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Protein

Cadherin-15

Gene

Cdh15

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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; cadherins may thus contribute to the sorting of heterogeneous cell types. M-cadherin is part of the myogenic program and may provide a trigger for terminal muscle differentiation.

GO - Molecular functioni

  1. calcium ion binding Source: InterPro

GO - Biological processi

  1. homophilic cell adhesion via plasma membrane adhesion molecules Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_304595. CDO in myogenesis.
REACT_308832. Adherens junctions interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin-15
Alternative name(s):
Cadherin-14
Muscle cadherin
Short name:
M-cadherin
Gene namesi
Name:Cdh15
Synonyms:Cdh14
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:106672. Cdh15.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini60 – 605546ExtracellularSequence AnalysisAdd
BLAST
Transmembranei606 – 62520HelicalSequence AnalysisAdd
BLAST
Topological domaini626 – 784159CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. caveola Source: MGI
  2. extracellular vesicular exosome Source: MGI
  3. integral component of membrane Source: UniProtKB-KW
  4. neuromuscular junction Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Propeptidei22 – 5938Sequence AnalysisPRO_0000003807Add
BLAST
Chaini60 – 784725Cadherin-15PRO_0000003808Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi106 – 1061N-linked (GlcNAc...)1 Publication
Glycosylationi226 – 2261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi530 – 5301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi537 – 5371N-linked (GlcNAc...)1 Publication
Glycosylationi575 – 5751N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein

Proteomic databases

PaxDbiP33146.
PRIDEiP33146.

PTM databases

PhosphoSiteiP33146.

Expressioni

Tissue specificityi

Skeletal muscle.

Gene expression databases

BgeeiP33146.
CleanExiMM_CDH15.
GenevestigatoriP33146.

Interactioni

Protein-protein interaction databases

BioGridi198634. 2 interactions.
STRINGi10090.ENSMUSP00000034443.

Structurei

3D structure databases

SMRiP33146. Positions 46-467, 698-780.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini60 – 15192Cadherin 1PROSITE-ProRule annotationAdd
BLAST
Domaini152 – 259108Cadherin 2PROSITE-ProRule annotationAdd
BLAST
Domaini260 – 374115Cadherin 3PROSITE-ProRule annotationAdd
BLAST
Domaini375 – 480106Cadherin 4PROSITE-ProRule annotationAdd
BLAST
Domaini481 – 589109Cadherin 5PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi745 – 75612Ser-richAdd
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

Sequence similaritiesi

Contains 5 cadherin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG306443.
GeneTreeiENSGT00760000118906.
HOGENOMiHOG000231254.
HOVERGENiHBG106438.
InParanoidiP33146.
KOiK06809.
OMAiWVARFTI.
OrthoDBiEOG7RJPQM.
TreeFamiTF316817.

Family and domain databases

Gene3Di2.60.40.60. 4 hits.
4.10.900.10. 1 hit.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR027397. Catenin_binding_dom.
[Graphical view]
PfamiPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 4 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 5 hits.
PROSITEiPS00232. CADHERIN_1. 2 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P33146-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSALLLALG LLAQSLGLSW AVPEPKPSTL YPWRRASAPG RVRRAWVIPP
60 70 80 90 100
ISVSENHKRL PYPLVQIKSD KQQLGSVIYS IQGPGVDEEP RNVFSIDKFT
110 120 130 140 150
GRVYLNATLD REKTDRFRLR AFALDLGGST LEDPTDLEIV VVDQNDNRPA
160 170 180 190 200
FLQDVFRGRI LEGAIPGTFV TRAEATDADD PETDNAALRF SILEQGSPEF
210 220 230 240 250
FSIDEHTGEI RTVQVGLDRE VVAVYNLTLQ VADMSGDGLT ATASAIISID
260 270 280 290 300
DINDNAPEFT KDEFFMEAAE AVSGVDVGRL EVEDKDLPGS PNWVARFTIL
310 320 330 340 350
EGDPDGQFKI YTDPKTNEGV LSVVKPLDYE SREQYELRVS VQNEAPLQAA
360 370 380 390 400
APRARRGQTR VSVWVQDTNE APVFPENPLR TSIAEGAPPG TSVATFSARD
410 420 430 440 450
PDTEQLQRIS YSKDYDPEDW LQVDGATGRI QTQRVLSPAS PFLKDGWYRA
460 470 480 490 500
IILALDNAIP PSTATGTLSI EILEVNDHAP ALALPPSGSL CSEPDQGPGL
510 520 530 540 550
LLGATDEDLP PHGAPFHFQL NPRVPDLGRN WSVSQINVSH ARLRLRHQVS
560 570 580 590 600
EGLHRLSLLL QDSGEPPQQR EQTLNVTVCR CGSDGTCLPG AAALRGGGVG
610 620 630 640 650
VSLGALVIVL ASTVVLLVLI LLAALRTRFR GHSRGKSLLH GLQEDLRDNI
660 670 680 690 700
LNYDEQGGGE EDQDAYDINQ LRHPVEPRAT SRSLGRPPLR RDAPFSYVPQ
710 720 730 740 750
PHRVLPTSPS DIANFISDGL EAADSDPSVP PYDTALIYDY EGDGSVAGTL
760 770 780
SSILSSLGDE DQDYDYLRDW GPRFARLADM YGHQ
Length:784
Mass (Da):85,644
Last modified:July 27, 2011 - v3
Checksum:iA21D73960A6F0063
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261K → E in AAC23585 (PubMed:1840697).Curated
Sequence conflicti159 – 1591R → H in AAC23585 (PubMed:1840697).Curated
Sequence conflicti622 – 6221L → F in AAC23585 (PubMed:1840697).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC157978 mRNA. Translation: AAI57979.1.
M74541 mRNA. Translation: AAC23585.1.
AJ245402 Genomic DNA. Translation: CAB57281.2.
CCDSiCCDS22746.1.
PIRiA40986. IJMSCM.
RefSeqiNP_031688.2. NM_007662.2.
UniGeneiMm.1976.

