SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q62165

- DAG1_MOUSE

UniProt

Q62165 - DAG1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dystroglycan

Gene
Dag1, Dag-1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.3 Publications
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.3 Publications
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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei651 – 6522Cleavage; by autolysis By similarity
Sitei713 – 7142Cleavage; by MMP9 By 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
Complete GO annotation...

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 Alpha-dystroglycan : Secretedextracellular space By similarity 1 Publication
Chain Beta-dystroglycan : Cell membrane; 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.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini652 – 751100Extracellular Reviewed predictionAdd
BLAST
Transmembranei752 – 77221Helical; Reviewed predictionAdd
BLAST
Topological domaini773 – 893121Cytoplasmic Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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.
Mutagenesisi800 – 8012DE → AA: Complete loss of ANK3-binding.
Mutagenesisi803 – 8042DD → AA: Major reduction in ANK3-binding.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi139 – 1391N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi180 ↔ 2622 Publications
Glycosylationi377 – 3771O-linked (Man6P...) By similarity
Glycosylationi639 – 6391N-linked (GlcNAc...) Reviewed prediction
Glycosylationi647 – 6471N-linked (GlcNAc...) Reviewed prediction
Glycosylationi659 – 6591N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi667 ↔ 711 By similarity
Modified residuei890 – 8901Phosphotyrosine; by SRC By 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.1 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.
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.

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.3 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.

Miscellaneous databases

EvolutionaryTraceiQ62165.

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 recognition By similarityAdd
BLAST
Regioni47 – 6923O-glycosylated at one site By similarityAdd
BLAST
Regioni314 – 483170Mucin-like domain By similarityAdd
BLAST
Regioni461 – 48323O-glycosylated at seven sites with GalNAc By similarityAdd
BLAST
Regioni817 – 89377Required for interaction with CAV3 By similarityAdd
BLAST
Regioni878 – 89316Required for binding DMD and UTRN By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi774 – 7807Nuclear localization signal By similarity
Motifi887 – 8904PPXY motif By similarity

Compositional bias

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

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti448 – 4503TKK → SKE in CAA84293. 1 Publication
Sequence conflicti599 – 6002GD → PH in CAA84293. 1 Publication
Sequence conflicti643 – 6431I → V in CAA60031. 1 Publication
Sequence conflicti643 – 6431I → V in AAC52853. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 139 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

Similar proteinsi