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Database: UniProt/SWISS-PROT
Entry: ALG11_YARLI
LinkDB: ALG11_YARLI
Original site: ALG11_YARLI 
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
//
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