ALG11_YEAST
ID ALG11_YEAST Reviewed; 548 AA.
AC P53954; D6W1D1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase;
DE EC=2.4.1.131;
DE AltName: Full=Alpha-1,2-mannosyltransferase ALG11;
DE AltName: Full=Asparagine-linked glycosylation protein 11;
DE AltName: Full=Glycolipid 2-alpha-mannosyltransferase;
GN Name=ALG11; OrderedLocusNames=YNL048W; ORFNames=N2510, YNL2510W;
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, AND SUBCELLULAR LOCATION.
RX PubMed=11278778; DOI=10.1074/jbc.m010896200;
RA Cipollo J.F., Trimble R.B., Chi J.H., Yan Q., Dean N.;
RT "The yeast ALG11 gene specifies addition of the terminal alpha 1,2-Man to
RT the Man5GlcNAc2-PP-dolichol N-glycosylation intermediate formed on the
RT cytosolic side of the endoplasmic reticulum.";
RL J. Biol. Chem. 276:21828-21840(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1676;
RX PubMed=8533472; DOI=10.1002/yea.320111008;
RA Bergez P., Doignon F., Crouzet M.;
RT "The sequence of a 44 420 bp fragment located on the left arm of chromosome
RT XIV from Saccharomyces cerevisiae.";
RL Yeast 11:967-974(1995).
RN [3]
RP ERRATUM OF PUBMED:8533472.
RX PubMed=8904343;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<297::aid-yea940>3.0.co;2-d;
RA Bergez P., Doignon F., Crouzet M.;
RL Yeast 12:297-297(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8740423;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<493::aid-yea929>3.0.co;2-w;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 12.8 kb from the left arm of chromosome XIV reveals a
RT sigma element, a pro-tRNA and six complete open reading frames, one of
RT which encodes a protein similar to the human leukotriene A4 hydrolase.";
RL Yeast 12:493-499(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF
RP GLU-405 AND GLU-413.
RX PubMed=16878994; DOI=10.1021/bi060878o;
RA O'Reilly M.K., Zhang G., Imperiali B.;
RT "In vitro evidence for the dual function of Alg2 and Alg11: essential
RT mannosyltransferases in N-linked glycoprotein biosynthesis.";
RL Biochemistry 45:9593-9603(2006).
RN [7]
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 [8]
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 [9]
RP INTERACTION WITH ALG1.
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).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-84; GLY-85; GLY-87;
RP LYS-319; GLU-405; HIS-406; PHE-407 AND GLU-413, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=19929855; DOI=10.1042/bj20091121;
RA Absmanner B., Schmeiser V., Kaempf M., Lehle L.;
RT "Biochemical characterization, membrane association and identification of
RT amino acids essential for the function of Alg11 from Saccharomyces
RT cerevisiae, an alpha1,2-mannosyltransferase catalysing two sequential
RT glycosylation steps in the formation of the lipid-linked core
RT oligosaccharide.";
RL Biochem. J. 426:205-217(2010).
CC -!- FUNCTION: Required for N-linked oligosaccharide assembly. Has a role in
CC the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core
CC oligosaccharide on the cytoplasmic face of the endoplasmic reticulum.
CC {ECO:0000269|PubMed:11278778, ECO:0000269|PubMed:16878994,
CC ECO:0000269|PubMed:19929855}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-
CC D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + 2 GDP + 2 H(+); Xref=Rhea:RHEA:29523,
CC Rhea:RHEA-COMP:12626, Rhea:RHEA-COMP:12627, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132511,
CC ChEBI:CHEBI:132515; EC=2.4.1.131;
CC Evidence={ECO:0000269|PubMed:16878994, ECO:0000269|PubMed:19929855};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Interacts with ALG1. {ECO:0000269|PubMed:15044395}.
CC -!- INTERACTION:
CC P53954; P16661: ALG1; NbExp=2; IntAct=EBI-2497, EBI-2206309;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11278778}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:11278778}.
CC -!- MISCELLANEOUS: Present with 3140 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; U12141; AAA99664.1; -; Genomic_DNA.
DR EMBL; U62941; AAB49937.1; -; Genomic_DNA.
DR EMBL; X94547; CAA64234.1; -; Genomic_DNA.
DR EMBL; Z71324; CAA95916.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10497.1; -; Genomic_DNA.
DR PIR; S61096; S61096.
DR RefSeq; NP_014350.1; NM_001182887.1.
DR AlphaFoldDB; P53954; -.
DR BioGRID; 35776; 117.
