Cadherin-1 precursor - Mus musculus (Mouse)

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P09803 (CADH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 135. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cadherin-1

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

Gene names

Name:

Cdh1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	884 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.9
Subcellular location	Cell junction. Cell membrane; Single-pass type I membrane protein. Endosome By similarity. Golgi apparatus › trans-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
Post-translational modification	N-glycosylation at Asn-639 is essential for expression, folding and trafficking By similarity.
Sequence similarities	Contains 5 cadherin domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cell membrane Endosome Golgi apparatus Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cellular response to amino acid stimulus Inferred from direct assay. Source: MGI homophilic cell adhesion Inferred from electronic annotation. Source: InterPro protein homooligomerization Inferred from direct assay. Source: MGI protein metabolic process Inferred from direct assay. Source: MGI regulation of branching involved in salivary gland morphogenesis Inferred from mutant phenotype. Source: MGI regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay. Source: MGI regulation of protein localization at cell surface Inferred from mutant phenotype. Source: MGI regulation of water loss via skin Inferred from mutant phenotype. Source: MGI salivary gland cavitation Inferred from mutant phenotype. Source: MGI tight junction assembly Inferred from mutant phenotype. Source: MGI trophectodermal cell differentiation Inferred from mutant phenotype. Source: MGI
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell Schmidt-Lanterman incisure Inferred from direct assay. Source: BHF-UCL apical part of cell Inferred from direct assay. Source: MGI cell surface Inferred from direct assay. Source: MGI cell-cell adherens junction Inferred from direct assay. Source: MGI endosome Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW lateral loop Inferred from direct assay. Source: BHF-UCL node of Ranvier Inferred from direct assay. Source: BHF-UCL
Molecular function	RPTP-like protein binding Inferred from physical interaction. Source: MGI beta-catenin binding Inferred from physical interaction. Source: MGI calcium ion binding Inferred from direct assay. Source: MGI protein domain specific binding Inferred from physical interaction. Source: MGI protein phosphatase binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Ctnnb1	Q02248	13	EBI-984420,EBI-397872
CTNND1	O60716-29	3	EBI-984420,EBI-702059	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

Potential

Propeptide

24 – 156

133

Potential

PRO_0000003717

Chain

157 – 884

728

Cadherin-1

PRO_0000003718

Chain

703 – 884

182

E-Cad/CTF1 Potential

PRO_0000236070

Chain

734 – 884

151

E-Cad/CTF2 Potential

PRO_0000236071

Chain

753 – 884

132

E-Cad/CTF3 Potential

PRO_0000236072

Regions

Topological domain

157 – 709

553

Extracellular Potential

Transmembrane

710 – 733

Helical; Potential

Topological domain

734 – 884

151

Cytoplasmic Potential

Domain

157 – 264

108

Cadherin 1

Domain

265 – 377

113

Cadherin 2

Domain

378 – 488

111

Cadherin 3

Domain

489 – 595

107

Cadherin 4

Domain

596 – 699

104

Cadherin 5

Region

760 – 771

Required for binding CTNND1 and PSEN1 By similarity

Region

813 – 884

Required for binding alpha, beta and gamma catenins By similarity

Compositional bias

840 – 855

Ser-rich

Sites

Site

702 – 703

Cleavage; by a metalloproteinase By similarity

Site

733 – 734

Cleavage; by gamma-secretase/PS1 By similarity

Site

752 – 753

Cleavage; by caspase-3 By similarity

Amino acid modifications

Modified residue

840

Phosphoserine

Modified residue

842

Phosphoserine

Modified residue

848

Phosphoserine

Glycosylation

560

N-linked (GlcNAc...) Potential

Glycosylation

639

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

267

E → P in CAA43292. Ref.2

Sequence conflict

272

S → F in CAA43292. Ref.2

Secondary structure

884

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P09803 [UniParc].

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

FASTA

884

98,256

        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

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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: 3498123] [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: 1754391] [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: 3501370] [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: 1763063] [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: 7982500] [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: 8879495] [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: 16325582] [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: 18093941] [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: 20413591] [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: 8598933] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 157-370.
[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: 8785495] [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: 11348595] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 577-728 IN COMPLEX WITH CTNNB1, PHOSPHORYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X06115 mRNA. Translation: CAA29488.1.
X60961

X60975 Genomic DNA. Translation: CAA43292.1.
X06339 mRNA. Translation: CAA29645.1.
M81449 Genomic DNA. Translation: AAA37352.1.

IPI

IPI00318626.

PIR

IJMSCE. S04528.
S34438.

RefSeq

NP_033994.1. NM_009864.2.

UniGene

Mm.35605.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EDH	X-ray	2.00	A/B	156-380	[»]
1FF5	X-ray	2.93	A/B	157-374	[»]
1I7W	X-ray	2.00	B/D	734-884	[»]
1I7X	X-ray	3.00	B/D	734-884	[»]
1Q1P	X-ray	3.20	A	158-369	[»]
1SUH	NMR	-	A	156-300	[»]
2OMW	X-ray	1.85	B	158-256	[»]
2QVF	X-ray	2.40	B	157-369	[»]
3IFQ	X-ray	2.80	C/D	778-884	[»]
3LNE	X-ray	2.00	A	157-369	[»]
3LNF	X-ray	2.50	A/B	159-369	[»]
3LNG	X-ray	2.70	A/B	157-369	[»]
3LNH	X-ray	2.60	A/B	159-369	[»]
3LNI	X-ray	2.30	A/B	157-369	[»]
3Q2L	X-ray	2.70	A/B	157-369	[»]
3Q2N	X-ray	2.73	A/B	157-369	[»]
3Q2V	X-ray	3.40	A/B	157-700	[»]
3QRB	X-ray	1.80	A/B	157-369	[»]

ProteinModelPortal

P09803.

SMR

P09803. Positions 24-692, 784-877.

DisProt

DP00159.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29635N.

IntAct

P09803. 4 interactions.

MINT

MINT-121804.

STRING

P09803.

PTM databases

PhosphoSite

P09803.

Proteomic databases

PRIDE

P09803.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000000312; ENSMUSP00000000312; ENSMUSG00000000303.
ENSMUST00000167688; ENSMUSP00000132112; ENSMUSG00000000303.

GeneID

12550.

KEGG

mmu:12550.

Organism-specific databases

CTD

999.

MGI

MGI:88354. Cdh1.

Phylogenomic databases

eggNOG

roNOG05681.

HOGENOM

HBG505775.

HOVERGEN

HBG106438.

InParanoid

P09803.

OrthoDB

EOG4GF3DT.

Enzyme and pathway databases

Reactome

REACT_98458. Immune System.

Gene expression databases

ArrayExpress

P09803.

Bgee

P09803.

CleanEx

MM_CDH1.

Genevestigator

P09803.

GermOnline

ENSMUSG00000000303. Mus musculus.

Family and domain databases

InterPro

IPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR014868. Cadherin_pro_dom.
[Graphical view]

Gene3D

G3DSA:2.60.40.60. Cadherin. 4 hits.

K05689.

Pfam

PF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]

PRINTS

PR00205. CADHERIN.

SMART

SM00112. CA. 4 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]

SUPFAM

SSF49313. Cadherin. 6 hits.

PROSITE

PS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

SOURCE

Search...

Entry information

Entry name

CADH1_MOUSE

Accession

Primary (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:	January 25, 2012
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata 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

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 3 chains:

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents