIAVGTV ILRVTATDAD SGNFALIEYS LVDGEGKFAI
2460 2470 2480 2490 2500
NPNTGDISVL SSLDREKKDH YILTALAKDN PGDVASNRRE NSVQVVIRVL
2510 2520 2530 2540 2550
DVNDCRPQFS KPQFSTSVYE NEPAGTSVIT MLATDQDEGS NSQLTYSLEG
2560 2570 2580 2590 2600
PGMEAFSVDM DSGLVTTQRP LQSYERFNLT VVATDGGEPP LWGTTMLLVE
2610 2620 2630 2640 2650
VIDVNDNRPV FVRPPNGTIL HIKEEIPLRS NVYEVYATDN DEGLNGAVRY
2660 2670 2680 2690 2700
SFLKTTGNRD WEYFTIDPIS GLIQTAQRLD REKQAVYSLI LVASDLGQPV
2710 2720 2730 2740 2750
PYETMQPLQV ALEDIDDNEP LFVRPPKGSP QYQLLTVPEH SPRGTLVGNV
2760 2770 2780 2790 2800
TGAVDADEGP NAIVYYFIAA GDEDKNFHLQ PDGRLLVLRD LDRETEATFS
2810 2820 2830 2840 2850
FIVKASSNRS WTPPRGPSPA LDLLTDLTLQ EVRVVLEDIN DQPPRFTKAE
2860 2870 2880 2890 2900
YTAGVATDAK VGSELIQVLA LDADIGNNSL VFYGILAIHY FRALANDSED
2910 2920 2930 2940 2950
VGQVFTMGSV DGILRTFDLF MAYSPGYFVV DIVARDLAGH NDTAIIGIYI
2960 2970 2980 2990 3000
LRDDQRVKIV INEIPDRVRG FEEEFIRLLS NITGAIVNTD DVQFHVDMKG
3010 3020 3030 3040 3050
RVNFAQTELL IHVVNRDTNR ILDVDRVIQM IDENKEQLRN LFRNYNVLDV
3060 3070 3080 3090 3100
QPAISVQLPD DMSALQMAII VLAILLFLAA MLFVLMNWYY RTIHKRKLKA
3110 3120 3130 3140 3150
IVAGSAGNRG FIDIMDMPNT NKYSFDGSNP VWLDPFCRNL ELAAQAEHED
3160 3170 3180 3190 3200
DLPENLSEIA DLWNSPTRTH GTFGREPAAV KPDDDRYLRA AIQEYDNIAK
3210 3220 3230 3240 3250
LGQIIREGPI KGSLLKVVLE DYLRLKKLFA QRMVQKASSC HSSISELIHT
3260 3270 3280 3290 3300
DLEEEPGDHS PGQGSLRFRH KPPMELKGQD GIHMVHGSTG TLLATDLNSL
3310 3320 3330 3340 3350
PEDDQKGLDR SLETLTASEA TAFERNARTE SAKSTPLHKL RDVIMESPLE

ITEL
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 ENSGT00760000118805.
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.
ExpressionAtlasi Q99PF4. baseline and differential.
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: October 29, 2014
This is version 112 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