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Protein

Cadherin-1

Gene

Cdh1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi259 – 2591Calcium 1
Metal bindingi259 – 2591Calcium 2
Metal bindingi290 – 2901Calcium 3
Sitei702 – 7032Cleavage; by a metalloproteinaseBy similarity
Sitei733 – 7342Cleavage; by gamma-secretase/PS1By similarity
Sitei752 – 7532Cleavage; by caspase-3By similarity

GO - Molecular functioni

  • ankyrin binding Source: MGI
  • beta-catenin binding Source: MGI
  • calcium ion binding Source: MGI
  • cell adhesion molecule binding Source: MGI
  • gamma-catenin binding Source: MGI
  • glycoprotein binding Source: MGI
  • GTPase activating protein binding Source: MGI
  • protein domain specific binding Source: MGI
  • protein phosphatase binding Source: UniProtKB

GO - Biological processi

  • adherens junction organization Source: MGI
  • bicellular tight junction assembly Source: MGI
  • calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules Source: MGI
  • cellular response to amino acid stimulus Source: MGI
  • cellular response to indole-3-methanol Source: MGI
  • cellular response to lithium ion Source: MGI
  • cochlea development Source: MGI
  • decidualization Source: CACAO
  • embryo implantation Source: CACAO
  • epithelial cell morphogenesis Source: MGI
  • establishment of protein localization to plasma membrane Source: UniProtKB
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: InterPro
  • intestinal epithelial cell development Source: MGI
  • in utero embryonic development Source: MGI
  • negative regulation of canonical Wnt signaling pathway Source: MGI
  • negative regulation of cell-cell adhesion Source: MGI
  • negative regulation of epithelial cell proliferation Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription factor import into nucleus Source: MGI
  • protein homooligomerization Source: MGI
  • protein localization to plasma membrane Source: MGI
  • protein metabolic process Source: MGI
  • regulation of branching involved in salivary gland morphogenesis Source: MGI
  • regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  • regulation of neuron migration Source: MGI
  • regulation of protein localization Source: MGI
  • regulation of protein localization to cell surface Source: MGI
  • regulation of water loss via skin Source: MGI
  • salivary gland cavitation Source: MGI
  • sensory perception of sound Source: MGI
  • single organismal cell-cell adhesion Source: MGI
  • trophectodermal cell differentiation Source: MGI
  • uterine epithelium development Source: CACAO
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_275864. Degradation of the extracellular matrix.
REACT_300990. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_308832. Adherens junctions interactions.
REACT_319261. Integrin cell surface interactions.
REACT_343176. Apoptotic cleavage of cell adhesion proteins.
REACT_358203. RHO GTPases activate IQGAPs.

Names & Taxonomyi

Protein namesi
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:
Gene namesi
Name:Cdh1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:88354. Cdh1.

Subcellular locationi

  • Cell junction
  • Cell membrane; Single-pass type I membrane protein
  • Endosome By similarity
  • Golgi apparatustrans-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).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini157 – 709553ExtracellularSequence AnalysisAdd
BLAST
Transmembranei710 – 73324HelicalSequence AnalysisAdd
BLAST
Topological domaini734 – 884151CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • actin cytoskeleton Source: MGI
  • adherens junction Source: UniProtKB
  • aggresome Source: MGI
  • apical junction complex Source: MGI
  • apical part of cell Source: MGI
  • axon Source: MGI
  • axon terminus Source: MGI
  • basolateral plasma membrane Source: MGI
  • catenin complex Source: MGI
  • cell-cell adherens junction Source: MGI
  • cell-cell junction Source: MGI
  • cell junction Source: MGI
  • cell periphery Source: MGI
  • cell surface Source: MGI
  • cytoplasm Source: MGI
  • cytoplasmic side of plasma membrane Source: MGI
  • endosome Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • flotillin complex Source: UniProtKB
  • focal adhesion Source: MGI
  • integral component of membrane Source: MGI
  • lamellipodium Source: MGI
  • lateral loop Source: BHF-UCL
  • lateral plasma membrane Source: MGI
  • node of Ranvier Source: BHF-UCL
  • perinuclear region of cytoplasm Source: MGI
  • plasma membrane Source: MGI
  • Schmidt-Lanterman incisure Source: BHF-UCL
  • trans-Golgi network Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Endosome, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Propeptidei24 – 156133Sequence AnalysisPRO_0000003717Add
BLAST
Chaini157 – 884728Cadherin-1PRO_0000003718Add
BLAST
Chaini703 – 884182E-Cad/CTF1Sequence AnalysisPRO_0000236070Add
BLAST
Chaini734 – 884151E-Cad/CTF2Sequence AnalysisPRO_0000236071Add
BLAST
Chaini753 – 884132E-Cad/CTF3Sequence AnalysisPRO_0000236072Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi560 – 5601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi639 – 6391N-linked (GlcNAc...)Sequence Analysis
Modified residuei755 – 7551Phosphotyrosine; by SRCBy similarity
Modified residuei756 – 7561Phosphotyrosine; by SRCBy similarity
Modified residuei757 – 7571Phosphotyrosine; by SRCBy similarity
Modified residuei772 – 7721PhosphoserineBy similarity
Modified residuei795 – 7951PhosphoserineBy similarity
Modified residuei840 – 8401Phosphoserine1 Publication
Modified residuei842 – 8421Phosphoserine1 Publication
Modified residuei848 – 8481Phosphoserine1 Publication

