ID   ALG1_ASHGO              Reviewed;         471 AA.
AC   Q75BA5;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
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=ADL338C;
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, AND SEQUENCE REVISION TO 457.
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: 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; AE016817; AAS51581.2; -; Genomic_DNA.
DR   RefSeq; NP_983757.2; NM_209110.2.
DR   AlphaFoldDB; Q75BA5; -.
DR   SMR; Q75BA5; -.
DR   STRING; 33169.AAS51581; -.
DR   CAZy; GT33; Glycosyltransferase Family 33.
DR   EnsemblFungi; AAS51581; AAS51581; AGOS_ADL338C.
DR   GeneID; 4619892; -.
DR   KEGG; ago:AGOS_ADL338C; -.
DR   eggNOG; KOG2941; Eukaryota.
DR   HOGENOM; CLU_012079_0_0_1; -.
DR   InParanoid; Q75BA5; -.
DR   OMA; PLKVLWQ; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000000591; Chromosome IV.
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   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR028098; Glyco_trans_4-like_N.
DR   PANTHER; PTHR13036; PTHR13036; 1.
DR   Pfam; PF13579; Glyco_trans_4_4; 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..471
FT                   /note="Chitobiosyldiphosphodolichol beta-
FT                   mannosyltransferase"
FT                   /id="PRO_0000080252"
FT   TOPO_DOM        1..31
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        53..471
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   471 AA;  53594 MW;  9A6CC706672C83AC CRC64;
     MDTSSVTMHT ERACCHQAQR AVAAMLDKAP SWLIWTAVLY VGLPFMLYWA VPYLFYHNKT
     KSRRIAIYVL GDLGHSPRIC YHARSFSAAG WEVELCGYLE EQPPKDLLDD PRVTIRALPG
     ASNAGKSLGQ TARKVVLQTC HIVRQLWELR GCDYILIQNP PSIPLLPIVA IFKVLTRTRL
     ILDWHNFAYT VLQLRVGRFL HPLVLVSYAV EFLFSRMADY HITVTAAMKD YLVQSFLLPA
     RRIAVMYDRP GEQFRPLPAG ERGAALAEPF IRGYIPAGFD VQRGDTILVT STSFTLDEDI
     NVLFGALKIY ESAAAKFDTT LPRILLFVTG KGPLKGKYME EVRNYKWERC TIHFLWLSAE
     DYPRLLQLCD FGVSLHTSTS GLDLPMKVLD MFGSGLPAFV MDYPAIGELV QDRVNGLRFT
     TRRELEQCLI FAIKDEHTRK VLKENALLES KNRWHQSWAS AMSELQVVRQ S