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Q99PJ1 (PCD15_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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:
Protocadherin-15
Gene names
Name:Pcdh15
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1943 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-dependent cell-adhesion protein. Required for inner ear neuroepithelial cell elaboration and cochlear function. Probably involved in the maintenance of normal retinal function.

Subunit structure

antiparallel heterodimer with CDH23. Interacts with MYO7A. Interacts with USH1G; this interaction may recruit USH1G to the plasma membrane. Interacts with LHFPL5/TMHS; this interaction is required for efficient localization to hair bundles. Ref.6 Ref.9 Ref.10 Ref.12 Ref.13

Subcellular location

Cell membrane; Single-pass membrane protein. Note: Efficient localization to the plasma membrane requires the presence of LHFPL5. Ref.6 Ref.12

Isoform 1: Cell membrane; Single-pass type I membrane protein By similarity Ref.6 Ref.12.

Isoform 2: Cell membrane; Single-pass type I membrane protein By similarity Ref.6 Ref.12.

Isoform 3: Secreted Probable Ref.6 Ref.12.

Isoform 4: Cell membrane; Single-pass type I membrane protein By similarity Ref.6 Ref.12.

Isoform 5: Cell membrane; Single-pass type I membrane protein By similarity Ref.6 Ref.12.

Isoform 6: Cell membrane; Single-pass type I membrane protein By similarity Ref.6 Ref.12.

Isoform 7: Cell membrane; Single-pass type I membrane protein By similarity Ref.6 Ref.12.

Isoform 8: Cell membrane; Single-pass type I membrane protein By similarity Ref.6 Ref.12.

Isoform 9: Cell membrane; Single-pass type I membrane protein By similarity Ref.6 Ref.12.

Isoform 10: Cell membrane; Single-pass type I membrane protein By similarity Ref.6 Ref.12.

Isoform 11: Cell membrane; Single-pass type I membrane protein By similarity Ref.6 Ref.12.

Isoform 12: Cell membrane; Single-pass type I membrane protein By similarity Ref.6 Ref.12.

Isoform 13: Secreted Probable Ref.6 Ref.12.

Isoform 14: Secreted Probable Ref.6 Ref.12.

Isoform 15: Secreted Probable Ref.6 Ref.12.

Isoform 16: Secreted Probable Ref.6 Ref.12.

Isoform 17: Secreted Probable Ref.6 Ref.12.

Isoform 18: Cell membrane; Single-pass type I membrane protein By similarity Ref.6 Ref.12.

Isoform 19: Cell membrane; Single-pass type I membrane protein By similarity Ref.6 Ref.12.

Isoform 21: Secreted Probable Ref.6 Ref.12.

Isoform 22: Secreted Probable Ref.6 Ref.12.

Isoform 23: Secreted Probable Ref.6 Ref.12.

Tissue specificity

Expressed in brain and sensory epithelium of the developing inner ear. Expressed in the retina, in the photoreceptor inner segments, the outer plexiform layer, the inner nuclei layer and the ganglion cell layer and, more diffusely in the inner plexiform layer (at protein level). Not detected in the retinal pigment epithelium (at protein level). Expressed in the spleen, dorsal root ganglion, dorsal aspect of neural tube, floor plate and ependymal cells adjacent to the neural canal. Ref.2 Ref.8 Ref.9 Ref.10

Developmental stage

Highest level of expression is detected at embryonic day 16. Alternative splicing isoforms have different spatiotemporal expression patterns. In cochlear cultures at the equivalent of postnatal day 3, isoforms belonging to the CD1 (isoforms 1 through 9) and CD3 (isoforms 18 through 20) groups are highly expressed in hair bundles in the basal coils and moderately in those in the middle of the apical coil; they are hardly detectable in those at the apical end of the apical coil (at protein level). At the base of the cultured cochlea, in the more mature hair bundles, CD3 group isoforms are restricted to the tips of the shorter stereocilia in both inner and outer hair cells. By contrast, at the same stage, isoforms belonging to the CD2 group (isoforms 10 through 17) are highly expressed in hair bundles in the apex of the cochlea and, at lower levels, in those in the middle of the apical coil; they are hardly detectable at the base of the cochlea (at protein level). In mature hair bundles, CD1 group isoforms are distributed fairly evenly along most of the length of the stereocilia on auditory hair cells, whereas they are concentrated toward the upper third of the hair bundle in vestibular hair cells. In both the auditory and the vestibular organs, these isoforms are excluded from a region at the very tip of each stereocilium (at protein level). In contrast, CD2 group isoforms are undetectable in adult cochlear hair cells (at protein level). These isoforms are expressed in the entire hair bundle of the immature cells in the sensory epithelium of the early postnatal vestibule and only in the kinocilium in the more mature hair bundles (at protein level). CD3 group isoforms are detected in immature vestibular hair bundles, concentrated toward the tip of each stereocilium, as early as 15.5 dpc. They also localize to the tips of the shorter stereocilia in the mature vestibular hair bundles and are not detected at the tips of the stereocilia in the tallest row (at protein level). Ref.3

Domain

Cadherin repeats 1 and 2 mediate calcium-dependent heterophilic interaction with CDH23 (Ref.13).

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 (Ref.13).

Involvement in disease

Defects in Pcdh15 are the cause of the Ames waltzer (av) phenotype. It is characterized by deafness and a balance disorder, associated with the degeneration of inner ear neuroepithelia.

Sequence similarities

Contains 11 cadherin domains.

Ontologies

Keywords
   Biological processCell adhesion
Hearing
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
   DiseaseDeafness
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament organization

