ID MGAT1_RAT Reviewed; 447 AA. AC Q09325; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 24-JAN-2024, entry version 151. DE RecName: Full=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=Mgat1; Synonyms=Gnt1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Liver; RX PubMed=7764514; DOI=10.1271/bbb.58.200; RA Fukada T., Iida K., Kioka N., Sakai H., Komano T.; RT "Cloning of a cDNA encoding N-acetylglucosaminyltransferase I from rat RT liver and analysis of its expression in rat tissues."; RL Biosci. Biotechnol. Biochem. 58:200-201(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; 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: Initiates complex N-linked carbohydrate formation. Essential CC for the conversion of high-mannose to hybrid and complex N-glycans. 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 -!- SUBUNIT: Interacts with MGAT4D. Interacts with BRI3 (By similarity). CC {ECO:0000250|UniProtKB:P26572, ECO:0000250|UniProtKB:P27808}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type II CC membrane protein. Cytoplasm, perinuclear region CC {ECO:0000250|UniProtKB:P26572}. Note=Co-localizes with BRI3 at the CC perinuclear region. {ECO:0000250|UniProtKB:P26572}. CC -!- TISSUE SPECIFICITY: Appears to be present in all tissues. 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; D16302; BAA03807.1; -; mRNA. DR EMBL; BC074010; AAH74010.1; -; mRNA. DR PIR; JC2076; JC2076. DR RefSeq; NP_110488.1; NM_030861.1. DR RefSeq; XP_006246244.1; XM_006246182.3. DR RefSeq; XP_006246245.1; XM_006246183.3. DR RefSeq; XP_006246246.1; XM_006246184.3. DR RefSeq; XP_006246247.1; XM_006246185.3. DR RefSeq; XP_008765937.1; XM_008767715.2. DR AlphaFoldDB; Q09325; -. DR SMR; Q09325; -. DR IntAct; Q09325; 1. DR STRING; 10116.ENSRNOP00000068827; -. DR CAZy; GT13; Glycosyltransferase Family 13. DR iPTMnet; Q09325; -. DR PhosphoSitePlus; Q09325; -. DR jPOST; Q09325; -. DR PaxDb; 10116-ENSRNOP00000044560; -. DR Ensembl; ENSRNOT00000052360.2; ENSRNOP00000044560.1; ENSRNOG00000068826.1. DR Ensembl; ENSRNOT00000093956.1; ENSRNOP00000081587.1; ENSRNOG00000068826.1. DR Ensembl; ENSRNOT00000100116.1; ENSRNOP00000083147.1; ENSRNOG00000068826.1. DR Ensembl; ENSRNOT00000101283.1; ENSRNOP00000081858.1; ENSRNOG00000068826.1. DR Ensembl; ENSRNOT00000106126.1; ENSRNOP00000090215.1; ENSRNOG00000068826.1. DR Ensembl; ENSRNOT00000113892.1; ENSRNOP00000079270.1; ENSRNOG00000068826.1. DR Ensembl; ENSRNOT00000116725.1; ENSRNOP00000082878.1; ENSRNOG00000068826.1. DR Ensembl; ENSRNOT00055030999; ENSRNOP00055024983; ENSRNOG00055018286. DR Ensembl; ENSRNOT00055031006; ENSRNOP00055024989; ENSRNOG00055018286. DR Ensembl; ENSRNOT00055031011; ENSRNOP00055024994; ENSRNOG00055018286. DR Ensembl; ENSRNOT00055031027; ENSRNOP00055025008; ENSRNOG00055018286. DR Ensembl; ENSRNOT00055031033; ENSRNOP00055025014; ENSRNOG00055018286. DR Ensembl; ENSRNOT00055031037; ENSRNOP00055025018; ENSRNOG00055018286. DR Ensembl; ENSRNOT00055031046; ENSRNOP00055025027; ENSRNOG00055018286. DR Ensembl; ENSRNOT00060031138; ENSRNOP00060025238; ENSRNOG00060018162. DR Ensembl; ENSRNOT00060031156; ENSRNOP00060025254; ENSRNOG00060018162. DR Ensembl; ENSRNOT00060031166; ENSRNOP00060025264; ENSRNOG00060018162. DR Ensembl; ENSRNOT00060031183; ENSRNOP00060025281; ENSRNOG00060018162. DR Ensembl; ENSRNOT00060031187; ENSRNOP00060025285; ENSRNOG00060018162. DR