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Protein

Cadherin-1

Gene

Cdh1

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

Functioni

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).By similarity1 Publication
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)DescriptionActionsGraphical viewLength
Metal bindingi259Calcium 11
Metal bindingi259Calcium 21
Metal bindingi290Calcium 31

GO - Molecular functioni

  • alpha-catenin binding Source: MGI
  • ankyrin binding Source: MGI
  • beta-catenin binding Source: BHF-UCL
  • cadherin binding Source: GO_Central
  • calcium ion binding Source: MGI
  • cell adhesion molecule binding Source: MGI
  • cytoskeletal protein binding Source: MGI
  • gamma-catenin binding Source: MGI
  • GTPase activating protein binding Source: MGI
  • identical protein binding Source: IntAct
  • protein domain specific binding Source: MGI
  • protein homodimerization activity Source: GO_Central
  • protein phosphatase binding Source: UniProtKB

GO - Biological processi

Keywordsi

Biological processCell adhesion
LigandCalcium, Metal-binding

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:88354 Cdh1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini157 – 709ExtracellularSequence analysisAdd BLAST553
Transmembranei710 – 733HelicalSequence analysisAdd BLAST24
Topological domaini734 – 884CytoplasmicSequence analysisAdd BLAST151

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
PropeptideiPRO_000000371724 – 156Sequence analysisAdd BLAST133
ChainiPRO_0000003718157 – 884Cadherin-1Add BLAST728
ChainiPRO_0000236070703 – 884E-Cad/CTF1Sequence analysisAdd BLAST182
ChainiPRO_0000236071734 – 884E-Cad/CTF2Sequence analysisAdd BLAST151
ChainiPRO_0000236072753 – 884E-Cad/CTF3Sequence analysisAdd BLAST132

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi560N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi639N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei755Phosphotyrosine; by SRCBy similarity1
Modified residuei756Phosphotyrosine; by SRCBy similarity1
Modified residuei757Phosphotyrosine; by SRCBy similarity1
Modified residuei772PhosphoserineBy similarity1
Modified residuei795PhosphoserineBy similarity1
Modified residuei840Phosphoserine1 Publication1
Modified residuei842Phosphoserine1 Publication1
Modified residuei848Phosphoserine1 Publication1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei702 – 703Cleavage; by a metalloproteinaseBy similarity2
Sitei733 – 734Cleavage; by gamma-secretase/PS1By similarity2
Sitei752 – 753Cleavage; by caspase-3By similarity2

Keywords - PTMi

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

Proteomic databases

MaxQBiP09803
PaxDbiP09803
PeptideAtlasiP09803
PRIDEiP09803

PTM databases

iPTMnetiP09803
PhosphoSitePlusiP09803

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

CleanExiMM_CDH1

Interactioni

Subunit structurei

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).By similarity6 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198631, 37 interactors
CORUMiP09803
DIPiDIP-29635N
IntActiP09803, 38 interactors
MINTiP09803
STRINGi10090.ENSMUSP00000000312

Structurei

Secondary structure

1884
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

DisProtiDP00159
ProteinModelPortaliP09803
SMRiP09803
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09803

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini157 – 264Cadherin 1PROSITE-ProRule annotationAdd BLAST108
Domaini265 – 377Cadherin 2PROSITE-ProRule annotationAdd BLAST113
Domaini378 – 488Cadherin 3PROSITE-ProRule annotationAdd BLAST111
Domaini489 – 595Cadherin 4PROSITE-ProRule annotationAdd BLAST107
Domaini596 – 699Cadherin 5PROSITE-ProRule annotationAdd BLAST104

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni760 – 771Required for binding CTNND1 and PSEN1By similarityAdd BLAST12
Regioni813 – 884Required for binding alpha, beta and gamma cateninsBy similarityAdd BLAST72

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi840 – 855Ser-richAdd BLAST16