Inferred from mutant phenotype PubMed 11124469. Source: MGI

adult walking behavior

Inferred from mutant phenotype PubMed 11124469. Source: MGI

auditory receptor cell differentiation

Inferred from mutant phenotype Ref.9. Source: MGI

auditory receptor cell stereocilium organization

Inferred from mutant phenotype PubMed 10978835PubMed 11124469PubMed 16887306Ref.12. Source: MGI

detection of mechanical stimulus involved in equilibrioception

Inferred from mutant phenotype Ref.9. Source: MGI

detection of mechanical stimulus involved in sensory perception of sound

Inferred from mutant phenotype Ref.9. Source: MGI

homophilic cell adhesion

Inferred from electronic annotation. Source: InterPro

inner ear development

Inferred from mutant phenotype PubMed 10978835PubMed 15811708. Source: MGI

locomotory behavior

Inferred from mutant phenotype PubMed 10430593PubMed 10978835PubMed 15811708PubMed 16962269. Source: MGI

morphogenesis of an epithelium

Inferred from mutant phenotype Ref.1. Source: MGI

multicellular organism growth

Inferred from mutant phenotype PubMed 10978835. Source: MGI

nonmotile primary cilium assembly

Inferred from mutant phenotype Ref.9. Source: MGI

righting reflex

Inferred from mutant phenotype PubMed 10978835PubMed 15811708. Source: MGI

sensory perception of sound

Inferred from mutant phenotype PubMed 10430593PubMed 10978835PubMed 11124469PubMed 14570705Ref.9PubMed 5093631PubMed 9653653. Source: MGI

startle response

Inferred from mutant phenotype PubMed 15811708. Source: MGI

visual perception

Inferred from mutant phenotype Ref.2. Source: MGI

   Cellular_componentcytoplasm

Inferred from direct assay Ref.9. Source: MGI

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from sequence or structural similarity Ref.1. Source: MGI

photoreceptor outer segment

Inferred from direct assay PubMed 14570705. Source: MGI

plasma membrane

Inferred from direct assay Ref.12. Source: MGI

stereocilium

Inferred from direct assay PubMed 14570705. Source: HGNC

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ush1cQ9ES643EBI-6556746,EBI-7418968

Alternative products

This entry describes 26 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99PJ1-1)

Also known as: CD1-1;

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: Q99PJ1-2)

Also known as: CD1-2;

The sequence of this isoform differs from the canonical sequence as follows:
     31-35: Missing.
Isoform 3 (identifier: Q99PJ1-3)

Also known as: CD1-3/5;

The sequence of this isoform differs from the canonical sequence as follows:
     31-35: Missing.
     645-689: ATDREGDPIT...ALDRESTDRY → HRDSQPREGS...HCEHSGDGRQ
     690-1943: Missing.
Isoform 4 (identifier: Q99PJ1-4)

Also known as: CD1-4;

The sequence of this isoform differs from the canonical sequence as follows:
     31-35: Missing.
     1461-1463: MHN → I
Isoform 5 (identifier: Q99PJ1-5)

Also known as: CD1-6;

The sequence of this isoform differs from the canonical sequence as follows:
     31-35: Missing.
     600-671: RHSICTVYIEVLPPNNQSPPRFPQLMYSLEVSEAMRIGAILLNLQATDREGDPITYAIENGDPQRVFNLSET → S
Isoform 6 (identifier: Q99PJ1-6)

Also known as: CD1-7;

The sequence of this isoform differs from the canonical sequence as follows:
     31-35: Missing.
     1407-1409: Missing.
     1461-1463: MHN → I
Isoform 7 (identifier: Q99PJ1-7)

Also known as: CD1-8;

The sequence of this isoform differs from the canonical sequence as follows:
     31-35: Missing.
     204-240: Missing.
     1407-1409: Missing.
     1461-1463: MHN → I
Isoform 8 (identifier: Q99PJ1-8)

Also known as: CD1-9;

The sequence of this isoform differs from the canonical sequence as follows:
     31-57: Missing.
Isoform 9 (identifier: Q99PJ1-9)

Also known as: CD1-10;

The sequence of this isoform differs from the canonical sequence as follows:
     31-57: Missing.
     1407-1409: Missing.
Isoform 10 (identifier: Q99PJ1-10)

Also known as: CD2-1;

The sequence of this isoform differs from the canonical sequence as follows:
     440-440: D → DVPPGGVP
     1463-1943: NLFLLYHFEQ...VQPHSQSTSL → KYEMPQYGSR...ANSEGYNTAL
Isoform 11 (identifier: Q99PJ1-11)

Also known as: CD2-2;

The sequence of this isoform differs from the canonical sequence as follows:
     31-35: Missing.
     1463-1523: NLFLLYHFEQ...PNPARTFSFV → KSYPWNLGLI...KLKRNMKKKR
     1524-1943: Missing.
Isoform 12 (identifier: Q99PJ1-12)

Also known as: CD2-3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-368: Missing.
     369-371: VIK → MTM
     440-440: D → DVPPGGVP
     1463-1523: NLFLLYHFEQ...PNPARTFSFV → KSYPWNLGLI...KLKRNMKKKR
     1524-1943: Missing.
Isoform 13 (identifier: Q99PJ1-13)

Also known as: CD2-4;

The sequence of this isoform differs from the canonical sequence as follows:
     31-35: Missing.
     298-331: EELNPILVTPPIQAIDQDRNIQPPSDRPGILYSI → DFGSLRSGANSWCQGCGGVHRCPSPWRRLLPRRL
     332-1943: Missing.
Isoform 14 (identifier: Q99PJ1-14)

Also known as: CD2-5;

The sequence of this isoform differs from the canonical sequence as follows:
     31-35: Missing.
     335-339: TPEDY → RARES
     340-1943: Missing.
Isoform 15 (identifier: Q99PJ1-15)

Also known as: CD2-6;

The sequence of this isoform differs from the canonical sequence as follows:
     31-35: Missing.
     372-655: AEQDNGHPLP...TDREGDPITY → VEPEKVKKPK...ANSEGYNTAL
     656-1943: Missing.
Isoform 16 (identifier: Q99PJ1-16)

Also known as: CD2-7;

The sequence of this isoform differs from the canonical sequence as follows:
     31-35: Missing.
     441-725: TKDPELHLFL...NDNAPVFDPY → VEPEKVKKPK...ANSEGYNTAL
     726-1943: Missing.
Isoform 17 (identifier: Q99PJ1-17)

Also known as: CD2-8;

The sequence of this isoform differs from the canonical sequence as follows:
     31-35: Missing.
     703-986: TSTATVNIVV...FPYPASIFDV → VEPEKVKKPK...ANSEGYNTAL
     987-1943: Missing.
Isoform 18 (identifier: Q99PJ1-18)

Also known as: CD3-1;

The sequence of this isoform differs from the canonical sequence as follows:
     1463-1682: NLFLLYHFEQ...SHFSFSTLPT → KYEMPQYGSR...NSLHIPMTKL
     1683-1943: Missing.
Isoform 19 (identifier: Q99PJ1-19)

Also known as: CD3-2;

