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Entry version 161 (22 Apr 2020)
Sequence version 1 (01 May 2000)
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Protein

Cadherin-1

Gene

Cdh1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi261Calcium 1By similarity1
Metal bindingi261Calcium 2By similarity1
Metal bindingi292Calcium 3By similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell adhesion
LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-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

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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:
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Cdh1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Rat genome database

More...
RGDi
69279 Cdh1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini24 – 713ExtracellularSequence analysisAdd BLAST690
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei714 – 734HelicalSequence analysisAdd BLAST21
Topological domaini735 – 886CytoplasmicSequence analysisAdd BLAST152

Keywords - Cellular componenti

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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 23Sequence analysisAdd BLAST23
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000000371924 – 158Sequence analysisAdd BLAST135
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi284O-linked (Man...) serineBy similarity1
Glycosylationi289O-linked (Man...) serineBy similarity1
Glycosylationi362O-linked (Man...) threonineBy similarity1
Glycosylationi474O-linked (Man...) threonineBy similarity1
Glycosylationi476O-linked (Man...) threonineBy similarity1
Glycosylationi513O-linked (Man...) threonineBy similarity1
Glycosylationi562N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi580O-linked (Man...) threonineBy similarity1
Glycosylationi582O-linked (Man...) threonineBy similarity1
Glycosylationi584O-linked (Man...) threonineBy similarity1
Glycosylationi641N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

During apoptosis or with calcium influx, cleaved by a membrane-bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3 (By similarity). Processing by the metalloproteinase, induced by calcium influx, causes disruption of cell-cell adhesion and the subsequent release of beta-catenin into the cytoplasm (By similarity). The residual membrane-tethered cleavage product is rapidly degraded via an intracellular proteolytic pathway (By similarity). Cleavage by caspase-3 releases the cytoplasmic tail resulting in disintegration of the actin microfilament system (By similarity). The gamma-secretase-mediated cleavage promotes disassembly of adherens junctions (By similarity). During development of the cochlear organ of Corti, cleavage by ADAM10 at adherens junctions promotes pillar cell separation (By similarity).By similarity
N-glycosylation at Asn-641 is essential for expression, folding and trafficking. Addition of bisecting N-acetylglucosamine by MGAT3 modulates its cell membrane location (By similarity).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
O-glycosylated. O-manosylated by TMTC1, TMTC2, TMTC3 or TMTC4. Ser-289 and Thr-513 are O-manosylated by TMTC2 or TMTC4 but not TMTC1 or TMTC3.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>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

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9R0T4

PRoteomics IDEntifications database

More...
PRIDEi
Q9R0T4

PTM databases

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9R0T4

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q9R0T4

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000020151 Expressed in colon and 7 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9R0T4 RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 (By similarity).

Interacts with the TRPV4 and CTNNB1 complex (By similarity).

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 (By similarity). Alternatively, the CTNNA1-containing complex may be linked to F-actin by other proteins such as LIMA1 (By similarity). 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 DDR1; this stabilizes CDH1 at the cell surface and inhibits its internalization (By similarity).

Interacts with RAPGEF2 (By similarity).

Interacts with RAB8B (PubMed:12639940).

Interacts with KLRG1 (By similarity).

Forms a ternary complex composed of ADAM10, CADH1 and EPHA4; within the complex, CADH1 is cleaved by ADAM10 which disrupts adherens junctions (By similarity).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
249721, 3 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000027346

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9R0T4

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi842 – 857Ser-richAdd BLAST16

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3594 Eukaryota
ENOG410XQHI LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157175

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_005284_2_1_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9R0T4

KEGG Orthology (KO)

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KOi
K05689

Identification of Orthologs from Complete Genome Data

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OMAi
SFLVHAW

Database of Orthologous Groups

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OrthoDBi
182239at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9R0T4

TreeFam database of animal gene trees

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TreeFami
TF316817

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
4.10.900.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View 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

The PANTHER Classification System

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PANTHERi
PTHR24027 PTHR24027, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00028 Cadherin, 5 hits
PF01049 Cadherin_C, 1 hit
PF08758 Cadherin_pro, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00205 CADHERIN

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00112 CA, 4 hits
SM01055 Cadherin_pro, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49313 SSF49313, 6 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00232 CADHERIN_1, 3 hits
PS50268 CADHERIN_2, 5 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA9AEE28EB797A547
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AB017696 mRNA Translation: BAA84920.1
AF177680 mRNA Translation: AAF87055.1
AJ000540 mRNA Translation: CAA04173.1

NCBI Reference Sequences

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RefSeqi
NP_112624.1, NM_031334.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSRNOT00000027346; ENSRNOP00000027346; ENSRNOG00000020151

Database of genes from NCBI RefSeq genomes

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GeneIDi
83502

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:83502

UCSC genome browser

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UCSCi
RGD:69279 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

3D structure databases

SMRiQ9R0T4
ModBaseiSearch...

Protein-protein interaction databases

BioGridi249721, 3 interactors
STRINGi10116.ENSRNOP00000027346

PTM databases

PhosphoSitePlusiQ9R0T4
SwissPalmiQ9R0T4

Proteomic databases

PaxDbiQ9R0T4
PRIDEiQ9R0T4

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
999
RGDi69279 Cdh1

Phylogenomic databases

eggNOGiKOG3594 Eukaryota
ENOG410XQHI LUCA
GeneTreeiENSGT00940000157175
HOGENOMiCLU_005284_2_1_1
InParanoidiQ9R0T4
KOiK05689
OMAiSFLVHAW
OrthoDBi182239at2759
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

Protein Ontology

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PROi
PR:Q9R0T4

Gene expression databases

BgeeiENSRNOG00000020151 Expressed in colon and 7 other tissues
GenevisibleiQ9R0T4 RN

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, 5 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCADH1_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9R0T4
Secondary accession number(s): O35794, Q9JIV9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: April 22, 2020
This is version 161 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome
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