[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Pancreas; DOI=10.1007/BF00996219; PubMed=8459805 [NCBI, ExPASy, EBI, Israel, Japan] Bussemakers M.J.G., Mees S.G.M., van Bokhoven A., Debruyne F.M.J., Schalken J.A.; "Molecular cloning and characterization of the human E-cadherin cDNA."; Mol. Biol. Rep. 17:123-128(1993).
[2]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GASTRIC ADENOCARCINOMA 274-GLY--PRO-277 DEL. DOI=10.1073/pnas.91.5.1858; PubMed=8127895 [NCBI, ExPASy, EBI, Israel, Japan] Oda T., Kanai Y., Oyama T., Yoshiura K., Shimoyama Y., Birchmeier W., Sugimura T., Hirohashi S.; "E-cadherin gene mutations in human gastric carcinoma cell lines."; Proc. Natl. Acad. Sci. U.S.A. 91:1858-1862(1994).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1006/bbrc.1994.1656; PubMed=8185635 [NCBI, ExPASy, EBI, Israel, Japan] Rimm D.L., Morrow J.S.; "Molecular cloning of human E-cadherin suggests a novel subdivision of the cadherin superfamily."; Biochem. Biophys. Res. Commun. 200:1754-1761(1994).
[4]	NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 586-591, PROTEOLYTIC PROCESSING, AND SUBCELLULAR LOCATION. TISSUE=Epidermal carcinoma; DOI=10.1038/sj.onc.1203191; PubMed=10597309 [NCBI, ExPASy, EBI, Israel, Japan] Ito K., Okamoto I., Araki N., Kawano Y., Nakao M., Fujiyama S., Tomita K., Mimori T., Saya H.; "Calcium influx triggers the sequential proteolysis of extracellular and cytoplasmic domains of E-cadherin, leading to loss of beta-catenin from cell-cell contacts."; Oncogene 18:7080-7090(1999).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-478; THR-617; MET-832 AND LYS-880. NIEHS SNPs program; Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16. DOI=10.1006/bbrc.1994.2321; PubMed=8093045 [NCBI, ExPASy, EBI, Israel, Japan] Bussemakers M.J.G., Giroldi L.A., van Bokhoven A., Schalken J.A.; "Transcriptional regulation of the human E-cadherin gene in human prostate cancer cell lines: characterization of the human E-cadherin gene promoter."; Biochem. Biophys. Res. Commun. 203:1284-1290(1994).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16. TISSUE=Placenta; DOI=10.1073/pnas.92.16.7416; PubMed=7543680 [NCBI, ExPASy, EBI, Israel, Japan] Yoshiura K., Kanai Y., Ochiai A., Shimoyama Y., Sugimura T., Hirohashi S.; "Silencing of the E-cadherin invasion-suppressor gene by CpG methylation in human carcinomas."; Proc. Natl. Acad. Sci. U.S.A. 92:7416-7419(1995).
[8]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-882. TISSUE=Placenta; DOI=10.1016/0888-7543(95)80212-5; PubMed=7601454 [NCBI, ExPASy, EBI, Israel, Japan] Berx G., Staes K., van Hengel J., Molemans F., Bussemakers M.J.G., van Bokhoven A., van Roy F.; "Cloning and characterization of the human invasion suppressor gene E-cadherin (CDH1)."; Genomics 26:281-289(1995).
[9]	NUCLEOTIDE SEQUENCE [MRNA] OF 172-311. TISSUE=Liver; DOI=10.1111/j.1432-0436.1988.tb00593.x; PubMed=3263290 [NCBI, ExPASy, EBI, Israel, Japan] Mansouri A., Spurr N., Goodfellow P.N., Kemler R.; "Characterization and chromosomal localization of the gene encoding the human cell adhesion molecule uvomorulin."; Differentiation 38:67-71(1988).
[10]	NUCLEOTIDE SEQUENCE [MRNA] OF 265-392. TISSUE=Liver; Frixen U.H.; Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases.
[11]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 337-476, AND VARIANTS DIFFUSE GASTRIC CANCER ALA-370 AND ASP-473. PubMed=8033105 [NCBI, ExPASy, EBI, Israel, Japan] Becker K.-F., Atkinson M.J., Reich U., Becker I., Nekarda H., Siewert J.R., Hoefler H.; "E-cadherin gene mutations provide clues to diffuse type gastric carcinomas."; Cancer Res. 54:3845-3852(1994).
[12]	PROTEIN SEQUENCE OF 701-714 AND 732-742, PROTEOLYTIC PROCESSING BY GAMMA-SECRETASE/PS1 AND A MEMBRANE-BOUND METALLOPROTEINASE, AND MUTAGENESIS OF 759-GLY--GLY-761. DOI=10.1093/emboj/21.8.1948; PubMed=11953314 [NCBI, ExPASy, EBI, Israel, Japan] Marambaud P., Shioi J., Serban G., Georgakopoulos A., Sarner S., Nagy V., Baki L., Wen P., Efthimiopoulos S., Shao Z., Wisniewski T., Robakis N.K.; "A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions."; EMBO J. 21:1948-1956(2002).
[13]	DOMAIN CATENIN BINDING. DOI=10.1073/pnas.87.11.4246; PubMed=2349235 [NCBI, ExPASy, EBI, Israel, Japan] Ozawa M., Ringwald M., Kemler R.; "Uvomorulin-catenin complex formation is regulated by a specific domain in the cytoplasmic region of the cell adhesion molecule."; Proc. Natl. Acad. Sci. U.S.A. 87:4246-4250(1990).
