ALG6_YEAST
ID ALG6_YEAST Reviewed; 544 AA.
AC Q12001; D6W268; E9P8Y7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase;
DE EC=2.4.1.267 {ECO:0000269|PubMed:8877369};
DE AltName: Full=Asparagine-linked glycosylation protein 6;
DE AltName: Full=Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol alpha-1,3-glucosyltransferase;
DE AltName: Full=Dolichyl-P-Glc:Man9GlcNAc2-PP-dolichyl glucosyltransferase;
GN Name=ALG6; OrderedLocusNames=YOR002W; ORFNames=UNA544;
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=8896276;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1091::aid-yea22>3.0.co;2-i;
RA Sterky F., Holmberg A., Pettersson B., Uhlen M.;
RT "The sequence of a 30 kb fragment on the left arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 15 open reading frames, five of which
RT correspond to previously identified genes.";
RL Yeast 12:1091-1095(1996).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND CHARACTERIZATION.
RX PubMed=8877369; DOI=10.1093/glycob/6.5.493;
RA Reiss G., te Heesen S., Zimmerman J., Robbins P.W., Aebi M.;
RT "Isolation of the ALG6 locus of Saccharomyces cerevisiae required for
RT glucosylation in the N-linked glycosylation pathway.";
RL Glycobiology 6:493-498(1996).
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 first 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 Man(9)GlcNAc(2)-PP-Dol. {ECO:0000269|PubMed:8877369}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-glucosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->3)-alpha-
CC D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-
CC alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + H(+); Xref=Rhea:RHEA:30635, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9528, Rhea:RHEA-COMP:12631, Rhea:RHEA-
CC COMP:12632, ChEBI:CHEBI:15378, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:132520, ChEBI:CHEBI:132521; EC=2.4.1.267;
CC Evidence={ECO:0000269|PubMed:8877369};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:8877369}.
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; U43491; AAC49481.1; -; Genomic_DNA.
DR EMBL; Z74910; CAA99190.1; -; Genomic_DNA.
DR EMBL; AY692895; AAT92914.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10784.1; -; Genomic_DNA.
DR PIR; S61985; S61985.
DR RefSeq; NP_014644.1; NM_001183421.1.
DR PDB; 6SNH; EM; 3.90 A; X=1-544.
DR PDB; 6SNI; EM; 3.00 A; X=1-544.
DR PDBsum; 6SNH; -.
DR PDBsum; 6SNI; -.
DR AlphaFoldDB; Q12001; -.
DR SMR; Q12001; -.
DR BioGRID; 34405; 342.
DR STRING; 4932.YOR002W; -.
DR CAZy; GT57; Glycosyltransferase Family 57.
DR iPTMnet; Q12001; -.
DR PaxDb; Q12001; -.
DR PRIDE; Q12001; -.
DR ABCD; Q12001; 1 sequenced antibody.
DR EnsemblFungi; YOR002W_mRNA; YOR002W; YOR002W.
DR GeneID; 854163; -.
DR KEGG; sce:YOR002W; -.
DR SGD; S000005528; ALG6.
DR VEuPathDB; FungiDB:YOR002W; -.
DR eggNOG; KOG2575; Eukaryota.
DR GeneTree; ENSGT00940000153733; -.
DR HOGENOM; CLU_008110_2_1_1; -.
DR InParanoid; Q12001; -.
DR OMA; RQWYFNT; -.
DR BioCyc; MetaCyc:YOR002W-MON; -.
DR BioCyc; YEAST:YOR002W-MON; -.
DR BRENDA; 2.4.1.267; 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:Q12001; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12001; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IMP:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042281; F:dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase activity; IMP:SGD.
DR GO; GO:0016758; F:hexosyltransferase activity; IMP:SGD.
DR GO; GO:0009060; P:aerobic respiration; IMP:SGD.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IMP:SGD.
DR GO; GO:0006486; P:protein glycosylation; IMP:SGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR039488; ALG6.
DR InterPro; IPR004856; Glyco_trans_ALG6/ALG8.
DR PANTHER; PTHR12413; PTHR12413; 1.
DR PANTHER; PTHR12413:SF1; PTHR12413:SF1; 1.
DR Pfam; PF03155; Alg6_Alg8; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..544
FT /note="Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-
FT glucosyltransferase"
FT /id="PRO_0000174161"
FT TOPO_DOM 1..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 57..104
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..171
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..263
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..332
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 354..356
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..425
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..481
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..508
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..544
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CONFLICT 203
FT /note="M -> V (in Ref. 4; AAT92914)"
FT /evidence="ECO:0000305"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:6SNI"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 69..80
FT /evidence="ECO:0007829|PDB:6SNI"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:6SNI"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 102..118
FT /evidence="ECO:0007829|PDB:6SNI"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:6SNI"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:6SNI"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 141..153
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 173..184
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:6SNI"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 200..216
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 219..230
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 259..281
FT /evidence="ECO:0007829|PDB:6SNI"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 287..297
FT /evidence="ECO:0007829|PDB:6SNI"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:6SNI"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:6SNI"
FT TURN 317..319
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 328..351
FT /evidence="ECO:0007829|PDB:6SNI"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 359..373
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 383..391
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 399..413
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 416..420
FT /evidence="ECO:0007829|PDB:6SNI"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 425..439
FT /evidence="ECO:0007829|PDB:6SNI"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 477..490
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:6SNI"
FT TURN 497..499
FT /evidence="ECO:0007829|PDB:6SNI"
FT STRAND 504..509
FT /evidence="ECO:0007829|PDB:6SNI"
FT HELIX 510..535
FT /evidence="ECO:0007829|PDB:6SNI"
SQ SEQUENCE 544 AA; 62783 MW; 64BFA11A1F6D02B7 CRC64;
MAIGKRLLVN KPAEESFYAS PMYDFLYPFR PVGNQWLPEY IIFVCAVILR CTIGLGPYSG
KGSPPLYGDF EAQRHWMEIT QHLPLSKWYW YDLQYWGLDY PPLTAFHSYL LGLIGSFFNP
SWFALEKSRG FESPDNGLKT YMRSTVIISD ILFYFPAVIY FTKWLGRYRN QSPIGQSIAA
SAILFQPSLM LIDHGHFQYN SVMLGLTAYA INNLLDEYYA MAAVCFVLSI CFKQMALYYA
PIFFAYLLSR SLLFPKFNIA RLTVIAFATL ATFAIIFAPL YFLGGGLKNI HQCIHRIFPF
ARGIFEDKVA NFWCVTNVFV KYKERFTIQQ LQLYSLIATV IGFLPAMIMT LLHPKKHLLP
YVLIACSMSF FLFSFQVHEK TILIPLLPIT LLYSSTDWNV LSLVSWINNV ALFTLWPLLK
KDGLHLQYAV SFLLSNWLIG NFSFITPRFL PKSLTPGPSI SSINSDYRRR SLLPYNVVWK
SFIIGTYIAM GFYHFLDQFV APPSKYPDLW VLLNCAVGFI CFSIFWLWSY YKIFTSGSKS
MKDL