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.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3594 Eukaryota
ENOG410XQHI LUCA
HOGENOMiHOG000231254
HOVERGENiHBG106438
InParanoidiP09803
KOiK05689
PhylomeDBiP09803
TreeFamiTF316817

Family and domain databases

Gene3Di4.10.900.10, 1 hit
InterProiView protein in InterPro
IPR039808 Cadherin
IPR002126 Cadherin-like_dom
IPR015919 Cadherin-like_sf
IPR020894 Cadherin_CS
IPR000233 Cadherin_cytoplasmic-dom
IPR014868 Cadherin_pro_dom
IPR027397 Catenin_binding_dom_sf
PANTHERiPTHR24027 PTHR24027, 1 hit
PfamiView protein in Pfam
PF00028 Cadherin, 5 hits
PF01049 Cadherin_C, 1 hit
PF08758 Cadherin_pro, 1 hit
PRINTSiPR00205 CADHERIN
SMARTiView protein in SMART
SM00112 CA, 4 hits
SM01055 Cadherin_pro, 1 hit
SUPFAMiSSF49313 SSF49313, 6 hits
PROSITEiView protein in PROSITE
PS00232 CADHERIN_1, 3 hits
PS50268 CADHERIN_2, 4 hits

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0R4IZW5A0A0R4IZW5_MOUSE
Cadherin 1, isoform CRA_b
Cdh1 mCG_20483
884Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti267E → P in CAA43292 (PubMed:1754391).Curated1
Sequence conflicti272S → F in CAA43292 (PubMed:1754391).Curated1

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_009864.3
UniGeneiMm.35605

Genome annotation databases

GeneIDi12550
KEGGimmu:12550
UCSCiuc009ngi.1 mouse

Similar proteinsi

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_009864.3
UniGeneiMm.35605

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198631, 37 interactors
CORUMiP09803
DIPiDIP-29635N
IntActiP09803, 38 interactors
MINTiP09803
STRINGi10090.ENSMUSP00000000312

PTM databases

iPTMnetiP09803
PhosphoSitePlusiP09803

Proteomic databases

MaxQBiP09803
PaxDbiP09803
PeptideAtlasiP09803
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

eggNOGiKOG3594 Eukaryota
ENOG410XQHI LUCA
HOGENOMiHOG000231254
HOVERGENiHBG106438
InParanoidiP09803
KOiK05689
PhylomeDBiP09803
TreeFamiTF316817

Miscellaneous databases

ChiTaRSiCdh1 mouse
EvolutionaryTraceiP09803
PROiPR:P09803
SOURCEiSearch...

Gene expression databases

CleanExiMM_CDH1

Family and domain databases

Gene3Di4.10.900.10, 1 hit
InterProiView protein in InterPro
IPR039808 Cadherin
IPR002126 Cadherin-like_dom
IPR015919 Cadherin-like_sf
IPR020894 Cadherin_CS
IPR000233 Cadherin_cytoplasmic-dom
IPR014868 Cadherin_pro_dom
IPR027397 Catenin_binding_dom_sf
PANTHERiPTHR24027 PTHR24027, 1 hit
PfamiView protein in Pfam
PF00028 Cadherin, 5 hits
PF01049 Cadherin_C, 1 hit
PF08758 Cadherin_pro, 1 hit
PRINTSiPR00205 CADHERIN
SMARTiView protein in SMART
SM00112 CA, 4 hits
SM01055 Cadherin_pro, 1 hit
SUPFAMiSSF49313 SSF49313, 6 hits
PROSITEiView protein in PROSITE
PS00232 CADHERIN_1, 3 hits
PS50268 CADHERIN_2, 4 hits
ProtoNetiSearch...

Entry informationi

Entry nameiCADH1_MOUSE
AccessioniPrimary (citable) accession number: P09803
Secondary accession number(s): Q61377
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 7, 2018
This is version 206 of the entry and version 1 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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