CADH1_MOUSE
ID CADH1_MOUSE Reviewed; 884 AA.
AC P09803; Q61377;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 228.
DE RecName: Full=Cadherin-1;
DE AltName: Full=ARC-1;
DE AltName: Full=Epithelial cadherin;
DE Short=E-cadherin;
DE AltName: Full=Uvomorulin;
DE AltName: CD_antigen=CD324;
DE Contains:
DE RecName: Full=E-Cad/CTF1;
DE Contains:
DE RecName: Full=E-Cad/CTF2;
DE Contains:
DE RecName: Full=E-Cad/CTF3;
DE Flags: Precursor;
GN Name=Cdh1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR;
RX PubMed=3498123; DOI=10.1038/329341a0;
RA Nagafuchi A., Shirayoshi Y., Okazari K., Yasuda K., Takeichi M.;
RT "Transformation of cell adhesion properties by exogenously introduced E-
RT cadherin cDNA.";
RL Nature 329:341-343(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=1754391; DOI=10.1093/nar/19.23.6533;
RA Ringwald M., Baribault H., Schmidt C., Kemler R.;
RT "The structure of the gene coding for the mouse cell adhesion molecule
RT uvomorulin.";
RL Nucleic Acids Res. 19:6533-6539(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 174-884, AND PROTEIN SEQUENCE OF 157-181.
RX PubMed=3501370; DOI=10.1002/j.1460-2075.1987.tb02697.x;
RA Ringwald M., Schuh R., Vestweber D., Eistetter H., Lottspeich F., Engel J.,
RA Doelz R., Jaehnig F., Epplen J., Mayer S., Mueller C., Kemler R.;
RT "The structure of cell adhesion molecule uvomorulin. Insights into the
RT molecular mechanism of Ca2+-dependent cell adhesion.";
RL EMBO J. 6:3647-3653(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RX PubMed=1763063; DOI=10.1073/pnas.88.24.11495;
RA Behrens J., Loewrick O., Klein-Hitpass L., Birchmeier W.;
RT "The E-cadherin promoter: functional analysis of a G.C-rich region and an
RT epithelial cell-specific palindromic regulatory element.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:11495-11499(1991).
RN [5]
RP IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
RX PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9;
RA Butz S., Kemler R.;
RT "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell
RT adhesion.";
RL FEBS Lett. 355:195-200(1994).
RN [6]
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=8879495; DOI=10.1095/biolreprod55.4.822;
RA Munro S.B., Blaschuk O.W.;
RT "A comprehensive survey of the cadherins expressed in the testes of fetal,
RT immature, and adult mice utilizing the polymerase chain reaction.";
RL Biol. Reprod. 55:822-827(1996).
RN [7]
RP NOT A RECEPTOR FOR L.MONOCYTOGENES, AND MUTAGENESIS OF GLU-172.
RX PubMed=10406800; DOI=10.1093/emboj/18.14.3956;
RA Lecuit M., Dramsi S., Gottardi C., Fedor-Chaiken M., Gumbiner B.,
RA Cossart P.;
RT "A single amino acid in E-cadherin responsible for host specificity towards
RT the human pathogen Listeria monocytogenes.";
RL EMBO J. 18:3956-3963(1999).
RN [8]
RP FUNCTION.
RX PubMed=11976333; DOI=10.1074/jbc.m201984200;
RA Meigs T.E., Fedor-Chaiken M., Kaplan D.D., Brackenbury R., Casey P.J.;
RT "Galpha12 and Galpha13 negatively regulate the adhesive functions of
RT cadherin.";
RL J. Biol. Chem. 277:24594-24600(2002).
RN [9]
RP RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, AND LACK OF
RP ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
RX PubMed=16325582; DOI=10.1016/j.cell.2005.09.020;
RA Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.;
RT "Deconstructing the cadherin-catenin-actin complex.";
RL Cell 123:889-901(2005).