The sequence of this isoform differs from the canonical sequence as follows:
     31-35: Missing.
     1463-1682: NLFLLYHFEQ...SHFSFSTLPT → KYEMPQYGSR...NSLHIPMTKL
     1683-1943: Missing.
Isoform 20 (identifier: Q99PJ1-20)

Also known as: CD3-3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1252: Missing.
     1407-1667: FKVRQAECTK...QLKSLSSGSS → GGFAPEHQLL...NSLHIPMTKL
     1668-1943: Missing.
Isoform 21 (identifier: Q99PJ1-21)

Also known as: SI-1;

The sequence of this isoform differs from the canonical sequence as follows:
     1131-1176: NTAKVYIEIQ...SVLRVKATDR → LSVIPCSWRT...STRAASVPIH
     1177-1943: Missing.
Isoform 22 (identifier: Q99PJ1-22)

Also known as: SI-2;

The sequence of this isoform differs from the canonical sequence as follows:
     31-35: Missing.
     1131-1176: NTAKVYIEIQ...SVLRVKATDR → LSVIPCSWRT...STRAASVPIH
     1177-1943: Missing.
Isoform 23 (identifier: Q99PJ1-23)

Also known as: SI-3;

The sequence of this isoform differs from the canonical sequence as follows:
     31-35: Missing.
     441-961: Missing.
     1131-1176: NTAKVYIEIQ...SVLRVKATDR → LSVIPCSWRT...STRAASVPIH
     1177-1943: Missing.
Isoform 24 (identifier: Q99PJ1-24)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     31-600: Missing.
     1464-1473: Missing.
Isoform 25 (identifier: Q99PJ1-25)

The sequence of this isoform differs from the canonical sequence as follows:
     1462-1943: HNLFLLYHFE...VQPHSQSTSL → YEMPQYGSRR...ANSEGYNTAL
Isoform 26 (identifier: Q99PJ1-26)

The sequence of this isoform differs from the canonical sequence as follows:
     1407-1409: Missing.
     1462-1943: HNLFLLYHFE...VQPHSQSTSL → YEMPQYGSRR...NSLHIPMTKL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Chain27 – 19431917Protocadherin-15
PRO_0000003999

Regions

Topological domain27 – 13811355Extracellular Potential
Transmembrane1382 – 140221Helical; Potential
Topological domain1403 – 1943541Cytoplasmic Potential
Domain45 – 152108Cadherin 1
Domain153 – 270118Cadherin 2
Domain283 – 400118Cadherin 3
Domain401 – 514114Cadherin 4
Domain515 – 621107Cadherin 5
Domain622 – 722101Cadherin 6
Domain724 – 824101Cadherin 7
Domain825 – 931107Cadherin 8
Domain932 – 1040109Cadherin 9
Domain1042 – 1149108Cadherin 10
Domain1150 – 1264115Cadherin 11
Compositional bias1437 – 144812Poly-Pro
Compositional bias1772 – 17787Poly-Pro
Compositional bias1804 – 18129Poly-Pro

Amino acid modifications

Glycosylation571N-linked (GlcNAc...) Potential
Glycosylation1021N-linked (GlcNAc...) Potential
Glycosylation2061N-linked (GlcNAc...) Potential
Glycosylation4241N-linked (GlcNAc...) Potential
Glycosylation5641N-linked (GlcNAc...) Potential
Glycosylation6671N-linked (GlcNAc...) Potential
Glycosylation7291N-linked (GlcNAc...) Potential
Glycosylation7731N-linked (GlcNAc...) Potential
Glycosylation8261N-linked (GlcNAc...) Potential
Glycosylation8561N-linked (GlcNAc...) Potential
Glycosylation10691N-linked (GlcNAc...) Potential
Glycosylation10891N-linked (GlcNAc...) Potential
Glycosylation11801N-linked (GlcNAc...) Potential
Disulfide bond37 ↔ 125 Ref.13

