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P09803 (CADH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 160. 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

Names and origin

Protein namesRecommended name:
Cadherin-1
Alternative name(s):
ARC-1
Epithelial cadherin
Short name=E-cadherin
Uvomorulin
CD_antigen=CD324

Cleaved into the following 3 chains:

  1. E-Cad/CTF1
  2. E-Cad/CTF2
  3. E-Cad/CTF3
Gene names
Name:Cdh1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length884 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. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7 By similarity.

E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production By similarity.

Subunit structure

Homodimer; disulfide-linked. Component of an E-cadherin/ catenin adhesion complex composed of at least E-cadherin/CDH1, beta-catenin/CTNNB1 or gamma-catenin/JUP, and potentially alpha-catenin/CTNNA1; the complex is located to adherens junctions. The stable association of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-actin when assembled in the complex. Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1. Interaction with PSEN1, cleaves CDH1 resulting in the disassociation of cadherin-based adherens junctions (CAJs). Interacts with AJAP1, CTNND1 and DLGAP5 By similarity. Interacts with TBC1D2. Interacts with LIMA1. Interacts with CAV1 By similarity. Interacts with the TRPV4 and CTNNB1 complex. Interacts with PIP5K1C By similarity. Interacts with RAB8B. Interacts with DDR1; this stabilizes CDH1 at the cell surface and inhibits its internalization By similarity. Interacts with RAPGEF2 By similarity. Ref.5 Ref.9

Subcellular location

Cell junction. Cell membrane; Single-pass type I membrane protein. Endosome By similarity. Golgi apparatustrans-Golgi network By similarity. Note: Colocalizes with DLGAP5 at sites of cell-cell contact in intestinal epithelial cells. Anchored to actin microfilaments through association with alpha-, beta- and gamma-catenin. Sequential proteolysis induced by apoptosis or calcium influx, results in translocation from sites of cell-cell contact to the cytoplasm. Colocalizes with RAB11A endosomes during its transport from the Golgi apparatus to the plasma membrane By similarity.

Tissue specificity

Non-neural epithelial tissues.

Developmental stage

In the testis, expression is highest in fetal gonad, then decreases 5-fold in newborn. Detectable in 7-day-old but not in 21-day-old or adult. 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.

Post-translational modification

N-glycosylation at Asn-639 is essential for expression, folding and trafficking By similarity.

Ubiquitinated by a SCF complex containing SKP2, which requires prior phosphorylation by CK1/CSNK1A1. Ubiquitinated by CBLL1/HAKAI, requires prior phosphorylation at Tyr-756 By similarity.

Sequence similarities

Contains 5 cadherin domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Endosome
Golgi apparatus
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell-cell adhesion

Inferred from mutant phenotype PubMed 15148305PubMed 16368433. Source: MGI

cellular response to amino acid stimulus

Inferred from direct assay PubMed 20548288. Source: MGI

cellular response to indole-3-methanol

Inferred from electronic annotation. Source: Ensembl

cellular response to lithium ion

Inferred from electronic annotation. Source: Ensembl

cochlea development

Inferred from mutant phenotype PubMed 21925491. Source: MGI

epithelial cell morphogenesis

Inferred from mutant phenotype PubMed 22766025. Source: MGI

homophilic cell adhesion

Inferred from electronic annotation. Source: InterPro

in utero embryonic development

Inferred from mutant phenotype PubMed 15775979. Source: MGI

intestinal epithelial cell development

Inferred from mutant phenotype PubMed 22766025. Source: MGI

negative regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 22766025. Source: MGI

negative regulation of cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

negative regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 22766025. Source: MGI

neuron projection development

Inferred from electronic annotation. Source: Ensembl

pituitary gland development

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription factor import into nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from direct assay PubMed 12460580. Source: MGI

protein localization to plasma membrane

Inferred from electronic annotation. Source: Ensembl

protein metabolic process

Inferred from direct assay PubMed 12655059. Source: MGI

regulation of branching involved in salivary gland morphogenesis

Inferred from mutant phenotype PubMed 18816447. Source: MGI

regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 15192701. Source: MGI

regulation of neuron migration

Inferred from direct assay PubMed 23434913. Source: MGI

regulation of protein localization

Inferred from mutant phenotype PubMed 15775979. Source: MGI

regulation of protein localization to cell surface

Inferred from mutant phenotype PubMed 15775979. Source: MGI

regulation of water loss via skin

Inferred from mutant phenotype PubMed 15775979. Source: MGI

response to drug

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

salivary gland cavitation

Inferred from mutant phenotype PubMed 18816447. Source: MGI

sensory perception of sound

Inferred from mutant phenotype PubMed 21925491. Source: MGI

synapse assembly

Inferred from electronic annotation. Source: Ensembl

tight junction assembly

Inferred from mutant phenotype PubMed 15775979. Source: MGI

trophectodermal cell differentiation

Inferred from mutant phenotype PubMed 17138661. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

