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Protein

Cadherin-2

Gene

Cdh2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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; cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence (PubMed:24952463). CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi262Calcium 11 Publication1
Metal bindingi262Calcium 21 Publication1
Metal bindingi293Calcium 31 Publication1

GO - Molecular functioni

  • alpha-catenin binding Source: MGI
  • calcium ion binding Source: InterPro
  • enzyme binding Source: UniProtKB
  • gamma-catenin binding Source: MGI
  • protein phosphatase binding Source: UniProtKB

GO - Biological processi

  • blood vessel morphogenesis Source: MGI
  • brain morphogenesis Source: MGI
  • calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules Source: MGI
  • cell adhesion Source: MGI
  • cell-cell adhesion mediated by cadherin Source: UniProtKB
  • cell migration Source: MGI
  • cerebral cortex development Source: MGI
  • establishment of protein localization to plasma membrane Source: UniProtKB
  • glial cell differentiation Source: UniProtKB
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: MGI
  • homeostasis of number of cells Source: MGI
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: MGI
  • negative regulation of canonical Wnt signaling pathway Source: MGI
  • neuroepithelial cell differentiation Source: MGI
  • neuroligin clustering involved in postsynaptic membrane assembly Source: BHF-UCL
  • neuronal stem cell population maintenance Source: UniProtKB
  • positive regulation of MAPK cascade Source: MGI
  • positive regulation of synaptic vesicle clustering Source: BHF-UCL
  • radial glial cell differentiation Source: MGI
  • regulation of oligodendrocyte progenitor proliferation Source: MGI
  • regulation of postsynaptic density protein 95 clustering Source: BHF-UCL
  • striated muscle cell differentiation Source: MGI
  • telencephalon development Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-375170. CDO in myogenesis.
R-MMU-418990. Adherens junctions interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin-2
Alternative name(s):
Neural cadherin
Short name:
N-cadherin
CD_antigen: CD325
Gene namesi
Name:Cdh2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:88355. Cdh2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini160 – 724ExtracellularSequence analysisAdd BLAST565
Transmembranei725 – 745HelicalSequence analysisAdd BLAST21
Topological domaini746 – 906CytoplasmicSequence analysisAdd BLAST161

GO - Cellular componenti

  • adherens junction Source: MGI
  • apical plasma membrane Source: MGI
  • basolateral plasma membrane Source: MGI
  • catenin complex Source: MGI
  • cell-cell adherens junction Source: MGI
  • cell-cell junction Source: MGI
  • cortical actin cytoskeleton Source: Ensembl
  • cytoplasm Source: MGI
  • dendrite Source: GOC-OWL
  • extracellular exosome Source: MGI
  • fascia adherens Source: MGI
  • focal adhesion Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • intercalated disc Source: UniProtKB
  • lamellipodium Source: MGI
  • membrane Source: MGI
  • plasma membrane Source: UniProtKB
  • plasma membrane raft Source: UniProtKB
  • presynaptic active zone Source: GOC-OWL
  • synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi262D → A: Abolishes dimerization. 1 Publication1
Mutagenesisi293D → A: Severely impaired the binding of calcium to all three sites. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
PropeptideiPRO_000000373326 – 159Sequence analysisAdd BLAST134
ChainiPRO_0000003734160 – 906Cadherin-2Add BLAST747

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi190N-linked (GlcNAc...)Sequence analysis1
Glycosylationi273N-linked (GlcNAc...)Sequence analysis1
Glycosylationi325N-linked (GlcNAc...)Sequence analysis1
Glycosylationi402N-linked (GlcNAc...)Sequence analysis1
Glycosylationi572N-linked (GlcNAc...)Sequence analysis1
Glycosylationi651N-linked (GlcNAc...)Sequence analysis1
Glycosylationi692N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Cleaved by MMP24. Ectodomain cleavage leads to the generation of a soluble 90 kDa amino-terminal soluble fragment and a 45 kDa membrane-bound carboxy-terminal fragment 1 (CTF1), which is further cleaved by gamma-secretase into a 35 kDa. Cleavage in neural stem cells by MMP24 affects CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate neural stem cell quiescence.2 Publications

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein

Proteomic databases

MaxQBiP15116.
PaxDbiP15116.
PeptideAtlasiP15116.
PRIDEiP15116.

