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Cadherin-1 (ARC-1) (Epithelial cadherin) (E-cadherin) (Uvomorulin) (CD antigen CD324) [Cleaved into: E-Cad/CTF1; E-Cad/CTF2; E-Cad/CTF3]

 CADH1_MOUSE             Reviewed;         884 AA.
P09803; Q61377;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
18-JUL-2018, entry version 203.
RecName: Full=Cadherin-1;
AltName: Full=ARC-1;
AltName: Full=Epithelial cadherin;
Short=E-cadherin;
AltName: Full=Uvomorulin;
AltName: CD_antigen=CD324;
Contains:
RecName: Full=E-Cad/CTF1;
Contains:
RecName: Full=E-Cad/CTF2;
Contains:
RecName: Full=E-Cad/CTF3;
Flags: Precursor;
Name=Cdh1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ICR;
PubMed=3498123; DOI=10.1038/329341a0;
Nagafuchi A., Shirayoshi Y., Okazari K., Yasuda K., Takeichi M.;
"Transformation of cell adhesion properties by exogenously introduced
E-cadherin cDNA.";
Nature 329:341-343(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
PubMed=1754391; DOI=10.1093/nar/19.23.6533;
Ringwald M., Baribault H., Schmidt C., Kemler R.;
"The structure of the gene coding for the mouse cell adhesion molecule
uvomorulin.";
Nucleic Acids Res. 19:6533-6539(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 174-884, AND PROTEIN SEQUENCE OF
157-181.
PubMed=3501370;
Ringwald M., Schuh R., Vestweber D., Eistetter H., Lottspeich F.,
Engel J., Doelz R., Jaehnig F., Epplen J., Mayer S., Mueller C.,
Kemler R.;
"The structure of cell adhesion molecule uvomorulin. Insights into the
molecular mechanism of Ca2+-dependent cell adhesion.";
EMBO J. 6:3647-3653(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
PubMed=1763063; DOI=10.1073/pnas.88.24.11495;
Behrens J., Loewrick O., Klein-Hitpass L., Birchmeier W.;
"The E-cadherin promoter: functional analysis of a G.C-rich region and
an epithelial cell-specific palindromic regulatory element.";
Proc. Natl. Acad. Sci. U.S.A. 88:11495-11499(1991).
[5]
IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9;
Butz S., Kemler R.;
"Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell
adhesion.";
FEBS Lett. 355:195-200(1994).
[6]
DEVELOPMENTAL STAGE.
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=8879495; DOI=10.1095/biolreprod55.4.822;
Munro S.B., Blaschuk O.W.;
"A comprehensive survey of the cadherins expressed in the testes of
fetal, immature, and adult mice utilizing the polymerase chain
reaction.";
Biol. Reprod. 55:822-827(1996).
[7]
FUNCTION.
PubMed=11976333; DOI=10.1074/jbc.M201984200;
Meigs T.E., Fedor-Chaiken M., Kaplan D.D., Brackenbury R., Casey P.J.;
"Galpha12 and Galpha13 negatively regulate the adhesive functions of
cadherin.";
J. Biol. Chem. 277:24594-24600(2002).
[8]
RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, AND LACK OF
ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
PubMed=16325582; DOI=10.1016/j.cell.2005.09.020;
Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.;
"Deconstructing the cadherin-catenin-actin complex.";
Cell 123:889-901(2005).
[9]
LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
PubMed=18093941; DOI=10.1073/pnas.0710504105;
Abe K., Takeichi M.;
"EPLIN mediates linkage of the cadherin catenin complex to F-actin and
stabilizes the circumferential actin belt.";
Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, Lung, and Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
INTERACTION WITH TRPV4 AND CTNNB1.
PubMed=20413591; DOI=10.1074/jbc.M110.103606;
Sokabe T., Fukumi-Tominaga T., Yonemura S., Mizuno A., Tominaga M.;
"The TRPV4 channel contributes to intercellular junction formation in
keratinocytes.";
J. Biol. Chem. 285:18749-18758(2010).
[12]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 157-370, AND CALCIUM-BINDING
SITES.
