Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Cadherin-1

Gene

Cdh1

Organism
Rattus norvegicus (Rat)
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)DescriptionActionsGraphical viewLength
Metal bindingi261Calcium 1By similarity1
Metal bindingi261Calcium 2By similarity1
Metal bindingi292Calcium 3By similarity1

GO - Molecular functioni

GO - Biological processi

  • adherens junction organization Source: Ensembl
  • cellular response to indole-3-methanol Source: Ensembl
  • cellular response to lithium ion Source: Ensembl
  • establishment of protein localization to plasma membrane Source: Ensembl
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: InterPro
  • negative regulation of cell-cell adhesion Source: Ensembl
  • neuron projection development Source: RGD
  • pituitary gland development Source: RGD
  • positive regulation of transcription, DNA-templated Source: Ensembl
  • positive regulation of transcription factor import into nucleus Source: Ensembl
  • response to drug Source: RGD
  • response to organic substance Source: RGD
  • response to toxic substance Source: RGD
  • single organismal cell-cell adhesion Source: DFLAT
  • synapse assembly Source: RGD
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-1474228. Degradation of the extracellular matrix.
R-RNO-216083. Integrin cell surface interactions.
R-RNO-351906. Apoptotic cleavage of cell adhesion proteins.
R-RNO-418990. Adherens junctions interactions.
R-RNO-5626467. RHO GTPases activate IQGAPs.

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin-1
Alternative name(s):
Epithelial cadherin
Short name:
E-cadherin
Uvomorulin
CD_antigen: CD324
Cleaved into the following 3 chains:
Gene namesi
Name:Cdh1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 19

Organism-specific databases

RGDi69279. 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)DescriptionActionsGraphical viewLength
Topological domaini24 – 713ExtracellularSequence analysisAdd BLAST690
Transmembranei714 – 734HelicalSequence analysisAdd BLAST21
Topological domaini735 – 886CytoplasmicSequence analysisAdd BLAST152

GO - Cellular componenti

Complete GO annotation...

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_000000371924 – 158Sequence analysisAdd BLAST135
ChainiPRO_0000003720159 – 886Cadherin-1Add BLAST728
ChainiPRO_0000236073705 – 886E-Cad/CTF1Sequence analysisAdd BLAST182
ChainiPRO_0000236074736 – 886E-Cad/CTF2Sequence analysisAdd BLAST151
ChainiPRO_0000236075755 – 886E-Cad/CTF3Sequence analysisAdd BLAST132

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi562N-linked (GlcNAc...)Sequence analysis1
Glycosylationi641N-linked (GlcNAc...)Sequence analysis1
Modified residuei757Phosphotyrosine; by SRCBy similarity1
Modified residuei758Phosphotyrosine; by SRCBy similarity1
Modified residuei759Phosphotyrosine; by SRCBy similarity1
Modified residuei774PhosphoserineBy similarity1
Modified residuei797PhosphoserineBy similarity1
Modified residuei842PhosphoserineBy similarity1
Modified residuei844PhosphoserineBy similarity1
Modified residuei850PhosphoserineBy similarity1

Post-translational modificationi

N-glycosylation at Asn-641 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-758 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei704 – 705Cleavage; by a metalloproteinaseBy similarity2
Sitei735 – 736Cleavage; by gamma-secretase/PS1By similarity2
Sitei754 – 755Cleavage; by caspase-3By similarity2

Keywords - PTMi

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

Proteomic databases

PaxDbiQ9R0T4.
PRIDEiQ9R0T4.

PTM databases

PhosphoSitePlusiQ9R0T4.
SwissPalmiQ9R0T4.

Miscellaneous databases

PMAP-CutDBQ9R0T4.

Expressioni

Gene expression databases

BgeeiENSRNOG00000020151.
GenevisibleiQ9R0T4. RN.

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. Interacts with the TRPV4 and CTNNB1 complex (By similarity). Interacts with PIP5K1C. Interacts with DDR1; this stabilizes CDH1 at the cell surface and inhibits its internalization (By similarity). Interacts with RAPGEF2 (By similarity). Interacts with RAB8B.By similarity1 Publication

Protein-protein interaction databases

BioGridi249721. 3 interactors.
STRINGi10116.ENSRNOP00000027346.

Structurei

3D structure databases

ProteinModelPortaliQ9R0T4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini159 – 266Cadherin 1PROSITE-ProRule annotationAdd BLAST108
Domaini267 – 379Cadherin 2PROSITE-ProRule annotationAdd BLAST113
Domaini380 – 490Cadherin 3PROSITE-ProRule annotationAdd BLAST111
Domaini491 – 597Cadherin 4PROSITE-ProRule annotationAdd BLAST107
Domaini598 – 701Cadherin 5PROSITE-ProRule annotationAdd BLAST104

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni762 – 773Required for binding CTNND1 and PSEN1By similarityAdd BLAST12
Regioni815 – 886Required for binding alpha, beta andBy similarityAdd BLAST72

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi842 – 857Ser-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.By similarity