RN [10]
RP LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
RX PubMed=18093941; DOI=10.1073/pnas.0710504105;
RA Abe K., Takeichi M.;
RT "EPLIN mediates linkage of the cadherin catenin complex to F-actin and
RT stabilizes the circumferential actin belt.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP INTERACTION WITH TRPV4 AND CTNNB1.
RX PubMed=20413591; DOI=10.1074/jbc.m110.103606;
RA Sokabe T., Fukumi-Tominaga T., Yonemura S., Mizuno A., Tominaga M.;
RT "The TRPV4 channel contributes to intercellular junction formation in
RT keratinocytes.";
RL J. Biol. Chem. 285:18749-18758(2010).
RN [13]
RP GLYCOSYLATION AT SER-282; SER-287; THR-360; THR-472; THR-474; THR-511;
RP THR-578; THR-580 AND THR-582.
RX PubMed=28973932; DOI=10.1073/pnas.1708319114;
RA Larsen I.S.B., Narimatsu Y., Joshi H.J., Siukstaite L., Harrison O.J.,
RA Brasch J., Goodman K.M., Hansen L., Shapiro L., Honig B., Vakhrushev S.Y.,
RA Clausen H., Halim A.;
RT "Discovery of an O-mannosylation pathway selectively serving cadherins and
RT protocadherins.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:11163-11168(2017).
RN [14]
RP IDENTIFICATION IN COMPLEX WITH ADAM10 AND EPHA4, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=30639848; DOI=10.1016/j.isci.2018.12.017;
RA Defourny J., Peuckert C., Kullander K., Malgrange B.;
RT "EphA4-ADAM10 Interplay Patterns the Cochlear Sensory Epithelium through
RT Local Disruption of Adherens Junctions.";
RL IScience 11:246-257(2019).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 157-370, AND CALCIUM-BINDING
RP SITES.
RX PubMed=8598933; DOI=10.1038/380360a0;
RA Nagar B., Overduin M., Ikura M., Rini J.M.;
RT "Structural basis of calcium-induced E-cadherin rigidification and
RT dimerization.";
RL Nature 380:360-364(1996).
RN [16]
RP STRUCTURE BY NMR OF 157-260.
RX PubMed=8785495; DOI=10.1007/bf00202035;
RA Overduin M., Tong K.I., Kay C.M., Ikura M.;
RT "1H, 15N and 13C resonance assignments and monomeric structure of the
RT amino-terminal extracellular domain of epithelial cadherin.";
RL J. Biomol. NMR 7:173-189(1996).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 577-728 IN COMPLEX WITH CTNNB1,
RP AND PHOSPHORYLATION.
RX PubMed=11348595; DOI=10.1016/s0092-8674(01)00330-0;
RA Huber A.H., Weis W.I.;
RT "The structure of the beta-catenin/E-cadherin complex and the molecular
RT basis of diverse ligand recognition by beta-catenin.";
RL Cell 105:391-402(2001).
RN [18] {ECO:0007744|PDB:2OMW}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 158-256 IN COMPLEX WITH
RP L.MONOCYTOGENES INLA, AND MUTAGENESIS OF GLU-172 AND GLN-220.
RX PubMed=17540170; DOI=10.1016/j.cell.2007.03.049;
RA Wollert T., Pasche B., Rochon M., Deppenmeier S., van den Heuvel J.,
RA Gruber A.D., Heinz D.W., Lengeling A., Schubert W.D.;
RT "Extending the host range of Listeria monocytogenes by rational protein
RT design.";
RL Cell 129:891-902(2007).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 778-884 IN COMPLEX WITH HUMAN JUP,
RP AND PHOSPHORYLATION AT SER-840; SER-842 AND SER-848.
