ID   GNT1A_KLULA             Reviewed;         460 AA.
AC   Q9Y761; Q6CWL7;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Glucose N-acetyltransferase 1-A;
DE            EC=2.4.1.-;
DE   AltName: Full=N-acetylglucosaminyltransferase A;
GN   Name=GNT1-A; OrderedLocusNames=KLLA0B03135g;
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 [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 201343 / MG1/2;
RX   PubMed=10037760; DOI=10.1074/jbc.274.10.6641;
RA   Guillen E., Abeijon C., Hirschberg C.B.;
RT   "The genes for the Golgi apparatus N-acetylglucosaminyltransferase and the
RT   UDP-N-acetylglucosamine transporter are contiguous in Kluyveromyces
RT   lactis.";
RL   J. Biol. Chem. 274:6641-6646(1999).
RN   [2]
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: N-acetylglucosaminyltransferase involved in the Golgi-
CC       specific modification of N-linked glycans. {ECO:0000250,
CC       ECO:0000269|PubMed:10037760}.
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; AF106080; AAD25740.1; -; Genomic_DNA.
DR   EMBL; CR382122; CAH02065.1; -; Genomic_DNA.
DR   RefSeq; XP_451672.1; XM_451672.1.
DR   AlphaFoldDB; Q9Y761; -.
DR   STRING; 28985.XP_451672.1; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   EnsemblFungi; CAH02065; CAH02065; KLLA0_B03135g.
DR   GeneID; 2896915; -.
DR   KEGG; kla:KLLA0_B03135g; -.
DR   eggNOG; KOG1950; Eukaryota.
DR   HOGENOM; CLU_034860_1_0_1; -.
DR   InParanoid; Q9Y761; -.
DR   OMA; DSEEICN; -.
DR   Proteomes; UP000000598; Chromosome B.
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..460
FT                   /note="Glucose N-acetyltransferase 1-A"
FT                   /id="PRO_0000087529"
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..453
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           197..199
FT                   /note="DXD"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        326
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        344
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   460 AA;  53169 MW;  9163B78C47590A2F CRC64;
     MAFGSRRKIK AILVAASAMV FISLLGTFGS DSVYEKIKTF DVSWGSNVSG GLSSMLQKKK
     TVLYDPENIK QIPYSTIQKL YDHELESVTN IDWSQYAYVN YVADKNYVCS SMIHFNRLHE
     SGTQAKLVML VAKELTELPE DDSVTRMLAQ FKEISDNCIV KPVENIVLSQ GSAQWMTSMT
     KLRVFGMVEY KRIVYFDSDS IITRNMDELF FLPDYIQFAA PATYWFLNDN DLPQLIEDNK
     QIALANNQTA ELTEIEDILQ QKIDDSEDIY NFLPNLPKRL YPKSDNARID STDNTYFKYA
     ATLMVIKPEQ EMFERLEQEV LPKYLNTTNK YDMDLINIEF YDFNGTAEAQ KKLYDQSPQS
     FKPSMLVLPF NQYTLLTKTI REKNRVKLLS NDMLGYETKK PTDFRDASYY HFSDSPIGKP
     WKYKGLEDIP CNPGDSEEIC NAWHSIFSNF WDGRAKYCVA