{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q14118","secondaryAccessions":["A8K6M7","Q969J9"],"uniProtkbId":"DAG1_HUMAN","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2009-05-05","entryVersion":225,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:2666"}],"value":"Dystroglycan 1"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8268918"}],"value":"Dystroglycan"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:2666"}],"value":"Dystrophin-associated glycoprotein 1"}}],"contains":[{"recommendedName":{"fullName":{"value":"Alpha-dystroglycan"},"shortNames":[{"value":"Alpha-DG"}]}},{"recommendedName":{"fullName":{"value":"Beta-dystroglycan"},"shortNames":[{"value":"Beta-DG"}]}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:2666"}],"value":"DAG1"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q62165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26290588"}],"value":"The dystroglycan complex is involved in a number of signaling events and processes including laminin deposition and extracellular matrix assembly, acetylcholine receptor clustering, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, epithelial polarization, and epithelium branching morphogenesis (By similarity). Required for the formation of photoreceptor ribbon synapses, and long-term maintenance of inhibitory synapses in cerebellar Purkinje cells (By similarity). 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 (PubMed:26290588)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O18738"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q28685"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q62165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26290588"}],"value":"Extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains. As a receptor for laminin is involved in extracellular matrix assembly, and activation of the PI3K/AKT pathway regulating cell apoptotic signals in muscle (By similarity). Binding of laminin LAMA1 to alpha-dystroglycan also initiates 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 (By similarity). Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells (By similarity). Also acts as a receptor for laminin LAMA5 (By similarity). 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. 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 (By similarity). In the retina, it is required for the formation of photoreceptor ribbon synapses through its interaction with pikachurin (EGFLAM) (By similarity). 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 (PubMed:26290588)"}],"commentType":"FUNCTION","molecule":"Alpha-dystroglycan"},{"texts":[{"value":"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"}],"commentType":"FUNCTION","molecule":"Beta-dystroglycan"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16254364"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17360738"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19324387"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9851927"}],"value":"(Microbial infection) Acts as a receptor for lassa virus and lymphocytic choriomeningitis virus glycoprotein and class C new-world arenaviruses (PubMed:16254364, PubMed:17360738, PubMed:19324387). Acts as a Schwann cell receptor for Mycobacterium leprae, the causative organism of leprosy, but only in the presence of the G-domain of LAMA2 (PubMed:9851927)"}],"commentType":"FUNCTION","molecule":"Alpha-dystroglycan"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q28685"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q62165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10767429"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10769203"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10988290"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11495720"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11724572"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12592373"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22205389"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26290588"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26848865"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27493216"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7592992"}],"value":"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 alpha-dystroglycan) with LARGE1; the interaction enhances laminin binding (By similarity). Interacts with SGCD. Interacts with AGR2 and AGR3. Interacts (beta-dystroglycan) with DMD; the interaction is inhibited by phosphorylation on the PPXY motif. Interacts (beta-dystroglycan, via its PPXY motif) with UTRN (via its WWW and ZZ domains); the interaction is inhibited by phosphorylation on the PPXY motif. Interacts (beta-dystroglycan, via its phosphorylated PPXY motif) with the SH2 domain-containing proteins, FYN, CSK, NCK and SHC. Interacts (beta-dystroglycan) with CAV3 (via a central WW-like domain); the interaction disrupts the binding of DMD. Beta-dystroglycan 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 (By similarity). Interacts with POMGNT1 (PubMed:27493216). Beta-dystroglycan interacts with CD93 (PubMed:26848865). Alpha-dystroglycan interacts with HSPG2; the interaction is required for acetylcholinesterase (AChE) localization at the neuromuscular junctions (NMJ) (By similarity). Alpha-dystroglycan interacts with AGRN; the interaction is required for up-regulation of SOX9 and cartilage formation (PubMed:22205389, PubMed:26290588). Alpha-dystroglycan interacts with pikachurin (EGFLAM); the interaction is required for photoreceptor ribbon synapse formation (By similarity)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16254364"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19324387"}],"value":"(Microbial infection) Interacts with lassa virus and lymphocytic choriomeningitis virus glycoprotein (PubMed:16254364, PubMed:19324387)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9851927"}],"value":"(Microbial infection) Interacts with surface molecules of mycobacterium leprae"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q14118","intActId":"EBI-1755945"},"interactantTwo":{"uniProtKBAccession":"P16333","geneName":"NCK1","intActId":"EBI-389883"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14118","intActId":"EBI-1755945"},"interactantTwo":{"uniProtKBAccession":"Q3T1J5","geneName":"Ank3","intActId":"EBI-2133962"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"chainId":"PRO_0000021065","intActId":"EBI-20738807"},"interactantTwo":{"uniProtKBAccession":"Q14118","geneName":"DAG1","chainId":"PRO_0000021066","intActId":"EBI-20738802"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"chainId":"PRO_0000021066","intActId":"EBI-20738802"},"interactantTwo":{"uniProtKBAccession":"P46939","geneName":"UTRN","intActId":"EBI-295856"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Alpha-dystroglycan","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q62165"}],"value":"Localized to inhibitory synapses in the cerebellar cortex"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9851927"}],"value":"Secreted, extracellular space","id":"SL-0112"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q62165"}],"value":"Secreted, extracellular space, extracellular matrix, basement membrane","id":"SL-0025"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q62165"}],"value":"Synapse","id":"SL-0258"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Beta-dystroglycan","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q62165"}],"value":"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 the presence of ANK2 (By similarity). 