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GNT1_YEAST
ID   GNT1_YEAST              Reviewed;         491 AA.
AC   Q12096; D6W318;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=Glucose N-acetyltransferase 1;
DE            EC=2.4.1.-;
DE   AltName: Full=N-acetylglucosaminyltransferase;
GN   Name=GNT1; OrderedLocusNames=YOR320C; ORFNames=O6145;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8896266;
RX   DOI=10.1002/(sici)1097-0061(199609)12:10b<1021::aid-yea981>3.0.co;2-7;
RA   Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A.,
RA   Schweizer M.;
RT   "Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome
RT   XV reveals regions of similarity to chromosomes I and XIII.";
RL   Yeast 12:1021-1031(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   FUNCTION, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=12651885; DOI=10.1093/glycob/cwg063;
RA   Yoko-o T., Wiggins C.A.R., Stolz J., Peak-Chew S.Y., Munro S.;
RT   "An N-acetylglucosaminyltransferase of the Golgi apparatus of the yeast
RT   Saccharomyces cerevisiae that can modify N-linked glycans.";
RL   Glycobiology 13:581-589(2003).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16107716; DOI=10.1128/mcb.25.17.7696-7710.2005;
RA   Inadome H., Noda Y., Adachi H., Yoda K.;
RT   "Immunoisolation of the yeast Golgi subcompartments and characterization of
RT   a novel membrane protein, Svp26, discovered in the Sed5-containing
RT   compartments.";
RL   Mol. Cell. Biol. 25:7696-7710(2005).
CC   -!- FUNCTION: N-acetylglucosaminyltransferase involved in the Golgi-
CC       specific modification of N-linked glycans.
CC       {ECO:0000269|PubMed:12651885}.
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   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12651885}.
CC   -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the GNT1 family. {ECO:0000305}.
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DR   EMBL; X90565; CAA62175.1; -; Genomic_DNA.
DR   EMBL; Z75228; CAA99640.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA11084.1; -; Genomic_DNA.
DR   PIR; S58330; S58330.
DR   RefSeq; NP_014965.3; NM_001183740.3.
DR   AlphaFoldDB; Q12096; -.
DR   BioGRID; 34706; 62.
DR   DIP; DIP-2557N; -.
DR   STRING; 4932.YOR320C; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   MaxQB; Q12096; -.
DR   PaxDb; Q12096; -.
DR   PRIDE; Q12096; -.
DR   EnsemblFungi; YOR320C_mRNA; YOR320C; YOR320C.
DR   GeneID; 854498; -.
DR   KEGG; sce:YOR320C; -.
DR   SGD; S000005847; GNT1.
DR   VEuPathDB; FungiDB:YOR320C; -.
DR   eggNOG; KOG1950; Eukaryota.
DR   HOGENOM; CLU_034860_1_0_1; -.
DR   InParanoid; Q12096; -.
DR   OMA; ILPHRVY; -.
DR   BioCyc; YEAST:G3O-33800-MON; -.
DR   Reactome; R-SCE-3322077; Glycogen synthesis.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   Reactome; R-SCE-70221; Glycogen breakdown (glycogenolysis).
DR   PRO; PR:Q12096; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q12096; protein.
DR   GO; GO:0005797; C:Golgi medial cisterna; IDA:SGD.
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; IDA:SGD.
DR   GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IMP:SGD.
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   1: Evidence at protein level;
KW   Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix; Vacuole.
FT   CHAIN           1..491
FT                   /note="Glucose N-acetyltransferase 1"
FT                   /id="PRO_0000087536"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..31
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..491
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   MOTIF           198..200
FT                   /note="DXD"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        425
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   491 AA;  57578 MW;  22BD797B1EBF7A32 CRC64;
     MRLISKRRIR FIVFILFGVL TVFVVSRLVV HFQYNQEIKF YKKYFQQRKD GLHEIYNPLE
     IKQIPKETID DLYTARLDKE LKNGEVIEWS KFAYVNYVTN ADYLCNTLII FNDLKQEFET
     KAKLVLLISK DLLDPNTSSN VAYISSLLNK IQAIDEDQVV IKLIDNIVKP KDTTPWNESL
     TKLLVFNQTE FDRVIYLDND AILRSSLDEL FFLPNYIKFA APLTYWFLSN SDLEKSYHET
     RHREKQPINL QSYTKVLTKR IGKGQMIYNH LPSLPHSLYL NSNNIAQDII SSTSSLSPLF
     DFQSSKKVGK LKFASNLMVI NPSKEAFDEI VNVMLPKILN KKEKYDMDLI NEEMYNLKKI
     IYKQFIFFRK VRKLFKPEVL VLPFARYGLL TGSLRNPRHY SIIYNDVLGY KTLDNDGNDI
     PVGLNDSVAY SKYIHFSDYP LAKPWNYPSM KEFECIVKEE DAEDSKLEHQ ACDLWNSVYA
     SYIQSREICL V
 
 
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