Post-translational modificationi

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).By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP09803.
PaxDbiP09803.
PRIDEiP09803.

PTM databases

PhosphoSiteiP09803.

Expressioni

Tissue specificityi

Non-neural epithelial tissues.

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiP09803.
CleanExiMM_CDH1.
GenevisibleiP09803. MM.

Interactioni

Subunit structurei

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). Interacts with RAPGEF2 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Cdk5r1P618092EBI-984420,EBI-7840438
Ctnnb1Q0224813EBI-984420,EBI-397872
CTNND1O60716-293EBI-984420,EBI-702059From a different organism.
PTPRMP288273EBI-984420,EBI-2257317From a different organism.
SKP2Q133092EBI-984420,EBI-456291From a different organism.

Protein-protein interaction databases

BioGridi198631. 16 interactions.
DIPiDIP-29635N.
IntActiP09803. 12 interactions.
MINTiMINT-121804.
STRINGi10090.ENSMUSP00000000312.

Structurei

Secondary structure

1
884
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi160 – 1667Combined sources
Beta strandi171 – 1799Combined sources
Helixi183 – 1864Combined sources
Beta strandi190 – 1978Combined sources
Turni198 – 2003Combined sources
Beta strandi201 – 2033Combined sources
Beta strandi206 – 2094Combined sources
Turni211 – 2133Combined sources
Beta strandi215 – 2184Combined sources
Turni224 – 2263Combined sources
Beta strandi228 – 23811Combined sources
Turni239 – 2413Combined sources
Beta strandi243 – 2453Combined sources
Beta strandi248 – 2558Combined sources
Beta strandi263 – 2653Combined sources
Beta strandi267 – 2748Combined sources
Beta strandi282 – 2854Combined sources
Turni294 – 2963Combined sources
Helixi298 – 3003Combined sources
Beta strandi303 – 3119Combined sources
Beta strandi314 – 3163Combined sources
Beta strandi318 – 3214Combined sources
Turni323 – 3253Combined sources
Beta strandi327 – 3304Combined sources
Turni337 – 3393Combined sources
Beta strandi342 – 3509Combined sources
Helixi352 – 3543Combined sources
Beta strandi358 – 36811Combined sources
Beta strandi376 – 38914Combined sources
Beta strandi396 – 3983Combined sources
Turni409 – 4113Combined sources
Beta strandi413 – 4197Combined sources
Beta strandi425 – 4295Combined sources
Turni431 – 4333Combined sources
Beta strandi436 – 4427Combined sources
Turni446 – 4483Combined sources
Beta strandi450 – 46213Combined sources
Beta strandi471 – 48010Combined sources
Beta strandi487 – 4926Combined sources
Beta strandi494 – 4985Combined sources
Beta strandi506 – 5094Combined sources
Beta strandi524 – 5296Combined sources
Beta strandi535 – 5373Combined sources
Turni539 – 5413Combined sources
Beta strandi543 – 5464Combined sources
Turni555 – 5573Combined sources
Beta strandi560 – 57011Combined sources
Beta strandi573 – 5753Combined sources
Beta strandi579 – 58810Combined sources
Beta strandi596 – 5983Combined sources
Beta strandi603 – 6086Combined sources
Beta strandi612 – 6176Combined sources
Beta strandi624 – 6274Combined sources
Beta strandi631 – 6344Combined sources
Beta strandi637 – 6393Combined sources
Beta strandi641 – 6433Combined sources
Beta strandi649 – 6557Combined sources
Beta strandi668 – 6703Combined sources
Beta strandi673 – 6753Combined sources
Beta strandi684 – 6885Combined sources
Beta strandi785 – 7895Combined sources
Turni806 – 8083Combined sources
Helixi818 – 8225Combined sources
Beta strandi824 – 8274Combined sources
Beta strandi830 – 8345Combined sources
Turni864 – 8663Combined sources
Helixi869 – 8713Combined sources
Helixi872 – 8776Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EDHX-ray2.00A/B156-380[»]
1FF5X-ray2.93A/B157-374[»]
1I7WX-ray2.00B/D734-884[»]
1I7XX-ray3.00B/D734-884[»]
1Q1PX-ray3.20A158-369[»]
1SUHNMR-A156-300[»]
2OMWX-ray1.85B158-256[»]
2QVFX-ray2.40B157-369[»]
3IFQX-ray2.80C/D778-884[»]
3LNEX-ray2.00A157-369[»]
3LNFX-ray2.50A/B157-369[»]
3LNGX-ray2.70A/B157-369[»]
3LNHX-ray2.60A/B157-369[»]
3LNIX-ray2.30A/B157-369[»]
3Q2LX-ray2.70A/B157-369[»]
3Q2NX-ray2.73A/B157-369[»]
3Q2VX-ray3.40A/B157-700[»]
3QRBX-ray1.80A/B157-369[»]
4QD2X-ray2.40E/J157-369[»]
DisProtiDP00159.
ProteinModelPortaliP09803.
SMRiP09803. Positions 157-692, 784-877.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09803.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini157 – 264108Cadherin 1PROSITE-ProRule annotationAdd
BLAST
Domaini265 – 377113Cadherin 2PROSITE-ProRule annotationAdd
BLAST
Domaini378 – 488111Cadherin 3PROSITE-ProRule annotationAdd
BLAST
Domaini489 – 595107Cadherin 4PROSITE-ProRule annotationAdd
BLAST
Domaini596 – 699104Cadherin 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni760 – 77112Required for binding CTNND1 and PSEN1By similarityAdd
BLAST
Regioni813 – 88472Required for binding alpha, beta and gamma cateninsBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi840 – 85516Ser-richAdd
BLAST