Sequence similaritiesi

Contains 5 cadherin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
GeneTreeiENSGT00760000118906.
HOGENOMiHOG000231254.
HOVERGENiHBG106438.
InParanoidiQ9R0T4.
KOiK05689.
OMAiWRDAANW.
OrthoDBiEOG091G05OA.
PhylomeDBiQ9R0T4.
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.
[Graphical view]
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. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9R0T4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGARCRSFSA LLLLLQVSSW LCQQPESESD SCRPGFSSEV YTFLVPERHL
60 70 80 90 100
ERGHILGRVK FEGCTGRPRT AFFSEDSRFK VSTDGVITVK RHLKLHKLET
110 120 130 140 150
SFLVHAWDSS YRKLSTKVTL KSLGHHHHRH HHRDPVSESN PELLTFPSFH
160 170 180 190 200
QGLRRQKRDW VIPPINCPEN QKGEFPQRLV QIKSNRDKET TVFYSITGPG
210 220 230 240 250
ADKPPVGVFI IERETGWLKV TQPLDREAID KYLLYSHAVS SNGEAVEDPM
260 270 280 290 300
EIVVTVTDQN DNRPEFIQEV FEGSVAEGAL PGTSVMQVSA TDADDDINTY
310 320 330 340 350
NAAIAYTILS QDPELPHKNM FTVNRDTGVI SVVTSGLDRE SYPTYTLVVQ
360 370 380 390 400
AADLQGEGLS TTAKAVITVK DINDNAPIFN PSTYQGQVLE NEVGARIATL
410 420 430 440 450
KVTDDDAPNT PAWNAVYTVV NDPDHQFTVI TDPKTNEGIL KTAKGLDFEA
460 470 480 490 500
KQQYILHVTV ENEEPFEGSL VPSTATVTVD VVDVNEAPIF VPAEKRVEVP
510 520 530 540 550
EDFGVGLEIA SYTAREPDTF MEQKITYRIW RDTANWLEIN PETGVISTRA
560 570 580 590 600
EMDREDSEHV KNSTYTALII ATDDGSPIAT GTGTLLLVLS DVNDNAPIPE
610 620 630 640 650
PRNMQFCQRN PKPHVITILD PDLPPNTSPF TAELTHGASV NWTIEYNDAE
660 670 680 690 700
QESLILQPRK DLEIGEYKIN LKLSDNQNKD QVTTLEVHVC DCEGTVNNCM
710 720 730 740 750
KAISLEAGLQ VPAILGILGG ILALLILILL LLLFLRRRTV VKEPLLPPDD
760 770 780 790 800
DTRDNVYYYD EEGGGEEDQD FDLSQLHRGL DARPEVIRND VAPTLMSMPQ
810 820 830 840 850
YRPRPANPDE IGNFIDENLK AADSDPTAPP YDSLLVFDYE GSGSEAASLS
860 870 880
SLNSSESDQD QDYDYLNEWG NRFKKLADMY GGGEED
Length:886
Mass (Da):98,715
Last modified:May 1, 2000 - v1
Checksum:iA9AEE28EB797A547
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017696 mRNA. Translation: BAA84920.1.
AF177680 mRNA. Translation: AAF87055.1.
AJ000540 mRNA. Translation: CAA04173.1.
RefSeqiNP_112624.1. NM_031334.1.
UniGeneiRn.1303.

Genome annotation databases

EnsembliENSRNOT00000027346; ENSRNOP00000027346; ENSRNOG00000020151.
GeneIDi83502.
KEGGirno:83502.
UCSCiRGD:69279. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017696 mRNA. Translation: BAA84920.1.
AF177680 mRNA. Translation: AAF87055.1.
AJ000540 mRNA. Translation: CAA04173.1.
RefSeqiNP_112624.1. NM_031334.1.
UniGeneiRn.1303.

3D structure databases

ProteinModelPortaliQ9R0T4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249721. 3 interactors.
STRINGi10116.ENSRNOP00000027346.

PTM databases

PhosphoSitePlusiQ9R0T4.
SwissPalmiQ9R0T4.

Proteomic databases

PaxDbiQ9R0T4.
PRIDEiQ9R0T4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027346; ENSRNOP00000027346; ENSRNOG00000020151.
GeneIDi83502.
KEGGirno:83502.
UCSCiRGD:69279. rat.

Organism-specific databases

CTDi999.
RGDi69279. Cdh1.

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
GeneTreeiENSGT00760000118906.
HOGENOMiHOG000231254.
HOVERGENiHBG106438.
InParanoidiQ9R0T4.
KOiK05689.
OMAiWRDAANW.
OrthoDBiEOG091G05OA.
PhylomeDBiQ9R0T4.
TreeFamiTF316817.

Enzyme and pathway databases

ReactomeiR-RNO-1474228. Degradation of the extracellular matrix.
R-RNO-216083. Integrin cell surface interactions.
R-RNO-351906. Apoptotic cleavage of cell adhesion proteins.
R-RNO-418990. Adherens junctions interactions.
R-RNO-5626467. RHO GTPases activate IQGAPs.

Miscellaneous databases

PMAP-CutDBQ9R0T4.
PROiQ9R0T4.

Gene expression databases

BgeeiENSRNOG00000020151.
GenevisibleiQ9R0T4. RN.

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.
[Graphical view]
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. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCADH1_RAT
AccessioniPrimary (citable) accession number: Q9R0T4
Secondary accession number(s): O35794, Q9JIV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 135 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.