ALG10_YEAST
ID ALG10_YEAST Reviewed; 525 AA.
AC P50076; D6VV08;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 155.
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=DIE2; Synonyms=ALG10; OrderedLocusNames=YGR227W; ORFNames=G8547;
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=7565092; DOI=10.1111/j.1365-2958.1995.tb02302.x;
RA Nikawa J., Hosaka K.;
RT "Isolation and characterization of genes that promote the expression of
RT inositol transporter gene ITR1 in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 16:301-308(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8701610;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<385::aid-yea910>3.0.co;2-g;
RA van der Aart Q.J.M., Kleine K., Steensma H.Y.;
RT "Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1
RT region from the right arm of Saccharomyces cerevisiae chromosome VII.";
RL Yeast 12:385-390(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 266.
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, AND SUBCELLULAR LOCATION.
RX PubMed=9597543; DOI=10.1093/glycob/8.5.455;
RA Burda P., Aebi M.;
RT "The ALG10 locus of Saccharomyces cerevisiae encodes the alpha-1,2
RT glucosyltransferase of the endoplasmic reticulum: the terminal glucose of
RT the lipid-linked oligosaccharide is required for efficient N-linked
RT glycosylation.";
RL Glycobiology 8:455-462(1998).
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 {ECO:0000269|PubMed:9597543}.
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 Evidence={ECO:0000269|PubMed:9597543};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:9597543}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9597543}.
CC -!- SIMILARITY: Belongs to the ALG10 glucosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; D38049; BAA07239.1; -; Genomic_DNA.
DR EMBL; X87941; CAA61176.1; -; Genomic_DNA.
DR EMBL; Z73012; CAA97255.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08319.2; -; Genomic_DNA.
DR PIR; S57691; S57691.
DR RefSeq; NP_011743.2; NM_001181356.2.
DR AlphaFoldDB; P50076; -.
DR BioGRID; 33480; 143.
DR IntAct; P50076; 6.
DR MINT; P50076; -.
DR STRING; 4932.YGR227W; -.
DR CAZy; GT59; Glycosyltransferase Family 59.
DR TCDB; 9.B.231.1.1; the die2/alg10 glycosyl transferase (die2/alg10) family.
DR PaxDb; P50076; -.
DR PRIDE; P50076; -.
DR EnsemblFungi; YGR227W_mRNA; YGR227W; YGR227W.
DR GeneID; 853142; -.
DR KEGG; sce:YGR227W; -.
DR SGD; S000003459; DIE2.
DR VEuPathDB; FungiDB:YGR227W; -.
DR eggNOG; KOG2642; Eukaryota.
DR GeneTree; ENSGT00390000012906; -.
DR HOGENOM; CLU_017053_1_0_1; -.
DR InParanoid; P50076; -.
DR OMA; FNCGNLY; -.
DR BioCyc; MetaCyc:YGR227W-MON; -.
DR BioCyc; YEAST:YGR227W-MON; -.
DR BRENDA; 2.4.1.256; 984.
DR UniPathway; UPA00378; -.
DR PRO; PR:P50076; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P50076; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
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:0106073; F:dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity; IDA:SGD.
DR GO; GO:0004583; F:dolichyl-phosphate-glucose-glycolipid alpha-glucosyltransferase activity; TAS:Reactome.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; TAS:SGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:SGD.
DR InterPro; IPR016900; Alg10.
DR PANTHER; PTHR12989; PTHR12989; 1.
DR Pfam; PF04922; DIE2_ALG10; 1.
DR PIRSF; PIRSF028810; Alpha1_2_glucosyltferase_Alg10; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..525
FT /note="Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-
FT glucosyltransferase"
FT /id="PRO_0000215463"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 266
FT /note="I -> K (in Ref. 2; CAA61176 and 3; CAA97255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 61793 MW; CCA51CE249A4AB6E CRC64;
MDAKKNTGEA NNDVLEEEAA IQLIAPGIAR NLTQEVITGI FCNVVIYPLL LIYFVLTFRY
MTTNIVPYEF IDEKFHVGQT LTYLKGKWTQ WDPKITTPPG IYILGLINYY CIKPIFKSWS
TLTILRLVNL LGGIIVFPIL VLRPIFLFNA LGFWPVSLMS FPLMTTYYYL FYTDVWSTIL
ILQSLSCVLT LPFGPVKSIW LSAFFAGVSC LFRQTNIIWT GFIMILAVER PAILQKQFNT
HTFNNYLKLF IHAIDDFSNL VLPYMINFVL FFIYLIWNRS ITLGDKSSHS AGLHIVQIFY
CFTFITVFSL PIWISRNFMK LYKLRIKRKP VQTFFEFIGI MLIIRYFTKV HPFLLADNRH
YTFYLFRRLI GNKSRLIKYF FMTPIYHFST FAYLEVMRPN QLTFHPITPL PIKEPVHLPI
QLTHVSWTAL ITCTMVTIVP SPLFEPRYYI LPYFFWRIFI TCSCEPLIKD LKPAKEGENP
ITISSTKRLF MEFLWFMLFN VVTLVIFSKV SFPWTTEPYL QRIIW