[14]	COMPONENT OF THE PSEN1/E-CADHERIN/CATENIN ADHESION COMPLEX WITH PSEN1; CDH1; CTNNA1 AND CTNNB1/CTNND1. DOI=10.1016/S1097-2765(00)80219-1; PubMed=10635315 [NCBI, ExPASy, EBI, Israel, Japan] Georgakopoulos A., Marambaud P., Efthimiopoulos S., Shioi J., Cui W., Li H.-C., Schutte M., Gordon R., Holstein G.R., Martinelli G., Mehta P., Friedrich V.L. Jr., Robakis N.K.; "Presenilin-1 forms complexes with the cadherin/catenin cell-cell adhesion system and is recruited to intercellular and synaptic contacts."; Mol. Cell 4:893-902(1999).
[15]	PROTEOLYTIC PROCESSING. DOI=10.1074/jbc.M006102200; PubMed=11076937 [NCBI, ExPASy, EBI, Israel, Japan] Steinhusen U., Weiske J., Badock V., Tauber R., Bommert K., Huber O.; "Cleavage and shedding of E-cadherin after induction of apoptosis."; J. Biol. Chem. 276:4972-4980(2001).
[16]	INTERACTION WITH PSEN1. DOI=10.1073/pnas.041603398; PubMed=11226248 [NCBI, ExPASy, EBI, Israel, Japan] Baki L., Marambaud P., Efthimiopoulos S., Georgakopoulos A., Wen P., Cui W., Shioi J., Koo E., Ozawa M., Friedrich V.L., Robakis N.K.; "Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex."; Proc. Natl. Acad. Sci. U.S.A. 98:2381-2386(2001).
[17]	INTERCHAIN DISULFIDE BOND. DOI=10.1074/jbc.M200916200; PubMed=11856755 [NCBI, ExPASy, EBI, Israel, Japan] Makagiansar I.T., Nguyen P.D., Ikesue A., Kuczera K., Dentler W., Urbauer J.L., Galeva N., Alterman M., Siahaan T.J.; "Disulfide bond formation promotes the cis- and trans-dimerization of the E-cadherin-derived first repeat."; J. Biol. Chem. 277:16002-16010(2002).
[18]	INTERACTION WITH DLGAP5, AND SUBCELLULAR LOCATION. DOI=10.1074/jbc.M309843200; PubMed=14699157 [NCBI, ExPASy, EBI, Israel, Japan] Laprise P., Viel A., Rivard N.; "Human homolog of disc-large is required for adherens junction assembly and differentiation of human intestinal epithelial cells."; J. Biol. Chem. 279:10157-10166(2004).
[19]	INTERACTION WITH AJAP1. TISSUE=Brain; DOI=10.1091/mbc.E03-05-0281; PubMed=14595118 [NCBI, ExPASy, EBI, Israel, Japan] Bharti S., Handrow-Metzmacher H., Zickenheiner S., Zeitvogel A., Baumann R., Starzinski-Powitz A.; "Novel membrane protein shrew-1 targets to cadherin-mediated junctions in polarized epithelial cells."; Mol. Biol. Cell 15:397-406(2004).
[20]	COMPONENT OF PSEN1/CATENIN/CADHERIN COMPLEX WITH PSEN1; CDH1 AND CTNNB1, AND MUTAGENESIS OF 759-GLY--GLY-761. DOI=10.1074/jbc.M507503200; PubMed=16126725 [NCBI, ExPASy, EBI, Israel, Japan] Serban G., Kouchi Z., Baki L., Georgakopoulos A., Litterst C.M., Shioi J., Robakis N.K.; "Cadherins mediate both the association between PS1 and beta-catenin and the effects of PS1 on beta-catenin stability."; J. Biol. Chem. 280:36007-36012(2005).
[21]	FUNCTION OF E-CAD/CTF2. DOI=10.1111/j.1471-4159.2005.03616.x; PubMed=16417575 [NCBI, ExPASy, EBI, Israel, Japan] Agiostratidou G., Muros R.M., Shioi J., Marambaud P., Robakis N.K.; "The cytoplasmic sequence of E-cadherin promotes non-amyloidogenic degradation of A beta precursors."; J. Neurochem. 96:1182-1188(2006).
[22]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 156-255 IN COMPLEX WITH LISTERIA INTERNALIN. DOI=10.1016/S0092-8674(02)01136-4; PubMed=12526809 [NCBI, ExPASy, EBI, Israel, Japan] Schubert W.-D., Urbanke C., Ziehm T., Beier V., Machner M.P., Domann E., Wehland J., Chakraborty T., Heinz D.W.; "Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin."; Cell 111:825-836(2002).
[23]	REVIEW ON VARIANTS. DOI=10.1002/(SICI)1098-1004(1998)12:4<226::AID-HUMU2>3.0.CO;2-D; PubMed=9744472 [NCBI, ExPASy, EBI, Israel, Japan] Berx G., Becker K.-F., Hoefler H., van Roy F.; "Mutations of the human E-cadherin (CDH1) gene."; Hum. Mutat. 12:226-237(1998).
[24]	VARIANT LOBULAR BREAST CARCINOMA SER-315. PubMed=7961105 [NCBI, ExPASy, EBI, Israel, Japan] Kanai Y., Oda T., Tsuda H., Ochiai A., Hirohashi S.; "Point mutation of the E-cadherin gene in invasive lobular carcinoma of the breast."; Jpn. J. Cancer Res. 85:1035-1039(1994).
[25]	VARIANTS ENDOMETRIAL CANCER THR-617 AND VAL-711, AND VARIANT OVARIAN CANCER GLY-838. DOI=10.1038/ng0594-98; PubMed=8075649 [NCBI, ExPASy, EBI, Israel, Japan] Risinger J.I., Berchuck A., Kohler M.F., Boyd J.; "Mutations of the E-cadherin gene in human gynecologic cancers."; Nat. Genet. 7:98-102(1994).
