P09803 (CADH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › 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. Interacts with RAB8B. Interacts with DDR1; this stabilizes CDH1 at the cell surface and inhibits its internalization By similarity. Ref.5 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
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 process	Cell adhesion
Cellular component	Cell junction Cell membrane Endosome Golgi apparatus Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium Metal-binding
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell-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: Compara cellular response to lithium ion Inferred from electronic annotation. Source: Compara cochlea development Inferred from mutant phenotype PubMed 21925491. Source: MGI homophilic cell adhesion Inferred from electronic annotation. Source: InterPro negative regulation of cell-cell adhesion Inferred from electronic annotation. Source: Compara neuron projection development Inferred from electronic annotation. Source: Compara pituitary gland development Inferred from electronic annotation. Source: Compara positive regulation of transcription factor import into nucleus Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara protein homooligomerization Inferred from direct assay PubMed 12460580. Source: MGI protein localization to plasma membrane Inferred from electronic annotation. Source: Compara 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 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: Compara response to toxin Inferred from electronic annotation. Source: Compara 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: Compara tight junction assembly Inferred from mutant phenotype PubMed 15775979. Source: MGI trophectodermal cell differentiation Inferred from mutant phenotype PubMed 17138661. Source: MGI
Cellular_component	Golgi 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: Compara aggresome Inferred from electronic annotation. Source: Compara apical junction complex Inferred from electronic annotation. Source: Compara apical part of cell Inferred from direct assay PubMed 14758363. Source: MGI axon terminus Inferred from direct assay PubMed 17392463. Source: MGI basolateral plasma membrane Inferred from direct assay PubMed 15788452PubMed 20016102PubMed 20089884PubMed 20551175PubMed 20637190. Source: MGI catenin complex Inferred from electronic annotation. Source: Compara 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 endosome Inferred from electronic annotation. Source: UniProtKB-SubCell focal adhesion Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW internal side of plasma membrane Inferred from electronic annotation. Source: Compara lateral loop Inferred from direct assay PubMed 20237282. Source: BHF-UCL lateral plasma membrane Inferred from electronic annotation. Source: Compara node of Ranvier Inferred from direct assay PubMed 20237282. Source: BHF-UCL perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara trans-Golgi network Inferred from electronic annotation. Source: Compara
Molecular_function	calcium ion binding Inferred from direct assay PubMed 12460580. Source: MGI
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.
SKP2	Q13309	2	EBI-984420,EBI-456291	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

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

24

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

12

Required for binding CTNND1 and PSEN1 By similarity

Region

813 – 884

72

Required for binding alpha, beta and gamma catenins By similarity

Compositional bias

840 – 855

16

Ser-rich

Sites

Metal binding

259

1

Calcium 1

Metal binding

259

1

Calcium 2

Metal binding

290

1

Calcium 3

Site

702 – 703

2

Cleavage; by a metalloproteinase By similarity

Site

733 – 734

2

Cleavage; by gamma-secretase/PS1 By similarity

Site

752 – 753

2

Cleavage; by caspase-3 By similarity

Amino acid modifications

Modified residue

755

1

Phosphotyrosine; by SRC By similarity

Modified residue

756

1

Phosphotyrosine; by SRC By similarity

Modified residue

757

1

Phosphotyrosine; by SRC By similarity

Modified residue

840

1

Phosphoserine Ref.13

Modified residue

842

1

Phosphoserine Ref.13

Modified residue

848

1

Phosphoserine Ref.13

Glycosylation

560

1

N-linked (GlcNAc...) Potential

Glycosylation

639

1

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

267

1

E → P in CAA43292. Ref.2

Sequence conflict

272

1

S → F in CAA43292. Ref.2

Secondary structure

1

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884

Helix Strand Turn

Details...

Beta strand

160 – 166

7

Beta strand

171 – 179

9

Helix

183 – 186

4

Beta strand

190 – 197

8

Turn

198 – 200

3

Beta strand

201 – 203

3

Beta strand

206 – 209

4

Turn

211 – 213

3

Beta strand

215 – 218

4

Turn

224 – 226

3

Beta strand

228 – 238

11

Turn

239 – 241

3

Beta strand

243 – 245

3

Beta strand

248 – 255

8

Beta strand

263 – 265

3

Beta strand

267 – 274

8

Beta strand

282 – 285

4

Turn

294 – 296

3

Helix

298 – 300

3

Beta strand

303 – 311

9

Beta strand

314 – 316

3

Beta strand

318 – 321

4

Turn

323 – 325

3

Beta strand

327 – 330

4

Turn

337 – 339

3

Beta strand

342 – 350

9

Helix

352 – 354

3

Beta strand

358 – 368

11

Beta strand

376 – 389

14

Beta strand

396 – 398

3

Turn

409 – 411

3

Beta strand

413 – 419

7

Beta strand

425 – 429

5

Turn

431 – 433

3

Beta strand

436 – 442

7

Turn

446 – 448

3

Beta strand

450 – 462

13

Beta strand

471 – 480

10

Beta strand

487 – 492

6

Beta strand

494 – 498

5

Beta strand

506 – 509

4

Beta strand

524 – 529

6

Beta strand

535 – 537

3

Turn

539 – 541

3

Beta strand

543 – 546

4

Turn

555 – 557

3

Beta strand

560 – 570

11

Beta strand

573 – 575

3

Beta strand

579 – 588

10

Beta strand

596 – 598

3

Beta strand

603 – 608

6

Beta strand

612 – 617

6

Beta strand

624 – 627

4

Beta strand

631 – 634

4

Beta strand

637 – 639

3

Beta strand

641 – 643

3

Beta strand

649 – 655

7

Beta strand

668 – 670

3

Beta strand

673 – 675

3

Beta strand

684 – 688

5

Beta strand

785 – 789

5

Turn

806 – 808

3

Helix

818 – 822

5

Beta strand

824 – 827

4

Beta strand

830 – 834

5

Turn

864 – 866

3

Helix

869 – 871

3

Helix

872 – 877

6

Sequences

	Sequence		Length	Mass (Da)
	P09803 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 7A6444148D3D5983	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

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 , 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.

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	[»]

DisProt

DP00159.

ProteinModelPortal

P09803.

SMR

P09803. Positions 157-692, 784-877.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29635N.

IntAct

P09803. 7 interactions.

MINT

MINT-121804.

PTM databases

PhosphoSite

P09803.

Proteomic databases

PaxDb

P09803.

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

NOG328838.

GeneTree

ENSGT00700000104066.

HOGENOM

HOG000231254.

HOVERGEN

HBG106438.

InParanoid

P09803.

KO

K05689.

OrthoDB

EOG4GF3DT.

Enzyme and pathway databases

Reactome

REACT_107772. Immune System.

Gene expression databases

Bgee

P09803.

CleanEx

MM_CDH1.

Genevestigator

P09803.

GermOnline

ENSMUSG00000000303. Mus musculus.

Family and domain databases

Gene3D

2.60.40.60. 6 hits.

InterPro

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

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

ChiTaRS

CDH1. mouse.

EvolutionaryTrace

P09803.

NextBio

281598.

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:	May 1, 2013
This is version 150 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program