STT3A
entrez
3703
canonical
uniprot
P46977
canonical
ensembl
ENSG00000134910
resolver
ensp
ENSP00000376472
resolver
ensp
ENSP00000432820
resolver
ensp
ENSP00000436962
resolver
ensp
ENSP00000575749
resolver
ensp
ENSP00000606209
resolver
ensp
ENSP00000707917
resolver
genesymbol
STT3A
resolver
genesymbol_syn
ITM1
resolver
genesymbol_syn
TMC
resolver
hgnc
HGNC:6172
resolver
uniprot
B4DJ24
resolver
uniprot
E9PNQ1
resolver
uniprot
Q86XU9
resolver
uniprot
Q8TE35
resolver
uniprot
Q8WUB4
resolver
uniprot_entry
STT3A_HUMAN
resolver
uniprot_sec
B4DJ24
resolver
uniprot_sec
E9PNQ1
resolver
uniprot_sec
Q86XU9
resolver
uniprot_sec
Q8TE35
resolver
uniprot_sec
Q8WUB4
resolver
activity_regulation
ACTIVITY REGULATION: STT3A, but not STT3B, is specifically inhibited by the N-glycosylation inhibitor NGI-235, which prevents productive binding pose of the glycan donor in the active site of STT3A. {ECO:0000269|PubMed:38670073}.
uniprot
proteins
amino_acid_sequence
MTKFGFLRLSYEKQDTLLKLLILSMAAVLSFSTRLFAVLRFESVIHEFDPYFNYRTTRFLAEEGFYKFHNWFDDRAWYPLGRIIGGTIYPGLMITSAAIYHVLHFFHITIDIRNVCVFLAPLFSSFTTIVTYHLTKELKDAGAGLLAAAMIAVVPGYISRSVAGSYDNEGIAIFCMLLTYYMWIKAVKTGSICWAAKCALAYFYMVSSWGGYVFLINLIPLHVLVLMLTGRFSHRIYVAYCTVYCLGTILSMQISFVGFQPVLSSEHMAAFGVFGLCQIHAFVDYLRSKLNPQQFEVLFRSVISLVGFVLLTVGALLMLTGKISPWTGRFYSLLDPSYAKNNIPIIASVSEHQPTTWSSYYFDLQLLVFMFPVGLYYCFSNLSDARIFIIMYGVTSMYFSAVMVRLMLVLAPVMCILSGIGVSQVLSTYMKNLDISRPDKKSKKQQDSTYPIKNEVASGMILVMAFFLITYTFHSTWVTSEAYSSPSIVLSARGGDGSRIIFDDFREAYYWLRHNTPEDAKVMSWWDYGYQITAMANRTILVDNNTWNNTHISRVGQAMASTEEKAYEIMRELDVSYVLVIFGGLTGYSSDDINKFLWMVRIGGSTDTGKHIKENDYYTPTGEFRVDREGSPVLLNCLMYKMCYYRFGQVYTEAKRPPGFDRVRNAEIGNKDFELDVLEEAYTTEHWLVRIYKVKDLDNRGLSRT
uniprot
proteins
disease_involvement
DISEASE: Congenital disorder of glycosylation 1W, autosomal recessive (CDG1WAR) [MIM:615596]: A form of congenital disorder of glycosylation, a multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. {ECO:0000269|PubMed:23842455}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Congenital disorder of glycosylation 1W, autosomal dominant (CDG1WAD) [MIM:619714]: A form of congenital disorder of glycosylation, a multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. CDG1WAD patients show variable skeletal anomalies, short stature, macrocephaly, and dysmorphic features. Some have impaired intellectual development. Additional features include increased muscle tone and muscle cramps. {ECO:0000269|PubMed:34653363}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.4.99.18
uniprot
proteins
function
FUNCTION: Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:19167329, PubMed:31296534, PubMed:31831667, PubMed:34653363, PubMed:38670073, PubMed:39509507). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER) (PubMed:19167329, PubMed:31296534, PubMed:31831667, PubMed:34653363, PubMed:38670073, PubMed:39509507). All subunits are required for a maximal enzyme activity (PubMed:19167329, PubMed:31831667, PubMed:34653363). This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (PubMed:19167329). STT3A is present in the majority of OST complexes and mediates cotranslational N-glycosylation of most sites on target proteins, while STT3B-containing complexes are required for efficient post-translational glycosylation and mediate glycosylation of sites that have been skipped by STT3A (PubMed:19167329, PubMed:38670073, PubMed:39509507). STT3A-containing OST-A complex is also required to prevent hyperglycosylation of some target proteins by preventing glycosylation of facultative sites before folding of target proteins is completed (PubMed:39509507). {ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:31296534, ECO:0000269|PubMed:31831667, ECO:0000269|PubMed:34653363, ECO:0000269|PubMed:38670073, ECO:0000269|PubMed:39509507}.
uniprot
proteins
mass_dalton
80530
uniprot
proteins
mutagenesis
MUTAGEN 209; /note="W->F: In LLO mutant; abolished oligosaccharyl transferase activity due to defects in binding lipid-linked oligosaccharide; when associated with A-405 and A-530."; /evidence="ECO:0000269|PubMed:39509507"; MUTAGEN 256; /note="F->P: Confers resistance to inhibitor N-glycosylation inhibitor NGI-1."; /evidence="ECO:0000269|PubMed:38670073"; MUTAGEN 260; /note="Q->R: Confers resistance to inhibitor N-glycosylation inhibitor NGI-1."; /evidence="ECO:0000269|PubMed:38670073"; MUTAGEN 266; /note="E->K: Confers resistance to inhibitor N-glycosylation inhibitor NGI-1."; /evidence="ECO:0000269|PubMed:38670073"; MUTAGEN 331; /note="Y->H: Confers resistance to inhibitor N-glycosylation inhibitor NGI-1."; /evidence="ECO:0000269|PubMed:38670073"; MUTAGEN 405; /note="R->A: In LLO mutant; abolished oligosaccharyl transferase activity due to defects in binding lipid-linked oligosaccharide; when associated with F-209 and A-530."; /evidence="ECO:0000269|PubMed:39509507"; MUTAGEN 525..527; /note="WWD->AAA: Impaired ability to prevent hyperglycosylation of target proteins."; /evidence="ECO:0000269|PubMed:39509507"; MUTAGEN 530; /note="Y->A: In LLO mutant; abolished oligosaccharyl transferase activity due to defects in binding lipid-linked oligosaccharide; when associated with F-209 and A-405."; /evidence="ECO:0000269|PubMed:39509507
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:31831667, ECO:0000269|PubMed:38670073, ECO:0000269|PubMed:39509507}.
uniprot
proteins
protein_family
STT3 family
uniprot
proteins
pubmed
12887896
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19167329
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23606741
uniprot
proteins
pubmed
23842455
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25135935
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
31296534
uniprot
proteins
pubmed
31831667
uniprot
proteins
pubmed
34653363
uniprot
proteins
pubmed
36697828
uniprot
proteins
pubmed
38670073
uniprot
proteins
pubmed
39509507
uniprot
proteins
pubmed
8634329
uniprot
proteins
pubmed
8838310
uniprot
proteins
sequence_length
705
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:12887896}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P46978}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P46978}.
uniprot
proteins
transmembrane_region
TRANSMEM 18..38; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 120..138; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 141..158; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 170..189; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 192..206; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 212..228; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 234..259; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 268..287; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 301..321; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 357..379; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 386..402; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 407..428; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007"; TRANSMEM 454..473; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P39007
uniprot
proteins