Natural variations

Alternative sequence1 – 12521252Missing in isoform 20.
VSP_046576
Alternative sequence1 – 368368Missing in isoform 12.
VSP_046577
Alternative sequence31 – 600570Missing in isoform 24.
VSP_046578
Alternative sequence31 – 5727Missing in isoform 8 and isoform 9.
VSP_046579
Alternative sequence31 – 355Missing in isoform 2, isoform 3, isoform 4, isoform 5, isoform 6, isoform 7, isoform 11, isoform 13, isoform 14, isoform 15, isoform 16, isoform 17, isoform 19, isoform 22 and isoform 23.
VSP_046580
Alternative sequence204 – 24037Missing in isoform 7.
VSP_046581
Alternative sequence298 – 33134EELNP…ILYSI → DFGSLRSGANSWCQGCGGVH RCPSPWRRLLPRRL in isoform 13.
VSP_046582
Alternative sequence332 – 19431612Missing in isoform 13.
VSP_046583
Alternative sequence335 – 3395TPEDY → RARES in isoform 14.
VSP_046584
Alternative sequence340 – 19431604Missing in isoform 14.
VSP_046585
Alternative sequence369 – 3713VIK → MTM in isoform 12.
VSP_046586
Alternative sequence372 – 655284AEQDN…DPITY → VEPEKVKKPKVEIREPSEEE VVVTVEKPPAAEPTYPTWKR ARIFPMIFKKVRGLAEKRGI DLEGEEWRRRLDEEDKDYLQ LTLDQEEATESTVESEEESS DYTEYTETESEFSESETTEE SESETPSEEAEESSTPESEE SESTESEGEKARKNIVLARR RPVVEEIQEVKGKREEPPVE EEEEPPLEEEERAEEGEESE AAPMDESTDLEAQDVPEEGS AESVSMERGVESEESESELS SSSSTSESLSGGPWGFQVPE YDRRKDEEPKKSPGANSEGY NTAL in isoform 15.
VSP_046587
Alternative sequence4401D → DVPPGGVP in isoform 10 and isoform 12.
VSP_046588
Alternative sequence441 – 961521Missing in isoform 23.
VSP_046589
Alternative sequence441 – 725285TKDPE…VFDPY → VEPEKVKKPKVEIREPSEEE VVVTVEKPPAAEPTYPTWKR ARIFPMIFKKVRGLAEKRGI DLEGEEWRRRLDEEDKDYLQ LTLDQEEATESTVESEEESS DYTEYTETESEFSESETTEE SESETPSEEAEESSTPESEE SESTESEGEKARKNIVLARR RPVVEEIQEVKGKREEPPVE EEEEPPLEEEERAEEGEESE AAPMDESTDLEAQDVPEEGS AESVSMERGVESEESESELS SSSSTSESLSGGPWGFQVPE YDRRKDEEPKKSPGANSEGY NTAL in isoform 16.
VSP_046590
Alternative sequence600 – 67172RHSIC…NLSET → S in isoform 5.
VSP_046591
Alternative sequence645 – 68945ATDRE…STDRY → HRDSQPREGSRPREHRPLHP HRHSLRWQTGWNLNCHCEHS GDGRQ in isoform 3.
VSP_046592
Alternative sequence656 – 19431288Missing in isoform 15.
VSP_046593
Alternative sequence690 – 19431254Missing in isoform 3.
VSP_046594
Alternative sequence703 – 986284TSTAT…SIFDV → VEPEKVKKPKVEIREPSEEE VVVTVEKPPAAEPTYPTWKR ARIFPMIFKKVRGLAEKRGI DLEGEEWRRRLDEEDKDYLQ LTLDQEEATESTVESEEESS DYTEYTETESEFSESETTEE SESETPSEEAEESSTPESEE SESTESEGEKARKNIVLARR RPVVEEIQEVKGKREEPPVE EEEEPPLEEEERAEEGEESE AAPMDESTDLEAQDVPEEGS AESVSMERGVESEESESELS SSSSTSESLSGGPWGFQVPE YDRRKDEEPKKSPGANSEGY NTAL in isoform 17.
VSP_046595
Alternative sequence726 – 19431218Missing in isoform 16.
VSP_046596
Alternative sequence987 – 1943957Missing in isoform 17.
VSP_046597
Alternative sequence1131 – 117646NTAKV…KATDR → LSVIPCSWRTQVSKSLGLEL GVPVSHSVESGTRTGSSTRA ASVPIH in isoform 21, isoform 22 and isoform 23.
VSP_046598
Alternative sequence1177 – 1943767Missing in isoform 21, isoform 22 and isoform 23.
VSP_046599
Alternative sequence1407 – 1667261FKVRQ…SSGSS → GGFAPEHQLLRPSLLKPEEL SMESGIDPGQEYGQDYYSYE HGYEMPQYGSRRRLLPPAGQ EEYGEVIGEAEEEYEEEEWA RKRMIKLVVDREYESSSPGE DSAPESQRSRTHKPSGRSNV NGNIYIAQNGSVVRTRRACV ADNLKVPSPGLLGRHLKKLD TLAGTREENVPLNTLFKGPF STEKAKRTPTLVTFAPCPVV AEHSAVKPSGTRLKHTAEQE SMVDSRLSRESMEFHGDSAP SDEEELWMGPWNSLHIPMTK L in isoform 20.
VSP_046600
Alternative sequence1407 – 14093Missing in isoform 6, isoform 7, isoform 9 and isoform 26.
VSP_046601
Alternative sequence1461 – 14633MHN → I in isoform 4, isoform 6 and isoform 7.
VSP_046602
Alternative sequence1462 – 1943482HNLFL…QSTSL → YEMPQYGSRRRLLPPAGQEE YGEVIGEAEEEYEEEEVEPE KVKKPKVEIREPSEEEVVVT VEKPPAAEPTYPTWKRARIF PMIFKKVRGLAEKRGIDLEG EEWRRRLDEEDKDYLQLTLD QEEATESTVESEEESSDYTE YTETESEFSESETTEESESE TPSEEAEESSTPESEESEST ESEGEKARKNIVLARRRPVV EEIQEVKGKREEPPVEEEEE PPLEEEERAEEGEESEAAPM DESTDLEAQDVPEEGSAESV SMERGVESEESESELSSSSS TSESLSGGPWGFQVPEYDRR KDEEPKKSPGANSEGYNTAL in isoform 25.
VSP_046603
Alternative sequence1462 – 1943482HNLFL…QSTSL → YEMPQYGSRRRLLPPAGQEE YGEVIGEAEEEYEEEEWARK RMIKLVVDREYESSSPGEDS APESQRSRTHKPSGRSNVNG NIYIAQNGSVVRTRRACVAD NLKVPSPGLLGRHLKKLDTL AGTREENVPLNTLFKGPFST EKAKRTPTLVTFAPCPVVAE HSAVKPSGTRLKHTAEQESM VDSRLSRESMEFHGDSAPSD EEELWMGPWNSLHIPMTKL in isoform 26.
VSP_046604
Alternative sequence1463 – 1943481NLFLL…QSTSL → KYEMPQYGSRRRLLPPAGQE EYGEVIGEAEEEYEEEEVEP EKVKKPKVEIREPSEEEVVV TVEKPPAAEPTYPTWKRARI FPMIFKKVRGLAEKRGIDLE GEEWRRRLDEEDKDYLQLTL DQEEATESTVESEEESSDYT EYTETESEFSESETTEESES ETPSEEAEESSTPESEESES TESEGEKARKNIVLARRRPV VEEIQEVKGKREEPPVEEEE EPPLEEEERAEEGEESEAAP MDESTDLEAQDVPEEGSAES VSMERGVESEESESELSSSS STSESLSGGPWGFQVPEYDR RKDEEPKKSPGANSEGYNTA L in isoform 10.
VSP_046605
Alternative sequence1463 – 1682220NLFLL…STLPT → KYEMPQYGSRRRLLPPAGQE EYGEVIGEAEEEYEEEEWAR KRMIKLVVDREYESSSPGED SAPESQRSRTHKPSGRSNVN GNIYIAQNGSVVRTRRACVA DNLKVPSPGLLGRHLKKLDT LAGTREENVPLNTLFKGPFS TEKAKRTPTLVTFAPCPVVA EHSAVKPSGTRLKHTAEQES MVDSRLSRESMEFHGDSAPS DEEELWMGPWNSLHIPMTKL in isoform 18 and isoform 19.
VSP_046606
Alternative sequence1463 – 152361NLFLL…TFSFV → KSYPWNLGLILARNMDKIIT VMSMGMRCPSMEVAVDCCHL LDRRNTAKSLVKLKRNMKKK R in isoform 11 and isoform 12.
VSP_046607
Alternative sequence1464 – 147310Missing in isoform 24.
VSP_046608
Alternative sequence1524 – 1943420Missing in isoform 11 and isoform 12.
VSP_046609
Alternative sequence1668 – 1943276Missing in isoform 20.
VSP_046610
Alternative sequence1683 – 1943261Missing in isoform 18 and isoform 19.
VSP_046611