PubMed=8598933; DOI=10.1038/380360a0;
Nagar B., Overduin M., Ikura M., Rini J.M.;
"Structural basis of calcium-induced E-cadherin rigidification and
dimerization.";
Nature 380:360-364(1996).
[13]
STRUCTURE BY NMR OF 157-260.
PubMed=8785495; DOI=10.1007/BF00202035;
Overduin M., Tong K.I., Kay C.M., Ikura M.;
"1H, 15N and 13C resonance assignments and monomeric structure of the
amino-terminal extracellular domain of epithelial cadherin.";
J. Biomol. NMR 7:173-189(1996).
[14]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 577-728 IN COMPLEX WITH
CTNNB1, AND PHOSPHORYLATION.
PubMed=11348595; DOI=10.1016/S0092-8674(01)00330-0;
Huber A.H., Weis W.I.;
"The structure of the beta-catenin/E-cadherin complex and the
molecular basis of diverse ligand recognition by beta-catenin.";
Cell 105:391-402(2001).
[15]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 778-884 IN COMPLEX WITH HUMAN
JUP, AND PHOSPHORYLATION AT SER-840; SER-842 AND SER-848.
PubMed=19759396; DOI=10.1074/jbc.M109.047928;
Choi H.J., Gross J.C., Pokutta S., Weis W.I.;
"Interactions of plakoglobin and beta-catenin with desmosomal
cadherins: basis of selective exclusion of alpha- and beta-catenin
from desmosomes.";
J. Biol. Chem. 284:31776-31788(2009).
-!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins
(PubMed:11976333). 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 (PubMed:11976333). Has a
potent invasive suppressor role. It is a ligand for integrin
alpha-E/beta-7 (By similarity). {ECO:0000250|UniProtKB:P12830,
ECO:0000269|PubMed:11976333}.
-!- FUNCTION: E-Cad/CTF2 promotes non-amyloidogenic degradation of
Abeta precursors. Has a strong inhibitory effect on APP C99 and
C83 production (By similarity). {ECO:0000250|UniProtKB:P12830}.
-!- SUBUNIT: Homodimer; disulfide-linked (By similarity). 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 (PubMed:7982500, PubMed:19759396). Interacts
with the TRPV4 and CTNNB1 complex (PubMed:20413591,
PubMed:11348595). Interacts with CTNND1 (By similarity). The
stable association of CTNNA1 is controversial as CTNNA1 was shown
not to bind to F-actin when assembled in the complex
(PubMed:16325582). Alternatively, the CTNNA1-containing complex
may be linked to F-actin by other proteins such as LIMA1
(PubMed:18093941). Interaction with PSEN1, cleaves CDH1 resulting
in the disassociation of cadherin-based adherens junctions (CAJs)
(By similarity). Interacts with AJAP1 and DLGAP5 (By similarity).
Interacts with TBC1D2 (By similarity). Interacts with LIMA1 (By
similarity). Interacts with CAV1 (By similarity). Interacts with
PIP5K1C (By similarity). Interacts with RAB8B (By similarity).
Interacts with DDR1; this stabilizes CDH1 at the cell surface and
inhibits its internalization (By similarity). Interacts with
RAPGEF2 (By similarity). Interacts with KLRG1 (By similarity).
{ECO:0000250|UniProtKB:P12830, ECO:0000250|UniProtKB:Q9R0T4,
ECO:0000269|PubMed:11348595, ECO:0000269|PubMed:16325582,
ECO:0000269|PubMed:18093941, ECO:0000269|PubMed:19759396,
ECO:0000269|PubMed:20413591, ECO:0000269|PubMed:7982500}.
