A4GCT_HUMAN
ID A4GCT_HUMAN Reviewed; 340 AA.
AC Q9UNA3; Q0VDK1; Q0VDK2;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Alpha-1,4-N-acetylglucosaminyltransferase;
DE Short=Alpha4GnT;
DE EC=2.4.1.- {ECO:0000269|PubMed:10430883};
GN Name=A4GNT;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Stomach;
RX PubMed=10430883; DOI=10.1073/pnas.96.16.8991;
RA Nakayama J., Yeh J.-C., Misra A.K., Ito S., Katsuyama T., Fukuda M.;
RT "Expression cloning of a human alpha1, 4-N-acetylglucosaminyltransferase
RT that forms GlcNAcalpha1-->4Galbeta-->R, a glycan specifically expressed in
RT the gastric gland mucous cell-type mucin.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8991-8996(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-218.
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).
CC -!- FUNCTION: Catalyzes the transfer of N-acetylglucosamine (GlcNAc) to
CC core 2 branched O-glycans (PubMed:10430883). Necessary for the
CC synthesis of type III mucin which is specifically produced in the
CC stomach, duodenum, and pancreatic duct (PubMed:10430883). May protect
CC against inflammation-associated gastric adenocarcinomas (By
CC similarity). {ECO:0000250|UniProtKB:Q14BT6,
CC ECO:0000269|PubMed:10430883}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000305|PubMed:10430883}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in stomach and pancreas.
CC {ECO:0000269|PubMed:10430883}.
CC -!- DOMAIN: The conserved DXD motif is involved in enzyme activity.
CC {ECO:0000250|UniProtKB:Q9JI93}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 32 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Alpha-
CC 1,4-N-acetylglucosaminyltransferase;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_532";
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DR EMBL; AF141315; AAD48406.1; -; mRNA.
DR EMBL; BC119639; AAI19640.1; -; mRNA.
DR EMBL; BC119640; AAI19641.1; -; mRNA.
DR CCDS; CCDS3097.1; -.
DR RefSeq; NP_057245.1; NM_016161.2.
DR RefSeq; XP_016862032.1; XM_017006543.1.
DR RefSeq; XP_016862033.1; XM_017006544.1.
DR AlphaFoldDB; Q9UNA3; -.
DR BioGRID; 119330; 59.
DR IntAct; Q9UNA3; 11.
DR STRING; 9606.ENSP00000236709; -.
DR CAZy; GT32; Glycosyltransferase Family 32.
DR GlyGen; Q9UNA3; 4 sites.
DR PhosphoSitePlus; Q9UNA3; -.
DR BioMuta; A4GNT; -.
DR DMDM; 25452797; -.
DR MassIVE; Q9UNA3; -.
DR PaxDb; Q9UNA3; -.
DR PeptideAtlas; Q9UNA3; -.
DR PRIDE; Q9UNA3; -.
DR ProteomicsDB; 85276; -.
DR Antibodypedia; 2373; 362 antibodies from 35 providers.
DR DNASU; 51146; -.
DR Ensembl; ENST00000236709.4; ENSP00000236709.3; ENSG00000118017.4.
DR GeneID; 51146; -.
DR KEGG; hsa:51146; -.
DR MANE-Select; ENST00000236709.4; ENSP00000236709.3; NM_016161.3; NP_057245.1.
DR UCSC; uc003ers.2; human.
DR CTD; 51146; -.
DR DisGeNET; 51146; -.
DR GeneCards; A4GNT; -.
DR HGNC; HGNC:17968; A4GNT.
DR HPA; ENSG00000118017; Tissue enriched (stomach).
DR neXtProt; NX_Q9UNA3; -.
DR OpenTargets; ENSG00000118017; -.
DR PharmGKB; PA134960042; -.
DR VEuPathDB; HostDB:ENSG00000118017; -.
DR eggNOG; KOG1928; Eukaryota.
DR GeneTree; ENSGT00510000047981; -.
DR HOGENOM; CLU_049512_2_0_1; -.
DR InParanoid; Q9UNA3; -.
DR OMA; KIYPEWP; -.
DR OrthoDB; 1082380at2759; -.
DR PhylomeDB; Q9UNA3; -.
DR TreeFam; TF324053; -.
DR PathwayCommons; Q9UNA3; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SignaLink; Q9UNA3; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 51146; 6 hits in 1060 CRISPR screens.
DR ChiTaRS; A4GNT; human.
DR GenomeRNAi; 51146; -.
DR Pharos; Q9UNA3; Tbio.
DR PRO; PR:Q9UNA3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UNA3; protein.
DR Bgee; ENSG00000118017; Expressed in pylorus and 69 other tissues.
DR Genevisible; Q9UNA3; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IDA:MGI.
DR GO; GO:0016758; F:hexosyltransferase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; IDA:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
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 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..340
FT /note="Alpha-1,4-N-acetylglucosaminyltransferase"
FT /id="PRO_0000080583"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..340
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOTIF 167..169
FT /note="DXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9JI93"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 218
FT /note="A -> D (in dbSNP:rs2246945)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_022096"
SQ SEQUENCE 340 AA; 39497 MW; 00D667A8394300AB CRC64;
MRKELQLSLS VTLLLVCGFL YQFTLKSSCL FCLPSFKSHQ GLEALLSHRR GIVFLETSER
MEPPHLVSCS VESAAKIYPE WPVVFFMKGL TDSTPMPSNS TYPAFSFLSA IDNVFLFPLD
MKRLLEDTPL FSWYNQINAS AERNWLHISS DASRLAIIWK YGGIYMDTDV ISIRPIPEEN
FLAAQASRYS SNGIFGFLPH HPFLWECMEN FVEHYNSAIW GNQGPELMTR MLRVWCKLED
FQEVSDLRCL NISFLHPQRF YPISYREWRR YYEVWDTEPS FNVSYALHLW NHMNQEGRAV
IRGSNTLVEN LYRKHCPRTY RDLIKGPEGS VTGELGPGNK
