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Q9R0T4 (CADH1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cadherin-1
Alternative name(s):
Epithelial cadherin
Short name=E-cadherin
Uvomorulin
CD_antigen=CD324

Cleaved into the following 3 chains:

  1. E-Cad/CTF1
  2. E-Cad/CTF2
  3. E-Cad/CTF3
Gene names
Name:Cdh1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length886 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 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.

Subunit structure

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. Ref.4

Subcellular location

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.

Domain

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.

Post-translational modification

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.

Sequence similarities

Contains 5 cadherin domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Endosome
Golgi apparatus
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to amino acid stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to indole-3-methanol

Inferred from electronic annotation. Source: Ensembl

cellular response to lithium ion

Inferred from electronic annotation. Source: Ensembl

cochlea development

Inferred from electronic annotation. Source: Ensembl

epithelial cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

homophilic cell adhesion

Inferred from electronic annotation. Source: InterPro

intestinal epithelial cell development

Inferred from electronic annotation. Source: Ensembl

negative regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

negative regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

neuron projection development

Inferred from expression pattern PubMed 12387456. Source: RGD

pituitary gland development

Inferred from expression pattern PubMed 17373711. Source: RGD

positive regulation of transcription factor import into nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

protein localization to plasma membrane

Inferred from electronic annotation. Source: Ensembl

protein metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of branching involved in salivary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

regulation of protein localization to cell surface

Inferred from electronic annotation. Source: Ensembl

regulation of water loss via skin

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from expression pattern PubMed 16671876. Source: RGD

response to organic substance

Inferred from expression pattern PubMed 16997938. Source: RGD

response to toxic substance

Inferred from expression pattern PubMed 17120308. Source: RGD

salivary gland cavitation

Inferred from electronic annotation. Source: Ensembl

sensory perception of sound

Inferred from electronic annotation. Source: Ensembl

single organismal cell-cell adhesion

Traceable author statement PubMed 20299672. Source: DFLAT

synapse assembly

Inferred from mutant phenotype PubMed 12123610. Source: RGD

tight junction assembly

Inferred from electronic annotation. Source: Ensembl

trophectodermal cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentSchmidt-Lanterman incisure

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

aggresome

Inferred from electronic annotation. Source: Ensembl

apical junction complex

Inferred from electronic annotation. Source: Ensembl

apical part of cell

Inferred from electronic annotation. Source: Ensembl

axon terminus

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

catenin complex

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from electronic annotation. Source: Ensembl

cell-cell adherens junction

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 17167984. Source: RGD

cytoplasmic side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

focal adhesion

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lateral loop

Inferred from electronic annotation. Source: Ensembl

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

node of Ranvier

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 17167984. Source: RGD

trans-Golgi network

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.4. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 158135 Potential
PRO_0000003719
Chain159 – 886728Cadherin-1
PRO_0000003720
Chain705 – 886182E-Cad/CTF1 Potential
PRO_0000236073
Chain736 – 886151E-Cad/CTF2 Potential
PRO_0000236074
Chain755 – 886132E-Cad/CTF3 Potential
PRO_0000236075

Regions

Topological domain24 – 713690Extracellular Potential
Transmembrane714 – 73421Helical; Potential
Topological domain735 – 886152Cytoplasmic Potential
Domain159 – 266108Cadherin 1
Domain267 – 379113Cadherin 2
Domain380 – 490111Cadherin 3
Domain491 – 597107Cadherin 4
Domain598 – 701104Cadherin 5
Region762 – 77312Required for binding CTNND1 and PSEN1 By similarity
Region815 – 88672Required for binding alpha, beta and By similarity
Compositional bias842 – 85716Ser-rich

Sites

Metal binding2611Calcium 1 By similarity
Metal binding2611Calcium 2 By similarity
Metal binding2921Calcium 3 By similarity
Site704 – 7052Cleavage; by a metalloproteinase By similarity
Site735 – 7362Cleavage; by gamma-secretase/PS1 By similarity
Site754 – 7552Cleavage; by caspase-3 By similarity

Amino acid modifications

Modified residue7571Phosphotyrosine; by SRC By similarity
Modified residue7581Phosphotyrosine; by SRC By similarity
Modified residue7591Phosphotyrosine; by SRC By similarity
Modified residue8421Phosphoserine By similarity
Modified residue8441Phosphoserine By similarity
Modified residue8501Phosphoserine By similarity
Glycosylation5621N-linked (GlcNAc...) Potential
Glycosylation6411N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9R0T4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: A9AEE28EB797A547

FASTA88698,715
        10         20         30         40         50         60 
MGARCRSFSA LLLLLQVSSW LCQQPESESD SCRPGFSSEV YTFLVPERHL ERGHILGRVK 

        70         80         90        100        110        120 
FEGCTGRPRT AFFSEDSRFK VSTDGVITVK RHLKLHKLET SFLVHAWDSS YRKLSTKVTL 

