ALG2_YARLI
ID ALG2_YARLI Reviewed; 460 AA.
AC Q6C3V7;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=YALI0E31797g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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:0000250}.
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 -!- 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 -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC {ECO:0000305}.
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DR EMBL; CR382131; CAG80259.1; -; Genomic_DNA.
DR RefSeq; XP_504655.1; XM_504655.1.
DR AlphaFoldDB; Q6C3V7; -.
DR SMR; Q6C3V7; -.
DR STRING; 4952.CAG80259; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR EnsemblFungi; CAG80259; CAG80259; YALI0_E31797g.
DR GeneID; 2911827; -.
DR KEGG; yli:YALI0E31797g; -.
DR VEuPathDB; FungiDB:YALI0_E31797g; -.
DR HOGENOM; CLU_030619_1_0_1; -.
DR InParanoid; Q6C3V7; -.
DR OMA; TIFTSHC; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001300; Chromosome E.
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:0000033; F:alpha-1,3-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0004378; F:GDP-Man:Man1GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity; IEA:UniProtKB-EC.
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; IEA:EnsemblFungi.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IBA:GO_Central.
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; 2.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..460
FT /note="Alpha-1,3/1,6-mannosyltransferase ALG2"
FT /id="PRO_0000080270"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 460 AA; 52078 MW; 60BFA1CAFB06014F CRC64;
MRVAFIHPDL GIGGAERWVV DAAVGLQNLG HEVDIYTSYC NKSHCFDEVR DGLLKVTVLG
DTICPHTIKG KFAIFCATFR QLHLAYELKK GPGSKVDVFV VDQLSACVPL LKLWFPKARV
LFYGHFPDQL LVQNRNQMSL VKKAYRYPFD KFEEITTASA DRLVVNSHFT KDMFEKTFPA
TKNPLVIYPC VDTDIKEQQQ GLDRDMITAA SQYTFLLSIN RFERKKNILL AIEAFGEAQK
KSSNLKLAVA GGYDFRVNEN VEYLQELILA CEKLKLSHIS ITADKYAKLL EKDTPAAVWT
SIFKNDVIFF PSASNSFKNT LLHISKLLLY TPQNEHFGIV PLEGMLWKTP VLATNSGGPL
ETVKDNVGWT VEGKSELWAP VIDKVVHMNA SDYAVLQTEC VNWVNRFSQD TMASELEEAM
EEVRKKAPTE NVGWDYIRLG MWYSVLMTLT LSIVLLAIWP
