ALG1_YEAST
ID ALG1_YEAST Reviewed; 449 AA.
AC P16661; D6VQA9;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Chitobiosyldiphosphodolichol beta-mannosyltransferase;
DE EC=2.4.1.142;
DE AltName: Full=Asparagine-linked glycosylation protein 1;
DE AltName: Full=Beta-1,4-mannosyltransferase;
DE AltName: Full=GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase;
DE AltName: Full=GDP-mannose-dolichol diphosphochitobiose mannosyltransferase;
GN Name=ALG1; OrderedLocusNames=YBR110W; ORFNames=YBR0906;
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=2182636; DOI=10.1016/s0021-9258(19)39256-7;
RA Albright C.F., Robbins P.W.;
RT "The sequence and transcript heterogeneity of the yeast gene ALG1, an
RT essential mannosyltransferase involved in N-glycosylation.";
RL J. Biol. Chem. 265:7042-7049(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [3]
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 [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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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).
RN [7]
RP OLIGOMERIZATION, INTERACTION WITH ALG2 AND ALG11, AND MUTAGENESIS OF
RP GLU-278; GLY-310; HIS-356; ASP-363 AND ASP-370.
RX PubMed=15044395; DOI=10.1093/glycob/cwh072;
RA Gao X.-D., Nishikawa A., Dean N.;
RT "Physical interactions between the Alg1, Alg2, and Alg11
RT mannosyltransferases of the endoplasmic reticulum.";
RL Glycobiology 14:559-570(2004).
CC -!- FUNCTION: Participates in the formation of the lipid-linked precursor
CC oligosaccharide for N-glycosylation. Involved in assembling the
CC dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic
CC surface of the ER.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl
CC diphosphodolichol = beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:13865,
CC Rhea:RHEA-COMP:9520, Rhea:RHEA-COMP:11044, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57269, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:58472; EC=2.4.1.142;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer. Interacts with ALG2 and ALG11.
CC {ECO:0000269|PubMed:15044395}.
CC -!- INTERACTION:
CC P16661; P53954: ALG11; NbExp=2; IntAct=EBI-2206309, EBI-2497;
CC P16661; P43636: ALG2; NbExp=2; IntAct=EBI-2206309, EBI-2459;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 1890 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 33 subfamily. {ECO:0000305}.
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DR EMBL; J05416; AAA66322.1; -; Genomic_DNA.
DR EMBL; X78993; CAA55613.1; -; Genomic_DNA.
DR EMBL; Z35979; CAA85067.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07229.1; -; Genomic_DNA.
DR PIR; A35762; A35762.
DR RefSeq; NP_009668.3; NM_001178458.3.
DR AlphaFoldDB; P16661; -.
DR SMR; P16661; -.
DR BioGRID; 32814; 362.
DR DIP; DIP-7371N; -.
DR IntAct; P16661; 15.
DR MINT; P16661; -.
DR STRING; 4932.YBR110W; -.
DR CAZy; GT33; Glycosyltransferase Family 33.
DR iPTMnet; P16661; -.
DR MaxQB; P16661; -.
DR PaxDb; P16661; -.
DR PRIDE; P16661; -.
DR EnsemblFungi; YBR110W_mRNA; YBR110W; YBR110W.
DR GeneID; 852407; -.
DR KEGG; sce:YBR110W; -.
DR SGD; S000000314; ALG1.
DR VEuPathDB; FungiDB:YBR110W; -.
DR eggNOG; KOG2941; Eukaryota.
DR GeneTree; ENSGT00390000008647; -.
DR HOGENOM; CLU_012079_0_0_1; -.
DR InParanoid; P16661; -.
DR OMA; PLKVLWQ; -.
DR BioCyc; MetaCyc:YBR110W-MON; -.
DR BioCyc; YEAST:YBR110W-MON; -.
DR BRENDA; 2.4.1.142; 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:P16661; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P16661; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IPI:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019187; F:beta-1,4-mannosyltransferase activity; IDA:SGD.
DR GO; GO:0004578; F:chitobiosyldiphosphodolichol beta-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IMP:SGD.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IMP:SGD.
DR InterPro; IPR026051; ALG1-like.
DR InterPro; IPR001296; Glyco_trans_1.
DR PANTHER; PTHR13036; PTHR13036; 1.
DR Pfam; PF00534; Glycos_transf_1; 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..449
FT /note="Chitobiosyldiphosphodolichol beta-
FT mannosyltransferase"
FT /id="PRO_0000080259"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..449
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 435..449
FT /note="Required for oligomerization"
FT MOTIF 21..32
FT /note="Dolichol recognition"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 278
FT /note="E->K: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15044395"
FT MUTAGEN 310
FT /note="G->D: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15044395"
FT MUTAGEN 356
FT /note="H->Q: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15044395"
FT MUTAGEN 363
FT /note="D->A: No effect on enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15044395"
FT MUTAGEN 370
FT /note="D->A: No effect on enzymatic activity."
FT /evidence="ECO:0000269|PubMed:15044395"
SQ SEQUENCE 449 AA; 51929 MW; 662E0CB1632DED5A CRC64;
MFLEIPRWLL ALIILYLSIP LVVYYVIPYL FYGNKSTKKR IIIFVLGDVG HSPRICYHAI
SFSKLGWQVE LCGYVEDTLP KIISSDPNIT VHHMSNLKRK GGGTSVIFMV KKVLFQVLSI
FKLLWELRGS DYILVQNPPS IPILPIAVLY KLTGCKLIID WHNLAYSILQ LKFKGNFYHP
LVLISYMVEM IFSKFADYNL TVTEAMRKYL IQSFHLNPKR CAVLYDRPAS QFQPLAGDIS
RQKALTTKAF IKNYIRDDFD TEKGDKIIVT STSFTPDEDI GILLGALKIY ENSYVKFDSS
LPKILCFITG KGPLKEKYMK QVEEYDWKRC QIEFVWLSAE DYPKLLQLCD YGVSLHTSSS
GLDLPMKILD MFGSGLPVIA MNYPVLDELV QHNVNGLKFV DRRELHESLI FAMKDADLYQ
KLKKNVTQEA ENRWQSNWER TMRDLKLIH
