ID   ALG1_YARLI              Reviewed;         463 AA.
AC   Q6C3K2;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=YALI0E34133g;
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: 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       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       {ECO:0000305}.
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DR   EMBL; CR382131; CAG80366.1; -; Genomic_DNA.
DR   RefSeq; XP_504760.1; XM_504760.1.
DR   AlphaFoldDB; Q6C3K2; -.
DR   SMR; Q6C3K2; -.
DR   STRING; 4952.CAG80366; -.
DR   CAZy; GT33; Glycosyltransferase Family 33.
DR   EnsemblFungi; CAG80366; CAG80366; YALI0_E34133g.
DR   GeneID; 2911951; -.
DR   KEGG; yli:YALI0E34133g; -.
DR   VEuPathDB; FungiDB:YALI0_E34133g; -.
DR   HOGENOM; CLU_012079_0_0_1; -.
DR   InParanoid; Q6C3K2; -.
DR   OMA; PLKVLWQ; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:EnsemblFungi.
DR   InterPro; IPR026051; ALG1-like.
DR   PANTHER; PTHR13036; PTHR13036; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Glycosyltransferase; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..463
FT                   /note="Chitobiosyldiphosphodolichol beta-
FT                   mannosyltransferase"
FT                   /id="PRO_0000080258"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   463 AA;  52711 MW;  18D986BA71EBF758 CRC64;
     MKAWHWSVTL VVIYLAIPVI LYLLTRKDDR KPLSDIRKRK RTIVLVLGDL GRSPRMLYHA
     RSLARSGHKV DLCGYDGAKP FDEILNNDLI KIHHIPLILN TRKLPFVVFG ILKVIRQHWL
     LISLLYKLRG ADYLLVQNPP SIPTLGVVRF YNLFLSTRTK VVLDWHNFGY TILALKLPET
     HPMVKFAKFY EGFFGGRAFV HLCVTVLMGQ AMRKTFGMSG RRIVPLHDRP AFHFKPLSES
     EKLDVLRDFK ETLYDDMTAD HKIIVSSTSY TPDENFNILL DALALYDESK LDLPPLRVII
     TGKGPMMPEF LAKVEKLQLK RVSIRTAWLE FADYPRILGA AHLGVSLHES SSGYDLPMKV
     VDMFGCGIPV VSVDYAALSE LVKTNTNGVA VKGHVEMGNT FMSLFSNRGK LDNIKRGAMI
     ESRNTWDQTW VKTVGPLFDI GEYVQQRPDE DYDFSSSSSD DDH