[26]	VARIANT DIFFUSE GASTRIC CANCER PRO-193. PubMed=8797891 [NCBI, ExPASy, EBI, Israel, Japan] Muta H., Noguchi M., Kanai Y., Ochiai A., Nawata H., Hirohashi S.; "E-cadherin gene mutations in signet ring cell carcinoma of the stomach."; Jpn. J. Cancer Res. 87:843-848(1996).
[27]	VARIANTS GASTRIC CARCINOMA ASP-400 DEL AND 418-ASP--PHE-423 DEL. PubMed=9045944 [NCBI, ExPASy, EBI, Israel, Japan] Tamura G., Sakata K., Nishizuka S., Maesawa C., Suzuki Y., Iwaya T., Terashima M., Saito K., Satodate R.; "Inactivation of the E-cadherin gene in primary gastric carcinomas and gastric carcinoma cell lines."; Jpn. J. Cancer Res. 87:1153-1159(1996).
[28]	VARIANT THYROID CANCER THR-592. DOI=10.1002/(SICI)1097-0215(19970106)70:1<32::AID-IJC5>3.0.CO;2-7; PubMed=8985087 [NCBI, ExPASy, EBI, Israel, Japan] Soares P., Berx G., van Roy F., Sobrinho-Simoes M.; "E-cadherin gene alterations are rare events in thyroid tumors."; Int. J. Cancer 70:32-38(1997).
[29]	VARIANTS ASP-336 AND ILE-470. DOI=10.1038/32918; PubMed=9537325 [NCBI, ExPASy, EBI, Israel, Japan] Guilford P.J., Hopkins J.B.W., Harraway J., McLeod M., McLeod N., Harawira P., Taite H., Scoular R., Miller A., Reeve A.E.; "E-cadherin germline mutations in familial gastric cancer."; Nature 392:402-405(1998).
[30]	VARIANTS HDGC GLY-244 AND ALA-487. DOI=10.1007/s100380050137; PubMed=10319582 [NCBI, ExPASy, EBI, Israel, Japan] Yoon K.-A., Ku J.-L., Yang H.-K., Kim W.H., Park S.Y., Park J.-G.; "Germline mutations of E-cadherin gene in Korean familial gastric cancer patients."; J. Hum. Genet. 44:177-180(1999).
[31]	VARIANT COLORECTAL CANCER ALA-340. DOI=10.1136/gut.47.2.262; PubMed=10896919 [NCBI, ExPASy, EBI, Israel, Japan] Kim H.C., Wheeler J.M.D., Kim J.C., Ilyas M., Beck N.E., Kim B.S., Park K.C., Bodmer W.F.; "The E-cadherin gene (CDH1) variants T340A and L599V in gastric and colorectal cancer patients in Korea."; Gut 47:262-267(2000).
[32]	VARIANT ALA-270. PubMed=11705864 [NCBI, ExPASy, EBI, Israel, Japan] Ikonen T., Matikainen M., Mononen N., Hyytinen E.R., Helin H.J., Tommola S., Tammela T.L., Pukkala E., Schleutker J., Kallioniemi O.-P., Koivisto P.A.; "Association of E-cadherin germ-line alterations with prostate cancer."; Clin. Cancer Res. 7:3465-3471(2001).
[33]	VARIANT THR-592. PubMed=11562785 [NCBI, ExPASy, EBI, Israel, Japan] Salahshor S., Hou H., Diep C.B., Loukola A., Zhang H., Liu T., Chen J., Iselius L., Rubio C., Lothe R.A., Aaltonen L., Sun X.F., Lindmark G., Lindblom A.; "A germline E-cadherin mutation in a family with gastric and colon cancer."; Int. J. Mol. Med. 8:439-443(2001).
[34]	VARIANT HDGC ALA-340. DOI=10.1002/humu.10068; PubMed=11968083 [NCBI, ExPASy, EBI, Israel, Japan] Oliveira C., Bordin M.C., Grehan N., Huntsman D., Suriano G., Machado J.C., Kiviluoto T., Aaltonen L., Jackson C.E., Seruca R., Caldas C.; "Screening E-cadherin in gastric cancer families reveals germline mutations only in hereditary diffuse gastric cancer kindred."; Hum. Mutat. 19:510-517(2002).
[35]	VARIANT HDGC MET-832. DOI=10.1002/ijc.10633; PubMed=12216071 [NCBI, ExPASy, EBI, Israel, Japan] Yabuta T., Shinmura K., Tani M., Yamaguchi S., Yoshimura K., Katai H., Nakajima T., Mochiki E., Tsujinaka T., Takami M., Hirose K., Yamaguchi A., Takenoshita S., Yokota J.; "E-cadherin gene variants in gastric cancer families whose probands are diagnosed with diffuse gastric cancer."; Int. J. Cancer 101:434-441(2002).
[36]	VARIANTS GASTRIC CANCER THR-617 AND VAL-634, AND CHARACTERIZATION OF VARIANTS GASTRIC CANCER ALA-340; THR-617 AND VAL-634. DOI=10.1093/hmg/ddg048; PubMed=12588804 [NCBI, ExPASy, EBI, Israel, Japan] Suriano G., Oliveira C., Ferreira P., Machado J.C., Bordin M.C., De Wever O., Bruyneel E.A., Moguilevsky N., Grehan N., Porter T.R., Richards F.M., Hruban R.H., Roviello F., Huntsman D., Mareel M., Carneiro F., Caldas C., Seruca R.; "Identification of CDH1 germline missense mutations associated with functional inactivation of the E-cadherin protein in young gastric cancer probands."; Hum. Mol. Genet. 12:575-582(2003).
[37]	VARIANTS ILE-282 AND ASN-777. DOI=10.1186/bcr1637; PubMed=17224074 [NCBI, ExPASy, EBI, Israel, Japan] Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A., Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S., Kristensen V., Perou C.M., Boerresen-Dale A.-L.; "Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas."; Breast Cancer Res. 9:R5-R5(2007).