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"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18764929"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26848865"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"value":"Single-pass type I membrane protein","id":"SL-9905"}},{"location":{"value":"Cytoplasm, cytoskeleton","id":"SL-0090"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18764929"}],"value":"Nucleus, nucleoplasm","id":"SL-0190"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q62165"}],"value":"Cell membrane, sarcolemma","id":"SL-0238"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q62165"}],"value":"Synapse","id":"SL-0258"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q62165"}],"value":"Postsynaptic cell membrane","id":"SL-0219"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15175026"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8268918"}],"value":"Expressed in a variety of fetal and adult tissues. In epidermal tissue, located to the basement membrane. Also expressed in keratinocytes and fibroblasts"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"O18738"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12140558"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16254364"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17360738"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17905726"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19838169"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20044576"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20507882"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21987822"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23234360"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24256719"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27493216"}],"value":"O-glycosylated. 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 (PubMed:27493216). 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-317, Thr-319 and 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 (PubMed:20044576, PubMed:21987822, PubMed:23723439, PubMed:24256719). Glycosylation by LARGE1 is also required for perlecan binding (By similarity). The O-glycosyl hexose on Thr-367, Thr-369, Thr-372, Thr-381 and Thr-388 is probably mannose. 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)"}],"commentType":"PTM","molecule":"Alpha-dystroglycan"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16254364"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17360738"}],"value":"(Microbial infection) O-mannosylation is required for binding lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses"}],"commentType":"PTM","molecule":"Alpha-dystroglycan"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18764929"}],"value":"N-glycosylated"}],"commentType":"PTM","molecule":"Beta-dystroglycan"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15175026"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17905726"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18764929"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19946898"}],"value":"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"}],"commentType":"PTM"},{"texts":[{"value":"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"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Muscular dystrophy-dystroglycanopathy limb-girdle C9","diseaseAccession":"DI-03074","acronym":"MDDGC9","description":"An autosomal recessive muscular dystrophy showing onset in early childhood, and associated with intellectual disability without structural brain anomalies.","diseaseCrossReference":{"database":"MIM","id":"613818"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21388311"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25503980"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry. MDDGC7 is caused by DAG1 mutations that interfere with normal post-translational processing, resulting in defective DAG1 glycosylation and impaired interactions with extracellular-matrix components. Other muscular dystrophy-dystroglycanopathies are caused by defects in enzymes involved in protein O-glycosylation"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A9","diseaseAccession":"DI-04533","acronym":"MDDGA9","description":"An autosomal recessive disorder characterized by congenital muscular dystrophy associated with cobblestone lissencephaly and other brain anomalies, eye malformations, profound intellectual disability, and death usually in the first years of life. Included diseases are the more severe Walker-Warburg syndrome and the slightly less severe muscle-eye-brain disease.","diseaseCrossReference":{"database":"MIM","id":"616538"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24052401"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25934851"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"WEB RESOURCE","resourceName":"Wikipedia","resourceUrl":"https://en.wikipedia.org/wiki/Dystroglycan","ftp":false,"note":"Dystroglycan entry"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Chain","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":653,"modifier":"EXACT"}},"description":"Alpha-dystroglycan","featureId":"PRO_0000021065"},{"type":"Chain","location":{"start":{"value":654,"modifier":"EXACT"},"end":{"value":895,"modifier":"EXACT"}},"description":"Beta-dystroglycan","featureId":"PRO_0000021066"},{"type":"Topological domain","location":{"start":{"value":654,"modifier":"EXACT"},"end":{"value":749,"modifier":"EXACT"}},"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":750,"modifier":"EXACT"},"end":{"value":775,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Topological 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