ALG5_YEAST
ID ALG5_YEAST Reviewed; 334 AA.
AC P40350; D6W3E3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Dolichyl-phosphate beta-glucosyltransferase {ECO:0000303|PubMed:8076653};
DE Short=DolP-glucosyltransferase {ECO:0000303|PubMed:8076653};
DE EC=2.4.1.117 {ECO:0000269|PubMed:8076653};
DE AltName: Full=Asparagine-linked glycosylation protein 5 {ECO:0000303|PubMed:8076653};
GN Name=ALG5 {ECO:0000303|PubMed:8076653}; OrderedLocusNames=YPL227C;
GN ORFNames=P1437;
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], FUNCTION, CATALYTIC ACTIVITY, DISRUPTION
RP PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=8076653; DOI=10.1111/j.1432-1033.1994.tb19996.x;
RA Te Heesen S., Lehle L., Weissmann A., Aebi M.;
RT "Isolation of the ALG5 locus encoding the UDP-glucose:dolichyl-phosphate
RT glucosyltransferase from Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 224:71-79(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Endoplasmic reticulum membrane-bound UDP-glucose:dolichyl-
CC phosphate glucosyltransferase involved in protein N-linked
CC glycosylation. {ECO:0000269|PubMed:8076653}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl phosphate + UDP-alpha-D-glucose = a dolichyl beta-
CC D-glucosyl phosphate + UDP; Xref=Rhea:RHEA:15401, Rhea:RHEA-
CC COMP:9517, Rhea:RHEA-COMP:9528, ChEBI:CHEBI:57525, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.117;
CC Evidence={ECO:0000269|PubMed:8076653};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:8076653}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:8076653}; Single-pass type II membrane protein
CC {ECO:0000255}. Note=Its interaction with the substrate UDP-glucose may
CC occur at the cytoplasmic side of the ER, whereas the steps utilizing
CC dolichyl beta-D-glucosyl phosphate take place in the lumen of the ER.
CC {ECO:0000269|PubMed:8076653}.
CC -!- DISRUPTION PHENOTYPE: Leads to a loss of UDP-glucose:dolichyl-phosphate
CC glucosyltransferase activity and a concomitant underglycosylation of
CC carboxypeptidase Y. {ECO:0000269|PubMed:8076653}.
CC -!- MISCELLANEOUS: Present with 5800 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 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; X77573; CAA54680.1; -; Genomic_DNA.
DR EMBL; X94561; CAA64260.1; -; Genomic_DNA.
DR EMBL; Z73583; CAA97942.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11209.1; -; Genomic_DNA.
DR PIR; S48136; S48136.
DR RefSeq; NP_015097.1; NM_001184041.1.
DR AlphaFoldDB; P40350; -.
DR SMR; P40350; -.
DR BioGRID; 35958; 252.
DR DIP; DIP-5651N; -.
DR IntAct; P40350; 25.
DR MINT; P40350; -.
DR STRING; 4932.YPL227C; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR iPTMnet; P40350; -.
DR MaxQB; P40350; -.
DR PaxDb; P40350; -.
DR PRIDE; P40350; -.
DR EnsemblFungi; YPL227C_mRNA; YPL227C; YPL227C.
DR GeneID; 855874; -.
DR KEGG; sce:YPL227C; -.
DR SGD; S000006148; ALG5.
DR VEuPathDB; FungiDB:YPL227C; -.
DR eggNOG; KOG2977; Eukaryota.
DR GeneTree; ENSGT00940000153481; -.
DR HOGENOM; CLU_033536_9_1_1; -.
DR InParanoid; P40350; -.
DR OMA; MVNTDAV; -.
DR BioCyc; MetaCyc:YPL227C-MON; -.
DR BioCyc; YEAST:YPL227C-MON; -.
DR Reactome; R-SCE-480985; Synthesis of dolichyl-phosphate-glucose.
DR UniPathway; UPA00378; -.
DR PRO; PR:P40350; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P40350; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004581; F:dolichyl-phosphate beta-glucosyltransferase activity; IDA:SGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:UniProtKB.
DR CDD; cd04188; DPG_synthase; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR035518; DPG_synthase.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..334
FT /note="Dolichyl-phosphate beta-glucosyltransferase"
FT /id="PRO_0000059097"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8076653"
FT TRANSMEM 13..33
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..334
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:8076653"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 334 AA; 38347 MW; 639A88DDED879217 CRC64;
MRALRFLIEN RNTVFFTLLV ALVLSLYLLV YLFSHTPRPP YPEELKYIAI DEKGHEVSRA
LPNLNEHQDD EEIFLSVVIP SYNETGRILL MLTDAISFLK EKYGSRWEIV IVDDGSTDNT
TQYCLKICKE QFKLNYEQFR IIKFSQNRGK GGAVRQGFLH IRGKYGLFAD ADGASKFSDV
EKLIDAISKI ETSSTDLKTT KPAVAIGSRA HMVNTEAVIK RSMIRNCLMY GFHTLVFIFG
IRSIKDTQCG FKLFNRAAIL KIFPYLHTEG WIFDVEILIL AIRKRIQIEE IPISWHEVDG
SKMALAIDSI KMAKDLVIIR MAYLLGIYRD NKKC