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.
FUNCTION: E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta precursors. Has a strong inhibitory effect on APP C99 and C83 production.
SUBUNIT: Homodimer; disulfide-linked. Interacts directly, via the cytoplasmic domain, with CTNNB1 or JUP to form the PSEN1/cadherin/catenin adhesion complex which connects to the actin skeleton through the actin binding of alpha-catenin. Interaction with PSEN1, cleaves CDH1 resulting in the disassociation of cadherin-based adherens junctions (CAJs). Interacts with AJAP1, CTNND1 and DLGAP5.
INTERACTION:
P35222:CTNNB1; NbExp=1; IntAct=EBI-727477, EBI-491549;
P11362:FGFR1; NbExp=1; IntAct=EBI-727477, EBI-1028277;
P25146:inlA (xeno); NbExp=1; IntAct=EBI-727477, EBI-1035388;
P62136:PPP1CA; NbExp=2; IntAct=EBI-727477, EBI-357253;
Q15139:PRKD1; NbExp=3; IntAct=EBI-727477, EBI-1181072;
SUBCELLULAR LOCATION: Cell junction. Cell membrane; Single-pass type I membrane protein. 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.
TISSUE SPECIFICITY: Non-neural epithelial tissues.
PTM: During apoptosis or with calcium influx, cleaved by a membrane-bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3 to produce fragments of about 38 kDa (E-CAD/CTF1), 33 kDa (E-CAD/CTF2) and 29 kDa (E-CAD/CTF3), respectively. Processing by the metalloproteinase, induced by calcium influx, causes disruption of cell-cell adhesion and the subsequent release of beta-catenin into the cytoplasm. The residual membrane-tethered cleavage product is rapidly degraded via an intracellular proteolytic pathway. Cleavage by caspase-3 releases the cytoplasmic tail resulting in disintegration of the actin microfilament system. The gamma-secretase-mediated cleavage promotes disaaaembly of adherens junctions.
DISEASE: Defects in CDH1 are involved in dysfunction of the cell-cell adhesion system, triggering cancer invasion (gastric, breast, ovary, endometrium and thyroid) and metastasis.
DISEASE: Defects in CDH1 are a cause of gastric cancer [MIM:137215]; also known as hereditary familial diffuse gastric cancer (HDGC).
DISEASE: Defects in CDH1 are a cause of susceptibility to endometrial cancer [MIM:608089].
DISEASE: Defects in CDH1 are associated with ovarian cancer [MIM:167000]. Ovarian cancer is the leading cause of death from gynecologic malignancy. It is characterized by advanced presentation with loco-regional dissemination in the peritoneal cavity and the rare incidence of visceral metastases. These typical features relate to the biology of the disease, which is a principal determinant of outcome.
SIMILARITY: Contains 5 cadherin domains.
SEQUENCE CAUTION:
- Sequence=AAA61259.1; Type=Frameshift; Positions=16, 22, 25, 28, 31, 34, 52, 67, 73, 76, 94, 102, 633, 636;
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CDH1ID166ch16q22.html";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=CDH1";.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/cdh1/";.
WEB RESOURCE: Name=Wikipedia; Note=E-cadherin entry; URL="http://en.wikipedia.org/wiki/E-cadherin";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z13009; CAA78353.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z18923; CAA79356.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L08599; AAA61259.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ090940; AAY68225.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L34545; AAA21764.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D49685; BAA08537.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35402; CAA84586.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35403; CAA84586.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35404; CAA84586.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35405; CAA84586.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35406; CAA84586.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35407; CAA84586.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35408; CAA84586.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35409; CAA84586.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35410; CAA84586.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35411; CAA84586.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35412; CAA84586.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35413; CAA84586.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35414; CAA84586.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z35415; CAA84586.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X12790; CAA31279.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X52279; CAA36522.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S72492; AAD14108.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S72397; AAD14108.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S72491; AAD14108.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00025861; -.

S37654; IJHUCE.

NP_004351.1; -.

3D structure databases

PDB

1O6S; X-ray; 1.80 A; B=156-255.	[ExPASy / RCSB / EBI]
2O72; X-ray; 2.00 A; A=155-367.	[ExPASy / RCSB / EBI]
2OMT; X-ray; 2.00 A; B=156-255.	[ExPASy / RCSB / EBI]
2OMU; X-ray; 1.80 A; B=156-255.	[ExPASy / RCSB / EBI]
2OMV; X-ray; 1.90 A; B=156-255.	[ExPASy / RCSB / EBI]
2OMX; X-ray; 1.70 A; B=156-258.	[ExPASy / RCSB / EBI]
2OMY; X-ray; 1.70 A; B=156-255.	[ExPASy / RCSB / EBI]
2OMZ; X-ray; 1.60 A; B=156-255.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1O6S; -.
2O72; -.
2OMT; -.
2OMU; -.
2OMV; -.
2OMX; -.
2OMY; -.
2OMZ; -.

SMR

P12830; 802-877.

ModBase

P12830.

Protein-protein interaction databases

DIP

DIP:477N; -.

IntAct

P12830; 30.

PTM databases

PhosphoSite

P12830; -.

Enzyme and pathway databases

Pathway_Interaction_DB

a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
arf6_traffickingpathway; Arf6 trafficking events.
fgf_pathway; FGF signaling pathway.

Reactome

REACT_13552; Integrin cell surface interactions.
REACT_578; Apoptosis.
REACT_6900; Signaling in Immune system.

Organism-specific databases

GC16P067328; -.

HIX0038521; -.

HGNC:1748; CDH1.

CAB000087; -.
HPA004812; -.

MIM

137215; phenotype. [NCBI / EBI]
167000; phenotype. [NCBI / EBI]
192090; gene. [NCBI / EBI]
608089; phenotype. [NCBI / EBI]

Orphanet

26106; Gastric cancer, familial.