Schmidt-Lanterman incisure

Inferred from direct assay PubMed 20237282. Source: BHF-UCL

actin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

adherens junction

Inferred from direct assay PubMed 16275913. Source: UniProtKB

aggresome

Inferred from electronic annotation. Source: Ensembl

apical junction complex

Inferred from direct assay PubMed 17130295. Source: MGI

apical part of cell

Inferred from direct assay PubMed 14758363. Source: MGI

axon

Inferred from direct assay PubMed 17392463. Source: MGI

axon terminus

Inferred from direct assay PubMed 17392463. Source: MGI

basolateral plasma membrane

Inferred from direct assay PubMed 15788452PubMed 20016102PubMed 20089884PubMed 20551175PubMed 20637190PubMed 23266329. Source: MGI

catenin complex

Inferred from electronic annotation. Source: Ensembl

cell periphery

Inferred from direct assay PubMed 19289495. Source: MGI

cell surface

Inferred from direct assay PubMed 11511678. Source: MGI

cell-cell adherens junction

Inferred from direct assay PubMed 11706048PubMed 15292239PubMed 15630473PubMed 15788452PubMed 16510873PubMed 17544522PubMed 17666436PubMed 8582267. Source: MGI

cell-cell junction

Inferred from direct assay PubMed 11511678PubMed 15084279PubMed 15195140PubMed 17138661PubMed 18423437PubMed 18604197PubMed 18816447PubMed 20089884PubMed 20103531PubMed 21377456PubMed 21464233PubMed 21991325PubMed 9864371PubMed 9950951. Source: MGI

cytoplasmic side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

focal adhesion

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lateral loop

Inferred from direct assay PubMed 20237282. Source: BHF-UCL

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

node of Ranvier

Inferred from direct assay PubMed 20237282. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 11197537PubMed 12060406PubMed 15739225PubMed 15994295PubMed 16199027PubMed 16418220PubMed 16466397PubMed 16510873PubMed 18287078PubMed 18692037PubMed 19623612PubMed 20215345. Source: MGI

trans-Golgi network

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionbeta-catenin binding

Inferred from physical interaction PubMed 15057752. Source: MGI

calcium ion binding

Inferred from direct assay PubMed 12460580. Source: MGI

protein domain specific binding

Inferred from physical interaction PubMed 18794329. Source: MGI

protein phosphatase binding

Inferred from physical interaction PubMed 16973135. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Cdk5r1P618092EBI-984420,EBI-7840438
Ctnnb1Q0224813EBI-984420,EBI-397872
CTNND1O60716-293EBI-984420,EBI-702059From a different organism.
PTPRMP288273EBI-984420,EBI-2257317From a different organism.
SKP2Q133092EBI-984420,EBI-456291From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 156133 Potential
PRO_0000003717
Chain157 – 884728Cadherin-1
PRO_0000003718
Chain703 – 884182E-Cad/CTF1 Potential
PRO_0000236070
Chain734 – 884151E-Cad/CTF2 Potential
PRO_0000236071
Chain753 – 884132E-Cad/CTF3 Potential
PRO_0000236072

Regions

Topological domain157 – 709553Extracellular Potential
Transmembrane710 – 73324Helical; Potential
Topological domain734 – 884151Cytoplasmic Potential
Domain157 – 264108Cadherin 1
Domain265 – 377113Cadherin 2
Domain378 – 488111Cadherin 3
Domain489 – 595107Cadherin 4
Domain596 – 699104Cadherin 5
Region760 – 77112Required for binding CTNND1 and PSEN1 By similarity
Region813 – 88472Required for binding alpha, beta and gamma catenins By similarity
Compositional bias840 – 85516Ser-rich

Sites

Metal binding2591Calcium 1
Metal binding2591Calcium 2
Metal binding2901Calcium 3
Site702 – 7032Cleavage; by a metalloproteinase By similarity
Site733 – 7342Cleavage; by gamma-secretase/PS1 By similarity
Site752 – 7532Cleavage; by caspase-3 By similarity

Amino acid modifications

Modified residue7551Phosphotyrosine; by SRC By similarity
Modified residue7561Phosphotyrosine; by SRC By similarity
Modified residue7571Phosphotyrosine; by SRC By similarity
Modified residue8401Phosphoserine Ref.13
Modified residue8421Phosphoserine Ref.13
Modified residue8481Phosphoserine Ref.13
Glycosylation5601N-linked (GlcNAc...) Potential
Glycosylation6391N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2671E → P in CAA43292. Ref.2
Sequence conflict2721S → F in CAA43292. Ref.2