PTM databases

iPTMnetiP15116.
PhosphoSitePlusiP15116.

Expressioni

Developmental stagei

Expressed at all stages of testicular development with highest levels found in testes of 21-day-old mice.1 Publication

Gene expression databases

BgeeiENSMUSG00000024304.
CleanExiMM_CDH2.
ExpressionAtlasiP15116. baseline and differential.
GenevisibleiP15116. MM.

Interactioni

Subunit structurei

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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PTPN1P180313EBI-397974,EBI-968788From a different organism.

GO - Molecular functioni

  • alpha-catenin binding Source: MGI
  • enzyme binding Source: UniProtKB
  • gamma-catenin binding Source: MGI
  • protein phosphatase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi198637. 20 interactors.
DIPiDIP-31564N.
IntActiP15116. 10 interactors.
MINTiMINT-4089694.
STRINGi10090.ENSMUSP00000025166.

Structurei

Secondary structure

1906
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 43Combined sources4
Beta strandi55 – 57Combined sources3
Beta strandi69 – 72Combined sources4
Beta strandi76 – 82Combined sources7
Turni83 – 85Combined sources3
Beta strandi86 – 91Combined sources6
Beta strandi96 – 98Combined sources3
Beta strandi100 – 108Combined sources9
Turni109 – 112Combined sources4
Beta strandi113 – 121Combined sources9
Beta strandi166 – 171Combined sources6
Beta strandi176 – 182Combined sources7
Helixi186 – 190Combined sources5
Beta strandi194 – 199Combined sources6
Turni200 – 202Combined sources3
Beta strandi203 – 206Combined sources4
Beta strandi209 – 212Combined sources4
Turni214 – 216Combined sources3
Beta strandi218 – 221Combined sources4
Turni227 – 229Combined sources3
Beta strandi232 – 240Combined sources9
Turni242 – 244Combined sources3
Beta strandi246 – 248Combined sources3
Beta strandi251 – 258Combined sources8
Beta strandi266 – 268Combined sources3
Beta strandi270 – 277Combined sources8
Beta strandi285 – 288Combined sources4
Helixi300 – 302Combined sources3
Beta strandi305 – 313Combined sources9
Beta strandi321 – 323Combined sources3
Turni325 – 327Combined sources3
Beta strandi329 – 332Combined sources4
Turni339 – 341Combined sources3
Beta strandi344 – 353Combined sources10
Helixi354 – 356Combined sources3
Turni358 – 360Combined sources3
Beta strandi363 – 373Combined sources11
Beta strandi381 – 394Combined sources14
Beta strandi396 – 406Combined sources11
Turni414 – 416Combined sources3
Beta strandi421 – 425Combined sources5
Beta strandi431 – 435Combined sources5
Turni437 – 439Combined sources3
Beta strandi441 – 446Combined sources6
Turni452 – 454Combined sources3
Beta strandi456 – 463Combined sources8
Beta strandi466 – 468Combined sources3
Helixi478 – 480Combined sources3
Beta strandi481 – 489Combined sources9
Beta strandi496 – 508Combined sources13
Beta strandi515 – 518Combined sources4
Beta strandi526 – 528Combined sources3
Beta strandi532 – 538Combined sources7
Beta strandi544 – 546Combined sources3
Turni548 – 550Combined sources3
Beta strandi552 – 557Combined sources6
Beta strandi561 – 563Combined sources3
Beta strandi568 – 579Combined sources12
Beta strandi581 – 583Combined sources3
Beta strandi586 – 596Combined sources11
Beta strandi604 – 606Combined sources3
Beta strandi621 – 623Combined sources3
Beta strandi633 – 636Combined sources4
Beta strandi638 – 640Combined sources3
Beta strandi643 – 645Combined sources3
Helixi646 – 651Combined sources6
Beta strandi652 – 656Combined sources5
Beta strandi658 – 660Combined sources3
Beta strandi662 – 666Combined sources5
Beta strandi674 – 683Combined sources10
Beta strandi685 – 688Combined sources4
Beta strandi691 – 700Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4NUMX-ray3.30A/B/C/D160-374[»]
4NUPX-ray2.70A/B/C162-374[»]
4NUQX-ray2.12A160-374[»]
ProteinModelPortaliP15116.
SMRiP15116.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15116.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini160 – 267Cadherin 1PROSITE-ProRule annotationAdd BLAST108
Domaini268 – 382Cadherin 2PROSITE-ProRule annotationAdd BLAST115
Domaini383 – 497Cadherin 3PROSITE-ProRule annotationAdd BLAST115
Domaini498 – 603Cadherin 4PROSITE-ProRule annotationAdd BLAST106
Domaini604 – 717Cadherin 5PROSITE-ProRule annotationAdd BLAST114