DR DIP; DIP-7438N; -.
DR IntAct; P53954; 4.
DR MINT; P53954; -.
DR STRING; 4932.YNL048W; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; P53954; -.
DR MaxQB; P53954; -.
DR PaxDb; P53954; -.
DR PRIDE; P53954; -.
DR EnsemblFungi; YNL048W_mRNA; YNL048W; YNL048W.
DR GeneID; 855679; -.
DR KEGG; sce:YNL048W; -.
DR SGD; S000004993; ALG11.
DR VEuPathDB; FungiDB:YNL048W; -.
DR eggNOG; KOG1387; Eukaryota.
DR GeneTree; ENSGT00550000075118; -.
DR HOGENOM; CLU_017896_1_1_1; -.
DR InParanoid; P53954; -.
DR OMA; WKHFTLI; -.
DR BioCyc; MetaCyc:MON3O-36; -.
DR BioCyc; YEAST:MON3O-36; -.
DR BRENDA; 2.4.1.131; 984.
DR UniPathway; UPA00378; -.
DR PRO; PR:P53954; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53954; 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:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IMP:SGD.
DR GO; GO:0004377; F:GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity; IDA:SGD.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IDA:SGD.
DR GO; GO:0006486; P:protein glycosylation; IMP:SGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR CDD; cd03806; GT4_ALG11-like; 1.
DR DisProt; DP00618; -.
DR InterPro; IPR038013; ALG11.
DR InterPro; IPR031814; ALG11_N.
DR InterPro; IPR001296; Glyco_trans_1.
DR PANTHER; PTHR45919; PTHR45919; 1.
DR Pfam; PF15924; ALG11_N; 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..548
FT /note="GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-
FT mannosyltransferase"
FT /id="PRO_0000080280"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..548
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 84
FT /note="G->A,P: No effect."
FT /evidence="ECO:0000269|PubMed:19929855"
FT MUTAGEN 85
FT /note="G->A: No effect."
FT /evidence="ECO:0000269|PubMed:19929855"
FT MUTAGEN 85
FT /note="G->P: No activity."
FT /evidence="ECO:0000269|PubMed:19929855"
FT MUTAGEN 87
FT /note="G->A: No effect."
FT /evidence="ECO:0000269|PubMed:19929855"
FT MUTAGEN 87
FT /note="G->P: No activity."
FT /evidence="ECO:0000269|PubMed:19929855"
FT MUTAGEN 319
FT /note="K->A: Almost no activity."
FT /evidence="ECO:0000269|PubMed:19929855"
FT MUTAGEN 405
FT /note="E->A: Almost no activity."
FT /evidence="ECO:0000269|PubMed:16878994,
FT ECO:0000269|PubMed:19929855"
FT MUTAGEN 406
FT /note="H->A: Almost no activity."
FT /evidence="ECO:0000269|PubMed:19929855"
FT MUTAGEN 407
FT /note="F->A: Impaired activity."
FT /evidence="ECO:0000269|PubMed:19929855"
FT MUTAGEN 413
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:16878994,
FT ECO:0000269|PubMed:19929855"
SQ SEQUENCE 548 AA; 63143 MW; 2A3AD59924C762CC CRC64;
MGSAWTNYNF EEVKSHFGFK KYVVSSLVLV YGLIKVLTWI FRQWVYSSLN PFSKKSSLLN
RAVASCGEKN VKVFGFFHPY CNAGGGGEKV LWKAVDITLR KDAKNVIVIY SGDFVNGENV
TPENILNNVK AKFDYDLDSD RIFFISLKLR YLVDSSTWKH FTLIGQAIGS MILAFESIIQ
CPPDIWIDTM GYPFSYPIIA RFLRRIPIVT YTHYPIMSKD MLNKLFKMPK KGIKVYGKIL
YWKVFMLIYQ SIGSKIDIVI TNSTWTNNHI KQIWQSNTCK IIYPPCSTEK LVDWKQKFGT
AKGERLNQAI VLAQFRPEKR HKLIIESFAT FLKNLPDSVS PIKLIMAGST RSKQDENYVK
SLQDWSENVL KIPKHLISFE KNLPFDKIEI LLNKSTFGVN AMWNEHFGIA VVEYMASGLI
PIVHASAGPL LDIVTPWDAN GNIGKAPPQW ELQKKYFAKL EDDGETTGFF FKEPSDPDYN
TTKDPLRYPN LSDLFLQITK LDYDCLRVMG ARNQQYSLYK FSDLKFDKDW ENFVLNPICK
LLEEEERG