RX PubMed=19759396; DOI=10.1074/jbc.m109.047928;
RA Choi H.J., Gross J.C., Pokutta S., Weis W.I.;
RT "Interactions of plakoglobin and beta-catenin with desmosomal cadherins:
RT basis of selective exclusion of alpha- and beta-catenin from desmosomes.";
RL J. Biol. Chem. 284:31776-31788(2009).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins
CC (PubMed:11976333). They preferentially interact with themselves in a
CC homophilic manner in connecting cells; cadherins may thus contribute to
CC the sorting of heterogeneous cell types. CDH1 is involved in mechanisms
CC regulating cell-cell adhesions, mobility and proliferation of
CC epithelial cells (PubMed:11976333). Has a potent invasive suppressor
CC role. It is a ligand for integrin alpha-E/beta-7 (By similarity).
CC {ECO:0000250|UniProtKB:P12830, ECO:0000269|PubMed:11976333}.
CC -!- FUNCTION: E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta
CC precursors. Has a strong inhibitory effect on APP C99 and C83
CC production (By similarity). {ECO:0000250|UniProtKB:P12830}.
CC -!- FUNCTION: (Microbial infection) Does not function as a receptor for
CC L.monocytogenes internalin A (InlA); mutating a single surface-exposed
CC residue confers receptor activity to this protein and promotes uptake
CC of the bacteria. {ECO:0000269|PubMed:10406800}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Component of an
CC E-cadherin/ catenin adhesion complex composed of at least E-
CC cadherin/CDH1, beta-catenin/CTNNB1 or gamma-catenin/JUP, and
CC potentially alpha-catenin/CTNNA1; the complex is located to adherens
CC junctions (PubMed:7982500, PubMed:19759396). Interacts with the TRPV4
CC and CTNNB1 complex (PubMed:20413591, PubMed:11348595). Interacts with
CC CTNND1 (By similarity). The stable association of CTNNA1 is
CC controversial as CTNNA1 was shown not to bind to F-actin when assembled
CC in the complex (PubMed:16325582). Alternatively, the CTNNA1-containing
CC complex may be linked to F-actin by other proteins such as LIMA1
CC (PubMed:18093941). Interaction with PSEN1, cleaves CDH1 resulting in
CC the disassociation of cadherin-based adherens junctions (CAJs) (By
CC similarity). Interacts with AJAP1 and DLGAP5 (By similarity). Interacts
CC with TBC1D2 (By similarity). Interacts with LIMA1 (By similarity).
CC Interacts with CAV1 (By similarity). Interacts with PIP5K1C (By
CC similarity). Interacts with RAB8B (By similarity). Interacts with DDR1;
CC this stabilizes CDH1 at the cell surface and inhibits its
CC internalization (By similarity). Interacts with RAPGEF2 (By
CC similarity). Interacts with KLRG1 (By similarity). Forms a ternary
CC complex composed of ADAM10, CADH1 and EPHA4; within the complex, CADH1
CC is cleaved by ADAM10 which disrupts adherens junctions
CC (PubMed:30639848). Interacts with SPEF1 (By similarity).
CC {ECO:0000250|UniProtKB:P12830, ECO:0000250|UniProtKB:Q9R0T4,
CC ECO:0000269|PubMed:11348595, ECO:0000269|PubMed:16325582,
CC ECO:0000269|PubMed:18093941, ECO:0000269|PubMed:19759396,
CC ECO:0000269|PubMed:20413591, ECO:0000269|PubMed:30639848,
CC ECO:0000269|PubMed:7982500}.
CC -!- INTERACTION:
CC P09803; P09803: Cdh1; NbExp=12; IntAct=EBI-984420, EBI-984420;
CC P09803; P61809: Cdk5r1; NbExp=2; IntAct=EBI-984420, EBI-7840438;
CC P09803; Q02248: Ctnnb1; NbExp=16; IntAct=EBI-984420, EBI-397872;
CC P09803; O60716-29: CTNND1; Xeno; NbExp=3; IntAct=EBI-984420, EBI-702059;
CC P09803; A5HZZ4: ha70; Xeno; NbExp=6; IntAct=EBI-984420, EBI-16109901;
CC P09803; P28827: PTPRM; Xeno; NbExp=3; IntAct=EBI-984420, EBI-2257317;
CC P09803; Q13309: SKP2; Xeno; NbExp=2; IntAct=EBI-984420, EBI-456291;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:30639848}. Cell membrane; Single-pass type I
CC membrane protein. Endosome {ECO:0000250}. Golgi apparatus, trans-Golgi
CC network {ECO:0000250}. Note=Colocalizes with DLGAP5 at sites of cell-
CC cell contact in intestinal epithelial cells. Anchored to actin
CC microfilaments through association with alpha-, beta- and gamma-
CC catenin. Sequential proteolysis induced by apoptosis or calcium influx,
CC results in translocation from sites of cell-cell contact to the
CC cytoplasm. Colocalizes with RAB11A endosomes during its transport from
CC the Golgi apparatus to the plasma membrane (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in inner and outer pillar cells of the
CC organ of Corti (at protein level) (PubMed:30639848). Non-neural
CC epithelial tissues. {ECO:0000269|PubMed:30639848}.
CC -!- DEVELOPMENTAL STAGE: In the testis, expression is highest in fetal
CC gonad, then decreases 5-fold in newborn. Detectable in 7-day-old but
CC not in 21-day-old or adult. {ECO:0000269|PubMed:8879495}.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain.
CC -!- PTM: During apoptosis or with calcium influx, cleaved by a membrane-
CC bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3 (By
CC similarity). Processing by the metalloproteinase, induced by calcium
CC influx, causes disruption of cell-cell adhesion and the subsequent
CC release of beta-catenin into the cytoplasm (By similarity). The
CC residual membrane-tethered cleavage product is rapidly degraded via an
CC intracellular proteolytic pathway (By similarity). Cleavage by caspase-
CC 3 releases the cytoplasmic tail resulting in disintegration of the
CC actin microfilament system (By similarity). The gamma-secretase-
CC mediated cleavage promotes disassembly of adherens junctions (By
CC similarity). During development of the cochlear organ of Corti,
CC cleavage by ADAM10 at adherens junctions promotes pillar cell
CC separation (PubMed:30639848). {ECO:0000250|UniProtKB:P12830,
CC ECO:0000269|PubMed:30639848}.
CC -!- PTM: O-glycosylated. O-manosylated by TMTC1, TMTC2, TMTC3 or TMTC4.
CC Ser-287 and Thr-511 are O-manosylated by TMTC2 or TMTC4 but not TMTC1
CC or TMTC3. {ECO:0000269|PubMed:28973932}.
CC -!- PTM: N-glycosylation at Asn-639 is essential for expression, folding
CC and trafficking. Addition of bisecting N-acetylglucosamine by MGAT3
CC modulates its cell membrane location (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P12830}.
CC -!- PTM: Ubiquitinated by a SCF complex containing SKP2, which requires
CC prior phosphorylation by CK1/CSNK1A1. Ubiquitinated by CBLL1/HAKAI,
CC requires prior phosphorylation at Tyr-756 (By similarity).
CC {ECO:0000250}.
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DR EMBL; X06115; CAA29488.1; -; mRNA.
DR EMBL; X60961; CAA43292.1; -; Genomic_DNA.
DR EMBL; X60962; CAA43292.1; JOINED; Genomic_DNA.
DR EMBL; X60963; CAA43292.1; JOINED; Genomic_DNA.
DR EMBL; X60964; CAA43292.1; JOINED; Genomic_DNA.
DR EMBL; X60965; CAA43292.1; JOINED; Genomic_DNA.
DR EMBL; X60966; CAA43292.1; JOINED; Genomic_DNA.
DR EMBL; X60967; CAA43292.1; JOINED; Genomic_DNA.
DR EMBL; X60968; CAA43292.1; JOINED; Genomic_DNA.
DR EMBL; X60969; CAA43292.1; JOINED; Genomic_DNA.
DR EMBL; X60970; CAA43292.1; JOINED; Genomic_DNA.
