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ALG2_ASHGO
ID   ALG2_ASHGO              Reviewed;         514 AA.
AC   Q755C1;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=AFL098W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AE016819; AAS53276.1; -; Genomic_DNA.
DR   RefSeq; NP_985452.1; NM_210806.1.
DR   AlphaFoldDB; Q755C1; -.
DR   SMR; Q755C1; -.
DR   STRING; 33169.AAS53276; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   EnsemblFungi; AAS53276; AAS53276; AGOS_AFL098W.
DR   GeneID; 4621679; -.
DR   KEGG; ago:AGOS_AFL098W; -.
DR   eggNOG; KOG0853; Eukaryota.
DR   HOGENOM; CLU_030619_1_0_1; -.
DR   InParanoid; Q755C1; -.
DR   OMA; TIFTSHC; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000591; Chromosome VI.
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..514
FT                   /note="Alpha-1,3/1,6-mannosyltransferase ALG2"
FT                   /id="PRO_0000080262"
FT   TRANSMEM        443..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        468..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   514 AA;  57924 MW;  E671A1515FE25DBD CRC64;
     MMTPLNIALI HPDLGIGGAE RLVVDAAIGL QDQGHRVTIY TSHCDKNHCF EEIKRGDLKV
     VVVGDFLPTN ILGKFFILCA NLRQLALVFK LVINGSIDKH DLFIVDQLST CVPLLHLFSA
     SGRVLFYCHF PDQLLAQRKS LVSKLYRVPF DLLEQLTMGC SDSVVVNSYF TRSVFFDTFK
     ILRLNPRVVY PCVAMDELPI EKIDIGFYDQ IIGPNNRYYL SINRFERKKD IALALNAFKA
     SKEGHSSDTK LIICGGYDSR VAENVEYLSE LQLICEKANI AHVTIFYSEF SRTPEHYTFP
     TGVREKKVIF LASISSSLKE LLLKKAQLLL YTPSREHFGI VPLEAMKHGT PVLAVDNGGP
     LETVVTLKSD NQDTATGWLR RADAGIWAEA IDEQAEYVKK NPGIFATNGP KWVKDKFSRD
     AMTSSFLHNI DNIFMTDRVI QPWAVMVILA ASYILWRSSH VFGDACRYIY LLTGGILVLR
     SRYLLAIFWV LLFVMQPQLS VGVDTITATL KPKL
 
 
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