ID   ALG8_YEAST              Reviewed;         577 AA.
AC   P40351; D6W2D0;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   04-NOV-2026, entry version 171.
DE   RecName: Full=Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase {ECO:0000305|PubMed:3536907};
DE            EC=2.4.1.265 {ECO:0000269|PubMed:3536907};
DE   AltName: Full=Asparagine-linked glycosylation protein 8;
DE   AltName: Full=Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl alpha-1,3-glucosyltransferase;
DE   AltName: Full=Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl glucosyltransferase;
GN   Name=ALG8; OrderedLocusNames=YOR067C; ORFNames=YOR29-18;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8016100; DOI=10.1073/pnas.91.13.5977;
RA   Stagjar I., Te Heesen S., Aebi M.;
RT   "New phenotype of mutations deficient in glucosylation of the lipid-linked
RT   oligosaccharide: cloning of the ALG8 locus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:5977-5981(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9133743;
RX   DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA   Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT   "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT   presence of two tRNAs and 24 new open reading frames.";
RL   Yeast 13:379-390(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874; DOI=10.1038/387s098;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RX   PubMed=3536907; DOI=10.1016/s0021-9258(18)66754-7;
RA   Runge K.W., Robbins P.W.;
RT   "A new yeast mutation in the glucosylation steps of the asparagine-linked
RT   glycosylation pathway. Formation of a novel asparagine-linked
RT   oligosaccharide containing two glucose residues.";
RL   J. Biol. Chem. 261:15582-15590(1986).
RN   [6]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC   -!- FUNCTION: Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-
CC       glucosyltransferase that operates in the biosynthetic pathway of
CC       dolichol-linked oligosaccharides, the glycan precursors employed in
CC       protein asparagine (N)-glycosylation. The assembly of dolichol-linked
CC       oligosaccharides begins on the cytosolic side of the endoplasmic
CC       reticulum membrane and finishes in its lumen. The sequential addition
CC       of sugars to dolichol pyrophosphate produces dolichol-linked
CC       oligosaccharides containing fourteen sugars, including two GlcNAcs,
CC       nine mannoses and three glucoses. Once assembled, the oligosaccharide
CC       is transferred from the lipid to nascent proteins by
CC       oligosaccharyltransferases. In the lumen of the endoplasmic reticulum,
CC       adds the second glucose residue from dolichyl phosphate glucose (Dol-P-
CC       Glc) onto the lipid-linked oligosaccharide intermediate
CC       Glc(1)Man(9)GlcNAc(2)-PP-Dol to produce Glc(2)Man(9)GlcNAc(2)-PP-Dol.
CC       Glc(2)Man(9)GlcNAc(2)-PP-Dol is a substrate for ALG10, the following
CC       enzyme in the biosynthetic pathway. {ECO:0000269|PubMed:3536907}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-
CC         alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC         Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC         beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-
CC         dolichol + a di-trans,poly-cis-dolichyl beta-D-glucosyl phosphate =
CC         an alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-
CC         Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC         [alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-
CC         Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-
CC         trans,poly-cis-dolichol + a di-trans,poly-cis-dolichyl phosphate +
CC         H(+); Xref=Rhea:RHEA:31307, Rhea:RHEA-COMP:19498, Rhea:RHEA-
CC         COMP:19502, Rhea:RHEA-COMP:19521, Rhea:RHEA-COMP:19522,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC         ChEBI:CHEBI:132521, ChEBI:CHEBI:132522; EC=2.4.1.265;
CC         Evidence={ECO:0000269|PubMed:3536907};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31308;
CC         Evidence={ECO:0000269|PubMed:3536907};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:3536907}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:3536907}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ALG6/ALG8 glucosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; X75929; CAA53533.1; -; Genomic_DNA.
DR   EMBL; Z74975; CAA99260.1; -; Genomic_DNA.
DR   EMBL; Z70678; CAA94552.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10846.1; -; Genomic_DNA.
DR   PIR; S47961; S47961.
DR   RefSeq; NP_014710.1; NM_001183486.1.
DR   AlphaFoldDB; P40351; -.
DR   SMR; P40351; -.
DR   BioGRID; 34466; 238.
DR   DIP; DIP-7542N; -.
DR   FunCoup; P40351; 919.
DR   STRING; 4932.YOR067C; -.
DR   CAZy; GT57; Glycosyltransferase Family 57.
DR   iPTMnet; P40351; -.
DR   PaxDb; 4932-YOR067C; -.
DR   PeptideAtlas; P40351; -.
DR   EnsemblFungi; YOR067C_mRNA; YOR067C; YOR067C.
DR   GeneID; 854233; -.
DR   KEGG; sce:YOR067C; -.
DR   AGR; SGD:S000005593; -.
DR   SGD; S000005593; ALG8.
DR   VEuPathDB; FungiDB:YOR067C; -.
DR   eggNOG; KOG2576; Eukaryota.
DR   HOGENOM; CLU_022045_1_1_1; -.
DR   InParanoid; P40351; -.
DR   OMA; AAEECYL; -.
DR   OrthoDB; 1689333at2759; -.
DR   BioCyc; MetaCyc:YOR067C-MONOMER; -.
DR   BioCyc; YEAST:YOR067C-MONOMER; -.
DR   BRENDA; 2.4.1.265; 984.
DR   Reactome; R-SCE-446193; Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 854233; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P40351; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P40351; protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0042283; F:dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IMP:SGD.
DR   GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IMP:UniProtKB.
DR   InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR   PANTHER; PTHR12413; DOLICHYL GLYCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR12413:SF2; DOLICHYL PYROPHOSPHATE GLC1MAN9GLCNAC2 ALPHA-1,3-GLUCOSYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF03155; Alg6_Alg8; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..577
FT                   /note="Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-
FT                   glucosyltransferase"
FT                   /id="PRO_0000174168"
FT   TOPO_DOM        1..42
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..92
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..139
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..168
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..219
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        241..266
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        288..307
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        329..382
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        383..403
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        404..419
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        420..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        441..447
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        448..468
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        469..470
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        471..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        492..504
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        505..525
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        526..543
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        544..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        565..577
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   577 AA;  67385 MW;  A59716F526B7B5A6 CRC64;
     MKGDRSRQNM AVTKKAKLKK NDEPKKVLKT AATEKGEGSK RYSLWNFWIS TLFLKLLLIP
     DYFSTDFDVH RNWLAITNKL PISEWYYEHT SQWTLDYPPF FAYFEWFLSQ FVPKSVRDDG
     CLDIVEIGKF GLPTIVFQRL TVIFSEILLF VILQIYINTT KLSERSQSFV VASSIVLSPG
     FLIIDHIHFQ YNGFLFAILI GSIVAAKNKR YILCAVLYTT AICFKHIFLY LAPCYFVFLL
     RAYVLNVNNF KFKSYKDFLF LIRWANLLKL ATVVVGIFTI CFLPFAHQMP QVLSRLFPFS
     RGLTHAYWAP NFWALYSFMD KILTTVMLKL PYVHTFATKF IKPPLIPQNI KEINERLAAN
     NNGSKGLVQD VFFVILPQIP PKLTFILTIF YQVLAVLPLL FDPSFKRFVG SLTLCGLASF
     LFGWHVHEKA IMLVIIPFTF LVGFDRRLLV PFMLVASAGY VSLYPLLYKG QDFFIKTLYT
     YVWCIIYFAA FRKTTKISSS VERRIFFLDR LALTYIFSLL PIVTVLQILD EVKWRYSFLQ
     KFEFLGLMIY SVYCSLGIIS SWFALSWLYN FDELLWQ
//