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A4GCT_MOUSE
ID   A4GCT_MOUSE             Reviewed;         341 AA.
AC   Q14BT6;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Alpha-1,4-N-acetylglucosaminyltransferase {ECO:0000303|PubMed:22307328};
DE            Short=Alpha4GnT {ECO:0000303|PubMed:22307328};
DE            EC=2.4.1.- {ECO:0000305};
GN   Name=A4gnt {ECO:0000312|MGI:MGI:2143261};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000312|EMBL:AAI15616.1};
RN   [1] {ECO:0000312|EMBL:AC156497}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0000312|EMBL:EDL21015.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000312|EMBL:AAI15615.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4] {ECO:0000305}
RP   FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RX   PubMed=22307328; DOI=10.1172/jci59087;
RA   Karasawa F., Shiota A., Goso Y., Kobayashi M., Sato Y., Masumoto J.,
RA   Fujiwara M., Yokosawa S., Muraki T., Miyagawa S., Ueda M., Fukuda M.N.,
RA   Fukuda M., Ishihara K., Nakayama J.;
RT   "Essential role of gastric gland mucin in preventing gastric cancer in
RT   mice.";
RL   J. Clin. Invest. 122:923-934(2012).
CC   -!- FUNCTION: Catalyzes the transfer of N-acetylglucosamine (GlcNAc) to
CC       core 2 branched O-glycans. Necessary for the synthesis of type III
CC       mucin which is specifically produced in the stomach, duodenum, and
CC       pancreatic duct. May protect against inflammation-associated gastric
CC       adenocarcinoma. {ECO:0000269|PubMed:22307328}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000269|PubMed:22307328}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC       pass type II membrane protein {ECO:0000305}.
CC   -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC       {ECO:0000250|UniProtKB:Q9JI93}.
CC   -!- DISRUPTION PHENOTYPE: Viable with no gross defects. Gastric mucosa
CC       cells and duodenal Brunner's glands have an altered O-linked
CC       glycosylation profile with complete loss of terminal alpha-1,4-linked
CC       N-acetylglucosamine residues (alpha-GlcNAc). Animals develop
CC       spontaneous gastric adenocarcinomas, with all individuals affected by
CC       60 weeks of age. Hyperplasia of surface mucous cells and pyloric gland
CC       cells is observed as early as 5 weeks of age, associated with increased
CC       inflammatory responses in the gastric mucosa.
CC       {ECO:0000269|PubMed:22307328}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 32 family.
CC       {ECO:0000305}.
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DR   EMBL; AC156497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC157949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466560; EDL21015.1; -; Genomic_DNA.
DR   EMBL; BC115614; AAI15615.1; -; mRNA.
DR   EMBL; BC115615; AAI15616.1; -; mRNA.
DR   CCDS; CCDS40740.1; -.
DR   RefSeq; NP_001070892.1; NM_001077424.2.
DR   RefSeq; XP_006511309.1; XM_006511246.3.
DR   AlphaFoldDB; Q14BT6; -.
DR   STRING; 10090.ENSMUSP00000045629; -.
DR   CAZy; GT32; Glycosyltransferase Family 32.
DR   GlyGen; Q14BT6; 1 site.
DR   iPTMnet; Q14BT6; -.
DR   PhosphoSitePlus; Q14BT6; -.
DR   MaxQB; Q14BT6; -.
DR   PaxDb; Q14BT6; -.
DR   PRIDE; Q14BT6; -.
DR   ProteomicsDB; 296426; -.
DR   Antibodypedia; 2373; 362 antibodies from 35 providers.
DR   Ensembl; ENSMUST00000042553; ENSMUSP00000045629; ENSMUSG00000037953.
DR   GeneID; 333424; -.
DR   KEGG; mmu:333424; -.
DR   UCSC; uc009rej.2; mouse.
DR   CTD; 51146; -.
DR   MGI; MGI:2143261; A4gnt.
DR   VEuPathDB; HostDB:ENSMUSG00000037953; -.
DR   eggNOG; KOG1928; Eukaryota.
DR   GeneTree; ENSGT00510000047981; -.
DR   HOGENOM; CLU_049512_2_0_1; -.
DR   InParanoid; Q14BT6; -.
DR   OMA; KIYPEWP; -.
DR   OrthoDB; 1082380at2759; -.
DR   PhylomeDB; Q14BT6; -.
DR   TreeFam; TF324053; -.
DR   Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 333424; 1 hit in 71 CRISPR screens.
DR   ChiTaRS; A4gnt; mouse.
DR   PRO; PR:Q14BT6; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q14BT6; protein.
DR   Bgee; ENSMUSG00000037953; Expressed in epithelium of stomach and 31 other tissues.
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:0008375; F:acetylglucosaminyltransferase activity; IMP:MGI.
DR   GO; GO:0016758; F:hexosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0009101; P:glycoprotein biosynthetic process; ISO:MGI.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0006493; P:protein O-linked glycosylation; IMP:MGI.
DR   InterPro; IPR007652; A1-4-GlycosylTfrase_dom.
DR   InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF04572; Gb3_synth; 1.
DR   Pfam; PF04488; Gly_transf_sug; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..341
FT                   /note="Alpha-1,4-N-acetylglucosaminyltransferase"
FT                   /id="PRO_0000439855"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        5..25
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..341
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   MOTIF           168..170
FT                   /note="DXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JI93"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   341 AA;  39276 MW;  17733C8FAFC37A44 CRC64;
     MLKEIYLSLS LVLVFACGLL YQLTMRSQCF FACLPPFSFP QGLDGLLRSG RSIMFIETSE
     RVEPPPMVSC AVESAAKIYP EQPIIFFMKG LRDSVQLTSN TSYPAFSLLS AINNVFFVPL
     DMERLFKDTP LFSWYTKVNS STEKHWLHVS SDAARLAIIW KYGGIYMDTD VISLQPIPEE
     NFLAAQGSRH SSNGVFGFLP HHPFLWACME NFVEHYDSTI WGNQGPQLMT RMLRVWCRLK
     DFHGLGDLKC LNISFLHPQR FYPIPYPQWK RYYQVWDKEP SFNESYALHL WNYMNKEGKT
     VVRGSKTLVE NLYQKHCPKT YRVLIQGAEG TVSKKPGTGS R
 
 
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