-!- INTERACTION:
Self; NbExp=12; IntAct=EBI-984420, EBI-984420;
P61809:Cdk5r1; NbExp=2; IntAct=EBI-984420, EBI-7840438;
Q02248:Ctnnb1; NbExp=15; IntAct=EBI-984420, EBI-397872;
O60716-29:CTNND1 (xeno); NbExp=3; IntAct=EBI-984420, EBI-702059;
A5HZZ4:ha70 (xeno); NbExp=6; IntAct=EBI-984420, EBI-16109901;
P28827:PTPRM (xeno); NbExp=3; IntAct=EBI-984420, EBI-2257317;
Q13309:SKP2 (xeno); NbExp=2; IntAct=EBI-984420, EBI-456291;
-!- SUBCELLULAR LOCATION: Cell junction
{ECO:0000250|UniProtKB:P12830}. Cell membrane; Single-pass type I
membrane protein. Endosome {ECO:0000250}. Golgi apparatus, trans-
Golgi network {ECO:0000250}. 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). {ECO:0000250}.
-!- 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. {ECO:0000269|PubMed:8879495}.
-!- 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.
-!- PTM: N-glycosylation at Asn-639 is essential for expression,
folding and trafficking. {ECO:0000250}.
-!- PTM: 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). {ECO:0000250}.
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EMBL; X06115; CAA29488.1; -; mRNA.
EMBL; X60961; CAA43292.1; -; Genomic_DNA.
EMBL; X60962; CAA43292.1; JOINED; Genomic_DNA.
EMBL; X60963; CAA43292.1; JOINED; Genomic_DNA.
EMBL; X60964; CAA43292.1; JOINED; Genomic_DNA.
EMBL; X60965; CAA43292.1; JOINED; Genomic_DNA.
EMBL; X60966; CAA43292.1; JOINED; Genomic_DNA.
EMBL; X60967; CAA43292.1; JOINED; Genomic_DNA.
EMBL; X60968; CAA43292.1; JOINED; Genomic_DNA.
EMBL; X60969; CAA43292.1; JOINED; Genomic_DNA.
EMBL; X60970; CAA43292.1; JOINED; Genomic_DNA.
EMBL; X60971; CAA43292.1; JOINED; Genomic_DNA.
EMBL; X60972; CAA43292.1; JOINED; Genomic_DNA.
EMBL; X60973; CAA43292.1; JOINED; Genomic_DNA.
EMBL; X60974; CAA43292.1; JOINED; Genomic_DNA.
EMBL; X60975; CAA43292.1; JOINED; Genomic_DNA.
EMBL; X06339; CAA29645.1; -; mRNA.
EMBL; M81449; AAA37352.1; -; Genomic_DNA.
CCDS; CCDS22638.1; -.
PIR; S04528; IJMSCE.
PIR; S34438; S34438.
RefSeq; NP_033994.1; NM_009864.3.
UniGene; Mm.35605; -.
PDB; 1EDH; X-ray; 2.00 A; A/B=156-380.
PDB; 1FF5; X-ray; 2.93 A; A/B=157-374.
PDB; 1I7W; X-ray; 2.00 A; B/D=734-884.
PDB; 1I7X; X-ray; 3.00 A; B/D=734-884.
PDB; 1Q1P; X-ray; 3.20 A; A=158-369.
PDB; 1SUH; NMR; -; A=156-300.
PDB; 2OMW; X-ray; 1.85 A; B=158-256.
PDB; 2QVF; X-ray; 2.40 A; B=157-369.
PDB; 3IFQ; X-ray; 2.80 A; C/D=778-884.
PDB; 3LNE; X-ray; 2.00 A; A=157-369.
PDB; 3LNF; X-ray; 2.50 A; A/B=157-369.
PDB; 3LNG; X-ray; 2.70 A; A/B=157-369.
PDB; 3LNH; X-ray; 2.60 A; A/B=157-369.
PDB; 3LNI; X-ray; 2.30 A; A/B=157-369.
PDB; 3Q2L; X-ray; 2.70 A; A/B=157-369.
