ID   ALG1_KLULA              Reviewed;         447 AA.
AC   Q6CVU2;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
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=KLLA0B09405g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
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DR   EMBL; CR382122; CAH02340.1; -; Genomic_DNA.
DR   RefSeq; XP_451947.1; XM_451947.1.
DR   AlphaFoldDB; Q6CVU2; -.
DR   SMR; Q6CVU2; -.
DR   STRING; 28985.XP_451947.1; -.
DR   CAZy; GT33; Glycosyltransferase Family 33.
DR   EnsemblFungi; CAH02340; CAH02340; KLLA0_B09405g.
DR   GeneID; 2896930; -.
DR   KEGG; kla:KLLA0_B09405g; -.
DR   eggNOG; KOG2941; Eukaryota.
DR   HOGENOM; CLU_012079_1_1_1; -.
DR   InParanoid; Q6CVU2; -.
DR   OMA; PLKVLWQ; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000598; Chromosome B.
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..447
FT                   /note="Chitobiosyldiphosphodolichol beta-
FT                   mannosyltransferase"
FT                   /id="PRO_0000080256"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..447
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        432
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   447 AA;  51620 MW;  6133706F353A8A4E CRC64;
     MSVFGFDNIP TWLWWLLAIY LATPFVLYVV QPYLFYEGKS TKTRILIVVL GDLGHSPRIL
     YHARSFSKAG FQVELSGYVD SDIPTDILDD DNIEIHGLKK YGSEKGLLVK ALKQGLQLCS
     MFWKLRAVDY ILLQNPPTIP ILPIAVVVKT FSRAKLIIDW HNLGYTILQM KFKDQFLHPL
     VLLAYLIEWI FAKFANYHLT VTKAMKTYLV EKFGIDGKKI AVLYDRPGKQ FSPLKEADDR
     EALLKQEFIA KYIPKEFDIS KDKIFVTSTS FTPDEDISVL IGSFKIYENS FQKFDQTLPR
     ILCFITGKGP LQEKIVKQVQ DFKWDRVQVE FLWLSSEDYP KLLRLCDYGV SLHTSSSGLD
     LPMKILDMFG SGLPVICMNY PVLDELVQQN VNGLKFADRR ELHEALIFSV KDEQVHQEIK
     RGALRESKNR WNESWESALS ELKIIHK