DR EMBL; X60971; CAA43292.1; JOINED; Genomic_DNA.
DR EMBL; X60972; CAA43292.1; JOINED; Genomic_DNA.
DR EMBL; X60973; CAA43292.1; JOINED; Genomic_DNA.
DR EMBL; X60974; CAA43292.1; JOINED; Genomic_DNA.
DR EMBL; X60975; CAA43292.1; JOINED; Genomic_DNA.
DR EMBL; X06339; CAA29645.1; -; mRNA.
DR EMBL; M81449; AAA37352.1; -; Genomic_DNA.
DR CCDS; CCDS22638.1; -.
DR PIR; S04528; IJMSCE.
DR PIR; S34438; S34438.
DR RefSeq; NP_033994.1; NM_009864.3.
DR PDB; 1EDH; X-ray; 2.00 A; A/B=156-380.
DR PDB; 1FF5; X-ray; 2.93 A; A/B=157-374.
DR PDB; 1I7W; X-ray; 2.00 A; B/D=734-884.
DR PDB; 1I7X; X-ray; 3.00 A; B/D=734-884.
DR PDB; 1Q1P; X-ray; 3.20 A; A=158-369.
DR PDB; 1SUH; NMR; -; A=156-300.
DR PDB; 2OMW; X-ray; 1.85 A; B=158-256.
DR PDB; 2QVF; X-ray; 2.40 A; B=157-369.
DR PDB; 3IFQ; X-ray; 2.80 A; C/D=778-884.
DR PDB; 3LNE; X-ray; 2.00 A; A=157-369.
DR PDB; 3LNF; X-ray; 2.50 A; A/B=157-369.
DR PDB; 3LNG; X-ray; 2.70 A; A/B=157-369.
DR PDB; 3LNH; X-ray; 2.60 A; A/B=157-369.
DR PDB; 3LNI; X-ray; 2.30 A; A/B=157-369.
DR PDB; 3Q2L; X-ray; 2.70 A; A/B=157-369.
DR PDB; 3Q2N; X-ray; 2.73 A; A/B=157-369.
DR PDB; 3Q2V; X-ray; 3.40 A; A/B=157-700.
DR PDB; 3QRB; X-ray; 1.80 A; A/B=157-369.
DR PDB; 4QD2; X-ray; 2.40 A; E/J=157-369.
DR PDB; 7AR4; X-ray; 2.60 A; PaP=783-798.
DR PDBsum; 1EDH; -.
DR PDBsum; 1FF5; -.
DR PDBsum; 1I7W; -.
DR PDBsum; 1I7X; -.
DR PDBsum; 1Q1P; -.
DR PDBsum; 1SUH; -.
DR PDBsum; 2OMW; -.
DR PDBsum; 2QVF; -.
DR PDBsum; 3IFQ; -.
DR PDBsum; 3LNE; -.
DR PDBsum; 3LNF; -.
DR PDBsum; 3LNG; -.
DR PDBsum; 3LNH; -.
DR PDBsum; 3LNI; -.
DR PDBsum; 3Q2L; -.
DR PDBsum; 3Q2N; -.
DR PDBsum; 3Q2V; -.
DR PDBsum; 3QRB; -.
DR PDBsum; 4QD2; -.
DR PDBsum; 7AR4; -.
DR AlphaFoldDB; P09803; -.
DR SMR; P09803; -.
DR BioGRID; 198631; 42.
DR CORUM; P09803; -.
DR DIP; DIP-29635N; -.
DR IntAct; P09803; 41.
DR MINT; P09803; -.
DR STRING; 10090.ENSMUSP00000000312; -.
DR GlyGen; P09803; 11 sites.
DR iPTMnet; P09803; -.
DR PhosphoSitePlus; P09803; -.
DR CPTAC; non-CPTAC-3565; -.
DR jPOST; P09803; -.
DR MaxQB; P09803; -.
DR PaxDb; P09803; -.
