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Q62165

- DAG1_MOUSE

UniProt

Q62165 - DAG1_MOUSE

Protein

Dystroglycan

Gene

Dag1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 4 (11 Jul 2001)
      Previous versions | rss
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    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 similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei651 – 6522Cleavage; by autolysisBy similarity
    Sitei713 – 7142Cleavage; by MMP9By similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. protein binding Source: IntAct
    3. structural constituent of muscle Source: Ensembl

    GO - Biological processi

    1. basement membrane organization Source: MGI
    2. branching involved in salivary gland morphogenesis Source: MGI
    3. calcium-dependent cell-matrix adhesion Source: Ensembl
    4. commissural neuron axon guidance Source: MGI
    5. cytoskeletal anchoring at plasma membrane Source: InterPro
    6. epithelial tube branching involved in lung morphogenesis Source: MGI
    7. membrane protein ectodomain proteolysis Source: Ensembl
    8. microtubule anchoring Source: Ensembl
    9. modulation by virus of host morphology or physiology Source: Ensembl
    10. morphogenesis of an epithelial sheet Source: MGI
    11. myelination in peripheral nervous system Source: UniProtKB
    12. negative regulation of cell migration Source: Ensembl
    13. negative regulation of MAPK cascade Source: Ensembl
    14. negative regulation of protein kinase B signaling Source: Ensembl
    15. nerve maturation Source: UniProtKB
    16. NLS-bearing protein import into nucleus Source: Ensembl
    17. response to peptide hormone Source: Ensembl
    18. Schwann cell development Source: UniProtKB

    Keywords - Biological processi

    Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_216309. Integrin cell surface interactions.

    Protein family/group databases

    MEROPSiS72.001.

    Names & Taxonomyi

    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
    Gene namesi
    Name:Dag1
    Synonyms:Dag-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:101864. Dag1.

    Subcellular locationi

    Chain Beta-dystroglycan : Cell membrane By similarity; Single-pass type I membrane protein By similarity. Cytoplasmcytoskeleton. Nucleusnucleoplasm. Cell membranesarcolemma. Cell junctionsynapsepostsynaptic cell membrane
    Note: The monomeric form translocates to the nucleus via the action of importins and depends on RAN. Nuclear transport is inhibited by Tyr-892 phosphorylation. In skeletal muscle, this phosphorylated form locates to a vesicular internal membrane compartment. In muscle cells, sarcolemma localization requires the presence of ANK2, while localization to costameres requires the presence of ANK3. Localizes to neuromuscular junctions (NMJs). In adult muscle, NMJ localization depends upon ANK2 presence, but not in newborn animals. In peripheral nerves, localizes to the Schwann cell membrane. Colocalizes with ERM proteins in Schwann-cell microvilli.

    GO - Cellular componenti

    1. basement membrane Source: MGI
    2. basolateral plasma membrane Source: Ensembl
    3. cell-cell adherens junction Source: Ensembl
    4. cell-cell junction Source: MGI
    5. cell outer membrane Source: UniProtKB
    6. contractile ring Source: Ensembl
    7. costamere Source: Ensembl
    8. cytoskeleton Source: UniProtKB-SubCell
    9. dystroglycan complex Source: MGI
    10. extracellular space Source: UniProtKB-SubCell
    11. filopodium Source: Ensembl
    12. focal adhesion Source: Ensembl
    13. integral component of membrane Source: UniProtKB-KW
    14. lamellipodium Source: Ensembl
    15. membrane Source: MGI
    16. membrane raft Source: MGI
    17. node of Ranvier Source: UniProtKB
    18. nucleoplasm Source: UniProtKB-SubCell
    19. plasma membrane Source: MGI
    20. postsynaptic membrane Source: UniProtKB-SubCell
    21. sarcolemma Source: MGI