Experimental info

Mutagenesis481I → A: Strongly reduced interaction with CDH23. Ref.13
Mutagenesis1391R → G: Impaired interaction with CDH23. Ref.13
Sequence conflict6081I → T in AAG53891. Ref.1
Sequence conflict6081I → T in AAY24693. Ref.2
Sequence conflict6081I → T in ABC79259. Ref.3
Sequence conflict6081I → T in ABC79260. Ref.3
Sequence conflict6081I → T in ABC79261. Ref.3
Sequence conflict6081I → T in ABC79262. Ref.3
Sequence conflict6081I → T in ABC79264. Ref.3
Sequence conflict6081I → T in ABC79265. Ref.3
Sequence conflict6081I → T in ABC79266. Ref.3
Sequence conflict6081I → T in ABC79267. Ref.3
Sequence conflict6081I → T in ABC79268. Ref.3
Sequence conflict6081I → T in ABC79269. Ref.3
Sequence conflict6081I → T in ABC79270. Ref.3
Sequence conflict6081I → T in ABC79276. Ref.3
Sequence conflict6081I → T in ABC79277. Ref.3
Sequence conflict9011V → A in AAG53891. Ref.1
Sequence conflict9011V → A in AAY24693. Ref.2
Sequence conflict9011V → A in ABC79259. Ref.3
Sequence conflict9011V → A in ABC79261. Ref.3
Sequence conflict9011V → A in ABC79263. Ref.3
Sequence conflict9011V → A in ABC79264. Ref.3
Sequence conflict9011V → A in ABC79265. Ref.3
Sequence conflict9011V → A in ABC79266. Ref.3
Sequence conflict9011V → A in ABC79267. Ref.3
Sequence conflict9011V → A in ABC79268. Ref.3
Sequence conflict9011V → A in ABC79269. Ref.3
Sequence conflict9011V → A in ABC79270. Ref.3
Sequence conflict9011V → A in ABC79276. Ref.3
Sequence conflict9011V → A in ABC79277. Ref.3
Sequence conflict17481S → F in AAG53891. Ref.1
Sequence conflict17481S → F in AAY24693. Ref.2
Sequence conflict17481S → F in ABC79259. Ref.3
Sequence conflict17481S → F in ABC79261. Ref.3
Sequence conflict17481S → F in ABC79263. Ref.3
Sequence conflict17481S → F in ABC79264. Ref.3
Sequence conflict17481S → F in ABC79265. Ref.3
Sequence conflict17481S → F in ABC79266. Ref.3
Sequence conflict17481S → F in ABC79267. Ref.3
Sequence conflict18481S → F in AAG53891. Ref.1
Sequence conflict18481S → F in AAY24693. Ref.2
Sequence conflict18481S → F in ABC79259. Ref.3
Sequence conflict18481S → F in ABC79261. Ref.3
Sequence conflict18481S → F in ABC79263. Ref.3
Sequence conflict18481S → F in ABC79264. Ref.3
Sequence conflict18481S → F in ABC79265. Ref.3
Sequence conflict18481S → F in ABC79266. Ref.3
Sequence conflict18481S → F in ABC79267. Ref.3
Sequence conflict18591W → G in BAE24546. Ref.4

Secondary structure

......................................................... 1943
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (CD1-1) [UniParc].

Last modified June 26, 2013. Version 3.
Checksum: 6FD6836082655855

FASTA1,943214,738
        10         20         30         40         50         60 
MFLQFAVWKC LPHGILIASL LVVSWGQYDD DWQYEDCKLA RGGPPATIVA IDEESRNGTI 

        70         80         90        100        110        120 
LVDNMLIKGT AGGPDPTIEL SLKDNVDYWV LLDPVKQMLF LNSTGRVLDR DPPMNIHSIV 

       130        140        150        160        170        180 
VQVQCVNKKV GTVIYHEVRI VVRDRNDNSP TFKHESYYAT VNELTPVGTT IFTGFSGDNG 

       190        200        210        220        230        240 
ATDIDDGPNG QIEYVIQYNP EDPTSNDTFE IPLMLTGNVV LRKRLNYEDK TRYYVIIQAN 

       250        260        270        280        290        300 
DRAQNLNERR TTTTTLTVDV LDGDDLGPMF LPCVLVPNTR DCRPLTYQAA IPELRTPEEL 

       310        320        330        340        350        360 
NPILVTPPIQ AIDQDRNIQP PSDRPGILYS ILVGTPEDYP RFFHMHPRTA ELTLLEPVNR 

       370        380        390        400        410        420 
DFHQKFDLVI KAEQDNGHPL PAFASLHIEI LDENNQSPYF TMPSYQGYIL ESAPVGATIS 

       430        440        450        460        470        480 
ESLNLTTPLR IVALDKDIED TKDPELHLFL NDYTSVFTVT PTGITRYLTL LQPVDREEQQ 

       490        500        510        520        530        540 
TYTFLITAFD GVQESEPVVV NIRVMDANDN TPTFPEISYD VYVYTDMSPG DSVIQLTAVD 

       550        560        570        580        590        600 
ADEGSNGEIS YEILVGGKGD FVINKTTGLV SIAPGVELIV GQTYALTVQA SDNAPPAERR 

       610        620        630        640        650        660 
HSICTVYIEV LPPNNQSPPR FPQLMYSLEV SEAMRIGAIL LNLQATDREG DPITYAIENG 

       670        680        690        700        710        720 
DPQRVFNLSE TTGILSLGKA LDRESTDRYI LIVTASDGRP DGTSTATVNI VVTDVNDNAP 

       730        740        750        760        770        780 
VFDPYLPRNL SVVEEEANAF VGQVRATDPD AGINGQVHYS LGNFNNLFRI TSNGSIYTAV 

       790        800        810        820        830        840 
KLNREARDHY ELVVVATDGA VHPRHSTLTL YIKVLDIDDN SPVFTNSTYT VVVEENLPAG 

       850        860        870        880        890        900 
TSFLQIEAKD VDLGANVSYR IRSPEVKHLF ALHPFTGELS LLRSLDYEAF PDQEASITFL 

       910        920        930        940        950        960 
VEAFDIYGTM PPGIATVTVI VKDMNDYPPV FSKRIYKGMV APDAVKGTPI TTVYAEDADP 

