ID   GNT1_DEBHA              Reviewed;         464 AA.
AC   Q6BUZ2;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Glucose N-acetyltransferase 1;
DE            EC=2.4.1.-;
DE   AltName: Full=N-acetylglucosaminyltransferase;
GN   Name=GNT1; OrderedLocusNames=DEHA2C06710g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}. Vacuole membrane
CC       {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GNT1 family. {ECO:0000305}.
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DR   EMBL; CR382135; CAG86035.2; -; Genomic_DNA.
DR   RefSeq; XP_457977.2; XM_457977.1.
DR   AlphaFoldDB; Q6BUZ2; -.
DR   STRING; 4959.XP_457977.2; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   EnsemblFungi; CAG86035; CAG86035; DEHA2C06710g.
DR   GeneID; 2899986; -.
DR   KEGG; dha:DEHA2C06710g; -.
DR   VEuPathDB; FungiDB:DEHA2C06710g; -.
DR   eggNOG; KOG1950; Eukaryota.
DR   HOGENOM; CLU_034860_1_2_1; -.
DR   InParanoid; Q6BUZ2; -.
DR   OMA; ILPHRVY; -.
DR   OrthoDB; 1424146at2759; -.
DR   Proteomes; UP000000599; Chromosome C.
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:InterPro.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:InterPro.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR030518; GNT1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR11183:SF121; PTHR11183:SF121; 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..464
FT                   /note="Glucose N-acetyltransferase 1"
FT                   /id="PRO_0000087534"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..35
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..464
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           167..169
FT                   /note="DXD"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        310
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   464 AA;  54445 MW;  D3966642BB7A5576 CRC64;
     MKLVLGNGLV NLSWEYMLSF SILLYFIFTQ LIFVFEDHSL AKNLKVIPSE VINALFDNFN
     KNLNFDKYAY VQYATDFDYL NLAIINFIVL RRSSTKIPNL VVLFNRALQE DKNRFDGLRD
     LSLRYSVTLK PIPIIENVNA ESPTWSKSFT KFHIFNEVKY DRIVYFDADS MLLHTQWNDN
     SSIVNNESNV PENLDELFTI PEIIDIALPQ AYWLTKHTKA SGKIKAPDGK GYQDEITALI
     NEISKSVNDS LVFEKLPSLL VQSQKSNHRN NFFATHVMVV KPSNEIFNEL KKYVHNPWLW
     SLHKRHALRN KSDYDMEVLN KFIDNVLQEN ENFKVGILPH KVYGVLTGEF RELSHESFVS
     EAQFLPFITG ELNEQWRPIE IIRNIKLIHF SDSPIPKPWE GMNNFHFYNK FRIYCHDAGF
     DADLFNSLFP TSWKPRLTTD CDSVNIWNWI MAEYQKLHNE LWMV