ID   ALG2_CANGA              Reviewed;         458 AA.
AC   Q6FJJ9;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 103.
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=CAGL0M05731g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR380959; CAG62571.1; -; Genomic_DNA.
DR   RefSeq; XP_449595.1; XM_449595.1.
DR   AlphaFoldDB; Q6FJJ9; -.
DR   STRING; 5478.XP_449595.1; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   EnsemblFungi; CAG62571; CAG62571; CAGL0M05731g.
DR   GeneID; 2891643; -.
DR   KEGG; cgr:CAGL0M05731g; -.
DR   CGD; CAL0137195; CAGL0M05731g.
DR   VEuPathDB; FungiDB:CAGL0M05731g; -.
DR   eggNOG; KOG0853; Eukaryota.
DR   HOGENOM; CLU_030619_1_0_1; -.
DR   InParanoid; Q6FJJ9; -.
DR   OMA; TIFTSHC; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:EnsemblFungi.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..458
FT                   /note="Alpha-1,3/1,6-mannosyltransferase ALG2"
FT                   /id="PRO_0000080264"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        169
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   458 AA;  52255 MW;  C6AC3B19E3ACDEC0 CRC64;
     MVPAKKLKIA FVHPDLGIGG AERLVVDAAL GLQEAGHEVI IYTSHCDKTH CFEEVKNGTL
     KVEVFGDFLP TDLGKRFFIV FANLRQLYLT AKVVLSGRSK DKDVFIIDQL STCVPFFKLA
     NNKVLFYCHF PDQLLAIRTN WIKSLYRIPF DLLEQFTMYC SDEVVVNSNF TKSMYKKTFK
     YLQKNPNVIY PCVDTDTETL INDRDMQIGN LLVGKCPNFY LSINRYERKK NIELAIQAFA
     KASVENTNLV VCGGYDPRIH ENVQYLQELT CLCKELDLSY TVNHYSDFIE DSYSVNEIEK
     LFGAKVIFLT SISSSLKEFL IQNMQLLLYT PSYEHFGIVP LEAMKYGKPV LAVNNGGPVE
     TVVSYQKEDN EKSTTGWLRS ADADEWASAL IESKEVLNQN PELFKNNGPK RVIELFSRKA
     MTQEFETNIK LALRHTSNIS IIYVVSIIFA VLLKVFVF