PharmGKB

PA26282; -.

Gene expression databases

P12830; -.

P12830; -.

HS_CDH1; -.

ENSG00000039068; Homo sapiens.

Ontologies

GO:0015629;	Cellular component: actin cytoskeleton (inferred from direct assay from UniProtKB).
GO:0016342;	Cellular component: catenin complex (inferred from direct assay from UniProtKB).
GO:0005913;	Cellular component: cell-cell adherens junction (inferred from direct assay from UniProtKB).
GO:0005925;	Cellular component: focal adhesion (inferred from direct assay from HPA).
GO:0005794;	Cellular component: Golgi apparatus (inferred from direct assay from HPA).
GO:0016021;	Cellular component: integral to membrane (inferred from direct assay from UniProtKB).
GO:0016328;	Cellular component: lateral plasma membrane (inferred from direct assay from UniProtKB).
GO:0048471;	Cellular component: perinuclear region of cytoplasm (inferred from direct assay from UniProtKB).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0050839;	Molecular function: cell adhesion molecule binding (non-traceable author statement from UniProtKB).
GO:0016563;	Molecular function: transcription activator activity (inferred from direct assay from UniProtKB).
GO:0007156;	Biological process: homophilic cell adhesion (non-traceable author statement from UniProtKB).
GO:0042993;	Biological process: positive regulation of transcription factor import into nucleus (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR002126; Cadherin.
IPR000233; Cadherin_C_term.
IPR014868; Cadherin_pro.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.60; Cadherin; 4.

Pfam

PF00028; Cadherin; 5.
PF01049; Cadherin_C; 1.
PF08758; Cadherin_pro; 1.
Pfam graphical view of domain structure.

PRINTS

PR00205; CADHERIN.

SMART

SM00112; CA; 4.
SMART graphical view of domain structure.

PROSITE

PS00232; CADHERIN_1; 3.
PS50268; CADHERIN_2; 5.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P12830; -.

Genome annotation databases

Ensembl

ENSG00000039068; Homo sapiens. [Contig view]

GeneID

999; -.

KEGG

hsa:999; -.

NMPDR

fig|9606.3.peg.12460; -.

Phylogenomic databases

HOVERGEN

P12830; -.

Other

4200; -.

P12830; -.