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi863 – 878Ser-richAdd BLAST16

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. Calcium-binding sites are occupied sequentially in the order of site 3, then site 2 and site 1.

Sequence similaritiesi

Contains 5 cadherin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
GeneTreeiENSGT00760000118906.
HOGENOMiHOG000231254.
HOVERGENiHBG106438.
InParanoidiP15116.
KOiK06736.
OMAiHSGHLQR.
OrthoDBiEOG091G01FV.
TreeFamiTF316817.

Family and domain databases

Gene3Di2.60.40.60. 6 hits.
4.10.900.10. 1 hit.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR014868. Cadherin_pro_dom.
IPR027397. Catenin_binding_dom.
IPR030051. CDH2.
[Graphical view]
PANTHERiPTHR24027:SF79. PTHR24027:SF79. 1 hit.
PfamiPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 5 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 6 hits.
PROSITEiPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P15116-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCRIAGAPRT LLPLLAALLQ ASVEASGEIA LCKTGFPEDV YSAVLPKDVH
60 70 80 90 100
EGQPLLNVKF SNCNRKRKVQ YESSEPADFK VDEDGTVYAV RSFPLTAEQA
110 120 130 140 150
KFLIYAQDKE TQEKWQVAVN LSREPTLTEE PMKEPHEIEE IVFPRQLAKH
160 170 180 190 200
SGALQRQKRD WVIPPINLPE NSRGPFPQEL VRIRSDRDKN LSLRYSVTGP
210 220 230 240 250
GADQPPTGIF IINPISGQLS VTKPLDRELI ARFHLRAHAV DINGNQVENP
260 270 280 290 300
IDIVINVIDM NDNRPEFLHQ VWNGSVPEGS KPGTYVMTVT AIDADDPNAL
310 320 330 340 350
NGMLRYRILS QAPSTPSPNM FTINNETGDI ITVAAGLDRE KVQQYTLIIQ
360 370 380 390 400
ATDMEGNPTY GLSNTATAVI TVTDVNDNPP EFTAMTFYGE VPENRVDVIV
410 420 430 440 450
ANLTVTDKDQ PHTPAWNAAY RISGGDPTGR FAILTDPNSN DGLVTVVKPI
460 470 480 490 500
DFETNRMFVL TVAAENQVPL AKGIQHPPQS TATVSVTVID VNENPYFAPN
510 520 530 540 550
PKIIRQEEGL HAGTMLTTLT AQDPDRYMQQ NIRYTKLSDP ANWLKIDPVN
560 570 580 590 600
GQITTIAVLD RESPNVKNNI YNATFLASDN GIPPMSGTGT LQIYLLDIND
610 620 630 640 650
NAPQVLPQEA ETCETPEPNS INITALDYDI DPNAGPFAFD LPLSPVTIKR
660 670 680 690 700
NWTINRLNGD FAQLNLKIKF LEAGIYEVPI IITDSGNPPK SNISILRVKV
710 720 730 740 750
CQCDSNGDCT DVDRIVGAGL GTGAIIAILL CIIILLILVL MFVVWMKRRD
760 770 780 790 800
KERQAKQLLI DPEDDVRDNI LKYDEEGGGE EDQDYDLSQL QQPDTVEPDA
810 820 830 840 850
IKPVGIRRLD ERPIHAEPQY PVRSAAPHPG DIGDFINEGL KAADNDPTAP
860 870 880 890 900
PYDSLLVFDY EGSGSTAGSL SSLNSSSSGG DQDYDYLNDW GPRFKKLADM

