ID ALG11_YARLI Reviewed; 635 AA.
AC Q6C9T3;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 99.
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=YALI0D08558g;
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: 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 (By similarity). {ECO:0000250}.
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 -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC {ECO:0000305}.
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DR EMBL; CR382130; CAG80767.1; -; Genomic_DNA.
DR RefSeq; XP_502579.1; XM_502579.1.
DR AlphaFoldDB; Q6C9T3; -.
DR STRING; 284591.Q6C9T3; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR GlyCosmos; Q6C9T3; 2 sites, No reported glycans.
DR EnsemblFungi; CAG80767; CAG80767; YALI0_D08558g.
DR GeneID; 2910710; -.
DR KEGG; yli:YALI0D08558g; -.
DR VEuPathDB; FungiDB:YALI0_D08558g; -.
DR HOGENOM; CLU_017896_1_1_1; -.
DR InParanoid; Q6C9T3; -.
DR OMA; WKHFTLI; -.
DR OrthoDB; 197751at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001300; Chromosome D.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0004377; F:GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR CDD; cd03806; GT4_ALG11-like; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR038013; ALG11.
DR InterPro; IPR031814; ALG11_N.
DR InterPro; IPR001296; Glyco_trans_1.
DR PANTHER; PTHR45919; GDP-MAN:MAN(3)GLCNAC(2)-PP-DOL ALPHA-1,2-MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR45919:SF1; GDP-MAN:MAN(3)GLCNAC(2)-PP-DOL ALPHA-1,2-MANNOSYLTRANSFERASE; 1.
DR Pfam; PF15924; ALG11_N; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..635
FT /note="GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-
FT mannosyltransferase"
FT /id="PRO_0000080279"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 635 AA; 71363 MW; 50814E76F2CD6018 CRC64;
MALQLDLPTL HDLRVVLNAD FLAALAALLL LAVILVPLCS YISLYAWSAI LAFKLRSPPA
NWEKSIVKGV QANGTSTLFG FGFWQAAAVR RQLILQSNDP SYYSVTHVSR RSEIAISPED
RNTEFRNRAQ DSGAPRRVIY GFFHPYANAG GGGERVLWAA VKDTLMYDDN IICAIYCGEQ
DLPTRTSPST VLDAAVSNFH VTELADKELR KRIVFIGMRG RRLVDPKTWP RFTLMMQAAG
SVWMAWHGIS TLVPDVFVDT MGYPFAYPLV SWVTHVPVAA YVHYPVISKD MLATVSLKQS
PVRAALAVAK LVYWRVFALT YTFAGSYCSV VMTNSSWTNN HMQHMWWYNH KAEHIKIVYP
PCGTQALSEI AMSEETSARS PNIVYIAQFR PEKRHDIVLR EFNKFYKEYT EKYPNQPAPH
LTFVGTVRND DDKSRVYLLR LQARDLVNPD SVSFVLDAPF DKVRDILRTA SMGVNAMWNE
HFGIVVVEYM SAGLIPVVHN SGGPKCDIVV PYEGQSTGNS GTLSAMPSST SIRSHYEAVP
PGPTGFHFNC PGSDPTTDSG PSYDGEPIGT LAETLMRAFE LSESDTHNMR ARARESVKKR
FSNEQFGSHW QVRMRILEKL EQIRRGHRLT RGDFD
//