Ensembl; ENSRNOT00060031194; ENSRNOP00060025292; ENSRNOG00060018162. DR Ensembl; ENSRNOT00060031218; ENSRNOP00060025315; ENSRNOG00060018162. DR Ensembl; ENSRNOT00065008954; ENSRNOP00065006373; ENSRNOG00065005942. DR Ensembl; ENSRNOT00065008956; ENSRNOP00065006375; ENSRNOG00065005942. DR Ensembl; ENSRNOT00065008957; ENSRNOP00065006376; ENSRNOG00065005942. DR Ensembl; ENSRNOT00065008959; ENSRNOP00065006377; ENSRNOG00065005942. DR Ensembl; ENSRNOT00065008962; ENSRNOP00065006380; ENSRNOG00065005942. DR Ensembl; ENSRNOT00065008963; ENSRNOP00065006381; ENSRNOG00065005942. DR Ensembl; ENSRNOT00065008965; ENSRNOP00065006383; ENSRNOG00065005942. DR GeneID; 81519; -. DR KEGG; rno:81519; -. DR UCSC; RGD:620097; rat. DR AGR; RGD:620097; -. DR CTD; 4245; -. DR RGD; 620097; Mgat1. DR eggNOG; KOG1413; Eukaryota. DR GeneTree; ENSGT00530000063632; -. DR HOGENOM; CLU_022150_0_0_1; -. DR InParanoid; Q09325; -. DR OMA; KGYDLSW; -. DR OrthoDB; 4580at2759; -. DR PhylomeDB; Q09325; -. DR TreeFam; TF320555; -. DR Reactome; R-RNO-964739; N-glycan trimming and elongation in the cis-Golgi. DR UniPathway; UPA00378; -. DR PRO; PR:Q09325; -. DR Proteomes; UP000002494; Chromosome 10. DR Bgee; ENSRNOG00000031208; Expressed in thymus and 19 other cell types or tissues. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:0000139; C:Golgi membrane; ISO:RGD. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; ISO:RGD. DR GO; GO:0003827; F:alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity; ISO:RGD. DR GO; GO:0030145; F:manganese ion binding; ISO:RGD. DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISO:RGD. DR GO; GO:0006049; P:UDP-N-acetylglucosamine catabolic process; ISO:RGD. 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. DR Genevisible; Q09325; RN. PE 2: Evidence at transcript level; KW Cytoplasm; Disulfide bond; Glycosyltransferase; Golgi apparatus; Manganese; KW Membrane; Metal-binding; Reference proteome; Signal-anchor; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1..447 FT /note="Alpha-1,3-mannosyl-glycoprotein 2-beta-N- FT acetylglucosaminyltransferase" FT /id="PRO_0000191386" FT TOPO_DOM 1..6 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 7..29 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 30..447 FT /note="Lumenal" FT /evidence="ECO:0000255" FT ACT_SITE 291 FT /note="Proton acceptor" FT /evidence="ECO:0000255" FT BINDING 117 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 144 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 190 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 212 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 213 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000250" FT BINDING 322 FT /ligand="substrate" FT /evidence="ECO:0000250" FT DISULFID 115..145 FT /evidence="ECO:0000250" FT DISULFID 239..305 FT /evidence="ECO:0000250" SQ SEQUENCE 447 AA; 51586 MW; 1AB54107072C53A2 CRC64; MLKKQSAGLV LWGAIIFVGW NALLLLFFWT RPAPGRLPSD SALGDDPASL TREVIHLAED AEAELERQRG LLQQIKEHYS LWRQRWRVPT VAPPAWPRVP GTPSPAVIPI LVIACDRSTV RRCLDKLLHY RPSAEHFPII VSQDCGHEET AQVIASYGTA VTHIRQPDLS NIAVQPDHRK FQGYYKIARH YRWALGQIFN KFKFPAAVVV EDDLEVAPDF FEYFQATYPL LKADPSLWCV SAWNDNGKEQ MVDSSKPELL YRTDFFPGLG WLLLADLWAE LEPKWPKAFW DDWMRRPEQR KGRACIRPEI SRTMTFGRKG VSHGQFFDQH LKFIKLNQQF VPFTQLDLSY LQREAYDRDF LAQVYGAPQL QVEKVRTNDR KELGEVRVQY TSRDSFKAFA KALGVMDDLK SGVPRAGYRG IVTFQFRGRR VHLAPPETWN GYDPSWN //