Skip Header

Contribute Send feedback
Read comments (?) or add your own

P15116 (CADH2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 136. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cadherin-2
Alternative name(s):
Neural cadherin
Short name=N-cadherin
CD_antigen=CD325
Gene names
Name:Cdh2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length906 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density. Ref.7 Ref.8

Subunit structure

Interacts with CDCP1 By similarity. Interacts with PCDH8; this complex may also include TAOK2 By similarity. The interaction with PCDH8 may lead to internalization through TAOK2/p38 MAPK pathway. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Ref.7

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Developmental stage

Expressed at all stages of testicular development with highest levels found in testes of 21-day-old mice. Ref.6

Domain

Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain. Calcium-binding sites are occupied sequentially in the order of site 3, then site 2 and site 1.

Sequence similarities

Contains 5 cadherin domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   PTMCleavage on pair of basic residues
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood vessel morphogenesis

Inferred from mutant phenotype PubMed 15809310. Source: MGI

calcium-dependent cell-cell adhesion

Inferred from direct assay PubMed 14561752. Source: MGI

cell migration

Inferred from direct assay PubMed 14561752. Source: MGI

heterophilic cell-cell adhesion

Inferred from direct assay PubMed 8270638. Source: MGI

homophilic cell adhesion

Inferred from direct assay PubMed 14561752PubMed 8270638. Source: MGI

negative regulation of canonical Wnt receptor signaling pathway

Inferred from genetic interaction PubMed 19075000. Source: MGI

positive regulation of MAPK cascade

Inferred from genetic interaction PubMed 20160094. Source: MGI

striated muscle cell differentiation

Inferred from genetic interaction PubMed 20160094. Source: MGI

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 21947081. Source: MGI

catenin complex

Inferred from electronic annotation. Source: Compara

fascia adherens

Inferred from direct assay PubMed 11732910. Source: MGI

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lamellipodium

Inferred from direct assay PubMed 14657280. Source: MGI

synapse

Inferred from direct assay PubMed 14622577. Source: MGI

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PTPN1P180313EBI-397974,EBI-968788From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 159134 Potential
PRO_0000003733
Chain160 – 906747Cadherin-2
PRO_0000003734

Regions

Topological domain160 – 724565Extracellular Potential
Transmembrane725 – 74521Helical; Potential
Topological domain746 – 906161Cytoplasmic Potential
Domain160 – 267108Cadherin 1
Domain268 – 382115Cadherin 2
Domain383 – 497115Cadherin 3
Domain498 – 603106Cadherin 4
Domain604 – 717114Cadherin 5
Compositional bias863 – 87816Ser-rich

Sites

Metal binding2621Calcium 1
Metal binding2621Calcium 2
Metal binding2931Calcium 3

Amino acid modifications

Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation2731N-linked (GlcNAc...) Potential
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation4021N-linked (GlcNAc...) Potential
Glycosylation5721N-linked (GlcNAc...) Potential
Glycosylation6511N-linked (GlcNAc...) Potential
Glycosylation6921N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis2621D → A: Abolishes dimerization. Ref.9
Mutagenesis2931D → A: Severely impaired the binding of calcium to all three sites. Ref.9
Sequence conflict7 – 93APR → GRG in AAA37353. Ref.1
Sequence conflict565 – 5673NVK → YVQ in AAA37353. Ref.1
Sequence conflict6241T → A in AAA37353. Ref.1

Secondary structure

1 ...................................................................................................................................... 906
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P15116 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: BDAB8063A23E1F13

FASTA90699,796
        10         20         30         40         50         60 
MCRIAGAPRT LLPLLAALLQ ASVEASGEIA LCKTGFPEDV YSAVLPKDVH EGQPLLNVKF 

        70         80         90        100        110        120 
SNCNRKRKVQ YESSEPADFK VDEDGTVYAV RSFPLTAEQA KFLIYAQDKE TQEKWQVAVN 

       130        140        150        160        170        180 
LSREPTLTEE PMKEPHEIEE IVFPRQLAKH SGALQRQKRD WVIPPINLPE NSRGPFPQEL 

       190        200        210        220        230        240 
VRIRSDRDKN LSLRYSVTGP GADQPPTGIF IINPISGQLS VTKPLDRELI ARFHLRAHAV 

       250        260        270        280        290        300 
DINGNQVENP IDIVINVIDM NDNRPEFLHQ VWNGSVPEGS KPGTYVMTVT AIDADDPNAL 

       310        320        330        340        350        360 
NGMLRYRILS QAPSTPSPNM FTINNETGDI ITVAAGLDRE KVQQYTLIIQ ATDMEGNPTY 

       370        380        390        400        410        420 
GLSNTATAVI TVTDVNDNPP EFTAMTFYGE VPENRVDVIV ANLTVTDKDQ PHTPAWNAAY 

       430        440        450        460        470        480 
RISGGDPTGR FAILTDPNSN DGLVTVVKPI DFETNRMFVL TVAAENQVPL AKGIQHPPQS 

       490        500        510        520        530        540 
TATVSVTVID VNENPYFAPN PKIIRQEEGL HAGTMLTTLT AQDPDRYMQQ NIRYTKLSDP 

       550        560        570        580        590        600 
ANWLKIDPVN GQITTIAVLD RESPNVKNNI YNATFLASDN GIPPMSGTGT LQIYLLDIND 

       610        620        630        640        650        660 
NAPQVLPQEA ETCETPEPNS INITALDYDI DPNAGPFAFD LPLSPVTIKR NWTINRLNGD 

       670        680        690        700        710        720 
FAQLNLKIKF LEAGIYEVPI IITDSGNPPK SNISILRVKV CQCDSNGDCT DVDRIVGAGL 

       730        740        750        760        770        780 
GTGAIIAILL CIIILLILVL MFVVWMKRRD KERQAKQLLI DPEDDVRDNI LKYDEEGGGE 

       790        800        810        820        830        840 
EDQDYDLSQL QQPDTVEPDA IKPVGIRRLD ERPIHAEPQY PVRSAAPHPG DIGDFINEGL 

       850        860        870        880        890        900 
KAADNDPTAP PYDSLLVFDY EGSGSTAGSL SSLNSSSSGG DQDYDYLNDW GPRFKKLADM 


YGGGDD

« Hide

References

« Hide 'large scale' references
[1]"Neural cadherin: role in selective cell-cell adhesion."
Miyatani S., Shimamura K., Hatta M., Nagafuchi A., Nose A., Matsunaga M., Hatta K., Takeichi M.
Science 245:631-635(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Tamura K.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Genomic structure and chromosomal mapping of the mouse N-cadherin gene."
Miyatani S., Copeland N.G., Gilbert D.J., Jenkins N.A., Takeichi M.
Proc. Natl. Acad. Sci. U.S.A. 89:8443-8447(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: C57BL/6.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Strain: FVB/N.
Tissue: Liver.
[6]"A comprehensive survey of the cadherins expressed in the testes of fetal, immature, and adult mice utilizing the polymerase chain reaction."
Munro S.B., Blaschuk O.W.
Biol. Reprod. 55:822-827(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
Strain: C57BL/6.
Tissue: Testis.
[7]"N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-receptor signalling."
Cavallaro U., Niedermeyer J., Fuxa M., Christofori G.
Nat. Cell Biol. 3:650-657(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH FGFR4; PLCG1; FRS2; SRC; GAP43 AND CTTN.
[8]"Activity-induced protocadherin arcadlin regulates dendritic spine number by triggering N-cadherin endocytosis via TAO2beta and p38 MAP kinases."
Yasuda S., Tanaka H., Sugiura H., Okamura K., Sakaguchi T., Tran U., Takemiya T., Mizoguchi A., Yagita Y., Sakurai T., De Robertis E.M., Yamagata K.
Neuron 56:456-471(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PCDH8-MEDIATED ENDOCYTOSIS.
[9]"Sequential binding of calcium leads to dimerization in neural cadherin."
Vunnam N., Pedigo S.
Biochemistry 50:2973-2982(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: CALCIUM-BINDING SITES, MUTAGENESIS OF ASP-262 AND ASP-293.
[10]"Structural basis of cell-cell adhesion by cadherins."
Shapiro L., Fannon A.M., Kwong P.D., Thompson A., Lehmann M.S., Gruebel G., Legrand J.-F., Als-Nielsen J., Colman D.R., Hendrickson W.A.
Nature 374:327-337(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 160-267.
[11]"Structure-function analysis of cell adhesion by neural (N-) cadherin."
Tamura K., Shan W.S., Hendrickson W.A., Colman D.R., Shapiro L.
Neuron 20:1153-1163(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 160-374.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M31131 mRNA. Translation: AAA37353.1.
AB008811 mRNA. Translation: BAA23549.1.
S45011 Genomic DNA. Translation: AAB23356.1.
CH466557 Genomic DNA. Translation: EDK96930.1.
BC022107 mRNA. Translation: AAH22107.1.
IPIIPI00323134.
PIRIJMSCN. A32759.
RefSeqNP_031690.3. NM_007664.4.
UniGeneMm.257437.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NCGX-ray2.10A160-267[»]
1NCHX-ray2.10A/B160-267[»]
1NCIX-ray2.10A/B160-267[»]
1NCJX-ray3.40A160-374[»]
1OP4NMR-A24-159[»]
2QVIX-ray3.01A160-374[»]
3Q2WX-ray3.20A160-712[»]
ProteinModelPortalP15116.
SMRP15116. Positions 24-701, 818-904.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-31564N.
IntActP15116. 7 interactions.

PTM databases

PhosphoSiteP15116.

Proteomic databases

PaxDbP15116.
PRIDEP15116.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025166; ENSMUSP00000025166; ENSMUSG00000024304.
GeneID12558.
KEGGmmu:12558.

Organism-specific databases

CTD1000.
MGIMGI:88355. Cdh2.

Phylogenomic databases

eggNOGNOG251747.
GeneTreeENSGT00700000104413.
HOGENOMHOG000231254.
HOVERGENHBG106438.
InParanoidQ6GU11.
KOK06736.
OMAHSGHLQR.
OrthoDBEOG483D43.

Gene expression databases

ArrayExpressP15116.
BgeeP15116.
CleanExMM_CDH2.
GenevestigatorP15116.
GermOnlineENSMUSG00000024304. Mus musculus.

Family and domain databases

Gene3D2.60.40.60. 6 hits.
InterProIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR009124. Cadherin/Desmocollin.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR014868. Cadherin_pro_dom.
[Graphical view]
PfamPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]
PRINTSPR00205. CADHERIN.
PR01820. DESMOCOLLIN.
SMARTSM00112. CA. 5 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]
SUPFAMSSF49313. Cadherin. 6 hits.
PROSITEPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP15116.
NextBio281622.
SOURCESearch...

Entry information

Entry nameCADH2_MOUSE
AccessionPrimary (citable) accession number: P15116
Secondary accession number(s): Q64260, Q6GU11
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents