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Entry version 188 (16 Oct 2019)
Sequence version 4 (11 Jul 2001)
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Protein

Dystroglycan

Gene

Dag1

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

The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sacrolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.
Alpha-dystroglycan is an extracellular peripheral glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains, and for certain adenoviruses. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Also receptor for lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses.
Beta-dystroglycan is a transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity (By similarity).By similarity3 Publications

<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 processHost-virus interaction

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-3000178 ECM proteoglycans
R-MMU-5173105 O-linked glycosylation
R-MMU-9010553 Regulation of expression of SLITs and ROBOs

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S72.001

<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_and_taxonomy_section">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:
Dystroglycan
Alternative name(s):
Dystrophin-associated glycoprotein 1
Cleaved into the following 2 chains:
Alpha-dystroglycan
Short name:
Alpha-DG
Beta-dystroglycan
Short name:
Beta-DG
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Dag1
Synonyms:Dag-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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 9

Organism-specific databases

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

More...
MGIi
MGI:101864 Dag1

<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_location_section">'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 domaini652 – 751ExtracellularSequence analysisAdd BLAST100
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei752 – 772HelicalSequence analysisAdd BLAST21
Topological domaini773 – 893CytoplasmicSequence analysisAdd BLAST121

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus, Postsynaptic cell membrane, Secreted, Synapse

<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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Homozygous null mice embryos exhibit gross developmental abnormalities, beginning around 6.5 days of gestation, in the Reichert's membrane, an extraembryonic basement membrane. In peripheral nerves, ablation of DAG1 from 4 week-old mice causes abnormalities in nerve structure and function including mildly impaired sorting of axons, dysmyelination, axonal loss and aberrant nerve conduction. Laminin-binding is lost and there is disruption of the Schwann cell dystroglycan complex.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi796 – 798IIF → AAA: Complete loss of ANK3-binding. 1 Publication3
Mutagenesisi800 – 801DE → AA: Complete loss of ANK3-binding. 1 Publication2
Mutagenesisi803 – 804DD → AA: Major reduction in ANK3-binding. 1 Publication2

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3739252

<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 – 27Sequence analysisAdd BLAST27
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002106728 – 651Alpha-dystroglycanAdd BLAST624
ChainiPRO_0000021068652 – 893Beta-dystroglycanAdd BLAST242

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi139N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi180 ↔ 262Combined sources2 Publications
Glycosylationi315O-linked (Man6P...) threonineBy similarity1
Glycosylationi317O-linked (Man6P...) threonineBy similarity1
Glycosylationi377O-linked (Man6P...) threonineBy similarity1
Glycosylationi639N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi647N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi659N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi667 ↔ 711By similarity
<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 residuei788PhosphothreonineCombined sources1
Modified residuei890Phosphotyrosine; by SRCBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

O- and N-glycosylated (By similarity). POMGNT1 catalyzes the initial addition of N-acetylglucosamine, giving rise to the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety and thus providing the necessary basis for the addition of further carbohydrate moieties. Alpha-dystroglycan is heavily O-glycosylated comprising of up to two thirds of its mass and the carbohydrate composition differs depending on tissue type. Mucin-type O-glycosylation is important for ligand binding activity. O-mannosylation of alpha-DAG1 is found in high abundance in both brain and muscle where the most abundant glycan is Sia-alpha-2-3-Gal-beta-1-4-Glc-NAc-beta-1-2-Man. In muscle, glycosylation on Thr-315, Thr-317, Thr-379 by a phosphorylated O-mannosyl glycan with the structure 2-(N-acetylamido)-2-deoxygalactosyl-beta-1,3-2-(N-acetylamido)-2-deoxyglucosyl-beta-1,4-6-phosphomannose is mediated by like-acetylglucosaminyltransferase (LARGE1) protein amd is required for laminin binding. O-glycosylated in the N-terminal region with a core 1 or possibly core 8 glycan. The beta subunit is N-glycosylated (By similarity).By similarity1 Publication
Autolytic cleavage produces the alpha and beta subunits. In cutaneous cells, as well as in certain pathological conditions, shedding of beta-dystroglcan can occur releasing a peptide of about 30 kDa (By similarity).By similarity
SRC-mediated phosphorylation of the PPXY motif of the beta subunit recruits SH2 domain-containing proteins, but inhibits binding to WWW domain-containing proteins, DMD and UTRN. This phosphorylation also inhibits nuclear entry (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>Sitei651 – 652Cleavage; by autolysisBy similarity2
Sitei713 – 714Cleavage; by MMP9By similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...
CPTACi
non-CPTAC-3909