DR PeptideAtlas; P09803; -.
DR PRIDE; P09803; -.
DR ProteomicsDB; 265497; -.
DR DNASU; 12550; -.
DR GeneID; 12550; -.
DR KEGG; mmu:12550; -.
DR UCSC; uc009ngi.1; mouse.
DR CTD; 999; -.
DR MGI; MGI:88354; Cdh1.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; P09803; -.
DR OrthoDB; 182239at2759; -.
DR PhylomeDB; P09803; -.
DR TreeFam; TF316817; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs.
DR BioGRID-ORCS; 12550; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Cdh1; mouse.
DR EvolutionaryTrace; P09803; -.
DR PRO; PR:P09803; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P09803; protein.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0043679; C:axon terminus; IDA:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0016342; C:catenin complex; IDA:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016600; C:flotillin complex; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0043219; C:lateral loop; IDA:BHF-UCL.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR GO; GO:0033268; C:node of Ranvier; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:BHF-UCL.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0045294; F:alpha-catenin binding; IPI:MGI.
DR GO; GO:0030506; F:ankyrin binding; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; IDA:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; IMP:MGI.
DR GO; GO:0045295; F:gamma-catenin binding; ISO:MGI.
DR GO; GO:0032794; F:GTPase activating protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:MGI.
DR GO; GO:0034332; P:adherens junction organization; ISO:MGI.
DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:MGI.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IMP:MGI.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
DR GO; GO:0071681; P:cellular response to indole-3-methanol; ISO:MGI.
DR GO; GO:0071285; P:cellular response to lithium ion; ISO:MGI.
DR GO; GO:0090102; P:cochlea development; IDA:UniProtKB.
DR GO; GO:0046697; P:decidualization; IMP:CACAO.
DR GO; GO:0007566; P:embryo implantation; IMP:CACAO.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0060576; P:intestinal epithelial cell development; IMP:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISO:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:MGI.
DR GO; GO:0010955; P:negative regulation of protein processing; IMP:MGI.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:MGI.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0019538; P:protein metabolic process; IDA:MGI.
DR GO; GO:0060693; P:regulation of branching involved in salivary gland morphogenesis; IMP:MGI.
DR GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
DR GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR GO; GO:2001222; P:regulation of neuron migration; IDA:MGI.
DR GO; GO:0099576; P:regulation of protein catabolic process at postsynapse, modulating synaptic transmission; ISO:MGI.
DR GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; IMP:MGI.
DR GO; GO:0033561; P:regulation of water loss via skin; IMP:MGI.
DR GO; GO:0060662; P:salivary gland cavitation; IMP:MGI.
DR GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR GO; GO:0007416; P:synapse assembly; ISO:MGI.
DR GO; GO:0001829; P:trophectodermal cell differentiation; IMP:MGI.
DR GO; GO:0035847; P:uterine epithelium development; IMP:CACAO.
DR DisProt; DP00159; -.
DR Gene3D; 4.10.900.10; -; 1.