Genome annotation databases

EnsembliENSMUST00000034443; ENSMUSP00000034443; ENSMUSG00000031962.
GeneIDi12555.
KEGGimmu:12555.
UCSCiuc009ntv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC157978 mRNA. Translation: AAI57979.1.
M74541 mRNA. Translation: AAC23585.1.
AJ245402 Genomic DNA. Translation: CAB57281.2.
CCDSiCCDS22746.1.
PIRiA40986. IJMSCM.
RefSeqiNP_031688.2. NM_007662.2.
UniGeneiMm.1976.

3D structure databases

SMRiP33146. Positions 46-467, 698-780.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198634. 2 interactions.
STRINGi10090.ENSMUSP00000034443.

PTM databases

PhosphoSiteiP33146.

Proteomic databases

PaxDbiP33146.
PRIDEiP33146.

Protocols and materials databases

DNASUi12555.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034443; ENSMUSP00000034443; ENSMUSG00000031962.
GeneIDi12555.
KEGGimmu:12555.
UCSCiuc009ntv.1. mouse.

Organism-specific databases

CTDi1013.
MGIiMGI:106672. Cdh15.

Phylogenomic databases

eggNOGiNOG306443.
GeneTreeiENSGT00760000118906.
HOGENOMiHOG000231254.
HOVERGENiHBG106438.
InParanoidiP33146.
KOiK06809.
OMAiWVARFTI.
OrthoDBiEOG7RJPQM.
TreeFamiTF316817.

Enzyme and pathway databases

ReactomeiREACT_304595. CDO in myogenesis.
REACT_308832. Adherens junctions interactions.

Miscellaneous databases

NextBioi281610.
PROiP33146.
SOURCEiSearch...

Gene expression databases

BgeeiP33146.
CleanExiMM_CDH15.
GenevestigatoriP33146.

Family and domain databases

Gene3Di2.60.40.60. 4 hits.
4.10.900.10. 1 hit.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR027397. Catenin_binding_dom.
[Graphical view]
PfamiPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 4 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 5 hits.
PROSITEiPS00232. CADHERIN_1. 2 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Link D.
    Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H.
    Tissue: Muscle.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "Expression of M-cadherin, a member of the cadherin multigene family, correlates with differentiation of skeletal muscle cells."
    Donalies M., Cramer M., Ringwald M., Starzinski-Powitz A.
    Proc. Natl. Acad. Sci. U.S.A. 88:8024-8028(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Muscle.
  4. "Identification of imprinted loci by methylation-sensitive representational difference analysis: application to mouse distal chromosome 2."
    Kelsey G., Bodle D., Miller H.J., Beechey C.V., Coombes C., Peters J., Williamson C.M.
    Genomics 62:129-138(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 539-617.
  5. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
    Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
    Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-106 AND ASN-537.
    Tissue: Myoblast.

Entry informationi

Entry nameiCAD15_MOUSE
AccessioniPrimary (citable) accession number: P33146
Secondary accession number(s): B2RXU1, Q9QYZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: July 27, 2011
Last modified: April 1, 2015
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.