PDB; 3Q2N; X-ray; 2.73 A; A/B=157-369.
PDB; 3Q2V; X-ray; 3.40 A; A/B=157-700.
PDB; 3QRB; X-ray; 1.80 A; A/B=157-369.
PDB; 4QD2; X-ray; 2.40 A; E/J=157-369.
PDBsum; 1EDH; -.
PDBsum; 1FF5; -.
PDBsum; 1I7W; -.
PDBsum; 1I7X; -.
PDBsum; 1Q1P; -.
PDBsum; 1SUH; -.
PDBsum; 2OMW; -.
PDBsum; 2QVF; -.
PDBsum; 3IFQ; -.
PDBsum; 3LNE; -.
PDBsum; 3LNF; -.
PDBsum; 3LNG; -.
PDBsum; 3LNH; -.
PDBsum; 3LNI; -.
PDBsum; 3Q2L; -.
PDBsum; 3Q2N; -.
PDBsum; 3Q2V; -.
PDBsum; 3QRB; -.
PDBsum; 4QD2; -.
DisProt; DP00159; -.
ProteinModelPortal; P09803; -.
SMR; P09803; -.
BioGrid; 198631; 37.
CORUM; P09803; -.
DIP; DIP-29635N; -.
IntAct; P09803; 40.
MINT; P09803; -.
STRING; 10090.ENSMUSP00000000312; -.
iPTMnet; P09803; -.
PhosphoSitePlus; P09803; -.
MaxQB; P09803; -.
PaxDb; P09803; -.
PeptideAtlas; P09803; -.
PRIDE; P09803; -.
GeneID; 12550; -.
KEGG; mmu:12550; -.
UCSC; uc009ngi.1; mouse.
CTD; 999; -.
MGI; MGI:88354; Cdh1.
eggNOG; KOG3594; Eukaryota.
eggNOG; ENOG410XQHI; LUCA.
HOGENOM; HOG000231254; -.
HOVERGEN; HBG106438; -.
InParanoid; P09803; -.
KO; K05689; -.
PhylomeDB; P09803; -.
TreeFam; TF316817; -.
ChiTaRS; Cdh1; mouse.
EvolutionaryTrace; P09803; -.
PRO; PR:P09803; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_CDH1; -.
GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
GO; GO:0043296; C:apical junction complex; IDA:MGI.
GO; GO:0045177; C:apical part of cell; IDA:MGI.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0043679; C:axon terminus; IDA:MGI.
GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
GO; GO:0016342; C:catenin complex; IDA:MGI.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0016600; C:flotillin complex; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; ISO:MGI.
GO; GO:0030027; C:lamellipodium; ISO:MGI.
GO; GO:0043219; C:lateral loop; IDA:BHF-UCL.
GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
GO; GO:0033268; C:node of Ranvier; IDA:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:BHF-UCL.
GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
GO; GO:0045294; F:alpha-catenin binding; IPI:MGI.
GO; GO:0030506; F:ankyrin binding; ISO:MGI.
GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; IDA:MGI.
GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
GO; GO:0008092; F:cytoskeletal protein binding; IMP:MGI.
GO; GO:0045295; F:gamma-catenin binding; ISO:MGI.
GO; GO:0032794; F:GTPase activating protein binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0034332; P:adherens junction organization; ISO:MGI.
GO; GO:0070830; P:bicellular tight junction assembly; IMP:MGI.
GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:MGI.
GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
GO; GO:0071681; P:cellular response to indole-3-methanol; ISO:MGI.
GO; GO:0071285; P:cellular response to lithium ion; ISO:MGI.
GO; GO:0090102; P:cochlea development; IMP:MGI.
GO; GO:0046697; P:decidualization; IMP:CACAO.
GO; GO:0007566; P:embryo implantation; IMP:CACAO.
GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0060576; P:intestinal epithelial cell development; IMP:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:MGI.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISO:MGI.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
GO; GO:0010955; P:negative regulation of protein processing; IMP:MGI.
GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:MGI.
GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0051260; P:protein homooligomerization; IDA:MGI.
GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0019538; P:protein metabolic process; IDA:MGI.
GO; GO:0060693; P:regulation of branching involved in salivary gland morphogenesis; IMP:MGI.
GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
GO; GO:2001222; P:regulation of neuron migration; IDA:MGI.
GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
GO; GO:2000008; P:regulation of protein localization to cell surface; IMP:MGI.
GO; GO:0033561; P:regulation of water loss via skin; IMP:MGI.
GO; GO:0060662; P:salivary gland cavitation; IMP:MGI.
GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
GO; GO:0007416; P:synapse assembly; ISO:MGI.
GO; GO:0001829; P:trophectodermal cell differentiation; IMP:MGI.
GO; GO:0035847; P:uterine epithelium development; IMP:CACAO.
Gene3D; 4.10.900.10; -; 1.
InterPro; IPR002126; Cadherin.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR020894; Cadherin_CS.
InterPro; IPR000233; Cadherin_cytoplasmic-dom.
InterPro; IPR014868; Cadherin_pro_dom.
InterPro; IPR027397; Catenin_binding_dom_sf.
Pfam; PF00028; Cadherin; 5.
Pfam; PF01049; Cadherin_C; 1.
Pfam; PF08758; Cadherin_pro; 1.
PRINTS; PR00205; CADHERIN.
SMART; SM00112; CA; 4.
SMART; SM01055; Cadherin_pro; 1.
SUPFAM; SSF49313; SSF49313; 6.
PROSITE; PS00232; CADHERIN_1; 3.
PROSITE; PS50268; CADHERIN_2; 4.
1: Evidence at protein level;
3D-structure; Calcium; Cell adhesion; Cell junction; Cell membrane;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Endosome; Glycoprotein;
Golgi apparatus; Membrane; Metal-binding; Phosphoprotein;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix; Ubl conjugation.
SIGNAL 1 23 {ECO:0000255}.
PROPEP 24 156 {ECO:0000255}.
/FTId=PRO_0000003717.
CHAIN 157 884 Cadherin-1.
/FTId=PRO_0000003718.
CHAIN 703 884 E-Cad/CTF1. {ECO:0000255}.
/FTId=PRO_0000236070.
CHAIN 734 884 E-Cad/CTF2. {ECO:0000255}.
/FTId=PRO_0000236071.
CHAIN 753 884 E-Cad/CTF3. {ECO:0000255}.
/FTId=PRO_0000236072.
TOPO_DOM 157 709 Extracellular. {ECO:0000255}.
TRANSMEM 710 733 Helical. {ECO:0000255}.
TOPO_DOM 734 884 Cytoplasmic. {ECO:0000255}.
DOMAIN 157 264 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 265 377 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 378 488 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 489 595 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 596 699 Cadherin 5. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
REGION 760 771 Required for binding CTNND1 and PSEN1.
{ECO:0000250}.
REGION 813 884 Required for binding alpha, beta and
gamma catenins. {ECO:0000250}.
COMPBIAS 840 855 Ser-rich.
METAL 259 259 Calcium 1.
METAL 259 259 Calcium 2.
METAL 290 290 Calcium 3.
SITE 702 703 Cleavage; by a metalloproteinase.
{ECO:0000250}.
SITE 733 734 Cleavage; by gamma-secretase/PS1.
{ECO:0000250}.
SITE 752 753 Cleavage; by caspase-3. {ECO:0000250}.
MOD_RES 755 755 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P12830}.
MOD_RES 756 756 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P12830}.
MOD_RES 757 757 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:P12830}.
MOD_RES 772 772 Phosphoserine.
{ECO:0000250|UniProtKB:P12830}.
MOD_RES 795 795 Phosphoserine.
{ECO:0000250|UniProtKB:P12830}.