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi796 – 7983IIF → AAA: Complete loss of ANK3-binding. 1 Publication
    Mutagenesisi800 – 8012DE → AA: Complete loss of ANK3-binding. 1 Publication
    Mutagenesisi803 – 8042DD → AA: Major reduction in ANK3-binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 651624Alpha-dystroglycanPRO_0000021067Add
    BLAST
    Chaini652 – 893242Beta-dystroglycanPRO_0000021068Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi139 – 1391N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi180 ↔ 2622 Publications
    Glycosylationi377 – 3771O-linked (Man6P...)By similarity
    Glycosylationi639 – 6391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi647 – 6471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi659 – 6591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi667 ↔ 711By similarity
    Modified residuei890 – 8901Phosphotyrosine; by SRCBy similarity

    Post-translational modificationi

    O- and N-glycosylated By similarity. 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. O-glycosylated in the N-terminal region with a core 1 or possibly core 8 glycan. The beta subunit is N-glycosylated By similarity. In muscle, glycosylation on Thr-379 by a phosphorylated O-mannosyl glycan (N-acetylamido)-2-deoxyglucosyl-beta-1,4-6-phosphomannose is mediated by like-acetylglucosaminyltransferase (LARGE) protein amd is required for laminin binding. O-mannosylation is also required for binding lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses.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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ62165.
    PaxDbiQ62165.
    PRIDEiQ62165.

    PTM databases

    PhosphoSiteiQ62165.

    Miscellaneous databases

    PMAP-CutDBQ62165.

    Expressioni

    Tissue specificityi

    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.3 Publications

    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 E18.5 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

    ArrayExpressiQ62165.
    BgeeiQ62165.
    CleanExiMM_DAG1.
    GenevestigatoriQ62165.

    Interactioni

    Subunit structurei

    Monomer By similarity. 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 LARGE; the interaction enhances laminin binding By similarity. Interacts with AGR2 and AGR3. Interacts (betaDAG1) with DMD; the interaction is inhibited by phosphorylaion 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 By similarity. Interacts with SGCD. 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 similarity4 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi199048. 7 interactions.
    IntActiQ62165. 4 interactions.
    MINTiMINT-145749.

    Structurei

    Secondary structure

    1
    893
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi68 – 714
    Beta strandi76 – 794
    Helixi82 – 854
    Beta strandi90 – 967
    Beta strandi99 – 1013
    Beta strandi106 – 1094
    Turni110 – 1134
    Beta strandi114 – 1174
    Helixi121 – 1233
    Beta strandi125 – 13612
    Beta strandi142 – 15716
    Beta strandi186 – 1949
    Helixi197 – 1993
    Helixi202 – 21615
    Helixi220 – 2223
    Beta strandi224 – 2274
    Beta strandi239 – 2435
    Beta strandi254 – 26310
    Turni266 – 2683
    Helixi273 – 2819
    Helixi283 – 2886
    Beta strandi292 – 3009

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U2CX-ray2.30A58-303[»]
    DisProtiDP00491.
    ProteinModelPortaliQ62165.
    SMRiQ62165. Positions 58-303.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ62165.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini652 – 751100ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini773 – 893121CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei752 – 77221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini601 – 710110Peptidase S72Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni28 – 406379Required for laminin recognitionBy similarityAdd
    BLAST
    Regioni47 – 6923O-glycosylated at one siteBy similarityAdd
    BLAST
    Regioni314 – 483170Mucin-like domainBy similarityAdd
    BLAST
    Regioni461 – 48323O-glycosylated at seven sites with GalNAcBy similarityAdd
    BLAST
    Regioni817 – 89377Required for interaction with CAV3By similarityAdd
    BLAST
    Regioni878 – 89316Required for binding DMD and UTRNBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi774 – 7807Nuclear localization signalBy similarity
    Motifi887 – 8904PPXY motifBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi316 – 475160Pro-richAdd
    BLAST
    Compositional biasi807 – 89387Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 peptidase S72 domain.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG266557.
    GeneTreeiENSGT00390000008429.
    HOGENOMiHOG000072580.
    HOVERGENiHBG000078.
    InParanoidiQ62165.
    KOiK06265.
    OMAiAMICYRK.
    OrthoDBiEOG7KSX82.
    PhylomeDBiQ62165.
    TreeFamiTF328370.

