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 27-MAR-2024, entry version 160. 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; CC Note=Alpha-1,4-N-acetylglucosaminyltransferase; CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_532"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; Q9UNA3; -. DR BioGRID; 119330; 59. DR IntAct; Q9UNA3; 11. DR STRING; 9606.ENSP00000236709; -. DR CAZy; GT32; Glycosyltransferase Family 32. DR GlyCosmos; Q9UNA3; 4 sites, No reported glycans. DR GlyGen; Q9UNA3; 4 sites. DR PhosphoSitePlus; Q9UNA3; -. DR BioMuta; A4GNT; -. DR DMDM; 25452797; -. DR MassIVE; Q9UNA3; -. DR PaxDb; 9606-ENSP00000236709; -. DR PeptideAtlas; Q9UNA3; -. DR Antibodypedia; 2373; 396 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 AGR; HGNC:17968; -. 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; IWDCMEN; -. DR OrthoDB; 2235518at2759; -. 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 1138 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 70 other cell types or tissues. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IDA:MGI. 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 Gene3D; 3.90.550.20; -; 1. DR InterPro; IPR007652; A1-4-GlycosylTfrase_dom. DR InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR12042:SF22; ALPHA-1,4-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1. DR PANTHER; PTHR12042; LACTOSYLCERAMIDE 4-ALPHA-GALACTOSYLTRANSFERASE ALPHA- 1,4-GALACTOSYLTRANSFERASE; 1. DR Pfam; PF04572; Gb3_synth; 1. DR Pfam; PF04488; Gly_transf_sug; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR Genevisible; Q9UNA3; HS. 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 //