MOD_RES 840 840 Phosphoserine.
{ECO:0000269|PubMed:19759396}.
MOD_RES 842 842 Phosphoserine.
{ECO:0000269|PubMed:19759396}.
MOD_RES 848 848 Phosphoserine.
{ECO:0000269|PubMed:19759396}.
CARBOHYD 560 560 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 639 639 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 267 267 E -> P (in Ref. 2; CAA43292).
{ECO:0000305}.
CONFLICT 272 272 S -> F (in Ref. 2; CAA43292).
{ECO:0000305}.
STRAND 160 166 {ECO:0000244|PDB:3QRB}.
STRAND 171 179 {ECO:0000244|PDB:3QRB}.
HELIX 183 186 {ECO:0000244|PDB:3QRB}.
STRAND 190 197 {ECO:0000244|PDB:3QRB}.
TURN 198 200 {ECO:0000244|PDB:3QRB}.
STRAND 201 203 {ECO:0000244|PDB:3QRB}.
STRAND 206 209 {ECO:0000244|PDB:3QRB}.
TURN 211 213 {ECO:0000244|PDB:3QRB}.
STRAND 215 218 {ECO:0000244|PDB:3QRB}.
TURN 224 226 {ECO:0000244|PDB:3QRB}.
STRAND 228 238 {ECO:0000244|PDB:3QRB}.
TURN 239 241 {ECO:0000244|PDB:1Q1P}.
STRAND 243 245 {ECO:0000244|PDB:2OMW}.
STRAND 248 255 {ECO:0000244|PDB:3QRB}.
STRAND 263 265 {ECO:0000244|PDB:3QRB}.
STRAND 267 274 {ECO:0000244|PDB:3QRB}.
STRAND 282 285 {ECO:0000244|PDB:3QRB}.
TURN 294 296 {ECO:0000244|PDB:3QRB}.
HELIX 298 300 {ECO:0000244|PDB:1Q1P}.
STRAND 303 311 {ECO:0000244|PDB:3QRB}.
STRAND 314 316 {ECO:0000244|PDB:3Q2V}.
STRAND 318 321 {ECO:0000244|PDB:3QRB}.
TURN 323 325 {ECO:0000244|PDB:3QRB}.
STRAND 327 330 {ECO:0000244|PDB:3QRB}.
TURN 337 339 {ECO:0000244|PDB:3QRB}.
STRAND 342 350 {ECO:0000244|PDB:3QRB}.
HELIX 352 354 {ECO:0000244|PDB:3QRB}.
STRAND 358 368 {ECO:0000244|PDB:3QRB}.
STRAND 376 389 {ECO:0000244|PDB:3Q2V}.
STRAND 396 398 {ECO:0000244|PDB:3Q2V}.
TURN 409 411 {ECO:0000244|PDB:3Q2V}.
STRAND 413 419 {ECO:0000244|PDB:3Q2V}.
STRAND 425 429 {ECO:0000244|PDB:3Q2V}.
TURN 431 433 {ECO:0000244|PDB:3Q2V}.
STRAND 436 442 {ECO:0000244|PDB:3Q2V}.
TURN 446 448 {ECO:0000244|PDB:3Q2V}.
STRAND 450 462 {ECO:0000244|PDB:3Q2V}.
STRAND 471 480 {ECO:0000244|PDB:3Q2V}.
STRAND 487 492 {ECO:0000244|PDB:3Q2V}.
STRAND 494 498 {ECO:0000244|PDB:3Q2V}.
STRAND 506 509 {ECO:0000244|PDB:3Q2V}.
STRAND 524 529 {ECO:0000244|PDB:3Q2V}.
STRAND 535 537 {ECO:0000244|PDB:3Q2V}.
TURN 539 541 {ECO:0000244|PDB:3Q2V}.
STRAND 543 546 {ECO:0000244|PDB:3Q2V}.
TURN 555 557 {ECO:0000244|PDB:3Q2V}.