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    3.30.70.1040. 1 hit.
    InterProiIPR027468. Alpha-dystroglycan_domain_2.
    IPR006644. Cadg.
    IPR015919. Cadherin-like.
    IPR008465. DAG1.
    IPR013783. Ig-like_fold.
    [Graphical view]
    PfamiPF05454. DAG1. 1 hit.
    [Graphical view]
    SMARTiSM00736. CADG. 2 hits.
    [Graphical view]
    SUPFAMiSSF111006. SSF111006. 1 hit.
    SSF49313. SSF49313. 2 hits.
    PROSITEiPS51699. SEA_DG. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q62165-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVDNWLLHP LWGQTFLLLL SVAVAQAHWP SEPSEAVRDW KNQLEASMHS    50
    VLSDFQEAVP TVVGIPDGTA VVGRSFRVSI PTDLIASSGE IIKVSAAGKE 100
    ALPSWLHWDP HSHILEGLPL DTDKGVHYIS VSAARLGANG SHVPQTSSVF 150
    SIEVYPEDHN EPQSVRAASS DPGEVVPSAC AADEPVTVLT VILDADLTKM 200
    TPKQRIDLLN RMQSFSEVEL HNMKLVPVVN NRLFDMSAFM AGPGNAKKVV 250
    ENGALLSWKL GCSLNQNSVP DIRGVETPAR EGAMSAQLGY PVVGWHIANK 300
    KPTLPKRLRR QIHATPTPVT AIGPPTTAIQ EPPSRIVPTP TSPAIAPPTE 350
    TMAPPVRDPV PGKPTVTIRT RGAIIQTPTL GPIQPTRVSE AGTTVPGQIR 400
    PTLTIPGYVE PTAVITPPTT TTKKPRVSTP KPATPSTDSS TTTTRRPTKK 450
    PRTPRPVPRV TTKAPITRLE TASPPTRIRT TTSGVPRGGE PNQRPELKNH 500
    IDRVDAWVGT YFEVKIPSDT FYDNEDTTTD KLKLTLKLRE QQLVGEKSWV 550
    QFNSNSQLMY GLPDSSHVGK HEYFMHATDK GGLSAVDAFE IHVHKRPQGD 600
    KAPARFKARL AGDPAPVVND IHKKIALVKK LAFAFGDRNC SSITLQNITR 650
    GSIVVEWTNN TLPLEPCPKE QIIGLSRRIA DENGKPRPAF SNALEPDFKA 700
    LSIAVTGSGS CRHLQFIPVA PPSPGSSAAP ATEVPDRDPE KSSEDDVYLH 750
    TVIPAVVVAA ILLIAGIIAM ICYRKKRKGK LTLEDQATFI KKGVPIIFAD 800
    ELDDSKPPPS SSMPLILQEE KAPLPPPEYP NQSMPETTPL NQDTVGEYTP 850
    LRDEDPNAPP YQPPPPFTAP MEGKGSRPKN MTPYRSPPPY VPP 893
    Length:893
    Mass (Da):96,905
    Last modified:July 11, 2001 - v4
    Checksum:i59C081EA86AB0AC1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti448 – 4503TKK → SKE in CAA84293. (PubMed:7833916)Curated
    Sequence conflicti599 – 6002GD → PH in CAA84293. (PubMed:7833916)Curated
    Sequence conflicti643 – 6431I → V in CAA60031. (PubMed:9057818)Curated
    Sequence conflicti643 – 6431I → V in AAC52853. (PubMed:7833916)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_001263423.1. NM_001276494.1.
    NP_034147.1. NM_010017.4.
    XP_006511699.1. XM_006511636.1.
    UniGeneiMm.491797.
    Mm.7524.