Domaini

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.

Sequence similaritiesi

Contains 5 cadherin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG328838.
HOGENOMiHOG000231254.
HOVERGENiHBG106438.
InParanoidiP09803.
KOiK05689.
OrthoDBiEOG7PS1DS.
PhylomeDBiP09803.
TreeFamiTF316817.

Family and domain databases

Gene3Di2.60.40.60. 6 hits.
4.10.900.10. 1 hit.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR014868. Cadherin_pro_dom.
IPR027397. Catenin_binding_dom.
IPR030049. CDH1.
[Graphical view]
PANTHERiPTHR24027:SF252. PTHR24027:SF252. 1 hit.
PfamiPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 4 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 6 hits.
PROSITEiPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09803-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGARCRSFSA LLLLLQVSSW LCQELEPESC SPGFSSEVYT FPVPERHLER
60 70 80 90 100
GHVLGRVRFE GCTGRPRTAF FSEDSRFKVA TDGTITVKRH LKLHKLETSF
110 120 130 140 150
LVRARDSSHR ELSTKVTLKS MGHHHHRHHH RDPASESNPE LLMFPSVYPG
160 170 180 190 200
LRRQKRDWVI PPISCPENEK GEFPKNLVQI KSNRDKETKV FYSITGQGAD
210 220 230 240 250
KPPVGVFIIE RETGWLKVTQ PLDREAIAKY ILYSHAVSSN GEAVEDPMEI
260 270 280 290 300
VITVTDQNDN RPEFTQEVFE GSVAEGAVPG TSVMKVSATD ADDDVNTYNA
310 320 330 340 350
AIAYTIVSQD PELPHKNMFT VNRDTGVISV LTSGLDRESY PTYTLVVQAA
360 370 380 390 400
DLQGEGLSTT AKAVITVKDI NDNAPVFNPS TYQGQVPENE VNARIATLKV
410 420 430 440 450
TDDDAPNTPA WKAVYTVVND PDQQFVVVTD PTTNDGILKT AKGLDFEAKQ
460 470 480 490 500
QYILHVRVEN EEPFEGSLVP STATVTVDVV DVNEAPIFMP AERRVEVPED
510 520 530 540 550
FGVGQEITSY TAREPDTFMD QKITYRIWRD TANWLEINPE TGAIFTRAEM
560 570 580 590 600
DREDAEHVKN STYVALIIAT DDGSPIATGT GTLLLVLLDV NDNAPIPEPR
610 620 630 640 650
NMQFCQRNPQ PHIITILDPD LPPNTSPFTA ELTHGASVNW TIEYNDAAQE
660 670 680 690 700
SLILQPRKDL EIGEYKIHLK LADNQNKDQV TTLDVHVCDC EGTVNNCMKA
710 720 730 740 750
GIVAAGLQVP AILGILGGIL ALLILILLLL LFLRRRTVVK EPLLPPDDDT
760 770 780 790 800
RDNVYYYDEE GGGEEDQDFD LSQLHRGLDA RPEVTRNDVA PTLMSVPQYR
810 820 830 840 850
PRPANPDEIG NFIDENLKAA DSDPTAPPYD SLLVFDYEGS GSEAASLSSL
860 870 880
NSSESDQDQD YDYLNEWGNR FKKLADMYGG GEDD
Length:884
Mass (Da):98,256
Last modified:July 1, 1989 - v1
Checksum:i7A6444148D3D5983
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti267 – 2671E → P in CAA43292 (PubMed:1754391).Curated
Sequence conflicti272 – 2721S → F in CAA43292 (PubMed:1754391).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS22638.1.
PIRiS04528. IJMSCE.
S34438.
RefSeqiNP_033994.1. NM_009864.2.
UniGeneiMm.35605.

