Dag1
entrez
13138
canonical
uniprot
Q62165
canonical
ensembl
ENSMUSG00000039952
resolver
ensp
ENSMUSP00000079294
resolver
ensp
ENSMUSP00000128531
resolver
ensp
ENSMUSP00000130626
resolver
ensp
ENSMUSP00000142109
resolver
ensp
ENSMUSP00000197098
resolver
ensp
ENSMUSP00000197102
resolver
ensp
ENSMUSP00000197104
resolver
ensp
ENSMUSP00000197105
resolver
ensp
ENSMUSP00000197108
resolver
enst
ENSMUST00000080435
resolver
enst
ENSMUST00000166905
resolver
enst
ENSMUST00000171412
resolver
enst
ENSMUST00000191899
resolver
genesymbol
Dag1
resolver
uniprot
Q544G5
resolver
uniprot
Q61094
resolver
uniprot
Q61141
resolver
uniprot
Q61497
resolver
uniprot
Q8BPJ7
resolver
uniprot
Q8CBE6
resolver
uniprot_entry
DAG1_MOUSE
resolver
uniprot_entry
Q544G5_MOUSE
resolver
uniprot_entry
Q8BPJ7_MOUSE
resolver
uniprot_entry
Q8CBE6_MOUSE
resolver
uniprot_sec
Q61094
resolver
uniprot_sec
Q61141
resolver
uniprot_sec
Q61497
resolver
amino_acid_sequence
MSVDNWLLHPLWGQTFLLLLSVAVAQAHWPSEPSEAVRDWKNQLEASMHSVLSDFQEAVPTVVGIPDGTAVVGRSFRVSIPTDLIASSGEIIKVSAAGKEALPSWLHWDPHSHILEGLPLDTDKGVHYISVSAARLGANGSHVPQTSSVFSIEVYPEDHNEPQSVRAASSDPGEVVPSACAADEPVTVLTVILDADLTKMTPKQRIDLLNRMQSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIRGVETPAREGAMSAQLGYPVVGWHIANKKPTLPKRLRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIQPTRVSEAGTTVPGQIRPTLTIPGYVEPTAVITPPTTTTKKPRVSTPKPATPSTDSSTTTTRRPTKKPRTPRPVPRVTTKAPITRLETASPPTRIRTTTSGVPRGGEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDNEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHKRPQGDKAPARFKARLAGDPAPVVNDIHKKIALVKKLAFAFGDRNCSSITLQNITRGSIVVEWTNNTLPLEPCPKEQIIGLSRRIADENGKPRPAFSNALEPDFKALSIAVTGSGSCRHLQFIPVAPPSPGSSAAPATEVPDRDPEKSSEDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSMPETTPLNQDTVGEYTPLRDEDPNAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP
uniprot
proteins
function
FUNCTION: The dystroglycan complex is involved in a number of signaling events and processes including laminin deposition and extracellular matrix assembly, acetylcholine receptor (AChR) clustering, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, epithelial polarization, and epithelium branching morphogenesis. Required for the formation of photoreceptor ribbon synapses, and long-term maintenance of inhibitory synapses in cerebellar Purkinje cells (PubMed:18641643, PubMed:40473926). Also involved in the positive regulation of cartilage formation through agrin (AGRN) binding and up-regulation of SOX9, a transcription factor that plays a key role in chondrocytes differentiation (By similarity). {ECO:0000250|UniProtKB:Q14118, ECO:0000269|PubMed:10366602, ECO:0000269|PubMed:11798066, ECO:0000269|PubMed:12402286, ECO:0000269|PubMed:12797959, ECO:0000269|PubMed:12843252, ECO:0000269|PubMed:16098969, ECO:0000269|PubMed:16531403, ECO:0000269|PubMed:18641643, ECO:0000269|PubMed:40473926, ECO:0000269|PubMed:9175728, ECO:0000269|PubMed:9454835}.; FUNCTION: [Alpha-dystroglycan]: Extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains, and for certain adenoviruses. As a receptor for laminin is involved in extracellular matrix assembly, and activation of the PI3K/AKT pathway regulating cell apoptotic signals in muscle (PubMed:10366602, PubMed:12402286). Binding of laminin LAMA1 to alpha-dystroglycan also activates RAC1 signaling (PubMed:16475793). This process involves a signaling cascade in which Src kinases, c-Src or c-Fyn, phosphorylate syntrophin modifying its interaction with the adapter protein GRB2; this triggers recruitment of guanyl-nucleotide exchange factor SOS1 and activation of RAC1, finally resulting in c-Jun phosphorylation by MAPK8/JNK1 (By similarity). As a receptor for laminin LAMA1 is also involved in epithelium branching morphogenesis in salivary glang and lung (PubMed:11798066). Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells (By similarity). Also acts as a receptor for laminin LAMA5 (By similarity) (PubMed:10366602, PubMed:11798066, PubMed:12402286). In muscle cells, it is a receptor for laminin-1 (also known as laminin-111 or EHS laminin) and is involved in the stimulation of agrin-induced acetylcholine receptor (AChR) clustering, and formation of the synaptic basement membrane (PubMed:16531403, PubMed:9454835, PubMed:11157973). It is required for acetylcholinesterase (AChE) localization at the neuromuscular junctions (NMJ) through its binding with perlecan (HSPG2) and is, therefore, involved in the down-regulation of colinergic synaptic transmission (PubMed:11157973). In the retina, it is required for the formation of photoreceptor ribbon synapses through its interaction with pikachurin (EGFLAM) (PubMed:18641643). Also involved in the positive regulation of cartilage formation through agrin (AGRN) binding and up-regulation of SOX9, a transcription factor that plays a key role in chondrocytes differentiation (By similarity). {ECO:0000250|UniProtKB:O18738, ECO:0000250|UniProtKB:Q14118, ECO:0000250|UniProtKB:Q28685, ECO:0000269|PubMed:10366602, ECO:0000269|PubMed:11157973, ECO:0000269|PubMed:11798066, ECO:0000269|PubMed:12402286, ECO:0000269|PubMed:16531403, ECO:0000269|PubMed:18641643, ECO:0000269|PubMed:9454835}.; FUNCTION: [Beta-dystroglycan]: 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). {ECO:0000250, ECO:0000269|PubMed:12797959, ECO:0000269|PubMed:12843252, ECO:0000269|PubMed:9175728}.
uniprot
proteins
mass_dalton
96905
uniprot
proteins
mutagenesis
MUTAGEN 796..798; /note="IIF->AAA: Complete loss of ANK3-binding."; /evidence="ECO:0000269|PubMed:19109891"; MUTAGEN 800..801; /note="DE->AA: Complete loss of ANK3-binding."; /evidence="ECO:0000269|PubMed:19109891"; MUTAGEN 803..804; /note="DD->AA: Major reduction in ANK3-binding."; /evidence="ECO:0000269|PubMed:19109891
uniprot
proteins
post_translational_modification
PTM: [Alpha-dystroglycan]: O-glycosylated (PubMed:20044576). 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. 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 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 and is required for laminin binding. Glycosylation by LARGE1 is also required for perlecan (HSPG2) binding (PubMed:16098969). O-glycosylated in the N-terminal region with a core 1 or possibly core 8 glycan. The brain form displays a unique glycosylation pattern which is absent in other tissues; this form shows enhanced binding to laminin LAMA5 compared to the skeletal muscle form (By similarity). {ECO:0000250|UniProtKB:O18738, ECO:0000250|UniProtKB:Q14118, ECO:0000269|PubMed:16098969, ECO:0000269|PubMed:20044576}.; PTM: [Beta-dystroglycan]: N-glycosylated. {ECO:0000250|UniProtKB:Q14118}.; PTM: Autolytic cleavage produces the alpha and beta subunits. In cutaneous cells, as well as in certain pathological conditions, shedding of beta-dystroglycan can occur releasing a peptide of about 30 kDa (By similarity). {ECO:0000250}.; PTM: 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). {ECO:0000250}.
uniprot
proteins
pubmed
10022829
uniprot
proteins
pubmed
10366602
uniprot
proteins
pubmed
11157973
uniprot
proteins
pubmed
11430802
uniprot
proteins
pubmed
11495720
uniprot
proteins
pubmed
11798066
uniprot
proteins
pubmed
12402286
uniprot
proteins
pubmed
12670716
uniprot
proteins
pubmed
12797959
uniprot
proteins
pubmed
12843252
uniprot
proteins
pubmed
15326183
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16098969
uniprot
proteins
pubmed
16475793
uniprot
proteins
pubmed
16531403
uniprot
proteins
pubmed
16709410
uniprot
proteins
pubmed
18641643
uniprot
proteins
pubmed
19109891
uniprot
proteins
pubmed
20044576
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
25757569
uniprot
proteins
pubmed
40473926
uniprot
proteins
pubmed
7833916
uniprot
proteins
pubmed
8872465
uniprot
proteins
pubmed
9057818
uniprot
proteins
pubmed
9175728
uniprot
proteins
pubmed
9454835
uniprot
proteins
pubmed
9864373
uniprot
proteins
pubmed
9917844
uniprot
proteins
sequence_length
893
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Alpha-dystroglycan]: Secreted, extracellular space {ECO:0000250|UniProtKB:Q14118}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:11798066}. Synapse {ECO:0000269|PubMed:40473926}. Note=Localized to inhibitory synapses in the cerebellar cortex. {ECO:0000269|PubMed:40473926}.; SUBCELLULAR LOCATION: [Beta-dystroglycan]: Cell membrane {ECO:0000250|UniProtKB:Q14118}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q14118}. Cytoplasm, cytoskeleton. Nucleus, nucleoplasm. Cell membrane, sarcolemma. Synapse {ECO:0000269|PubMed:40473926}. Postsynaptic 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. Localized to inhibitory synapses in the cerebellar cortex (PubMed:40473926). {ECO:0000269|PubMed:40473926}.
uniprot
proteins
transmembrane_region
TRANSMEM 752..772; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins