ID   GNT1_CANGA              Reviewed;         501 AA.
AC   Q6FQ15;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Glucose N-acetyltransferase 1;
DE            EC=2.4.1.-;
DE   AltName: Full=N-acetylglucosaminyltransferase;
GN   Name=GNT1; OrderedLocusNames=CAGL0I09922g;
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: N-acetylglucosaminyltransferase involved in the Golgi-
CC       specific modification of N-linked glycans.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC       pass type II membrane protein {ECO:0000305}. Vacuole membrane
CC       {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GNT1 family. {ECO:0000305}.
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DR   EMBL; CR380955; CAG60616.1; -; Genomic_DNA.
DR   RefSeq; XP_447679.1; XM_447679.1.
DR   AlphaFoldDB; Q6FQ15; -.
DR   STRING; 5478.XP_447679.1; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   EnsemblFungi; CAG60616; CAG60616; CAGL0I09922g.
DR   GeneID; 2889277; -.
DR   KEGG; cgr:CAGL0I09922g; -.
DR   CGD; CAL0130352; CAGL0I09922g.
DR   VEuPathDB; FungiDB:CAGL0I09922g; -.
DR   eggNOG; KOG1950; Eukaryota.
DR   HOGENOM; CLU_034860_1_0_1; -.
DR   InParanoid; Q6FQ15; -.
DR   OMA; ILPHRVY; -.
DR   Proteomes; UP000002428; Chromosome I.
DR   GO; GO:0005797; C:Golgi medial cisterna; IEA:EnsemblFungi.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008375; F:acetylglucosaminyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:EnsemblFungi.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR002495; Glyco_trans_8.
DR   InterPro; IPR030518; GNT1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR11183:SF121; PTHR11183:SF121; 1.
DR   Pfam; PF01501; Glyco_transf_8; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix; Vacuole.
FT   CHAIN           1..501
FT                   /note="Glucose N-acetyltransferase 1"
FT                   /id="PRO_0000087533"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..501
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           197..199
FT                   /note="DXD"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   501 AA;  58333 MW;  2D304213BCF509E6 CRC64;
     MRLVSRRRLK GLALVAFALI GITIFVRILM EFQLEREVSF YKKFFRLKKD GLHGVYNPID
     IKQIPKQTID DLYRAKMETV SASKPIDWSK YAYVNYVTEP NYLCNTLIMF HALIKKFGTK
     AKLELLISNE LFKSEIQSRN EQVQRILKKI RELDSEQIVI KEVQNIVKPT DQSPWNESLT
     KLLVFGLTEY ERIIYLDNDA ILQDKMDELF FLPNDITFAA PLTYWFMSEK DLEKTYKEVQ
     HDKMSINLNK YTKQLSNRIR NGKEIYNHLP ALPQSLYLNS DRVAKEILDS TSSASPLFDA
     DSLKKVGKVK FASNLMVIKP SQETYDYIIN DCLPRIVNKK EKYDMDLINE ELYNLRHVVS
     RQVTLFRKLR SAFKPSILVL PFGTYGILTG SIRKPQEHMI MRNDILGYKN IDDEGNEIQK
     SIEEVVLNNK YIHFSDFPLG KPWAYSSFDQ LKCRVDPASS KDVAADQKNC DVWNSIYESY
     FTQRMVCSKD DSPKASEIQA A