Gene Ontology annotation through association of InterPro records with GO terms.
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt.
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara.
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods.
The roles of the dystrophin-associated glycoprotein complex at the synapse.
Next-generation sequencing to generate interactome datasets.
A proteome-scale map of the human interactome network.
Widespread macromolecular interaction perturbations in human genetic disorders.
Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing.
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Primary adhalinopathy: a common cause of autosomal recessive muscular dystrophy of variable severity.
Human adhalin is alternatively spliced and the gene is located on chromosome 17q21.
Missense mutations in the adhalin gene linked to autosomal recessive muscular dystrophy.
Characterization of the ATP-hydrolysing activity of alpha-sarcoglycan.
Ecto-ATPase activity of alpha-sarcoglycan (adhalin).
Falcon deep research on SGCA (Edison Scientific Literature)
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Alpha-sarcoglycan (α-SG) is one of four core transmembrane glycoproteins
(α, β, γ, δ) forming a tetrameric sarcoglycan complex embedded in the
dystrophin-associated glycoprotein complex (DGC) at the skeletal muscle
sarcolemma.
"α-SG is one of four core transmembrane glycoproteins (α, β, γ, δ) that
form a tetrameric sarcoglycan complex embedded in the DGC at the skeletal
muscle sarcolemma; the DGC links intracellular cytoskeleton (via dystrophin)
to the extracellular matrix and stabilizes the sarcolemma during contraction
"
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The dominant functional model is that α-SG is a structural/mechanoprotective
component of the DGC rather than a classic enzyme or transporter; it
strengthens the dystrophin–dystroglycan axis and protects the sarcolemma
from contraction-induced injury.
"The dominant functional model is that α-SG is a structural/mechanoprotective
component of the DGC: the sarcoglycan complex strengthens the
dystrophin–dystroglycan axis and helps protect the sarcolemma from
contraction-induced injury; it is also discussed as contributing to
mechanotransduction (“mechanosensor” role in disease tables)
"
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α-SG is a single-pass transmembrane protein with an extracellularly
oriented domain that matures through the ER→Golgi secretory pathway before
delivery to the sarcolemma.
"α-SG is described as a single-pass transmembrane protein with an
extracellularly oriented domain and is targeted to the plasma membrane
(sarcolemma) after maturation through the ER→Golgi secretory pathway
"
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Many pathogenic missense SGCA variants cause misfolding, ER retention, and
premature ERAD/proteasomal degradation, preventing sarcolemmal delivery and
causing secondary loss of other sarcoglycan complex members at the membrane.
"many pathogenic missense SGCA variants lead to misfolding, ER retention,
and premature degradation (e.g., via proteasome/ER-associated degradation),
preventing normal sarcolemmal delivery and causing secondary loss of other
sarcoglycan complex members at the membrane
"
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Some literature reports an extracellular ATP-binding domain and
Ca2+/Mg2+-dependent ecto-ATPase activity for α-SG, though this is a
specialized, less universally emphasized aspect relative to its structural
DGC role.
"Some literature additionally reports an extracellular ATP-binding domain
and Ca2+/Mg2+-dependent ecto-ATPase activity associated with α-SG; this
enzymatic-like activity is not the primary framing in most modern functional
summaries (which emphasize structural DGC roles), but it remains a recurring
observation in authoritative reviews/workshop material
"
SGCG,SGCZ and SGCA, SGCE bind SGCB:SGCD
DAG1(30-653), DAG1(654-895) and SSPN bind SGC
DGC complex binds laminins
SGC:DAG1:SSPN complex translocates to plasma membrane
Sarcoglycan complex (SGC) translocates to the Golgi membrane
Recruitment of dystrophin, dystrobrevin and syntrophin proteins to the DGC
DGC complex binds AGRN and HSPG2