Basic Information
Gene Structure
Domain
Regulation&
Interaction
Annotation
Orthologus Group
Pathway
Basic Information
Gene ID
EVM0025355
View in Genome Browser
Position
GWHASIS00000022:9641875-9651115 (+)
9240bp
Gene Type
gene
Gene Description (Protein Product)
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit
Organism
Acer catalpifolium
Also AS AT5G19690

Gene Structure

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Domain
Database EntryID E-Value Start end InterPro ID Description

Regulation&Interaction
Protein-protein interaction (PPI)
EVM0031785 Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser Thr consensus motif in nascent polypeptide chains
EVM0029708 Dol-P-Glc Glc(2)Man(9)GlcNAc(2)-PP-Dol
EVM0026268 dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit
Regulatory gene
EVM0001315 transcription factor that promotes early floral meristem identity in synergy with APETALA1; FRUITFULL and LEAFY. Is required subsequently for the transition of an inflorescence meristem into a floral meristem. Seems to be partially redundant to the function of APETALA1
EVM0003629 MADS-box protein
EVM0005245 MADS-box protein

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Annotation

Orthologous Group
Orthologous ID Species Number All hits in PereRegDB Hits of this species Orthologous Detail


Pathway
Go Pathway KEGG Pathway
GO Term Description GO Category
GO:0003674 molecular_function MF
GO:0003824 catalytic activity MF
GO:0004576 oligosaccharyl transferase activity MF
GO:0004579 dolichyl-diphosphooligosaccharide-protein glycotransferase activity MF
GO:0005575 cellular_component CC
GO:0005622 intracellular anatomical structure CC
GO:0005623 obsolete cell CC
GO:0005737 cytoplasm CC
GO:0005783 endoplasmic reticulum CC
GO:0005789 endoplasmic reticulum membrane CC
GO:0005886 plasma membrane CC
GO:0006464 protein modification process BP
GO:0006486 protein glycosylation BP
GO:0006487 protein N-linked glycosylation BP
GO:0006807 nitrogen compound metabolic process BP
GO:0006950 response to stress BP
GO:0006970 response to osmotic stress BP
GO:0008150 biological_process BP
GO:0008152 metabolic process BP
GO:0008250 oligosaccharyltransferase complex CC
GO:0009058 biosynthetic process BP
GO:0009059 macromolecule biosynthetic process BP
GO:0009100 glycoprotein metabolic process BP
GO:0009101 glycoprotein biosynthetic process BP
GO:0009628 response to abiotic stimulus BP
GO:0009651 response to salt stress BP
GO:0009987 cellular process BP
GO:0012505 endomembrane system CC
GO:0016020 membrane CC
GO:0016740 transferase activity MF
GO:0016757 glycosyltransferase activity MF
GO:0016758 hexosyltransferase activity MF
GO:0018193 peptidyl-amino acid modification BP
GO:0018196 obsolete peptidyl-asparagine modification BP
GO:0018279 protein N-linked glycosylation via asparagine BP
GO:0019538 protein metabolic process BP
GO:0031984 organelle subcompartment CC
GO:0032991 protein-containing complex CC
GO:0034645 cellular macromolecule biosynthetic process BP
GO:0036211 protein modification process BP
GO:0042175 nuclear outer membrane-endoplasmic reticulum membrane network CC
GO:0043170 macromolecule metabolic process BP
GO:0043226 organelle CC
GO:0043227 membrane-bounded organelle CC
GO:0043229 intracellular organelle CC
GO:0043231 intracellular membrane-bounded organelle CC
GO:0043412 macromolecule modification BP
GO:0043413 macromolecule glycosylation BP
GO:0043687 post-translational protein modification BP
GO:0044237 cellular metabolic process BP
GO:0044238 primary metabolic process BP
GO:0044249 cellular biosynthetic process BP
GO:0044260 cellular macromolecule metabolic process BP
GO:0044267 protein metabolic process BP
GO:0044422 obsolete organelle part CC
GO:0044424 obsolete intracellular part CC
GO:0044425 obsolete membrane part CC
GO:0044432 obsolete endoplasmic reticulum part CC
GO:0044444 obsolete cytoplasmic part CC
GO:0044446 obsolete intracellular organelle part CC
GO:0044464 obsolete cell part CC
GO:0047484 regulation of response to osmotic stress BP
GO:0048583 regulation of response to stimulus BP
GO:0050789 regulation of biological process BP
GO:0050896 response to stimulus BP
GO:0065007 biological regulation BP
GO:0070085 glycosylation BP
GO:0071704 organic substance metabolic process BP
GO:0071944 cell periphery CC
GO:0080134 regulation of response to stress BP
GO:0098796 membrane protein complex CC
GO:0098827 endoplasmic reticulum subcompartment CC
GO:1901135 carbohydrate derivative metabolic process BP
GO:1901137 carbohydrate derivative biosynthetic process BP
GO:1901564 organonitrogen compound metabolic process BP
GO:1901566 organonitrogen compound biosynthetic process BP
GO:1901576 organic substance biosynthetic process BP
GO:1902494 catalytic complex CC
GO:1990234 transferase complex CC
KEGG Term Name Description
map04141 Protein processing in endoplasmic reticulum The endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylated. Correctly folded proteins are packaged into transport vesicles that shuttle them to the Golgi complex. Misfolded proteins are retained within the ER lumen in complex with molecular chaperones. Proteins that are terminally misfolded bind to BiP and are directed toward degradation through the proteasome in a process called ER-associated degradation (ERAD). Accumulation of misfolded proteins in the ER causes ER stress and activates a signaling pathway called the unfolded protein response (UPR). In certain severe situations, however, the protective mechanisms activated by the UPR are not sufficient to restore normal ER function and cells die by apoptosis.
map01100 Metabolic pathways -
map00513 Various types of N-glycan biosynthesis -
map00510 N-Glycan biosynthesis N-glycans or asparagine-linked glycans are major constituents of glycoproteins in eukaryotes. N-glycans are covalently attached to asparagine with the consensus sequence of Asn-X-Ser/Thr by an N-glycosidic bond, GlcNAc b1- Asn. Biosynthesis of N-glycans begins on the cytoplasmic face of the ER membrane with the transferase reaction of UDP-GlcNAc and the lipid-like precursor P-Dol (dolichol phosphate) to generate GlcNAc a1- PP-Dol. After sequential addition of monosaccharides by ALG glycosyltransferases [MD:M00055], the N-glycan precursor is attached by the OST (oligosaccharyltransferase) complex to the polypeptide chain that is being synthesized and translocated through the ER membrane. The protein-bound N-glycan precursor is subsequently trimmed, extended, and modified in the ER and Golgi by a complex series of reactions catalyzed by membrane-bound glycosidases and glycosyltransferases. N-glycans thus synthesized are classified into three types: high-mannose type, complex type, and hybrid type. Defects in N-glycan biosynthesis lead to a variety of human diseases known as congenital disorders of glycosylation [DS:H00118 H00119].