DR IDEAL; IID50003; -.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR030049; CDH1.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR PANTHER; PTHR24027:SF319; PTHR24027:SF319; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF01049; Cadherin_C; 1.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 4.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Endosome; Glycoprotein; Golgi apparatus; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..156
FT /evidence="ECO:0000255"
FT /id="PRO_0000003717"
FT CHAIN 157..884
FT /note="Cadherin-1"
FT /id="PRO_0000003718"
FT CHAIN 703..884
FT /note="E-Cad/CTF1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000236070"
FT CHAIN 734..884
FT /note="E-Cad/CTF2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000236071"
FT CHAIN 753..884
FT /note="E-Cad/CTF3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000236072"
FT TOPO_DOM 157..709
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..733
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 734..884
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 157..264
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 265..377
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 378..488
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 489..595
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 596..699
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 119..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..771
FT /note="Required for binding CTNND1 and PSEN1"
FT /evidence="ECO:0000250"
FT REGION 813..884
FT /note="Required for binding alpha, beta and gamma catenins"
FT /evidence="ECO:0000250"
FT COMPBIAS 768..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 290
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT SITE 702..703
FT /note="Cleavage; by a metalloproteinase"
FT /evidence="ECO:0000250"
FT SITE 733..734
FT /note="Cleavage; by gamma-secretase/PS1"
FT /evidence="ECO:0000250"
FT SITE 752..753
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 755
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P12830"
FT MOD_RES 756
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P12830"
FT MOD_RES 757
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P12830"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12830"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12830"
FT MOD_RES 840
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19759396"
FT MOD_RES 842
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19759396"
FT MOD_RES 848
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19759396"
FT CARBOHYD 282
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:28973932"
FT CARBOHYD 287
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:28973932"
FT CARBOHYD 360
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:28973932"
FT CARBOHYD 472
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:28973932"
FT CARBOHYD 474
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:28973932"
FT CARBOHYD 511
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:28973932"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:28973932"
FT CARBOHYD 580
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:28973932"
FT CARBOHYD 582
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:28973932"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 172
FT /note="E->P: Adheres to and takes up L.monocytogenes InlA
FT coated beads."
FT /evidence="ECO:0000269|PubMed:10406800"
FT MUTAGEN 220
FT /note="Q->E: Increased affinity for L.monocytogenes InlA.
FT Greatly increased affinity; when associated with P-172."
FT /evidence="ECO:0000269|PubMed:17540170"
FT CONFLICT 267
FT /note="E -> P (in Ref. 2; CAA43292)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="S -> F (in Ref. 2; CAA43292)"
FT /evidence="ECO:0000305"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:3QRB"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:3QRB"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:3QRB"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:3QRB"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:3QRB"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:3QRB"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:3QRB"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:3QRB"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:3QRB"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:3QRB"
FT STRAND 228..238
FT /evidence="ECO:0007829|PDB:3QRB"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:1Q1P"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2OMW"
FT STRAND 248..255
FT /evidence="ECO:0007829|PDB:3QRB"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:3QRB"
FT STRAND 267..274
FT /evidence="ECO:0007829|PDB:3QRB"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:3QRB"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:3QRB"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:1Q1P"
FT STRAND 303..311
FT /evidence="ECO:0007829|PDB:3QRB"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:3QRB"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:3QRB"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:3QRB"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:3QRB"
FT STRAND 342..350
FT /evidence="ECO:0007829|PDB:3QRB"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:3QRB"
FT STRAND 358..368
FT /evidence="ECO:0007829|PDB:3QRB"
FT STRAND 376..389
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:3Q2V"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 413..419
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 425..429
FT /evidence="ECO:0007829|PDB:3Q2V"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:3Q2V"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 450..462
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 471..480
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 487..492
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 494..498
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 506..509
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 524..529
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:3Q2V"
FT TURN 539..541
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 543..546
FT /evidence="ECO:0007829|PDB:3Q2V"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 560..570
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 573..575
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 579..588
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 596..598
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 603..608
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 612..617
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 624..627
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 631..634
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 637..639
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 649..655
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 673..675
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 684..688
FT /evidence="ECO:0007829|PDB:3Q2V"
FT STRAND 785..789
FT /evidence="ECO:0007829|PDB:3IFQ"
FT TURN 806..808
FT /evidence="ECO:0007829|PDB:3IFQ"
FT HELIX 818..822
FT /evidence="ECO:0007829|PDB:1I7W"
FT STRAND 824..827
FT /evidence="ECO:0007829|PDB:1I7X"
FT STRAND 830..834
FT /evidence="ECO:0007829|PDB:3IFQ"
FT TURN 864..866
FT /evidence="ECO:0007829|PDB:1I7W"
FT HELIX 869..871
FT /evidence="ECO:0007829|PDB:1I7W"
FT HELIX 872..877
FT /evidence="ECO:0007829|PDB:1I7W"
SQ 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
