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Entry version 220 (07 Oct 2020)
Sequence version 1 (01 Jul 1989)
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Protein

Cadherin-1

Gene

Cdh1

Organism
Mus musculus (Mouse)
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 (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
(Microbial infection) Does not function as a receptor for L.monocytogenes internalin A (InlA); mutating a single surface-exposed residue confers receptor activity to this protein and promotes uptake of the bacteria.1 Publication

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 bindingi259Calcium 11
Metal bindingi259Calcium 21
Metal bindingi290Calcium 31

<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-MMU-1474228, Degradation of the extracellular matrix
R-MMU-216083, Integrin cell surface interactions
R-MMU-351906, Apoptotic cleavage of cell adhesion proteins
R-MMU-418990, Adherens junctions interactions
R-MMU-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):
ARC-1
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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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: Unplaced

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:88354, 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 domaini157 – 709ExtracellularSequence analysisAdd BLAST553
<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>Transmembranei710 – 733HelicalSequence analysisAdd BLAST24
Topological domaini734 – 884CytoplasmicSequence analysisAdd BLAST151

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi172E → P: Adheres to and takes up L.monocytogenes InlA coated beads. 1 Publication1
Mutagenesisi220Q → E: Increased affinity for L.monocytogenes InlA. Greatly increased affinity; when associated with P-172. 1 Publication1

<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_000000371724 – 156Sequence analysisAdd BLAST133
<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_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
<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>Glycosylationi282O-linked (Man...) serine1 Publication1
Glycosylationi287O-linked (Man...) serine1 Publication1
Glycosylationi360O-linked (Man...) threonine1 Publication1
Glycosylationi472O-linked (Man...) threonine1 Publication1
Glycosylationi474O-linked (Man...) threonine1 Publication1
Glycosylationi511O-linked (Man...) threonine1 Publication1
Glycosylationi560N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi578O-linked (Man...) threonine1 Publication1
Glycosylationi580O-linked (Man...) threonine1 Publication1
Glycosylationi582O-linked (Man...) threonine1 Publication1
Glycosylationi639N-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 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

<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 (PubMed:30639848).By similarity1 Publication
O-glycosylated. O-manosylated by TMTC1, TMTC2, TMTC3 or TMTC4. Ser-287 and Thr-511 are O-manosylated by TMTC2 or TMTC4 but not TMTC1 or TMTC3.1 Publication
N-glycosylation at Asn-639 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-756 (By similarity).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>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

The CPTAC Assay portal

More...
CPTACi
non-CPTAC-3565

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P09803

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P09803

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

More...
PaxDbi
P09803

PeptideAtlas

More...
PeptideAtlasi
P09803

PRoteomics IDEntifications database

More...
PRIDEi
P09803

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P09803, 11 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P09803

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

More...
PhosphoSitePlusi
P09803

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in inner and outer pillar cells of the organ of Corti (at protein level) (PubMed:30639848). Non-neural epithelial tissues.1 Publication

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>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

<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 (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).

Forms a ternary complex composed of ADAM10, CADH1 and EPHA4; within the complex, CADH1 is cleaved by ADAM10 which disrupts adherens junctions (PubMed:30639848).

By similarity7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
198631, 42 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P09803

Database of interacting proteins

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DIPi
DIP-29635N

Protein interaction database and analysis system

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IntActi
P09803, 42 interactors

Molecular INTeraction database

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MINTi
P09803

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000000312

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P09803, protein

<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

Secondary structure

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

3D structure databases

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

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SMRi
P09803

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P09803

<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>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
<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>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
<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 biasi840 – 855Ser-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.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3594, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P09803

KEGG Orthology (KO)

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KOi
K05689

Database of Orthologous Groups

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OrthoDBi
182239at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P09803

TreeFam database of animal gene trees

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TreeFami
TF316817

Family and domain databases

Database of protein disorder

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DisProti
DP00159

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
4.10.900.10, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

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IDEALi
IID50003

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, 4 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>Sequence (1+)i

<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.

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
<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:i7A6444148D3D5983
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>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
Cdh1
884Annotation 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti267E → P in CAA43292 (PubMed:1754391).Curated1
Sequence conflicti272S → F in CAA43292 (PubMed:1754391).Curated1

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

More...
DDBJi
Links Updated
X06115 mRNA Translation: CAA29488.1
X60961 X60975 Genomic DNA Translation: CAA43292.1
X06339 mRNA Translation: CAA29645.1
M81449 Genomic DNA Translation: AAA37352.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS22638.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S04528, IJMSCE
S34438

NCBI Reference Sequences

More...
RefSeqi
NP_033994.1, NM_009864.3

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
12550

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:12550

UCSC genome browser

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UCSCi
uc009ngi.1, mouse

<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
X06115 mRNA Translation: CAA29488.1
X60961 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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
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[»]
SMRiP09803
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi198631, 42 interactors
CORUMiP09803
DIPiDIP-29635N
IntActiP09803, 42 interactors
MINTiP09803
STRINGi10090.ENSMUSP00000000312

PTM databases

GlyGeniP09803, 11 sites
iPTMnetiP09803
PhosphoSitePlusiP09803

Proteomic databases

CPTACinon-CPTAC-3565
jPOSTiP09803
MaxQBiP09803
PaxDbiP09803
PeptideAtlasiP09803
PRIDEiP09803

Genome annotation databases

GeneIDi12550
KEGGimmu:12550
UCSCiuc009ngi.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
999
MGIiMGI:88354, Cdh1

Phylogenomic databases

eggNOGiKOG3594, Eukaryota
InParanoidiP09803
KOiK05689
OrthoDBi182239at2759
PhylomeDBiP09803
TreeFamiTF316817

Enzyme and pathway databases

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

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
12550, 0 hits in 18 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Cdh1, mouse
EvolutionaryTraceiP09803

Protein Ontology

More...
PROi
PR:P09803
RNActiP09803, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Family and domain databases

DisProtiDP00159
Gene3Di4.10.900.10, 1 hit
IDEALiIID50003
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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_MOUSE
<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: P09803
Secondary accession number(s): Q61377
<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: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 7, 2020
This is version 220 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

3D-structure, 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
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