Q3TDQ1

PR
Gene name
Stt3b
Protein name
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
Names
Oligosaccharyl transferase subunit STT3B, STT3-B, B6dom1 antigen, Source of immunodominant MHC-associated peptides
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:68292
EC number
2.4.99.18: Transferring other glycosyl groups
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-73 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q3TDQ1

Entry ID Method Resolution Chain Position Source
AF-Q3TDQ1-F1 Predicted AlphaFoldDB

1 variants for Q3TDQ1

Variant ID(s) Position Change Description Diseaes Association Provenance
776 E>D strain: A.BY, B10.H7 and C3H.SW; correlated with B6dom1-negative phenotype [UniProt] No

No associated diseases with Q3TDQ1

2 regional properties for Q3TDQ1

Type Name Position InterPro Accession
conserved_site Syntaxin/epimorphin, conserved site 228 - 268 IPR006012
domain SNARE-complex protein Syntaxin-18, N-terminal 4 - 95 IPR019529

Functions

Description
EC Number 2.4.99.18 Transferring other glycosyl groups
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
oligosaccharyltransferase complex A protein complex that is found in the endoplasmic reticulum membrane of eukaryotes and transfers lipid-linked oligosaccharide precursor to asparagine residues on nascent proteins. In yeast, the complex includes at least nine different subunits, whereas in mammalian cells at least three different forms of the complex have been detected.
oligosaccharyltransferase I complex An oligosaccharyltransferase (OST) complex that contains at least seven polypeptides and is the major OST complex in mammalian cells. Of the three forms of mammalian OST complex identified, the OSTI complex has the weakest affinity for ribosomes.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.

2 GO annotations of molecular function

Name Definition
dolichyl-diphosphooligosaccharide-protein glycotransferase activity Catalysis of the reaction: dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl diphosphate + a glycoprotein with the oligosaccharide chain attached by glycosylamine linkage to protein L-asparagine.
metal ion binding Binding to a metal ion.

7 GO annotations of biological process

Name Definition
co-translational protein modification The process of covalently altering one or more amino acids in a protein after translation has begun but before the protein has been released from the ribosome.
glycoprotein catabolic process The chemical reactions and pathways resulting in the breakdown of a glycoprotein, a protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide.
post-translational protein modification The process of covalently altering one or more amino acids in a protein after the protein has been completely translated and released from the ribosome.
protein N-linked glycosylation A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.
protein N-linked glycosylation via asparagine The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
response to unfolded protein Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an unfolded protein stimulus.
ubiquitin-dependent ERAD pathway The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.

9 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P39007 STT3 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q2KJI2 STT3A Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A Bos taurus (Bovine) PR
P46977 STT3A Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A Homo sapiens (Human) PR
Q8TCJ2 STT3B Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B Homo sapiens (Human) PR
P46978 Stt3a Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A Mus musculus (Mouse) PR
Q7XQ88 STT3B Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B Oryza sativa subsp japonica (Rice) PR
P46975 stt-3 Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt-3 Caenorhabditis elegans PR
Q93ZY3 STT3A Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A Arabidopsis thaliana (Mouse-ear cress) PR
Q9FX21 STT3B Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MAEPSAPESK HKSSLNSSPW SGLMALGNSR HGHHGPGTQS ASSAAAPKPG PPAGLSGGLS
70 80 90 100 110 120
QPAGWQSLLS FTILFLAWLA GFSSRLFAVI RFESIIHEFD PWFNYRSTHH LASHGFYEFL
130 140 150 160 170 180
NWFDERAWYP LGRIVGGTVY PGLMITAGLI HWILNTLNIT VHIRDVCVFL APTFSGLTSI
190 200 210 220 230 240
STFLLTRELW NQGAGLLAAC FIAIVPGYIS RSVAGSFDNE GIAIFALQFT YYLWVKSVKT
250 260 270 280 290 300
GSVFWTMCCC LSYFYMVSAW GGYVFIINLI PLHVFVLLLM QRYSKRVYIA YSTFYIVGLI
310 320 330 340 350 360
LSMQIPFVGF QPIRTSEHMA AAGVFALLQA YAFLQYLRDR LTKQEFQTLF FLGVSLAAGA
370 380 390 400 410 420
VFLSVIYLTY TGYIAPWSGR FYSLWDTGYA KIHIPIIASV SEHQPTTWVS FFFDLHILVC
430 440 450 460 470 480
TFPAGLWFCI KNINDERVFV ALYAISAVYF AGVMVRLMLT LTPVVCMLSA IAFSNVFEHY
490 500 510 520 530 540
LGDDMKRENP PVEDSSDEDD KRNPGNLYDK AGKVRKHVTE QEKPEEGLGP NIKSIVTMLM
550 560 570 580 590 600
LMLLMMFAVH CTWVTSNAYS SPSVVLASYN HDGTRNILDD FREAYFWLRQ NTDEHARVMS
610 620 630 640 650 660
WWDYGYQIAG MANRTTLVDN NTWNNSHIAL VGKAMSSNET AAYKIMRSLD VDYVLVIFGG
670 680 690 700 710 720
VIGYSGDDIN KFLWMVRIAE GEHPKDIREG DYFTQQGEFR VDKAGSPTLL NCLMYKMSYY
730 740 750 760 770 780
RFGEMQLDFR TPPGFDRTRN AEIGNKDIKF KHLEEAFTSE HWLVRIYKVK APDNRETLGH
790 800 810 820
KPRVTNIVPK QKYLSKKTTK RKRGYVKNKL VFKKGKKTSK KTV