GPT_YEAST
ID GPT_YEAST Reviewed; 448 AA.
AC P07286; D6VQN9;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase;
DE EC=2.7.8.15;
DE AltName: Full=GlcNAc-1-P transferase;
DE Short=G1PT;
DE Short=GPT;
DE AltName: Full=N-acetylglucosamine-1-phosphate transferase;
DE AltName: Full=Tunicamycin resistance protein 1;
GN Name=ALG7; Synonyms=TUR1; OrderedLocusNames=YBR243C; ORFNames=YBR1628;
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=3033607; DOI=10.1093/nar/15.8.3627;
RA Hartog K.O., Bishop B.;
RT "Genomic sequence coding for tunicamycin resistance in yeast.";
RL Nucleic Acids Res. 15:3627-3627(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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).
CC -!- FUNCTION: Catalyzes the initial step in the synthesis of dolichol-P-P-
CC oligosaccharides.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-
CC acetyl-alpha-D-glucosaminyl-diphosphodolichol + UMP;
CC Xref=Rhea:RHEA:13289, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9519,
CC ChEBI:CHEBI:57683, ChEBI:CHEBI:57705, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:58427; EC=2.7.8.15;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9H3H5};
CC -!- ACTIVITY REGULATION: Inhibited by tunicamycin.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC membrane protein.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. {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; Y00126; CAA68324.1; -; Genomic_DNA.
DR EMBL; Z36112; CAA85206.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07359.1; -; Genomic_DNA.
DR PIR; A27522; A27522.
DR RefSeq; NP_009802.3; NM_001178591.3.
DR AlphaFoldDB; P07286; -.
DR SMR; P07286; -.
DR BioGRID; 32938; 51.
DR DIP; DIP-5364N; -.
DR IntAct; P07286; 7.
DR MINT; P07286; -.
DR STRING; 4932.YBR243C; -.
DR iPTMnet; P07286; -.
DR MaxQB; P07286; -.
DR PaxDb; P07286; -.
DR PRIDE; P07286; -.
DR EnsemblFungi; YBR243C_mRNA; YBR243C; YBR243C.
DR GeneID; 852545; -.
DR KEGG; sce:YBR243C; -.
DR SGD; S000000447; ALG7.
DR VEuPathDB; FungiDB:YBR243C; -.
DR eggNOG; KOG2788; Eukaryota.
DR GeneTree; ENSGT00390000011424; -.
DR HOGENOM; CLU_029942_1_0_1; -.
DR InParanoid; P07286; -.
DR OMA; LVWMGPM; -.
DR BioCyc; MetaCyc:YBR243C-MON; -.
DR BioCyc; YEAST:YBR243C-MON; -.
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:P07286; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P07286; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0043541; C:UDP-N-acetylglucosamine transferase complex; IDA:SGD.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro.
DR GO; GO:0003975; F:UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase 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:0006487; P:protein N-linked glycosylation; IMP:SGD.
DR CDD; cd06855; GT_GPT_euk; 1.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR InterPro; IPR033895; GPT.
DR PANTHER; PTHR10571; PTHR10571; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycosyltransferase; Magnesium; Membrane;
KW Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..448
FT /note="UDP-N-acetylglucosamine--dolichyl-phosphate N-
FT acetylglucosaminephosphotransferase"
FT /id="PRO_0000108765"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 58..60
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT BINDING 70
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT BINDING 156
FT /ligand="dolichyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57683"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT BINDING 210..218
FT /ligand="dolichyl phosphate"
FT /ligand_id="ChEBI:CHEBI:57683"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT BINDING 223
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H5"
FT BINDING 336..338
FT /ligand="UDP-N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:57705"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H5"
SQ SEQUENCE 448 AA; 50368 MW; 00A617D831335637 CRC64;
MLRLFSLALI TCLIYYSKNQ GPSALVAAVG FGIAGYLATD MLIPRVGKSF IKIGLFGKDL
SKPGRPVLPE TIGAIPAAVY LFVMFIYIPF IFYKYMVITT SGGGHRDVSV VEDNGMNSNI
FPHDKLSEYL SAILCLESTV LLGIADDLFD LRWRHKFFLP AIAAIPLLMV YYVDFGVTHV
LIPGFMERWL KKTSVDLGLW YYVYMASMAI FCPNSINILA GVNGLEVGQC IVLAILALLN
DLLYFSMGPL ATRDSHRFSA VLIIPFLGVS LALWKWNRWP ATVFVGDTYC YFAGMVFAVV
GILGHFSKTM LLLFIPQIVN FIYSCPQLFK LVPCPRHRLP KFNEKDGLMY PSRANLKEEP
PKSIFKPILK LLYCLHLIDL EFDENNEIIS TSNMTLINLT LVWFGPMRED KLCNTILKLQ
FCIGILALLG RHAIGAIIFG HDNLWTVR