    Genome annotation databases

    EnsembliENSMUST00000080435; ENSMUSP00000079294; ENSMUSG00000039952.
    ENSMUST00000166905; ENSMUSP00000128531; ENSMUSG00000039952.
    ENSMUST00000171412; ENSMUSP00000130626; ENSMUSG00000039952.
    GeneIDi13138.
    KEGGimmu:13138.
    UCSCiuc009rox.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS23518.1.
    PIRi S59630.
    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_001263423.1. NM_001276494.1.
    NP_034147.1. NM_010017.4.
    XP_006511699.1. XM_006511636.1.
    UniGenei Mm.491797.
    Mm.7524.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U2C X-ray 2.30 A 58-303 [» ]
    DisProti DP00491.
    ProteinModelPortali Q62165.
    SMRi Q62165. Positions 58-303.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199048. 7 interactions.
    IntActi Q62165. 4 interactions.
    MINTi MINT-145749.

    Protein family/group databases

    MEROPSi S72.001.

    PTM databases

    PhosphoSitei Q62165.

    Proteomic databases

    MaxQBi Q62165.
    PaxDbi Q62165.
    PRIDEi Q62165.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000080435 ; ENSMUSP00000079294 ; ENSMUSG00000039952 .
    ENSMUST00000166905 ; ENSMUSP00000128531 ; ENSMUSG00000039952 .
    ENSMUST00000171412 ; ENSMUSP00000130626 ; ENSMUSG00000039952 .
    GeneIDi 13138.
    KEGGi mmu:13138.
    UCSCi uc009rox.1. mouse.

    Organism-specific databases

    CTDi 1605.
    MGIi MGI:101864. Dag1.

    Phylogenomic databases

    eggNOGi NOG266557.
    GeneTreei ENSGT00390000008429.
    HOGENOMi HOG000072580.
    HOVERGENi HBG000078.
    InParanoidi Q62165.
    KOi K06265.
    OMAi AMICYRK.
    OrthoDBi EOG7KSX82.
    PhylomeDBi Q62165.
    TreeFami TF328370.

    Enzyme and pathway databases

    Reactomei REACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_216309. Integrin cell surface interactions.

