ALG8_YEAST
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 03-AUG-2022, entry version 156.
DE RecName: Full=Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase;
DE EC=2.4.1.265;
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;
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, AND CATALYTIC ACTIVITY.
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: Adds the second 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(1)Man(9)GlcNAc(2)-PP-Dol.
CC {ECO:0000269|PubMed:3536907}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-
CC Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-
CC Glc-(1->3)-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-diphosphodolichol + H(+);
CC Xref=Rhea:RHEA:31307, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9528,
CC Rhea:RHEA-COMP:12632, Rhea:RHEA-COMP:12633, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57525, ChEBI:CHEBI:57683, ChEBI:CHEBI:132521,
CC ChEBI:CHEBI:132522; EC=2.4.1.265;
CC Evidence={ECO:0000269|PubMed:3536907};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
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; 237.
DR DIP; DIP-7542N; -.
DR MINT; P40351; -.
DR STRING; 4932.YOR067C; -.
DR CAZy; GT57; Glycosyltransferase Family 57.
DR iPTMnet; P40351; -.
DR MaxQB; P40351; -.
DR PaxDb; P40351; -.
DR PRIDE; P40351; -.
DR EnsemblFungi; YOR067C_mRNA; YOR067C; YOR067C.
DR GeneID; 854233; -.
DR KEGG; sce:YOR067C; -.
DR SGD; S000005593; ALG8.
DR VEuPathDB; FungiDB:YOR067C; -.
DR eggNOG; KOG2576; Eukaryota.
DR GeneTree; ENSGT00940000153733; -.
DR HOGENOM; CLU_022045_1_1_1; -.
DR InParanoid; P40351; -.
DR OMA; WDTFVGA; -.
DR BioCyc; MetaCyc:YOR067C-MON; -.
DR BioCyc; YEAST:YOR067C-MON; -.
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 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; IMP:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042283; F:dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IMP:SGD.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IMP:SGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IGI:SGD.
DR InterPro; IPR039487; ALG8.
DR InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR PANTHER; PTHR12413; PTHR12413; 1.
DR PANTHER; PTHR12413:SF2; PTHR12413:SF2; 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