       970        980        990       1000       1010       1020 
PGMPASRVRY RVDDVQFPYP ASIFDVEEDS GRVVTRVNLN EEPTTIFKLV VVAFDDGEPV 

      1030       1040       1050       1060       1070       1080 
MSSSATVRIL VLHPGEIPRF TQEEYRPPPV SELAARGTVV GVISAAAINQ SIVYSIVAGN 

      1090       1100       1110       1120       1130       1140 
EEDKFGINNV TGVIYVNSPL DYETRTSYVL RVQADSLEVV LANLRVPSKS NTAKVYIEIQ 

      1150       1160       1170       1180       1190       1200 
DENDHPPVFQ KKFYIGGVSE DARMFASVLR VKATDRDTGN YSAMAYRLII PPIKEGKEGF 

      1210       1220       1230       1240       1250       1260 
VVETYTGLIK TAMLFHNMRR SYFKFQVIAT DDYGKGLSGK ADVLVSVVNQ LDMQVIVSNV 

      1270       1280       1290       1300       1310       1320 
PPTLVEKKIE DLTEILDRYV QEQIPGAKVV VESIGARRHG DAYSLEDYSK CDLTVYAIDP 

      1330       1340       1350       1360       1370       1380 
QTNRAIDRNE LFKFLDGKLL DINKDFQPYY GEGGRILEIR TPEAVTSIKK RGESLGYTEG 

      1390       1400       1410       1420       1430       1440 
ALLALAFIII LCCIPAILVV LVSYRQFKVR QAECTKTARI QSAMPAAKPA APVPAAPAPP 

      1450       1460       1470       1480       1490       1500 
PPPPPPPPGA HLYEELGESA MHNLFLLYHF EQSRGNNSVP EDRSSHRDGM AFSSSTTESH 

      1510       1520       1530       1540       1550       1560 
EPAHVEGPLK ESQPNPARTF SFVPDEDNLS THNPLYMESI GQRSTNSDLQ PRTDFEELLA 

      1570       1580       1590       1600       1610       1620 
PRTQVKSQSL RGPREKIQRV WNQSVSFPRR LMWKAPNRPE TIDLVEWQIT NQRAECESAR 

      1630       1640       1650       1660       1670       1680 
CHPSQRGSSN VLLATEDAHE SEKEGGHRDT LIVQQTEQLK SLSSGSSFSS SWSHFSFSTL 

      1690       1700       1710       1720       1730       1740 
PTISRAVELG SEPNVVTSPA DCTLELSPPL RPRILNSLSS KRETPTCASD TEPKRNSFEI 

      1750       1760       1770       1780       1790       1800 
APHPPSISAP LPHPPLPRPP IAFTTFPLPL SPPNPPPPQL VTFSLPISTP PTSSLPLPPP 

      1810       1820       1830       1840       1850       1860 
LSLPPPPRPP APRLFPQPPS TSIPSTDSIS APAAKCTASA THARETTSTT QPPASNPQWG 

      1870       1880       1890       1900       1910       1920 
AEPHRHPKGI LRHVKNLAEL EKSVSNMYSH IEKNCPPADP SKLHTFCPAE KTGMKITHDQ 

      1930       1940 
SQETLVRVVE GIDVQPHSQS TSL 

« Hide

Isoform 2 (CD1-2) [UniParc].

Checksum: 40B0EB13DF4E5EFC
Show »

FASTA1,938214,016
Isoform 3 (CD1-3/5) [UniParc].

Checksum: 9042A0B5CB766F1F
Show »

FASTA68476,656
Isoform 4 (CD1-4) [UniParc].

Checksum: 3740C7F23545D42B
Show »

FASTA1,936213,747
Isoform 5 (CD1-6) [UniParc].

Checksum: EC9AFA9363BE7757
Show »

FASTA1,867205,990
Isoform 6 (CD1-7) [UniParc].

Checksum: C708CC475A755E15
Show »

FASTA1,933213,372
Isoform 7 (CD1-8) [UniParc].

Checksum: CAA46E2AA740CA6A
Show »

FASTA1,896209,000
Isoform 8 (CD1-9) [UniParc].

Checksum: A416619EE89EABC8
Show »

FASTA1,916211,721
Isoform 9 (CD1-10) [UniParc].

Checksum: FB42EBAEE0565806
Show »

FASTA1,913211,347
Isoform 10 (CD2-1) [UniParc].

Checksum: 5731151E416F5119
Show »

FASTA1,790198,941
Isoform 11 (CD2-2) [UniParc].

Checksum: 31FC7C15E9D26B80
Show »

FASTA1,518168,209
Isoform 12 (CD2-3) [UniParc].

Checksum: 48FB24E7A3CE682C
Show »

FASTA1,162127,964
Isoform 13 (CD2-4) [UniParc].

Checksum: FA6863C72C1324C2
Show »

FASTA32636,453
Isoform 14 (CD2-5) [UniParc].

Checksum: 8A4A6FECF06B3883
Show »

FASTA33437,309
Isoform 15 (CD2-6) [UniParc].

Checksum: 0E288A38E5D417FF
Show »

FASTA65073,340
Isoform 16 (CD2-7) [UniParc].

Checksum: FFC3D62480CD3DED
Show »

FASTA71980,894
Isoform 17 (CD2-8) [UniParc].

Checksum: 56619B194F1C4501
Show »

FASTA981109,606
Isoform 18 (CD3-1) [UniParc].

Checksum: 820F564D0CF70A21
Show »

FASTA1,682186,541
Isoform 19 (CD3-2) [UniParc].

Checksum: 2823260AD289185F
Show »

FASTA1,677185,819
Isoform 20 (CD3-3) [UniParc].

Checksum: 58702C92B3B8A8B1
Show »

FASTA41546,543
Isoform 21 (SI-1) [UniParc].

Checksum: 694D3FBB2455620D
Show »

FASTA1,176129,853
Isoform 22 (SI-2) [UniParc].

Checksum: F1F9A2CAA115DEA2
Show »

FASTA1,171129,132
Isoform 23 (SI-3) [UniParc].

Checksum: E3300DA7C9F333FB
Show »

FASTA65072,054
Isoform 24 (C) [UniParc].

Checksum: 5047B631063401AD
Show »

FASTA1,363149,922
Isoform 25 [UniParc].

Checksum: EE3878002ED66B31
Show »

FASTA1,781198,072
Isoform 26 [UniParc].