    Miscellaneous databases

    ChiTaRSi DAG1. mouse.
    EvolutionaryTracei Q62165.
    NextBioi 283210.
    PMAP-CutDB Q62165.
    PROi Q62165.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q62165.
    Bgeei Q62165.
    CleanExi MM_DAG1.
    Genevestigatori Q62165.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    3.30.70.1040. 1 hit.
    InterProi IPR027468. Alpha-dystroglycan_domain_2.
    IPR006644. Cadg.
    IPR015919. Cadherin-like.
    IPR008465. DAG1.
    IPR013783. Ig-like_fold.
    [Graphical view ]
    Pfami PF05454. DAG1. 1 hit.
    [Graphical view ]
    SMARTi SM00736. CADG. 2 hits.
    [Graphical view ]
    SUPFAMi SSF111006. SSF111006. 1 hit.
    SSF49313. SSF49313. 2 hits.
    PROSITEi PS51699. SEA_DG. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Dystroglycan is essential for early embryonic development: disruption of Reichert's membrane in Dag1-null mice."
      Williamson R.A., Henry M.D., Daniels K.J., Hrstka R.F., Lee J.C., Sunada Y., Ibraghimov-Beskrovnaya O., Campbell K.P.
      Hum. Mol. Genet. 6:831-841(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY.
      Strain: 129/SvJ.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Mammary gland.
    3. "Cloning and sequencing of mouse skeletal muscle alpha-dystroglycan."
      Brancaccio A., Ruegg M.A., Engel J.
      Matrix Biol. 14:681-685(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-650.
      Tissue: Skeletal muscle.
    4. Brancaccio A.
      Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 142-143.
    5. "Dystroglycan: brain localisation and chromosome mapping in the mouse."
      Gorecki D.C., Derry J.M.J., Barnard E.A.
      Hum. Mol. Genet. 3:1589-1597(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 352-650, TISSUE SPECIFICITY.
      Strain: C57BL/10.
      Tissue: Skeletal muscle.
    6. "Cloning and expression analyses of mouse dystroglycan gene: specific expression in maternal decidua at the peri-implantation stage."
      Yotsumoto S., Fujiwara H., Horton J.H., Mosby T.A., Wang X., Cui Y., Ko M.S.H.
      Hum. Mol. Genet. 5:1259-1267(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 620-893.
      Strain: C57BL/6J.
      Tissue: Decidua.
    7. "A single disulfide bridge (Cys182-Cys264) is crucial for alpha-dystroglycan N-terminal domain stability."
      Brancaccio A., Jeno P., Engel J.
      Ann. N. Y. Acad. Sci. 857:228-231(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BOND.
    8. "Molecular organization of sarcoglycan complex in mouse myotubes in culture."
      Chan Y.-M., Boennemann C.G., Lidov H.G.W., Kunkel L.M.
      J. Cell Biol. 143:2033-2044(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SGCD.
    9. "The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation."
      Ilsley J.L., Sudol M., Winder S.J.
      Cell. Signal. 13:625-632(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH DMD.
    10. "Expression of dystroglycan, fukutin and POMGnT1 during mouse cerebellar development."
      Henion T.R., Qu Q., Smith F.I.
      Brain Res. Mol. Brain Res. 112:177-181(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    11. "Expression of laminin receptors in schwann cell differentiation: evidence for distinct roles."
      Previtali S.C., Nodari A., Taveggia C., Pardini C., Dina G., Villa A., Wrabetz L., Quattrini A., Feltri M.L.
      J. Neurosci. 23:5520-5530(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, FUNCTION.
    12. "Unique role of dystroglycan in peripheral nerve myelination, nodal structure, and sodium channel stabilization."
      Saito F., Moore S.A., Barresi R., Henry M.D., Messing A., Ross-Barta S.E., Cohn R.D., Williamson R.A., Sluka K.A., Sherman D.L., Brophy P.J., Schmelzer J.D., Low P.A., Wrabetz L., Feltri M.L., Campbell K.P.
      Neuron 38:747-758(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, LIGAND-BINDING.
    13. "An ankyrin-based mechanism for functional organization of dystrophin and dystroglycan."
      Ayalon G., Davis J.Q., Scotland P.B., Bennett V.
      Cell 135:1189-1200(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANK3, SUBCELLULAR LOCATION, MUTAGENESIS OF 796-ILE--PHE-798; 800-ASP-GLU-801 AND 803-ASP-ASP-804.
    14. "O-mannosyl phosphorylation of alpha-dystroglycan is required for laminin binding."
      Yoshida-Moriguchi T., Yu L., Stalnaker S.H., Davis S., Kunz S., Madson M., Oldstone M.B., Schachter H., Wells L., Campbell K.P.
      Science 327:88-92(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE OF CARBOHYDRATES, LIGAND-BINDING, ADENOVIRUS BINDING, IDENTIFICATION BY MASS SPECTROMETRY.
    15. "The structure of the N-terminal region of murine skeletal muscle alpha-dystroglycan discloses a modular architecture."
      Bozic D., Sciandra F., Lamba D., Brancaccio A.
      J. Biol. Chem. 279:44812-44816(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 58-303 IN COMPLEX WITH LIGAND, DISULFIDE BOND.

    Entry informationi

    Entry nameiDAG1_MOUSE
    AccessioniPrimary (citable) accession number: Q62165
    Secondary accession number(s): Q61094, Q61141, Q61497
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 11, 2001
    Last modified: October 1, 2014
    This is version 140 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3