Encyclopedia of Proteome Dynamics

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EPDi
Q62165

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q62165

MaxQB - The MaxQuant DataBase

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MaxQBi
Q62165

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

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PaxDbi
Q62165

PeptideAtlas

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PeptideAtlasi
Q62165

PRoteomics IDEntifications database

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PRIDEi
Q62165

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
2270

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q62165

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

More...
PhosphoSitePlusi
Q62165

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q62165

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
Q62165

<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

Detected in sciatic nerve (at protein level) (PubMed:11430802). Expressed in a variety of tissues. In brain, expressed in the hippocampal formation, the olfactory bulb, the cerebellum and the thalamus. In the peripheral nerve system, expressed in Schwann cells.4 Publications

<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

Broadly expressed in late embryonic and early postnatal cerebellar neurons, including premigratory granule neurons of the external granule cell layer, but expression is largely down-regulated. Weak expression in Purkinje cells throughout development. Alpha- and beta-DG proteins are also present on the Bergmann glial scaffolds used by granule cells during early postnatal radial migration. In the peripheral nerve system, expression briefly precedes and parallels myelination. First expressed at 18.5 dpc in spinal roots, dorsal root ganglions and nerve trunks. At P1, at the onset of myelination, expressed in motor roots. At P5 and P15, expression progressively increases in sensory roots and peripheral nerves. Between postnatal 2 weeks and 18 months, localizes at the nodes of Ranvier as well as at the Schwann cell outer membrane.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000039952 Expressed in 316 organ(s), highest expression level in sciatic nerve

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q62165 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q62165 MM

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer. Heterodimer of alpha- and beta-dystroglycan subunits which are the central components of the dystrophin-glycoprotein complex. This complex then can form a dystrophin-associated glycoprotein complex (DGC) which is composed of three subcomplexes: a cytoplasmic complex comprised of DMD (or UTRN), DTNA and a number of syntrophins, such as SNTB1, SNTB2, SNTG1 and SNTG2, the transmembrane dystroglycan complex, and the sarcoglycan-sarcospan complex.

Interacts (via the N-terminal of alphaDAG1) with LARGE1; the interaction enhances laminin binding (By similarity).

Interacts with SGCD.

Interacts with AGR2 and AGR3.

Interacts (betaDAG1) with DMD; the interaction is inhibited by phosphorylation on the PPXY motif.

Interacts (betaDAG1, via its PPXY motif) with UTRN (via its WWW and ZZ domains); the interaction is inhibited by phosphorylation on the PPXY motif.

Interacts (betaDAG1, via its phosphorylated PPXY motif) with the SH2 domain-containing proteins, FYN, CSK, NCK and SHC.

Interacts (betaDAG1) with CAV3 (via a central WW-like domain); the interaction disrupts the binding of DMD. BetaDAG1 directly interacts with ANK3, but not with ANK2; this interaction does not interfere with DMD-binding and is required for retention at costameres (By similarity).

Identified in a dystroglycan complex that contains at least PRX, DRP2, UTRN, DMD and DAG1 (PubMed:11430802).

Interacts with POMGNT1 (By similarity).

By similarity5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
EgflamQ4VBE42EBI-2025154,EBI-2025048

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
199048, 7 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q62165

Protein interaction database and analysis system

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IntActi
Q62165, 9 interactors

Molecular INTeraction database

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MINTi
Q62165

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000130626

<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

1893
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
Q62165

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

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EvolutionaryTracei
Q62165

<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_and_domains_section">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>Domaini601 – 710Peptidase S72Add BLAST110

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>Regioni28 – 406Required for laminin recognitionBy similarityAdd BLAST379
Regioni47 – 69O-glycosylated at one siteBy similarityAdd BLAST23
Regioni314 – 483Mucin-like domainBy similarityAdd BLAST170
Regioni461 – 483O-glycosylated at seven sites with GalNAcBy similarityAdd BLAST23
Regioni817 – 893Required for interaction with CAV3By similarityAdd BLAST77
Regioni878 – 893Required for binding DMD and UTRNBy similarityAdd BLAST16

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi774 – 780Nuclear localization signalBy similarity7
Motifi887 – 890PPXY motifBy similarity4

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 biasi316 – 475Pro-richAdd BLAST160
Compositional biasi807 – 893Pro-richAdd BLAST87

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3781 Eukaryota
ENOG410XQTU LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000008429

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000072580

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q62165

KEGG Orthology (KO)

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KOi
K06265

Identification of Orthologs from Complete Genome Data

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OMAi
YDKEDTT

Database of Orthologous Groups

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OrthoDBi
163609at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q62165

TreeFam database of animal gene trees

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TreeFami
TF328370

Family and domain databases

Database of protein disorder

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DisProti
DP00491

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.10, 2 hits
3.30.70.1040, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027468 Alpha-dystroglycan_domain_2
IPR041631 Alpha_DG1_N2
IPR006644 Cadg
IPR015919 Cadherin-like_sf
IPR008465 DAG1_C
IPR013783 Ig-like_fold
IPR030398 SEA_DG_dom

Pfam protein domain database

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Pfami
View protein in Pfam
PF18424 a_DG1_N2, 1 hit
PF05454 DAG1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00736 CADG, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF111006 SSF111006, 1 hit
SSF49313 SSF49313, 2 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51699 SEA_DG, 1 hit

<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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 2 potential isoforms that are computationally mapped.Show allAlign All

Q62165-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSVDNWLLHP LWGQTFLLLL SVAVAQAHWP SEPSEAVRDW KNQLEASMHS
60 70 80 90 100
VLSDFQEAVP TVVGIPDGTA VVGRSFRVSI PTDLIASSGE IIKVSAAGKE
110 120 130 140 150
ALPSWLHWDP HSHILEGLPL DTDKGVHYIS VSAARLGANG SHVPQTSSVF
160 170 180 190 200
SIEVYPEDHN EPQSVRAASS DPGEVVPSAC AADEPVTVLT VILDADLTKM
210 220 230 240 250
TPKQRIDLLN RMQSFSEVEL HNMKLVPVVN NRLFDMSAFM AGPGNAKKVV
260 270 280 290 300
ENGALLSWKL GCSLNQNSVP DIRGVETPAR EGAMSAQLGY PVVGWHIANK
310 320 330 340 350
KPTLPKRLRR QIHATPTPVT AIGPPTTAIQ EPPSRIVPTP TSPAIAPPTE
360 370 380 390 400
TMAPPVRDPV PGKPTVTIRT RGAIIQTPTL GPIQPTRVSE AGTTVPGQIR
410 420 430 440 450
PTLTIPGYVE PTAVITPPTT TTKKPRVSTP KPATPSTDSS TTTTRRPTKK
460 470 480 490 500
PRTPRPVPRV TTKAPITRLE TASPPTRIRT TTSGVPRGGE PNQRPELKNH
510 520 530 540 550
IDRVDAWVGT YFEVKIPSDT FYDNEDTTTD KLKLTLKLRE QQLVGEKSWV
560 570 580 590 600
QFNSNSQLMY GLPDSSHVGK HEYFMHATDK GGLSAVDAFE IHVHKRPQGD
610 620 630 640 650
KAPARFKARL AGDPAPVVND IHKKIALVKK LAFAFGDRNC SSITLQNITR
660 670 680 690 700
GSIVVEWTNN TLPLEPCPKE QIIGLSRRIA DENGKPRPAF SNALEPDFKA
710 720 730 740 750
LSIAVTGSGS CRHLQFIPVA PPSPGSSAAP ATEVPDRDPE KSSEDDVYLH
760 770 780 790 800
TVIPAVVVAA ILLIAGIIAM ICYRKKRKGK LTLEDQATFI KKGVPIIFAD
810 820 830 840 850
ELDDSKPPPS SSMPLILQEE KAPLPPPEYP NQSMPETTPL NQDTVGEYTP
860 870 880 890
LRDEDPNAPP YQPPPPFTAP MEGKGSRPKN MTPYRSPPPY VPP
Length:893
Mass (Da):96,905
Last modified:July 11, 2001 - v4
<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:i59C081EA86AB0AC1
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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0A6YW41A0A0A6YW41_MOUSE
Dystroglycan
Dag1
38Annotation score:

Annotation score:1 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>
A0A0A6YXB6A0A0A6YXB6_MOUSE
Dystroglycan
Dag1
25Annotation score:

Annotation score:1 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 conflicti448 – 450TKK → SKE in CAA84293 (PubMed:7833916).Curated3
Sequence conflicti599 – 600GD → PH in CAA84293 (PubMed:7833916).Curated2
Sequence conflicti643I → V in CAA60031 (PubMed:9057818).Curated1
Sequence conflicti643I → V in AAC52853 (PubMed:7833916).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
U48854 Genomic DNA Translation: AAA99779.2
BC007150 mRNA Translation: AAH07150.1
X86073 mRNA Translation: CAA60031.1
Z34532 mRNA Translation: CAA84293.1
U43512 mRNA Translation: AAC52853.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS23518.1