CDH1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Calcium; Cell adhesion; Cell junction; Cell membrane; Cleavage on pair of basic residues; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Polymorphism; Repeat; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`	`Potential.`
`PROPEP`	`23 154`	`132`	`Potential.`	`PRO_0000003715`
`CHAIN`	`155 882`	`728`	`Cadherin-1.`	`PRO_0000003716`
`CHAIN`	`701 882`	`182`	`E-Cad/CTF1.`	`PRO_0000236067`
`CHAIN`	`732 882`	`151`	`E-Cad/CTF2.`	`PRO_0000236068`
`CHAIN`	`751 882`	`132`	`E-Cad/CTF3.`	`PRO_0000236069`
`TOPO_DOM`	`155 709`	`555`	`Extracellular (Potential).`
`TRANSMEM`	`710 730`	`21`	`Potential.`
`TOPO_DOM`	`731 882`	`152`	`Cytoplasmic (Potential).`
`DOMAIN`	`155 262`	`108`	`Cadherin 1.`
`DOMAIN`	`263 375`	`113`	`Cadherin 2.`
`DOMAIN`	`376 486`	`111`	`Cadherin 3.`
`DOMAIN`	`487 593`	`107`	`Cadherin 4.`
`DOMAIN`	`594 697`	`104`	`Cadherin 5.`
`REGION`	`758 769`	`12`	`Required for binding CTNND1 and PSEN1.`
`REGION`	`811 882`	`72`	`Required for binding alpha, beta and gamma catenins.`
`COMPBIAS`	`838 851`	`14`	`Ser-rich.`
`SITE`	`700 701`	`2`	`Cleavage; by a metalloproteinase.`
`SITE`	`731 732`	`2`	`Cleavage; by gamma-secretase/PS1.`
`SITE`	`750 751`	`2`	`Cleavage; by caspase-3.`
`MOD_RES`	`838 838`		`Phosphoserine (By similarity).`
`MOD_RES`	`840 840`		`Phosphoserine (By similarity).`
`MOD_RES`	`846 846`		`Phosphoserine (By similarity).`
`CARBOHYD`	`558 558`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`637 637`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`163 163`		`Interchain.`
`VARIANT`	`72 72`	`1`	`D -> N (in dbSNP:rs35606263 [NCBI]).`	`VAR_048500`
`VARIANT`	`123 123`	`1`	`H -> Y (in diffuse gastric cancer).`	`VAR_001306`
`VARIANT`	`193 193`	`1`	`T -> P (in diffuse gastric cancer).`	`VAR_001307 [3D]`
`VARIANT`	`244 244`	`1`	`D -> G (in HDGC).`	`VAR_008712 [3D]`
`VARIANT`	`270 270`	`1`	`S -> A (may contribute to prostate cancer).`	`VAR_013970`
`VARIANT`	`274 277`	`4`	`Missing (in gastric adenocarcinoma).`	`VAR_001308`
`VARIANT`	`282 282`	`1`	`M -> I (in a breast cancer sample; somatic mutation).`	`VAR_033026`
`VARIANT`	`315 315`	`1`	`N -> S (in lobular breast carcinoma).`	`VAR_001309`
`VARIANT`	`336 336`	`1`	`E -> D.`	`VAR_001310`
`VARIANT`	`340 340`	`1`	`T -> A (in HDGC and colorectal cancer; cells exhibited decreased aggregation increased invasiveness and non-uniform migration in vitro compared to cells transfected with wild-type sequence).`	`VAR_013971`
`VARIANT`	`370 370`	`1`	`D -> A (in diffuse gastric cancer).`	`VAR_001311`
`VARIANT`	`393 393`	`1`	`I -> N (in dbSNP:rs34466743 [NCBI]).`	`VAR_048501`
`VARIANT`	`400 400`	`1`	`Missing (in gastric carcinoma; loss of heterozygosity).`	`VAR_001312`
`VARIANT`	`418 423`	`6`	`Missing (in gastric carcinoma).`	`VAR_001313`
`VARIANT`	`463 463`	`1`	`E -> Q (in diffuse gastric cancer).`	`VAR_001314`
`VARIANT`	`470 470`	`1`	`T -> I.`	`VAR_001315`
`VARIANT`	`473 473`	`1`	`V -> D (in diffuse gastric cancer).`	`VAR_001317`
`VARIANT`	`473 473`	`1`	`V -> I (in dbSNP:rs36087757 [NCBI]).`	`VAR_048502`
`VARIANT`	`478 478`	`1`	`L -> P (in dbSNP:rs35520415 [NCBI]).`	`VAR_023357`
`VARIANT`	`487 487`	`1`	`V -> A (in HDGC).`	`VAR_008713`
`VARIANT`	`592 592`	`1`	`A -> T (in thyroid cancer; may play a role in colorectal carcinogenesis; dbSNP:rs35187787 [NCBI]).`	`VAR_001318`
`VARIANT`	`598 598`	`1`	`R -> Q (in diffuse gastric cancer).`	`VAR_001319`
`VARIANT`	`617 617`	`1`	`A -> T (in endometrial cancer; loss of heterozygosity; also found as a polymorphism; cells exhibited an intermediate phenotype concerning aggregation invasiveness and migration in vitro compared to cells transfected with wild-type sequence; dbSNP:rs33935154 [NCBI]).`	`VAR_001320`
`VARIANT`	`630 630`	`1`	`L -> V (in dbSNP:rs2276331 [NCBI]).`	`VAR_021868`
`VARIANT`	`634 634`	`1`	`A -> V (in gastric cancer; cells exhibited decreased aggregation increased invasiveness and non-uniform migration in vitro compared to cells transfected with wild-type sequence).`	`VAR_055431`
`VARIANT`	`695 695`	`1`	`C -> R (in dbSNP:rs9282655 [NCBI]).`	`VAR_021869`
`VARIANT`	`711 711`	`1`	`L -> V (in endometrial cancer).`	`VAR_001321`
`VARIANT`	`777 777`	`1`	`D -> N (in a breast cancer sample; somatic mutation).`	`VAR_033027`
`VARIANT`	`832 832`	`1`	`V -> M (in HDGC; dbSNP:rs35572355 [NCBI]).`	`VAR_023358`
`VARIANT`	`838 838`	`1`	`S -> G (in ovarian cancer; somatic mutation; loss of heterozygosity).`	`VAR_001322`
`VARIANT`	`880 880`	`1`	`E -> K (in dbSNP:rs34507583 [NCBI]).`	`VAR_023359`
`MUTAGEN`	`759 761`		`GGG->AAA: Binds to CTNNB1 but abolishes formation of the PSEN1/CTNNB1 complex; when associated with CTNNB1 D-431. Abolishes binding PSEN1. Abolishes gamma-secretase cleavage.`
`CONFLICT`	`10 10`		`A -> G (in Ref. 3; AAA61259).`
`CONFLICT`	`29 29`		`H -> L (in Ref. 3; AAA61259).`
`CONFLICT`	`47 47`		`E -> R (in Ref. 3; AAA61259).`
`CONFLICT`	`70 71`		`SL -> P (in Ref. 3; AAA61259).`
`CONFLICT`	`483 483`		`A -> G (in Ref. 3; AAA61259).`
`CONFLICT`	`530 530`		`A -> R (in Ref. 3; AAA61259).`
`CONFLICT`	`543 543`		`S -> F (in Ref. 2; CAA79356).`
`CONFLICT`	`615 615`		`I -> H (in Ref. 3; AAA61259).`
`CONFLICT`	`634 636`		`ASA -> RVP (in Ref. 3; AAA61259).`
`CONFLICT`	`868 868`		`R -> P (in Ref. 3; AAA61259).`
`CONFLICT`	`882 882`		`D -> H (in Ref. 3; AAA61259).`
`STRAND`	`161 164`	`4`
`STRAND`	`169 177`	`9`
`HELIX`	`181 184`	`4`
`STRAND`	`188 195`	`8`
`TURN`	`196 198`	`3`
`STRAND`	`199 201`	`3`
`STRAND`	`204 207`	`4`
`TURN`	`209 211`	`3`
`STRAND`	`213 216`	`4`
`TURN`	`222 224`	`3`
`STRAND`	`227 236`	`10`
`STRAND`	`241 243`	`3`
`STRAND`	`246 253`	`8`
`STRAND`	`261 272`	`12`
`STRAND`	`280 283`	`4`
`TURN`	`292 294`	`3`
`STRAND`	`301 309`	`9`
`STRAND`	`316 319`	`4`
`TURN`	`321 323`	`3`
`STRAND`	`325 328`	`4`
`TURN`	`335 337`	`3`
`STRAND`	`340 348`	`9`
`TURN`	`349 353`	`5`
`STRAND`	`356 366`	`11`