Genome annotation databases

GeneIDi12550.
KEGGimmu:12550.
UCSCiuc009ngi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS22638.1.
PIRiS04528. IJMSCE.
S34438.
RefSeqiNP_033994.1. NM_009864.2.
UniGeneiMm.35605.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EDHX-ray2.00A/B156-380[»]
1FF5X-ray2.93A/B157-374[»]
1I7WX-ray2.00B/D734-884[»]
1I7XX-ray3.00B/D734-884[»]
1Q1PX-ray3.20A158-369[»]
1SUHNMR-A156-300[»]
2OMWX-ray1.85B158-256[»]
2QVFX-ray2.40B157-369[»]
3IFQX-ray2.80C/D778-884[»]
3LNEX-ray2.00A157-369[»]
3LNFX-ray2.50A/B157-369[»]
3LNGX-ray2.70A/B157-369[»]
3LNHX-ray2.60A/B157-369[»]
3LNIX-ray2.30A/B157-369[»]
3Q2LX-ray2.70A/B157-369[»]
3Q2NX-ray2.73A/B157-369[»]
3Q2VX-ray3.40A/B157-700[»]
3QRBX-ray1.80A/B157-369[»]
4QD2X-ray2.40E/J157-369[»]
DisProtiDP00159.
ProteinModelPortaliP09803.
SMRiP09803. Positions 157-692, 784-877.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198631. 16 interactions.
DIPiDIP-29635N.
IntActiP09803. 12 interactions.
MINTiMINT-121804.
STRINGi10090.ENSMUSP00000000312.

PTM databases

PhosphoSiteiP09803.

Proteomic databases

MaxQBiP09803.
PaxDbiP09803.
PRIDEiP09803.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi12550.
KEGGimmu:12550.
UCSCiuc009ngi.1. mouse.

Organism-specific databases

CTDi999.
MGIiMGI:88354. Cdh1.

Phylogenomic databases

eggNOGiNOG328838.
HOGENOMiHOG000231254.
HOVERGENiHBG106438.
InParanoidiP09803.
KOiK05689.
OrthoDBiEOG7PS1DS.
PhylomeDBiP09803.
TreeFamiTF316817.

Enzyme and pathway databases

ReactomeiREACT_275864. Degradation of the extracellular matrix.
REACT_300990. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
REACT_308832. Adherens junctions interactions.
REACT_319261. Integrin cell surface interactions.
REACT_343176. Apoptotic cleavage of cell adhesion proteins.
REACT_358203. RHO GTPases activate IQGAPs.

Miscellaneous databases

ChiTaRSiCdh1. mouse.
EvolutionaryTraceiP09803.
NextBioi281598.
PROiP09803.
SOURCEiSearch...

Gene expression databases

BgeeiP09803.
CleanExiMM_CDH1.
GenevisibleiP09803. MM.

Family and domain databases

Gene3Di2.60.40.60. 6 hits.
4.10.900.10. 1 hit.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR014868. Cadherin_pro_dom.
IPR027397. Catenin_binding_dom.
IPR030049. CDH1.
[Graphical view]
PANTHERiPTHR24027:SF252. PTHR24027:SF252. 1 hit.
PfamiPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 4 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 6 hits.
PROSITEiPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiCADH1_MOUSE
AccessioniPrimary (citable) accession number: P09803
Secondary accession number(s): Q61377
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 22, 2015
This is version 175 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.