Protein sequence database of the Protein Information Resource

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PIRi
S59630

NCBI Reference Sequences

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RefSeqi
NP_001263410.1, NM_001276481.1
NP_001263411.1, NM_001276482.1
NP_001263414.1, NM_001276485.1
NP_001263415.1, NM_001276486.1
NP_001263421.1, NM_001276492.1
NP_001263422.1, NM_001276493.1
NP_034147.1, NM_010017.4
XP_006511699.1, XM_006511636.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000080435; ENSMUSP00000079294; ENSMUSG00000039952
ENSMUST00000166905; ENSMUSP00000128531; ENSMUSG00000039952
ENSMUST00000171412; ENSMUSP00000130626; ENSMUSG00000039952
ENSMUST00000191899; ENSMUSP00000142109; ENSMUSG00000039952

Database of genes from NCBI RefSeq genomes

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GeneIDi
13138

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:13138

UCSC genome browser

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UCSCi
uc009rox.2 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
U48854 Genomic DNA Translation: AAA99779.2
BC007150 mRNA Translation: AAH07150.1
X86073 mRNA Translation: CAA60031.1
Z34532 mRNA Translation: CAA84293.1
U43512 mRNA Translation: AAC52853.1
CCDSiCCDS23518.1
PIRiS59630
RefSeqiNP_001263410.1, NM_001276481.1
NP_001263411.1, NM_001276482.1
NP_001263414.1, NM_001276485.1
NP_001263415.1, NM_001276486.1
NP_001263421.1, NM_001276492.1
NP_001263422.1, NM_001276493.1
NP_034147.1, NM_010017.4
XP_006511699.1, XM_006511636.2

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
1U2CX-ray2.30A58-303[»]
4WIQX-ray1.59A50-313[»]
5N30X-ray1.80A50-312[»]
5N4HX-ray1.70A51-313[»]
SMRiQ62165
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi199048, 7 interactors
CORUMiQ62165
IntActiQ62165, 9 interactors
MINTiQ62165
STRINGi10090.ENSMUSP00000130626

Chemistry databases

ChEMBLiCHEMBL3739252

Protein family/group databases

MEROPSiS72.001

PTM databases

GlyConnecti2270
iPTMnetiQ62165
PhosphoSitePlusiQ62165
SwissPalmiQ62165

Proteomic databases

CPTACinon-CPTAC-3909
EPDiQ62165
jPOSTiQ62165
MaxQBiQ62165
PaxDbiQ62165
PeptideAtlasiQ62165
PRIDEiQ62165

Genome annotation databases

EnsembliENSMUST00000080435; ENSMUSP00000079294; ENSMUSG00000039952
ENSMUST00000166905; ENSMUSP00000128531; ENSMUSG00000039952
ENSMUST00000171412; ENSMUSP00000130626; ENSMUSG00000039952
ENSMUST00000191899; ENSMUSP00000142109; ENSMUSG00000039952
GeneIDi13138
KEGGimmu:13138
UCSCiuc009rox.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1605
MGIiMGI:101864 Dag1

Phylogenomic databases

eggNOGiKOG3781 Eukaryota
ENOG410XQTU LUCA
GeneTreeiENSGT00390000008429
HOGENOMiHOG000072580
InParanoidiQ62165
KOiK06265
OMAiYDKEDTT
OrthoDBi163609at2759
PhylomeDBiQ62165
TreeFamiTF328370

Enzyme and pathway databases

ReactomeiR-MMU-3000178 ECM proteoglycans
R-MMU-5173105 O-linked glycosylation
R-MMU-9010553 Regulation of expression of SLITs and ROBOs

Miscellaneous databases

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

More...
ChiTaRSi
Dag1 mouse
EvolutionaryTraceiQ62165
PMAP-CutDBiQ62165

Protein Ontology

More...
PROi
PR:Q62165

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000039952 Expressed in 316 organ(s), highest expression level in sciatic nerve
ExpressionAtlasiQ62165 baseline and differential
GenevisibleiQ62165 MM

Family and domain databases

DisProtiDP00491
Gene3Di2.60.40.10, 2 hits
3.30.70.1040, 1 hit
InterProiView protein in InterPro
IPR027468 Alpha-dystroglycan_domain_2
IPR041631 Alpha_DG1_N2
IPR006644 Cadg
IPR015919 Cadherin-like_sf
IPR008465 DAG1_C
IPR013783 Ig-like_fold
IPR030398 SEA_DG_dom
PfamiView protein in Pfam
PF18424 a_DG1_N2, 1 hit
PF05454 DAG1, 1 hit
SMARTiView protein in SMART
SM00736 CADG, 2 hits
SUPFAMiSSF111006 SSF111006, 1 hit
SSF49313 SSF49313, 2 hits
PROSITEiView protein in PROSITE
PS51699 SEA_DG, 1 hit

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 nameiDAG1_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: Q62165
Secondary accession number(s): Q61094, Q61141, Q61497
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 11, 2001
Last modified: October 16, 2019
This is version 188 of the entry and version 4 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, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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