Alg8
entrez
381903
canonical
uniprot
Q6P8H8
canonical
ensembl
ENSMUSG00000035704
resolver
ensp
ENSMUSP00000095901
resolver
enst
ENSMUST00000098300
resolver
genesymbol
Alg8
resolver
genesymbol_syn
Gm1089
resolver
uniprot
E9Q3H5
resolver
uniprot
Q3TKP5
resolver
uniprot_entry
ALG8_MOUSE
resolver
uniprot_sec
E9Q3H5
resolver
uniprot_sec
Q3TKP5
resolver
amino_acid_sequence
MAASGSATAGGHWFSALALGVTLLKCLLIPTYHSTDFEVHRNWLAITHSLPISQWYYEATSEWTLDYPPFFAWFEYALSHIAKYFDQEMLNIHNLNYYSSRTLLFQRFSVILTDALFVYAVHECCKCIDGKRTGKDLTEKPKFILSVLLLWNFGLLIVDHIHFQYNGFLSGLLLLSIARLFQKRHIEGALLFAVLLHLKHIYLYVAPAYGVYLLRSYCFTASKPDGSVRWSSFSVVRVTSLGLIVFLVSALSLGPFLALNQLPQVFSRLFPFKRGLCHAYWAPNFWALYNALDKVLSVIGLKLKLLDPSQIPRASMTSGLVQQFQHTVLPSVSPLATLICTLIAILPSVFCLWFKPQGPRGFLRCLVLCALSSFMFGWHVHEKAILLAILPMSLLSVEKAGDATVFLILATTGHYSLFPLLFTAPELPIKILLMLLFTVYSISSLKTLFRKEKPLFNWMETVYLLGLGPLEVCCEFLLPFTSWKLKYPFIPLLLTSVYCAVGITYAWTRLYASVLTGSLVSKTKKH
uniprot
proteins
ec_number
2.4.1.265
uniprot
proteins
function
FUNCTION: Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the second glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc(1)Man(9)GlcNAc(2)-PP-Dol to produce Glc(2)Man(9)GlcNAc(2)-PP-Dol. Glc(2)Man(9)GlcNAc(2)-PP-Dol is a substrate for ALG10, the following enzyme in the biosynthetic pathway (By similarity). Required for PKD1/Polycystin-1 maturation and localization to the plasma membrane of the primary cilia (PubMed:28375157). {ECO:0000250|UniProtKB:Q9BVK2, ECO:0000269|PubMed:28375157}.
uniprot
proteins
mass_dalton
59535
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:Q9BVK2}.
uniprot
proteins
protein_family
ALG6/ALG8 glucosyltransferase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
28375157
uniprot
proteins
sequence_length
526
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BVK2}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 9..29; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 108..128; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 143..163; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 188..208; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 238..258; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 334..354; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 361..380; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 400..422; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 427..449; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 461..481; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 487..507; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins