Q75AQ8

PR
Gene name
ALG10 (ADL138C)
Protein name
Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase
Names
Alpha-1,2-glucosyltransferase ALG10-A, Alpha-2-glucosyltransferase ALG10, Asparagine-linked glycosylation protein 10, Dolichyl-phosphoglucose-dependent glucosyltransferase ALG10
Species
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii)
KEGG Pathway
ago:AGOS_ADL138C
EC number
2.4.1.256: Hexosyltransferases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-48 (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 Q75AQ8

Entry ID Method Resolution Chain Position Source
AF-Q75AQ8-F1 Predicted AlphaFoldDB

No variants for Q75AQ8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q75AQ8

No associated diseases with Q75AQ8

2 regional properties for Q75AQ8

Type Name Position InterPro Accession
conserved_site Ammonium transporter, conserved site 191 - 216 IPR018047
domain Ammonium transporter AmtB-like domain 37 - 459 IPR024041

Functions

Description
EC Number 2.4.1.256 Hexosyltransferases
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 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.

1 GO annotations of molecular function

Name Definition
dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity Catalysis of the addition of the third glucose residue to the lipid-linked oligosaccharide precursor for N-linked glycosylation; the transfer of glucose from dolichyl phosphate glucose (Dol-P-Glc) on to the lipid-linked oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.

2 GO annotations of biological process

Name Definition
dolichol-linked oligosaccharide biosynthetic process The chemical reactions and pathways resulting in the formation of dolichol-linked oligosaccharide, usually by a stepwise addition of glycosyl chains to endoplasmic reticulum membrane-bound dolichol-P.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGGEATASEK ELQEREDQLS QQIQDEIVMG CVVNLALWPV LLGAAAYVAY KYNCSWVPYP
70 80 90 100 110 120
FIDEKFHVGQ TVRYLAGRWR EWDSKITTPP GLYVIGWAVQ RTVGLLVGWN TLSLLRLSNV
130 140 150 160 170 180
IGGLVVWPWF VLRPLYFFNA LAFWPATLSV FPLLTSYYFL YYTDVWSTIL IVGSLTLAVT
190 200 210 220 230 240
VPFGERASIW ASAICGLLSC LFRQTNIVWN AFVLVVVLER RTMIHKGFNS LRINNYLKLI
250 260 270 280 290 300
IHGIENWNSL VLPYAVNFAL FLIFLLYNGS VTLGDKSSHV AGFHLVQMFY CLLFITFFSV
310 320 330 340 350 360
PVWFCRSFLL NYVSRTVVYP IWTIFEILGI MMIIRFFTVV HPYLLADNRH IAFYLFKKLI
370 380 390 400 410 420
GRNRFLKYFV MAPIYHFSTF VYLEAVRPTV FFFHPILPIE VKSPVDLPLQ FTHISWSALI
430 440 450 460 470 480
ICTLLTVVPS PLFEPRYYIL PYIFWRIFLL VSPEPFFAVP TEMTYRFGNT RRLAVEFLWF
490 500
ILINAITIVI FATNAFAWET EASLQRIIW