Target intelligence / Profile preview

STT3 oligosaccharyltransferase complex catalytic subunit A (STT3A)

Target
STT3A
Molecular classification
Enzyme, Transferase, Multi-subunit membrane complex component
01

Overview

STT3 oligosaccharyltransferase complex catalytic subunit A (STT3A) is the **catalytic subunit** of the oligosaccharyltransferase (OST) complex, a multi-protein enzyme complex located in the **endoplasmic reticulum**. STT3A catalyzes the **transfer of preassembled glycans from a dolichol-pyrophosphate lipid carrier to asparagine residues** within the Asn-X-Ser/Thr consensus sequon of nascent polypeptides, performing **cotranslational N-glycosylation**—the initial and essential step of protein N-linked glycosylation in eukaryotes[1][2][5]. The STT3A-containing OST complex is functionally distinct from the STT3B-containing isoform: STT3A primarily mediates cotranslational glycosylation, while STT3B is required for efficient post-translational modification of glycosylation sites missed by STT3A[1][6]. Mutations in STT3A lead to human disease, specifically congenital disorders of glycosylation, characterized by defective N-linked protein glycosylation and a broad range of clinical symptoms[6]. STT3A complexes are evolutionarily conserved and are required for normal protein folding and quality control, as improper glycosylation can result in misfolded proteins and endoplasmic reticulum stress[1][3][6].

Other names
Dolichyl-diphosphooligosaccharide–protein glycosyltransferase subunit STT3AITM1TMCOligosaccharyltransferase subunit STT3AB5Integral membrane protein 1Transmembrane protein TMCMGC9042CDG1WADCDG1WAR
02

Biological functions

Protein N-glycosylationCotranslational modification of nascent polypeptidesAssociation with Sec61 protein translocation complexProtein folding and quality control in the endoplasmic reticulum
03

Disease associations

Congenital disorders of glycosylation (CDG type Iw, STT3A-CDG)Other disorders associated with protein hypoglycosylation
04

Safety considerations

Loss-of-function mutations can impair N-glycosylation, leading to congenital disorders and multisystem involvementGlycosylation defects can impact folding, trafficking, and function of multiple secretory and membrane proteins
05

Biomarkers

Glycosylation pattern biomarkers in STT3A-CDG and related glycosylation disorders

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