Secondary structure

..................................................................................................................................... 884
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09803 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 7A6444148D3D5983

FASTA88498,256
        10         20         30         40         50         60 
MGARCRSFSA LLLLLQVSSW LCQELEPESC SPGFSSEVYT FPVPERHLER GHVLGRVRFE 

        70         80         90        100        110        120 
GCTGRPRTAF FSEDSRFKVA TDGTITVKRH LKLHKLETSF LVRARDSSHR ELSTKVTLKS 

       130        140        150        160        170        180 
MGHHHHRHHH RDPASESNPE LLMFPSVYPG LRRQKRDWVI PPISCPENEK GEFPKNLVQI 

       190        200        210        220        230        240 
KSNRDKETKV FYSITGQGAD KPPVGVFIIE RETGWLKVTQ PLDREAIAKY ILYSHAVSSN 

       250        260        270        280        290        300 
GEAVEDPMEI VITVTDQNDN RPEFTQEVFE GSVAEGAVPG TSVMKVSATD ADDDVNTYNA 

       310        320        330        340        350        360 
AIAYTIVSQD PELPHKNMFT VNRDTGVISV LTSGLDRESY PTYTLVVQAA DLQGEGLSTT 

       370        380        390        400        410        420 
AKAVITVKDI NDNAPVFNPS TYQGQVPENE VNARIATLKV TDDDAPNTPA WKAVYTVVND 

       430        440        450        460        470        480 
PDQQFVVVTD PTTNDGILKT AKGLDFEAKQ QYILHVRVEN EEPFEGSLVP STATVTVDVV 

       490        500        510        520        530        540 
DVNEAPIFMP AERRVEVPED FGVGQEITSY TAREPDTFMD QKITYRIWRD TANWLEINPE 

       550        560        570        580        590        600 
TGAIFTRAEM DREDAEHVKN STYVALIIAT DDGSPIATGT GTLLLVLLDV NDNAPIPEPR 

       610        620        630        640        650        660 
NMQFCQRNPQ PHIITILDPD LPPNTSPFTA ELTHGASVNW TIEYNDAAQE SLILQPRKDL 

       670        680        690        700        710        720 
EIGEYKIHLK LADNQNKDQV TTLDVHVCDC EGTVNNCMKA GIVAAGLQVP AILGILGGIL 

       730        740        750        760        770        780 
ALLILILLLL LFLRRRTVVK EPLLPPDDDT RDNVYYYDEE GGGEEDQDFD LSQLHRGLDA 

       790        800        810        820        830        840 
RPEVTRNDVA PTLMSVPQYR PRPANPDEIG NFIDENLKAA DSDPTAPPYD SLLVFDYEGS 

