GNT1_ASPFU
ID GNT1_ASPFU Reviewed; 384 AA.
AC Q4WBL2;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Glucose N-acetyltransferase 1;
DE EC=2.4.1.-;
DE AltName: Full=N-acetylglucosaminyltransferase;
GN Name=gnt1; ORFNames=AFUA_8G02690;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000014; EAL84900.1; -; Genomic_DNA.
DR RefSeq; XP_746938.1; XM_741845.1.
DR AlphaFoldDB; Q4WBL2; -.
DR STRING; 746128.CADAFUBP00008167; -.
DR PRIDE; Q4WBL2; -.
DR EnsemblFungi; EAL84900; EAL84900; AFUA_8G02690.
DR GeneID; 3504359; -.
DR KEGG; afm:AFUA_8G02690; -.
DR VEuPathDB; FungiDB:Afu8g02690; -.
DR eggNOG; KOG1950; Eukaryota.
DR HOGENOM; CLU_034860_1_0_1; -.
DR InParanoid; Q4WBL2; -.
DR OMA; CRDREVW; -.
DR OrthoDB; 1424146at2759; -.
DR Proteomes; UP000002530; Chromosome 8.
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:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:InterPro.
DR GO; GO:0043934; P:sporulation; IEA:UniProt.
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..384
FT /note="Glucose N-acetyltransferase 1"
FT /id="PRO_0000087531"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..57
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..384
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOTIF 185..187
FT /note="DXD"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 384 AA; 44512 MW; 92212120ABF85377 CRC64;
MGNKKATLLP YRRDSASSEA DFFDIPDEPC LAIAKRQLRR IRTWIFFAVF IILILWFRRE
APSPAPVSHI DYNKVDWSRY AYSQYATSSA YLCNAVMVFE ALERLGSRAD RVLFYPEDWD
LFVADDHDRD SQLLVLAKEK YKALLVPISA EMIKAGGGSG ESWDKSIAKL LAFGETEYDR
VIHIDSDVTV LQSMDELFFL PPAKVAMPRA YWALPDTKTL SSLLIVIEPS YREFKALMES
AQPALHGQVE VDSNETQRYD MELLNNRYAD SALVLPHRQY GLVTGEFRKK DHRSFFGNDY
ETWDPDKVLA EAKLVHFSDW PLPKPWVLSN QKLLAEILPK CDFKPGTMQE RGCRDREVWK
SLYEDFRRRR KVCPKIRTIH TEYG