ID MGAT1_CAEEL Reviewed; 449 AA. AC Q11068; O76776; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 14-AUG-2001, sequence version 2. DT 27-MAR-2024, entry version 154. DE RecName: Full=Putative alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase; DE EC=2.4.1.101; DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I; DE Short=GNT-I; DE Short=GlcNAc-T I; GN Name=gly-13; ORFNames=B0416.6; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE. RX PubMed=9867843; DOI=10.1074/jbc.274.1.288; RA Chen S., Zhou S., Sarkar M., Spence A.M., Schachter H.; RT "Expression of three Caenorhabditis elegans N-acetylglucosaminyltransferase RT I genes during development."; RL J. Biol. Chem. 274:288-297(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). CC -!- FUNCTION: Initiates complex N-linked carbohydrate formation. Essential CC for the conversion of high-mannose to hybrid and complex N-glycans (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man- CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)- CC beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer CC 5A1,2) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D- CC GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man- CC (1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)- CC beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:11456, CC Rhea:RHEA-COMP:14367, Rhea:RHEA-COMP:14368, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:59087, CC ChEBI:CHEBI:60625; EC=2.4.1.101; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=The cofactor is mostly bound to the substrate. {ECO:0000250}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000250|UniProtKB:P26572}; Single-pass type II membrane protein CC {ECO:0000305}. Cytoplasm, perinuclear region CC {ECO:0000250|UniProtKB:P26572}. CC -!- DEVELOPMENTAL STAGE: Expressed throughout development. CC {ECO:0000269|PubMed:9867843}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 13 family. CC {ECO:0000305}. 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; AF082010; AAD03022.1; -; mRNA. DR EMBL; FO080200; CCD61925.1; -; Genomic_DNA. DR PIR; T43340; T43340. DR RefSeq; NP_509566.1; NM_077165.5. DR AlphaFoldDB; Q11068; -. DR SMR; Q11068; -. DR BioGRID; 46076; 7. DR STRING; 6239.B0416.6.1; -. DR CAZy; GT13; Glycosyltransferase Family 13. DR GlyCosmos; Q11068; 2 sites, No reported glycans. DR EPD; Q11068; -. DR PaxDb; 6239-B0416-6; -. DR PeptideAtlas; Q11068; -. DR EnsemblMetazoa; B0416.6.1; B0416.6.1; WBGene00001638. DR GeneID; 181160; -. DR KEGG; cel:CELE_B0416.6; -. DR UCSC; B0416.6; c. elegans. DR AGR; WB:WBGene00001638; -. DR WormBase; B0416.6; CE26434; WBGene00001638; gly-13. DR eggNOG; KOG1413; Eukaryota. DR GeneTree; ENSGT00530000063632; -. DR HOGENOM; CLU_022150_0_1_1; -. DR InParanoid; Q11068; -. DR OMA; KGYDLSW; -. DR OrthoDB; 4580at2759; -. DR PhylomeDB; Q11068; -. DR BRENDA; 2.4.1.101; 1045. DR Reactome; R-CEL-964739; N-glycan trimming and elongation in the cis-Golgi. DR UniPathway; UPA00378; -. DR PRO; PR:Q11068; -. DR Proteomes; UP000001940; Chromosome X. DR Bgee; WBGene00001638; Expressed in germ line (C elegans) and 4 other cell types or tissues. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:0005797; C:Golgi medial cisterna; ISS:WormBase. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase. DR GO; GO:0003827; F:alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity; ISS:WormBase. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:WormBase. DR CDD; cd02514; GT13_GLCNAC-TI; 1. DR Gene3D; 3.10.180.20; N-Acetylglucosaminyltransferase I, Domain 2; 1. DR InterPro; IPR004139; Glyco_trans_13. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR PANTHER; PTHR10468:SF0; ALPHA-1,3-MANNOSYL-GLYCOPROTEIN 2-BETA-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1. DR PANTHER; PTHR10468; PROTEIN O-LINKED-MANNOSE BETA-1,2-N-ACETYLGLUCOSAMINYLTRANSFERASE 1/ALPHA-1,3-MANNOSYL-GLYCOPROTEIN 2-BETA-N-ACETYLGLUCOSAMINYLTRANSFERASE; 1. DR Pfam; PF03071; GNT-I; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Disulfide bond; Glycoprotein; Glycosyltransferase; KW Golgi apparatus; Manganese; Membrane; Metal-binding; Reference proteome; KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..449 FT /note="Putative alpha-1,3-mannosyl-glycoprotein 2-beta-N- FT acetylglucosaminyltransferase" FT /id="PRO_0000191388" FT TOPO_DOM 1..6 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 7..23 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 24..449 FT /note="Lumenal" FT /evidence="ECO:0000255" FT ACT_SITE 279 FT /note="Proton acceptor" FT /evidence="ECO:0000255" FT BINDING 102 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 130 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 178 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 200 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 201 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250" FT BINDING 312 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CARBOHYD 28 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 159 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 100..131 FT /evidence="ECO:0000250" FT DISULFID 227..293 FT /evidence="ECO:0000250" SQ SEQUENCE 449 AA; 52151 MW; 8448210B2A78FC88 CRC64; MHAVTKIFII FIFVFILWTL YVENDITNRT RNTDNIDDLL ESANRLERLL KFEAKKIAAL AEDVHKIRAN RKGKHVIMEE MVSQDLKQWK DPIPVLVFSC NRAMAVRDHV EKLIRYRPSQ EKFPIIVTQD CDNENVKNEV KKFGDKVEYI KHLAGDKANI TIPPSHRQYT AYYRIARHYK LALNHVFVDK GYSSVIITED DLDISPDFFS YFSSTRYLLE NDEKLWCVTA WNDNGKQENI DMTAASTLYR SDFFAGLGWM MSSKTWHELE PIWPVGFWDD WMRDPARRKD RQCIRPEISR TGMMSYGKEG ASKGQFFSKH LAKIKVNDKY INFGKIDLDY LLPANFAKKT NLEVMKEAVE LSIDNVASFV LSSENKGKSV RVMYDGNIDY IRKADKLHIM HDFKAGVPRT AYDGIVTCFI NGIRIYLVPD RTKVSAYNPD WSVPPSFGE //