Checksum: 924FA442271BE3F4
Show »

FASTA1,677185,901

References

« Hide 'large scale' references
[1]"The mouse Ames waltzer hearing-loss mutant is caused by mutation of Pcdh15, a novel protocadherin gene."
Alagramam K.N., Murcia C.L., Kwon H.Y., Pawlowski K.S., Wright C.G., Woychik R.P.
Nat. Genet. 27:99-102(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Ames Waltzer deaf mice have reduced electroretinogram amplitudes and complex alternative splicing of Pcdh15 transcripts."
Haywood-Watson R.J. II, Ahmed Z.M., Kjellstrom S., Bush R.A., Takada Y., Hampton L.L., Battey J.F., Sieving P.A., Friedman T.B.
Invest. Ophthalmol. Vis. Sci. 47:3074-3084(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 24), TISSUE SPECIFICITY.
Tissue: Retina.
[3]"The tip-link antigen, a protein associated with the transduction complex of sensory hair cells, is protocadherin-15."
Ahmed Z.M., Goodyear R., Riazuddin S., Lagziel A., Legan P.K., Behra M., Burgess S.M., Lilley K.S., Wilcox E.R., Riazuddin S., Griffith A.J., Frolenkov G.I., Belyantseva I.A., Richardson G.P., Friedman T.B.
J. Neurosci. 26:7022-7034(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7; 8; 9; 10; 11; 12; 13; 14; 15; 16; 17; 18; 19; 20; 21; 22 AND 23), DEVELOPMENTAL STAGE.
Strain: C57BL/6J.
Tissue: Inner ear.
[4]"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] (ISOFORM 21), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1763-1943 (ISOFORMS 1/2/4/5/6/7/8/9).
Strain: C57BL/6J.
Tissue: Cerebellum.
[5]"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.
[6]"Usher type 1G protein sans is a critical component of the tip-link complex, a structure controlling actin polymerization in stereocilia."
Caberlotto E., Michel V., Foucher I., Bahloul A., Goodyear R.J., Pepermans E., Michalski N., Perfettini I., Alegria-Prevot O., Chardenoux S., Do Cruzeiro M., Hardelin J.P., Richardson G.P., Avan P., Weil D., Petit C.
Proc. Natl. Acad. Sci. U.S.A. 108:5825-5830(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1368-1943 (ISOFORMS 25 AND 26), INTERACTION WITH USH1G, SUBCELLULAR LOCATION.
Strain: Swiss.
Tissue: Cochlea.
[7]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1876-1882, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[8]"Expression of Pcdh15 in the inner ear, nervous system and various epithelia of the developing embryo."
Murcia C.L., Woychik R.P.
Mech. Dev. 105:163-166(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"Physical and functional interaction between protocadherin 15 and myosin VIIa in mechanosensory hair cells."
Senften M., Schwander M., Kazmierczak P., Lillo C., Shin J.B., Hasson T., Geleoc G.S., Gillespie P.G., Williams D., Holt J.R., Muller U.
J. Neurosci. 26:2060-2071(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYO7A, TISSUE SPECIFICITY.
[10]"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 CDH23, TISSUE SPECIFICITY.
[11]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[12]"TMHS is an integral component of the mechanotransduction machinery of cochlear hair cells."
Xiong W., Grillet N., Elledge H.M., Wagner T.F., Zhao B., Johnson K.R., Kazmierczak P., Muller U.
Cell 151:1283-1295(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LHFPL5.
[13]"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 27-259 IN COMPLEX WITH CALCIUM IONS AND CDH23, SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF ILE-48 AND ARG-139.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF281899 mRNA. Translation: AAG53891.1.
AY949849 mRNA. Translation: AAY24693.1.
DQ354396 mRNA. Translation: ABC79259.1.
DQ354397 mRNA. Translation: ABC79260.1.
DQ354398 mRNA. Translation: ABC79261.1.
DQ354399 mRNA. Translation: ABC79262.1.
DQ354400 mRNA. Translation: ABC79263.1.
DQ354401 mRNA. Translation: ABC79264.1.
DQ354402 mRNA. Translation: ABC79265.1.
DQ354403 mRNA. Translation: ABC79266.1.
DQ354404 mRNA. Translation: ABC79267.1.
DQ354405 mRNA. Translation: ABC79268.1.
DQ354406 mRNA. Translation: ABC79269.1.
DQ354407 mRNA. Translation: ABC79270.1.
DQ354408 mRNA. Translation: ABC79271.1.
DQ354409 mRNA. Translation: ABC79272.1.
DQ354410 mRNA. Translation: ABC79273.1.
DQ354411 mRNA. Translation: ABC79274.1.
DQ354412 mRNA. Translation: ABC79275.1.
DQ354413 mRNA. Translation: ABC79276.1.
DQ354414 mRNA. Translation: ABC79277.1.
DQ354415 mRNA. Translation: ABC79278.1.
DQ354416 mRNA. Translation: ABC79279.1.
DQ354417 mRNA. Translation: ABC79280.1.
DQ354418 mRNA. Translation: ABC79281.1.
AK139154 mRNA. Translation: BAE23903.1.
AK141024 mRNA. Translation: BAE24546.1.
AC108392 Genomic DNA. No translation available.
AC119894 Genomic DNA. No translation available.
AC121142 Genomic DNA. No translation available.
AC121602 Genomic DNA. No translation available.
AC121832 Genomic DNA. No translation available.
AC123032 Genomic DNA. No translation available.
AC123809 Genomic DNA. No translation available.
AC144802 Genomic DNA. No translation available.
AC147721 Genomic DNA. No translation available.
AC153858 Genomic DNA. No translation available.
AC158800 Genomic DNA. No translation available.
AC159477 Genomic DNA. No translation available.
AC186813 Genomic DNA. No translation available.
AC188091 Genomic DNA. No translation available.
CAAA01110489 Genomic DNA. No translation available.
HQ404375 mRNA. Translation: ADP09331.1.
HQ420254 mRNA. Translation: ADT91308.1.
RefSeqNP_001136207.1. NM_001142735.1.
NP_001136208.1. NM_001142736.1.
NP_001136209.1. NM_001142737.1.
NP_001136210.1. NM_001142738.1.
NP_001136211.1. NM_001142739.1.
NP_001136212.1. NM_001142740.1.
NP_001136213.1. NM_001142741.1.
NP_001136214.1. NM_001142742.1.
NP_001136215.1. NM_001142743.1.
NP_001136218.1. NM_001142746.1.
NP_001136219.1. NM_001142747.1.
NP_001136220.1. NM_001142748.1.
NP_001136232.1. NM_001142760.1.
NP_075604.2. NM_023115.3.
XP_006513206.1. XM_006513143.1.
XP_006513207.1. XM_006513144.1.
XP_006513208.1. XM_006513145.1.
XP_006513209.1. XM_006513146.1.
XP_006513210.1. XM_006513147.1.
XP_006513213.1. XM_006513150.1.
XP_006513219.1. XM_006513156.1.
UniGeneMm.338933.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4APXX-ray1.65B27-259[»]
4AQ8X-ray2.63C/D27-259[»]
4AQAX-ray1.96B27-259[»]
4AQEX-ray2.27B27-259[»]
4AXWX-ray2.23B27-259[»]
ProteinModelPortalQ99PJ1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198282. 3 interactions.
DIPDIP-42151N.
IntActQ99PJ1. 2 interactions.
MINTMINT-1895732.
STRING10090.ENSMUSP00000101066.