Sequence information

Length: 882 AA [This is the length of the unprocessed precursor]

Molecular weight: 97456 Da [This is the MW of the unprocessed precursor]

CRC64: E427118043A13C67 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGPWSRSLSA LLLLLQVSSW LCQEPEPCHP GFDAESYTFT VPRRHLERGR VLGRVNFEDC 

        70         80         90        100        110        120 
TGRQRTAYFS LDTRFKVGTD GVITVKRPLR FHNPQIHFLV YAWDSTYRKF STKVTLNTVG 

       130        140        150        160        170        180 
HHHRPPPHQA SVSGIQAELL TFPNSSPGLR RQKRDWVIPP ISCPENEKGP FPKNLVQIKS 

       190        200        210        220        230        240 
NKDKEGKVFY SITGQGADTP PVGVFIIERE TGWLKVTEPL DRERIATYTL FSHAVSSNGN 

       250        260        270        280        290        300 
AVEDPMEILI TVTDQNDNKP EFTQEVFKGS VMEGALPGTS VMEVTATDAD DDVNTYNAAI 

       310        320        330        340        350        360 
AYTILSQDPE LPDKNMFTIN RNTGVISVVT TGLDRESFPT YTLVVQAADL QGEGLSTTAT 

       370        380        390        400        410        420 
AVITVTDTND NPPIFNPTTY KGQVPENEAN VVITTLKVTD ADAPNTPAWE AVYTILNDDG 

       430        440        450        460        470        480 
GQFVVTTNPV NNDGILKTAK GLDFEAKQQY ILHVAVTNVV PFEVSLTTST ATVTVDVLDV 

       490        500        510        520        530        540 
NEAPIFVPPE KRVEVSEDFG VGQEITSYTA QEPDTFMEQK ITYRIWRDTA NWLEINPDTG 

       550        560        570        580        590        600 
AISTRAELDR EDFEHVKNST YTALIIATDN GSPVATGTGT LLLILSDVND NAPIPEPRTI 

       610        620        630        640        650        660 
FFCERNPKPQ VINIIDADLP PNTSPFTAEL THGASANWTI QYNDPTQESI ILKPKMALEV 

       670        680        690        700        710        720 
GDYKINLKLM DNQNKDQVTT LEVSVCDCEG AAGVCRKAQP VEAGLQIPAI LGILGGILAL 

       730        740        750        760        770        780 
LILILLLLLF LRRRAVVKEP LLPPEDDTRD NVYYYDEEGG GEEDQDFDLS QLHRGLDARP 

       790        800        810        820        830        840 
EVTRNDVAPT LMSVPRYLPR PANPDEIGNF IDENLKAADT DPTAPPYDSL LVFDYEGSGS 

       850        860        870        880 
EAASLSSLNS SESDKDQDYD YLNEWGNRFK KLADMYGGGE DD

P12830 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools