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Q9Z1Y3 (CADH2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cadherin-2
Alternative name(s):
Neural cadherin
Short name=N-cadherin
CD_antigen=CD325
Gene names
Name:Cdh2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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 By similarity.

Subunit structure

Interacts with CDCP1. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN By similarity. Interacts with PCDH8; this complex may also include TAOK2. The interaction with PCDH8 may lead to internalization through TAOK2/p38 MAPK pathway. Ref.3

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Tissue specificity

In testis, expressed in Sertoli and germ cells. Ref.1

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 By similarity.

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 termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium-dependent cell-cell adhesion

Inferred from mutant phenotype PubMed 11414796. Source: RGD

homophilic cell adhesion

Inferred from electronic annotation. Source: InterPro

protein heterooligomerization

Inferred from physical interaction PubMed 8834786. Source: RGD

regulation of Rho protein signal transduction

Inferred from mutant phenotype PubMed 16515795. Source: RGD

regulation of axonogenesis

Inferred from mutant phenotype PubMed 12657688. Source: RGD

regulation of myelination

Inferred from mutant phenotype PubMed 11414796. Source: RGD

regulation of protein localization

Inferred from mutant phenotype PubMed 16515795. Source: RGD

synapse assembly

Inferred from mutant phenotype PubMed 12125071. Source: RGD

   Cellular_componentT-tubule

Inferred from direct assay PubMed 15579534. Source: BHF-UCL

fascia adherens

Inferred from direct assay PubMed 16515795. Source: RGD

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

protein complex

Inferred from direct assay PubMed 12533412. Source: RGD

synapse

Inferred from direct assay PubMed 18179895. Source: BHF-UCL

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 159134 Potential
PRO_0000003735
Chain160 – 906747Cadherin-2
PRO_0000003736

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 By similarity
Metal binding2621Calcium 2 By similarity
Metal binding2931Calcium 3 By similarity

Amino acid modifications

Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation2731N-linked (GlcNAc...) Potential
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation4021N-linked (GlcNAc...) Potential
Glycosylation5721N-linked (GlcNAc...) Potential
Glycosylation6221N-linked (GlcNAc...) Potential
Glycosylation6511N-linked (GlcNAc...) Potential
Glycosylation6921N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis7401L → P: Decrease in PCDH8-binding; alone or when associated with G-741. Ref.3
Mutagenesis7411M → G: Decrease in PCDH8-binding; when associated with P-740. Ref.3
Sequence conflict71G → A in BAA84919. Ref.2
Sequence conflict481T → D in BAA84919. Ref.2
Sequence conflict1531A → R in BAA84919. Ref.2
Sequence conflict6461A → V in BAA84919. Ref.2
Sequence conflict6581N → K in BAA84919. Ref.2
Sequence conflict7241T → A in BAA84919. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9Z1Y3 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 97D9937FD8D1F8B5

FASTA90699,686
        10         20         30         40         50         60 
MCRIAGGPRT LLPLLAALLQ ASLEASGELA LCKTGFPEDV YSAVLPKTVH EGQPLLNVKF 

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

       130        140        150        160        170        180 
LSLEPSLTEE 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 LPLSPATIKR NWTITRLNGD 

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

       730        740        750        760        770        780 
GTGTIIAILL 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

[1]"Rat testicular N-cadherin: its complementary deoxyribonucleic acid cloning and regulation."
Chung S.S., Mo M.Y., Silvestrini B., Lee W.M., Cheng C.Y.
Endocrinology 139:1853-1862(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Testis.
[2]"Rat N-cadherin cDNA."
Asai K., Tada T., Yamamoto M., Tada A., Mizuno M., Eimoto T., Kato T.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[3]"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: INTERACTION WITH PCDH8, MUTAGENESIS OF LEU-740 AND MET-741.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF097593 mRNA. Translation: AAC83818.1.
AB017695 mRNA. Translation: BAA84919.1.
IPIIPI00362131.
RefSeqNP_112623.1. NM_031333.1.
UniGeneRn.23200.

3D structure databases

ProteinModelPortalQ9Z1Y3.
SMRQ9Z1Y3. Positions 24-374, 836-901.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-48902N.

PTM databases

PhosphoSiteQ9Z1Y3.

Proteomic databases

PaxDbQ9Z1Y3.
PRIDEQ9Z1Y3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID83501.
KEGGrno:83501.

Organism-specific databases

CTD1000.
RGD69280. Cdh2.

Phylogenomic databases

eggNOGNOG251747.
HOGENOMHOG000231254.
HOVERGENHBG106438.
InParanoidQ9Z1Y3.
KOK06736.
OrthoDBEOG483D43.

Gene expression databases

ArrayExpressQ9Z1Y3.
GenevestigatorQ9Z1Y3.
GermOnlineENSRNOG00000015602. Rattus norvegicus.

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

NextBio615916.

Entry information

Entry nameCADH2_RAT
AccessionPrimary (citable) accession number: Q9Z1Y3
Secondary accession number(s): Q9R0T5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 1999
Last modified: May 1, 2013
This is version 99 of the entry and version 1 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

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