ALG1_CANGA
ID ALG1_CANGA Reviewed; 450 AA.
AC Q6FLZ2;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Chitobiosyldiphosphodolichol beta-mannosyltransferase;
DE EC=2.4.1.142;
DE AltName: Full=Asparagine-linked glycosylation protein 1;
DE AltName: Full=Beta-1,4-mannosyltransferase;
DE AltName: Full=GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase;
DE AltName: Full=GDP-mannose-dolichol diphosphochitobiose mannosyltransferase;
GN Name=ALG1; OrderedLocusNames=CAGL0K12342g;
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: Participates in the formation of the lipid-linked precursor
CC oligosaccharide for N-glycosylation. Involved in assembling the
CC dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic
CC surface of the ER (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GDP-alpha-D-mannose + N,N'-diacetylchitobiosyl
CC diphosphodolichol = beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-
CC GlcNAc-diphosphodolichol + GDP + H(+); Xref=Rhea:RHEA:13865,
CC Rhea:RHEA-COMP:9520, Rhea:RHEA-COMP:11044, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57269, ChEBI:CHEBI:57527, ChEBI:CHEBI:58189,
CC ChEBI:CHEBI:58472; EC=2.4.1.142;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type II 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; CR380957; CAG61715.1; -; Genomic_DNA.
DR RefSeq; XP_448752.1; XM_448752.1.
DR AlphaFoldDB; Q6FLZ2; -.
DR SMR; Q6FLZ2; -.
DR STRING; 5478.XP_448752.1; -.
DR CAZy; GT33; Glycosyltransferase Family 33.
DR EnsemblFungi; CAG61715; CAG61715; CAGL0K12342g.
DR GeneID; 2889981; -.
DR KEGG; cgr:CAGL0K12342g; -.
DR CGD; CAL0134263; CAGL0K12342g.
DR VEuPathDB; FungiDB:CAGL0K12342g; -.
DR eggNOG; KOG2941; Eukaryota.
DR HOGENOM; CLU_012079_0_0_1; -.
DR InParanoid; Q6FLZ2; -.
DR OMA; PLKVLWQ; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002428; Chromosome K.
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:0004578; F:chitobiosyldiphosphodolichol beta-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:EnsemblFungi.
DR InterPro; IPR026051; ALG1-like.
DR InterPro; IPR001296; Glyco_trans_1.
DR PANTHER; PTHR13036; PTHR13036; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..450
FT /note="Chitobiosyldiphosphodolichol beta-
FT mannosyltransferase"
FT /id="PRO_0000080254"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..450
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 450 AA; 51945 MW; 23D405BAF7FB7724 CRC64;
MSWIQIPWSW VVTLIVTYLS LPLIIYYLVP YIFYGNKSSK KRIIIYVLGD IGHSPRMCYH
ARSFSEKGWQ VELCGYVEEQ VPGFIAEDPN IIVHALPTLT LQGNKRSIIF LVKKVLFQVS
AIIAQLWELR GSNYMLIQNP PSIPILPIAV FYRLSGCKLI IDWHNLAYSI MQLKFNGNFY
HPVVLASYVI EYIFGKFATY NLTVTEAMKE YLVNSFGLNP KRCVVLYDRP ATQFKPLTES
ESRTKLLDSE FIRDMIPEGF NVEKGDKIIV TSTSFTPDED ISILIGALKI YDNSYENLDK
SLPKILCFVT GKGPMKERYV KDVEEHDWQH VYVKFVWLKS EDYPRLLQLC DYGVSLHKSS
SGLDLPMKIL DMYGSGIPVI AYNYPVLGEL VKYNENGLKF LDRRELHESL IFAMKDPELY
KKLKQGALKE SQIRWNSSWQ SAMQELKLVA
