ALG10_YARLI
ID ALG10_YARLI Reviewed; 522 AA.
AC Q6CEA5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase;
DE EC=2.4.1.256;
DE AltName: Full=Alpha-1,2-glucosyltransferase ALG10-A;
DE AltName: Full=Alpha-2-glucosyltransferase ALG10;
DE AltName: Full=Asparagine-linked glycosylation protein 10;
DE AltName: Full=Dolichyl-phosphoglucose-dependent glucosyltransferase ALG10;
GN Name=ALG10; OrderedLocusNames=YALI0B17226g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Adds the third glucose residue to the lipid-linked
CC oligosaccharide precursor for N-linked glycosylation. Transfers glucose
CC from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked
CC oligosaccharide Glc(2)Man(9)GlcNAc(2)-PP-Dol.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-
CC alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate
CC + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + H(+); Xref=Rhea:RHEA:29543, Rhea:RHEA-COMP:9517,
CC Rhea:RHEA-COMP:9528, Rhea:RHEA-COMP:12633, Rhea:RHEA-COMP:12634,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:132522, ChEBI:CHEBI:132523; EC=2.4.1.256;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the ALG10 glucosyltransferase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382128; CAG83260.1; -; Genomic_DNA.
DR RefSeq; XP_501007.1; XM_501007.1.
DR AlphaFoldDB; Q6CEA5; -.
DR STRING; 4952.CAG83260; -.
DR CAZy; GT59; Glycosyltransferase Family 59.
DR EnsemblFungi; CAG83260; CAG83260; YALI0_B17226g.
DR GeneID; 2906680; -.
DR KEGG; yli:YALI0B17226g; -.
DR VEuPathDB; FungiDB:YALI0_B17226g; -.
DR HOGENOM; CLU_017053_1_0_1; -.
DR InParanoid; Q6CEA5; -.
DR OMA; FNCGNLY; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0106073; F:dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR016900; Alg10.
DR PANTHER; PTHR12989; PTHR12989; 1.
DR Pfam; PF04922; DIE2_ALG10; 1.
DR PIRSF; PIRSF028810; Alpha1_2_glucosyltferase_Alg10; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..522
FT /note="Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-
FT glucosyltransferase"
FT /id="PRO_0000215462"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 522 AA; 59346 MW; EC20373245751B42 CRC64;
MLTVPPLIPR LLLALTPLAT IAAAFFYFSQ TNVLQPTPYI DEIFHIPQTQ QYCKGHWNAW
DSKITTPPGL YIIGYAWARM LTLTGLSESE ACSTLSLRAV NLMAVVIYIP ATLYIIQRRV
WGSQAHFSAF SLVSFPLIWF YAALYYTDVW STATVLMALA FALSPRVPFY MVQLSALMCA
VSLFFRQTNI LWAAVVAVIA IENSHYSNGA PPKNGALAQI FSTISYTFQI ELPIFNILIS
YASVAVGFSF FLYINGGIAL GDKDNHVAGN HIPQVFYCAL FITTLGFPVW FTWAHLKAYI
SSSFSVLGLT VRPLFIFVLI PRLLKSYAIE HPFLLADNRH YVFYLWRRLL KPAIYSISVE
DVMQSQDAID PKTLDVISIG LKYALSAAIY FSLWNIWTTL TNSIPAAILV RGRGFNRRNG
KSISPAIDLQ CLTWPILLAM VFATLASLIP SPLIEPRYYI LPYLFWRIYM TPTTAGKRVN
TDARFLREWI WYMLINAATV YMFLYKPFEW AHEPGVLQRF MW