STRAND 560 570 {ECO:0000244|PDB:3Q2V}.
STRAND 573 575 {ECO:0000244|PDB:3Q2V}.
STRAND 579 588 {ECO:0000244|PDB:3Q2V}.
STRAND 596 598 {ECO:0000244|PDB:3Q2V}.
STRAND 603 608 {ECO:0000244|PDB:3Q2V}.
STRAND 612 617 {ECO:0000244|PDB:3Q2V}.
STRAND 624 627 {ECO:0000244|PDB:3Q2V}.
STRAND 631 634 {ECO:0000244|PDB:3Q2V}.
STRAND 637 639 {ECO:0000244|PDB:3Q2V}.
STRAND 641 643 {ECO:0000244|PDB:3Q2V}.
STRAND 649 655 {ECO:0000244|PDB:3Q2V}.
STRAND 668 670 {ECO:0000244|PDB:3Q2V}.
STRAND 673 675 {ECO:0000244|PDB:3Q2V}.
STRAND 684 688 {ECO:0000244|PDB:3Q2V}.
STRAND 785 789 {ECO:0000244|PDB:3IFQ}.
TURN 806 808 {ECO:0000244|PDB:3IFQ}.
HELIX 818 822 {ECO:0000244|PDB:1I7W}.
STRAND 824 827 {ECO:0000244|PDB:1I7X}.
STRAND 830 834 {ECO:0000244|PDB:3IFQ}.
TURN 864 866 {ECO:0000244|PDB:1I7W}.
HELIX 869 871 {ECO:0000244|PDB:1I7W}.
HELIX 872 877 {ECO:0000244|PDB:1I7W}.
SEQUENCE 884 AA; 98256 MW; 7A6444148D3D5983 CRC64;
MGARCRSFSA LLLLLQVSSW LCQELEPESC SPGFSSEVYT FPVPERHLER GHVLGRVRFE
GCTGRPRTAF FSEDSRFKVA TDGTITVKRH LKLHKLETSF LVRARDSSHR ELSTKVTLKS
MGHHHHRHHH RDPASESNPE LLMFPSVYPG LRRQKRDWVI PPISCPENEK GEFPKNLVQI
KSNRDKETKV FYSITGQGAD KPPVGVFIIE RETGWLKVTQ PLDREAIAKY ILYSHAVSSN
GEAVEDPMEI VITVTDQNDN RPEFTQEVFE GSVAEGAVPG TSVMKVSATD ADDDVNTYNA
AIAYTIVSQD PELPHKNMFT VNRDTGVISV LTSGLDRESY PTYTLVVQAA DLQGEGLSTT
AKAVITVKDI NDNAPVFNPS TYQGQVPENE VNARIATLKV TDDDAPNTPA WKAVYTVVND
PDQQFVVVTD PTTNDGILKT AKGLDFEAKQ QYILHVRVEN EEPFEGSLVP STATVTVDVV
DVNEAPIFMP AERRVEVPED FGVGQEITSY TAREPDTFMD QKITYRIWRD TANWLEINPE
TGAIFTRAEM DREDAEHVKN STYVALIIAT DDGSPIATGT GTLLLVLLDV NDNAPIPEPR
NMQFCQRNPQ PHIITILDPD LPPNTSPFTA ELTHGASVNW TIEYNDAAQE SLILQPRKDL
EIGEYKIHLK LADNQNKDQV TTLDVHVCDC EGTVNNCMKA GIVAAGLQVP AILGILGGIL
ALLILILLLL LFLRRRTVVK EPLLPPDDDT RDNVYYYDEE GGGEEDQDFD LSQLHRGLDA
RPEVTRNDVA PTLMSVPQYR PRPANPDEIG NFIDENLKAA DSDPTAPPYD SLLVFDYEGS
GSEAASLSSL NSSESDQDQD YDYLNEWGNR FKKLADMYGG GEDD


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