PTM databases

PhosphoSiteQ99PJ1.

Proteomic databases

PRIDEQ99PJ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000092420; ENSMUSP00000090076; ENSMUSG00000052613. [Q99PJ1-6]
ENSMUST00000105424; ENSMUSP00000101064; ENSMUSG00000052613. [Q99PJ1-2]
ENSMUST00000105426; ENSMUSP00000101066; ENSMUSG00000052613. [Q99PJ1-1]
ENSMUST00000105429; ENSMUSP00000101069; ENSMUSG00000052613. [Q99PJ1-5]
ENSMUST00000125006; ENSMUSP00000120056; ENSMUSG00000052613. [Q99PJ1-22]
ENSMUST00000125055; ENSMUSP00000114326; ENSMUSG00000052613. [Q99PJ1-3]
ENSMUST00000125517; ENSMUSP00000115399; ENSMUSG00000052613. [Q99PJ1-16]
ENSMUST00000126920; ENSMUSP00000121939; ENSMUSG00000052613. [Q99PJ1-8]
ENSMUST00000129404; ENSMUSP00000117731; ENSMUSG00000052613. [Q99PJ1-9]
ENSMUST00000131321; ENSMUSP00000122911; ENSMUSG00000052613. [Q99PJ1-4]
ENSMUST00000131724; ENSMUSP00000122466; ENSMUSG00000052613. [Q99PJ1-11]
ENSMUST00000134009; ENSMUSP00000120618; ENSMUSG00000052613. [Q99PJ1-23]
ENSMUST00000136096; ENSMUSP00000121534; ENSMUSG00000052613. [Q99PJ1-3]
ENSMUST00000144302; ENSMUSP00000122606; ENSMUSG00000052613. [Q99PJ1-13]
ENSMUST00000146682; ENSMUSP00000134863; ENSMUSG00000052613. [Q99PJ1-20]
ENSMUST00000147189; ENSMUSP00000122940; ENSMUSG00000052613. [Q99PJ1-7]
ENSMUST00000149977; ENSMUSP00000118833; ENSMUSG00000052613. [Q99PJ1-19]
ENSMUST00000151116; ENSMUSP00000119662; ENSMUSG00000052613. [Q99PJ1-10]
ENSMUST00000152655; ENSMUSP00000118201; ENSMUSG00000052613. [Q99PJ1-17]
ENSMUST00000152819; ENSMUSP00000123647; ENSMUSG00000052613. [Q99PJ1-15]
ENSMUST00000155701; ENSMUSP00000135495; ENSMUSG00000052613. [Q99PJ1-14]
ENSMUST00000177107; ENSMUSP00000135501; ENSMUSG00000052613. [Q99PJ1-18]
ENSMUST00000177420; ENSMUSP00000135849; ENSMUSG00000052613. [Q99PJ1-21]
GeneID11994.
KEGGmmu:11994.
UCSCuc007fpf.2. mouse.
uc007fpg.2. mouse.
uc007fpo.2. mouse.
uc007fpq.2. mouse.
uc011xfz.1. mouse.
uc011xgd.1. mouse.
uc011xge.1. mouse.
uc011xgf.1. mouse.

Organism-specific databases

CTD65217.
MGIMGI:1891428. Pcdh15.

Phylogenomic databases

eggNOGNOG253862.
GeneTreeENSGT00750000117340.
HOGENOMHOG000230919.
HOVERGENHBG053521.
InParanoidQ99PJ1.
KOK16500.
OMAELNPIVV.
OrthoDBEOG7ZWD0W.
TreeFamTF326779.

Gene expression databases

CleanExMM_PCDH15.
GenevestigatorQ99PJ1.

Family and domain databases

Gene3D2.60.40.60. 10 hits.
InterProIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
[Graphical view]
PfamPF00028. Cadherin. 8 hits.
[Graphical view]
PRINTSPR00205. CADHERIN.
SMARTSM00112. CA. 11 hits.
[Graphical view]
SUPFAMSSF49313. SSF49313. 10 hits.
PROSITEPS00232. CADHERIN_1. 4 hits.
PS50268. CADHERIN_2. 11 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio280177.
PROQ99PJ1.
SOURCESearch...

Entry information

Entry namePCD15_MOUSE
AccessionPrimary (citable) accession number: Q99PJ1
Secondary accession number(s): D6RCH0 expand/collapse secondary AC list , E9Q7D7, E9Q7R1, E9Q7R2, F6KJX4, F6KKG6, F6R5Z7, F6RBV2, F6U3Q6, F6UPC9, F6VPR3, F6WUN7, F6X715, F6XPA1, F6Y0A5, F6YP25, F6YZQ9, F7ASH0, F7CIN1, F7D5J8, F7DFU0, F8VQ61, H3BKS0, Q0ZM15, Q0ZM16, Q0ZM18, Q0ZM19, Q0ZM20, Q0ZM21, Q0ZM22, Q0ZM23, Q0ZM24, Q0ZM25, Q0ZM26, Q0ZM27, Q0ZM28, Q0ZM29, Q0ZM30, Q0ZM31, Q0ZM32, Q0ZM33, Q0ZM34, Q0ZM35, Q0ZM37, Q2VQG7, Q3URZ1, Q3UTS7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: June 26, 2013
Last modified: April 16, 2014
This is version 110 of the entry and version 3 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