       850        860        870        880 
GSEAASLSSL NSSESDQDQD YDYLNEWGNR FKKLADMYGG GEDD 

« Hide

References

[1]"Transformation of cell adhesion properties by exogenously introduced E-cadherin cDNA."
Nagafuchi A., Shirayoshi Y., Okazari K., Yasuda K., Takeichi M.
Nature 329:341-343(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ICR.
[2]"The structure of the gene coding for the mouse cell adhesion molecule uvomorulin."
Ringwald M., Baribault H., Schmidt C., Kemler R.
Nucleic Acids Res. 19:6533-6539(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[3]"The structure of cell adhesion molecule uvomorulin. Insights into the molecular mechanism of Ca2+-dependent cell adhesion."
Ringwald M., Schuh R., Vestweber D., Eistetter H., Lottspeich F., Engel J., Doelz R., Jaehnig F., Epplen J., Mayer S., Mueller C., Kemler R.
EMBO J. 6:3647-3653(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 174-884, PROTEIN SEQUENCE OF 157-181.
[4]"The E-cadherin promoter: functional analysis of a G.C-rich region and an epithelial cell-specific palindromic regulatory element."
Behrens J., Loewrick O., Klein-Hitpass L., Birchmeier W.
Proc. Natl. Acad. Sci. U.S.A. 88:11495-11499(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
[5]"Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell adhesion."
Butz S., Kemler R.
FEBS Lett. 355:195-200(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
[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]"Deconstructing the cadherin-catenin-actin complex."
Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.
Cell 123:889-901(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
[8]"EPLIN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt."
Abe K., Takeichi M.
Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
[9]"The TRPV4 channel contributes to intercellular junction formation in keratinocytes."
Sokabe T., Fukumi-Tominaga T., Yonemura S., Mizuno A., Tominaga M.
J. Biol. Chem. 285:18749-18758(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRPV4 AND CTNNB1.
[10]"Structural basis of calcium-induced E-cadherin rigidification and dimerization."
Nagar B., Overduin M., Ikura M., Rini J.M.
Nature 380:360-364(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 157-370, CALCIUM-BINDING SITES.
[11]"1H, 15N and 13C resonance assignments and monomeric structure of the amino-terminal extracellular domain of epithelial cadherin."
Overduin M., Tong K.I., Kay C.M., Ikura M.
J. Biomol. NMR 7:173-189(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 157-260.
[12]"The structure of the beta-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by beta-catenin."
Huber A.H., Weis W.I.
Cell 105:391-402(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 577-728 IN COMPLEX WITH CTNNB1, PHOSPHORYLATION.
[13]"Interactions of plakoglobin and beta-catenin with desmosomal cadherins: basis of selective exclusion of alpha- and beta-catenin from desmosomes."
Choi H.J., Gross J.C., Pokutta S., Weis W.I.
J. Biol. Chem. 284:31776-31788(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 778-884 IN COMPLEX WITH HUMAN JUP, PHOSPHORYLATION AT SER-840; SER-842 AND SER-848.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06115 mRNA. Translation: CAA29488.1.
X60961 expand/collapse EMBL AC list , X60962, X60963, X60964, X60965, X60966, X60967, X60968, X60969, X60970, X60971, X60972, X60973, X60974, X60975 Genomic DNA. Translation: CAA43292.1.
X06339 mRNA. Translation: CAA29645.1.
M81449 Genomic DNA. Translation: AAA37352.1.
PIRIJMSCE. S04528.
S34438.
RefSeqNP_033994.1. NM_009864.2.
UniGeneMm.35605.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EDHX-ray2.00A/B156-380[»]
1FF5X-ray2.93A/B157-374[»]
1I7WX-ray2.00B/D734-884[»]
1I7XX-ray3.00B/D734-884[»]
1Q1PX-ray3.20A158-369[»]
1SUHNMR-A156-300[»]
2OMWX-ray1.85B158-256[»]
2QVFX-ray2.40B157-369[»]
3IFQX-ray2.80C/D778-884[»]
3LNEX-ray2.00A157-369[»]
3LNFX-ray2.50A/B159-369[»]
3LNGX-ray2.70A/B157-369[»]
3LNHX-ray2.60A/B159-369[»]
3LNIX-ray2.30A/B157-369[»]
3Q2LX-ray2.70A/B157-369[»]
3Q2NX-ray2.73A/B157-369[»]
3Q2VX-ray3.40A/B157-700[»]
3QRBX-ray1.80A/B157-369[»]
DisProtDP00159.
ProteinModelPortalP09803.
SMRP09803. Positions 24-692, 784-877.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198631. 13 interactions.
DIPDIP-29635N.
IntActP09803. 12 interactions.
MINTMINT-121804.

PTM databases

PhosphoSiteP09803.

Proteomic databases

PaxDbP09803.
PRIDEP09803.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000000312; ENSMUSP00000000312; ENSMUSG00000000303.
ENSMUST00000167688; ENSMUSP00000132112; ENSMUSG00000000303.
GeneID12550.
KEGGmmu:12550.
UCSCuc009ngi.1. mouse.

Organism-specific databases

CTD999.
MGIMGI:88354. Cdh1.

Phylogenomic databases

eggNOGNOG328838.
GeneTreeENSGT00740000115112.
HOGENOMHOG000231254.
HOVERGENHBG106438.
InParanoidP09803.
KOK05689.
OrthoDBEOG7PS1DS.
PhylomeDBP09803.
TreeFamTF316817.

Enzyme and pathway databases

ReactomeREACT_98458. Immune System.

Gene expression databases

BgeeP09803.
CleanExMM_CDH1.
GenevestigatorP09803.

Family and domain databases

Gene3D2.60.40.60. 6 hits.
4.10.900.10. 1 hit.
InterProIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR014868. Cadherin_pro_dom.
IPR027397. Catenin_binding_dom.
[Graphical view]
PfamPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]
PRINTSPR00205. CADHERIN.
SMARTSM00112. CA. 4 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]
SUPFAMSSF49313. SSF49313. 6 hits.
PROSITEPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDH1. mouse.
EvolutionaryTraceP09803.
NextBio281598.
PROP09803.
SOURCESearch...

Entry information

Entry nameCADH1_MOUSE
AccessionPrimary (citable) accession number: P09803
Secondary accession number(s): Q61377
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 160 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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