       130        140        150        160        170        180 
KSLGHHHHRH HHRDPVSESN PELLTFPSFH QGLRRQKRDW VIPPINCPEN QKGEFPQRLV 

       190        200        210        220        230        240 
QIKSNRDKET TVFYSITGPG ADKPPVGVFI IERETGWLKV TQPLDREAID KYLLYSHAVS 

       250        260        270        280        290        300 
SNGEAVEDPM EIVVTVTDQN DNRPEFIQEV FEGSVAEGAL PGTSVMQVSA TDADDDINTY 

       310        320        330        340        350        360 
NAAIAYTILS QDPELPHKNM FTVNRDTGVI SVVTSGLDRE SYPTYTLVVQ AADLQGEGLS 

       370        380        390        400        410        420 
TTAKAVITVK DINDNAPIFN PSTYQGQVLE NEVGARIATL KVTDDDAPNT PAWNAVYTVV 

       430        440        450        460        470        480 
NDPDHQFTVI TDPKTNEGIL KTAKGLDFEA KQQYILHVTV ENEEPFEGSL VPSTATVTVD 

       490        500        510        520        530        540 
VVDVNEAPIF VPAEKRVEVP EDFGVGLEIA SYTAREPDTF MEQKITYRIW RDTANWLEIN 

       550        560        570        580        590        600 
PETGVISTRA EMDREDSEHV KNSTYTALII ATDDGSPIAT GTGTLLLVLS DVNDNAPIPE 

       610        620        630        640        650        660 
PRNMQFCQRN PKPHVITILD PDLPPNTSPF TAELTHGASV NWTIEYNDAE QESLILQPRK 

       670        680        690        700        710        720 
DLEIGEYKIN LKLSDNQNKD QVTTLEVHVC DCEGTVNNCM KAISLEAGLQ VPAILGILGG 

       730        740        750        760        770        780 
ILALLILILL LLLFLRRRTV VKEPLLPPDD DTRDNVYYYD EEGGGEEDQD FDLSQLHRGL 

       790        800        810        820        830        840 
DARPEVIRND VAPTLMSMPQ YRPRPANPDE IGNFIDENLK AADSDPTAPP YDSLLVFDYE 

       850        860        870        880 
GSGSEAASLS SLNSSESDQD QDYDYLNEWG NRFKKLADMY GGGEED 

« Hide

References

[1]Asai K., Tada T., Yamamoto M., Obayashi M., Mizuno M., Toda A., Eimoto T., Kato T.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Jejunum.
[2]"Multiple cadherin superfamily members with unique expression profiles are produced in rat testis."
Johnson K.J., Patel S.R., Boekelheide K.
Endocrinology 141:675-683(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 769-872.
Strain: Fischer 344.
Tissue: Testis.
[3]Gibbons K.L.
Thesis (1997), University of Technology / Sydney, Australia
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 779-846.
Tissue: Mammary tumor.
[4]"Rab8B GTPase and junction dynamics in the testis."
Lau A.S., Mruk D.D.
Endocrinology 144:1549-1563(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAB8B.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB017696 mRNA. Translation: BAA84920.1.
AF177680 mRNA. Translation: AAF87055.1.
AJ000540 mRNA. Translation: CAA04173.1.
RefSeqNP_112624.1. NM_031334.1.
UniGeneRn.1303.

3D structure databases

ProteinModelPortalQ9R0T4.
SMRQ9R0T4. Positions 159-376, 788-881.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249721. 3 interactions.

PTM databases

PhosphoSiteQ9R0T4.

Proteomic databases

PaxDbQ9R0T4.
PRIDEQ9R0T4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000027346; ENSRNOP00000027346; ENSRNOG00000020151.
GeneID83502.
KEGGrno:83502.
UCSCRGD:69279. rat.

Organism-specific databases

CTD999.
RGD69279. Cdh1.

Phylogenomic databases

eggNOGNOG328838.
GeneTreeENSGT00740000115112.
HOGENOMHOG000231254.
HOVERGENHBG106438.
InParanoidQ9R0T4.
KOK05689.
OMADFGVGQE.
OrthoDBEOG7PS1DS.
PhylomeDBQ9R0T4.
TreeFamTF316817.

Gene expression databases

GenevestigatorQ9R0T4.

Family and domain databases

Gene3D2.60.40.60. 6 hits.
4.10.900.10. 1 hit.
InterProIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR014868. Cadherin_pro_dom.
IPR027397. Catenin_binding_dom.
[Graphical view]
PfamPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
PF08758. Cadherin_pro. 1 hit.
[Graphical view]
PRINTSPR00205. CADHERIN.
SMARTSM00112. CA. 4 hits.
SM01055. Cadherin_pro. 1 hit.
[Graphical view]
SUPFAMSSF49313. SSF49313. 6 hits.
PROSITEPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio615920.
PMAP-CutDBQ9R0T4.
PROQ9R0T4.

Entry information

Entry nameCADH1_RAT
AccessionPrimary (citable) accession number: Q9R0T4
Secondary accession number(s): O35794, Q9JIV9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families