ALG2_YEAST
ID ALG2_YEAST Reviewed; 503 AA.
AC P43636; D6VU76;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Alpha-1,3/1,6-mannosyltransferase ALG2;
DE EC=2.4.1.132;
DE EC=2.4.1.257;
DE AltName: Full=Asparagine-linked glycosylation protein 2;
DE AltName: Full=GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase;
DE AltName: Full=GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase;
DE AltName: Full=GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase;
GN Name=ALG2; OrderedLocusNames=YGL065C;
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=8400550; DOI=10.1093/glycob/3.4.357;
RA Jackson B.J., Kukuruzinska M.A., Robbins P.;
RT "Biosynthesis of asparagine-linked oligosaccharides in Saccharomyces
RT cerevisiae: the alg2 mutation.";
RL Glycobiology 3:357-364(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9234674;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9;
RA Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT "The characterization of two new clusters of duplicated genes suggests a
RT 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
RL Yeast 13:861-869(1997).
RN [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF
RP GLU-335 AND GLU-343.
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 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 [8]
RP INTERACTION WITH ALG1, AND SUBCELLULAR LOCATION.
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 [9]
RP CHARACTERIZATION.
RX PubMed=12684507; DOI=10.1074/jbc.m302850200;
RA Thiel C., Schwarz M., Peng J., Grzmil M., Hasilik M., Braulke T.,
RA Kohlschuetter A., von Figura K., Lehle L., Koerner C.;
RT "A new type of congenital disorders of glycosylation (CDG-Ii) provides new
RT insights into the early steps of dolichol-linked oligosaccharide
RT biosynthesis.";
RL J. Biol. Chem. 278:22498-22505(2003).
CC -!- FUNCTION: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and
CC Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol
CC diphosphate. {ECO:0000269|PubMed:16878994}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-(1->3)-beta-D-
CC Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol +
CC GDP + H(+); Xref=Rhea:RHEA:29515, Rhea:RHEA-COMP:11044, Rhea:RHEA-
CC COMP:12624, ChEBI:CHEBI:15378, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:58472, ChEBI:CHEBI:132510; EC=2.4.1.132;
CC Evidence={ECO:0000269|PubMed:16878994};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol + GDP-alpha-D-mannose = alpha-D-Man-
CC (1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:29519,
CC Rhea:RHEA-COMP:12624, Rhea:RHEA-COMP:12626, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132510,
CC ChEBI:CHEBI:132511; EC=2.4.1.257;
CC Evidence={ECO:0000269|PubMed:16878994};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Interacts with ALG1. {ECO:0000269|PubMed:15044395}.
CC -!- INTERACTION:
CC P43636; P16661: ALG1; NbExp=2; IntAct=EBI-2459, EBI-2206309;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15044395}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15044395}.
CC -!- MISCELLANEOUS: Present with 1840 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; X87947; CAA61199.1; -; Genomic_DNA.
DR EMBL; Z72587; CAA96768.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08037.1; -; Genomic_DNA.
DR PIR; S64069; S64069.
DR RefSeq; NP_011450.1; NM_001180930.1.
DR AlphaFoldDB; P43636; -.
DR SMR; P43636; -.
DR BioGRID; 33182; 237.
DR DIP; DIP-5401N; -.
DR IntAct; P43636; 4.
DR STRING; 4932.YGL065C; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR iPTMnet; P43636; -.
DR MaxQB; P43636; -.
DR PaxDb; P43636; -.
DR PRIDE; P43636; -.
DR EnsemblFungi; YGL065C_mRNA; YGL065C; YGL065C.
DR GeneID; 852815; -.
DR KEGG; sce:YGL065C; -.
DR SGD; S000003033; ALG2.
DR VEuPathDB; FungiDB:YGL065C; -.
DR eggNOG; KOG0853; Eukaryota.
DR GeneTree; ENSGT00550000075033; -.
DR HOGENOM; CLU_030619_1_0_1; -.
DR InParanoid; P43636; -.
DR OMA; TIFTSHC; -.
DR BioCyc; MetaCyc:YGL065C-MON; -.
DR BioCyc; YEAST:YGL065C-MON; -.
DR BRENDA; 2.4.1.132; 984.
DR BRENDA; 2.4.1.257; 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:P43636; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P43636; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000033; F:alpha-1,3-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; TAS:Reactome.
DR GO; GO:0004378; F:GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity; IDA:SGD.
DR GO; GO:0102704; F:GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0033164; F:glycolipid 1,6-alpha-mannosyltransferase activity; IDA:SGD.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IDA:SGD.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR InterPro; IPR027054; ALG2.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR PANTHER; PTHR45918; PTHR45918; 1.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..503
FT /note="Alpha-1,3/1,6-mannosyltransferase ALG2"
FT /id="PRO_0000080271"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 335
FT /note="E->A: Severely affects activity, especially the
FT second mannosylation step."
FT /evidence="ECO:0000269|PubMed:16878994"
FT MUTAGEN 343
FT /note="E->A: No activity."
FT /evidence="ECO:0000269|PubMed:16878994"
FT CONFLICT 8
FT /note="T -> S (in Ref. 1; CAA61199)"
FT /evidence="ECO:0000305"
FT CONFLICT 237..238
FT /note="KA -> NG (in Ref. 1; CAA61199)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="T -> A (in Ref. 1; CAA61199)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="M -> I (in Ref. 1; CAA61199)"
FT /evidence="ECO:0000305"
FT CONFLICT 470..503
FT /note="FLFMATFMVLYFKNYLWGIYWAFVFALSYPYEEI -> SYLWPLLWYYILRT
FT TYGEFTGHLYSLSPTLMKKYNVYLNKQCIPPEEKIIYIGEEISKCK (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 58047 MW; 1200E1C8EA023DD4 CRC64;
MIEKDKRTIA FIHPDLGIGG AERLVVDAAL GLQQQGHSVI IYTSHCDKSH CFEEVKNGQL
KVEVYGDFLP TNFLGRFFIV FATIRQLYLV IQLILQKKVN AYQLIIIDQL STCIPLLHIF
SSATLMFYCH FPDQLLAQRA GLLKKIYRLP FDLIEQFSVS AADTVVVNSN FTKNTFHQTF
KYLSNDPDVI YPCVDLSTIE IEDIDKKFFK TVFNEGDRFY LSINRFEKKK DVALAIKAFA
LSEDQINDNV KLVICGGYDE RVAENVEYLK ELQSLADEYE LSHTTIYYQE IKRVSDLESF
KTNNSKIIFL TSISSSLKEL LLERTEMLLY TPAYEHFGIV PLEAMKLGKP VLAVNNGGPL
ETIKSYVAGE NESSATGWLK PAVPIQWATA IDESRKILQN GSVNFERNGP LRVKKYFSRE
AMTQSFEENV EKVIWKEKKY YPWEIFGISF SNFILHMAFI KILPNNPWPF LFMATFMVLY
FKNYLWGIYW AFVFALSYPY EEI