YGGGDD
Length:906
Mass (Da):99,796
Last modified:July 27, 2011 - v2
Checksum:iBDAB8063A23E1F13
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti7 – 9APR → GRG in AAA37353 (PubMed:2762814).Curated3
Sequence conflicti565 – 567NVK → YVQ in AAA37353 (PubMed:2762814).Curated3
Sequence conflicti624T → A in AAA37353 (PubMed:2762814).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29076.1.
PIRiA32759. IJMSCN.
RefSeqiNP_031690.3. NM_007664.5.
UniGeneiMm.257437.

Genome annotation databases

EnsembliENSMUST00000025166; ENSMUSP00000025166; ENSMUSG00000024304.
GeneIDi12558.
KEGGimmu:12558.
UCSCiuc008edx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29076.1.
PIRiA32759. IJMSCN.
RefSeqiNP_031690.3. NM_007664.5.
UniGeneiMm.257437.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4NUMX-ray3.30A/B/C/D160-374[»]
4NUPX-ray2.70A/B/C162-374[»]
4NUQX-ray2.12A160-374[»]
ProteinModelPortaliP15116.
SMRiP15116.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198637. 20 interactors.
DIPiDIP-31564N.
IntActiP15116. 10 interactors.
MINTiMINT-4089694.
STRINGi10090.ENSMUSP00000025166.

PTM databases

iPTMnetiP15116.
PhosphoSitePlusiP15116.

Proteomic databases

MaxQBiP15116.
PaxDbiP15116.
PeptideAtlasiP15116.
PRIDEiP15116.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025166; ENSMUSP00000025166; ENSMUSG00000024304.
GeneIDi12558.
KEGGimmu:12558.
UCSCiuc008edx.2. mouse.

Organism-specific databases

CTDi1000.
MGIiMGI:88355. Cdh2.

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
GeneTreeiENSGT00760000118906.
HOGENOMiHOG000231254.
HOVERGENiHBG106438.
InParanoidiP15116.
KOiK06736.
OMAiHSGHLQR.
OrthoDBiEOG091G01FV.
TreeFamiTF316817.

Enzyme and pathway databases

ReactomeiR-MMU-375170. CDO in myogenesis.
R-MMU-418990. Adherens junctions interactions.

Miscellaneous databases

EvolutionaryTraceiP15116.
PROiP15116.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024304.
CleanExiMM_CDH2.
ExpressionAtlasiP15116. baseline and differential.
GenevisibleiP15116. MM.

Family and domain databases

Gene3Di2.60.40.60. 6 hits.
4.10.900.10. 1 hit.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR014868. Cadherin_pro_dom.
IPR027397. Catenin_binding_dom.
IPR030051. CDH2.
[Graphical view]
PANTHERiPTHR24027:SF79. PTHR24027:SF79. 1 hit.
PfamiPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 5 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 6 hits.
PROSITEiPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCADH2_MOUSE
AccessioniPrimary (citable) accession number: P15116
Secondary accession number(s): Q64260, Q6GU11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 166 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

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 one 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.