ID MGAT1_RABIT Reviewed; 447 AA. AC P27115; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 24-JAN-2024, entry version 130. DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase; DE EC=2.4.1.101 {ECO:0000269|PubMed:1824724}; 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 Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC RP ACTIVITY, AND PATHWAY. RX PubMed=1824724; DOI=10.1073/pnas.88.1.234; RA Sarkar M., Hull E., Nishikawa Y., Simpson R.J., Moritz R.L., Dunn R., RA Schachter H.; RT "Molecular cloning and expression of cDNA encoding the enzyme that controls RT conversion of high-mannose to hybrid and complex N-glycans: UDP-N- RT acetylglucosamine: alpha-3-D-mannoside beta-1,2-N- RT acetylglucosaminyltransferase I."; RL Proc. Natl. Acad. Sci. U.S.A. 88:234-238(1991). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 106-447 ALONE AND IN COMPLEX WITH RP UDP-GLCNAC, ACTIVE SITE, COFACTOR, MANGANESE-BINDING SITE, RP SUBSTRATE-BINDING SITES, AND DISULFIDE BONDS. RX PubMed=11032794; DOI=10.1093/emboj/19.20.5269; RA Unligil U.M., Zhou S., Yuwaraj S., Sarkar M., Schachter H., Rini J.M.; RT "X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: RT catalytic mechanism and a new protein superfamily."; RL EMBO J. 19:5269-5280(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 106-447 IN COMPLEX WITH SUBSTRATE RP ANALOGS, MANGANESE-BINDING SITE, AND DISULFIDE BONDS. RX PubMed=16769084; DOI=10.1016/j.jmb.2006.04.058; RA Gordon R.D., Sivarajah P., Satkunarajah M., Ma D., Tarling C.A., RA Vizitiu D., Withers S.G., Rini J.M.; RT "X-ray crystal structures of rabbit N-acetylglucosaminyltransferase I (GnT RT I) in complex with donor substrate analogues."; RL J. Mol. Biol. 360:67-79(2006). CC -!- FUNCTION: Initiates complex N-linked carbohydrate formation. Essential CC for the conversion of high-mannose to hybrid and complex N-glycans. CC {ECO:0000269|PubMed:1824724}. 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 Evidence={ECO:0000269|PubMed:1824724}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:11032794}; CC Note=The cofactor is mostly bound to the substrate. CC {ECO:0000269|PubMed:11032794}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000269|PubMed:1824724}. 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 CC {ECO:0000250|UniProtKB:P26572}; Single-pass type II membrane protein CC {ECO:0000250|UniProtKB:P26572}. Cytoplasm, perinuclear region CC {ECO:0000250|UniProtKB:P26572}. Note=Co-localizes with BRI3 at the CC perinuclear region. {ECO:0000250|UniProtKB:P26572}. 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; M57301; AAA31493.1; -; mRNA. DR PIR; A38561; A38561. DR RefSeq; NP_001076214.1; NM_001082745.1. DR PDB; 1FO8; X-ray; 1.40 A; A=106-447. DR PDB; 1FO9; X-ray; 1.50 A; A=106-447. DR PDB; 1FOA; X-ray; 1.80 A; A=106-447. DR PDB; 2AM3; X-ray; 1.80 A; A=106-447. DR PDB; 2AM4; X-ray; 1.70 A; A=106-447. DR PDB; 2AM5; X-ray; 1.60 A; A=106-447. DR PDB; 2APC; X-ray; 1.50 A; A=106-447. DR PDBsum; 1FO8; -. DR PDBsum; 1FO9; -. DR PDBsum; 1FOA; -. DR PDBsum; 2AM3; -. DR PDBsum; 2AM4; -. DR PDBsum; 2AM5; -. DR PDBsum; 2APC; -. DR AlphaFoldDB; P27115; -. DR SMR; P27115; -. DR STRING; 9986.ENSOCUP00000037416; -. DR CAZy; GT13; Glycosyltransferase Family 13. DR Ensembl; ENSOCUT00000006540.3; ENSOCUP00000037416.1; ENSOCUG00000006544.3. DR GeneID; 100009521; -. DR KEGG; ocu:100009521; -. DR CTD; 4245; -. DR GeneTree; ENSGT00530000063632; -. DR InParanoid; P27115; -. DR OrthoDB; 4580at2759; -. DR BRENDA; 2.4.1.101; 1749. DR SABIO-RK; P27115; -. DR UniPathway; UPA00378; -. DR EvolutionaryTrace; P27115; -. DR Proteomes; UP000001811; Chromosome 11. DR Bgee; ENSOCUG00000006544; Expressed in left lung and 15 other cell types or tissues. DR GO; GO:0005797; C:Golgi medial cisterna; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003827; F:alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity; ISS:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB. DR GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; IDA:UniProtKB. DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl. DR GO; GO:0006013; P:mannose metabolic process; IDA:UniProtKB. DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:UniProtKB. DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB. DR GO; GO:0006049; P:UDP-N-acetylglucosamine catabolic process; IEA:Ensembl. 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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond; KW Glycosyltransferase; Golgi apparatus; Manganese; Membrane; Metal-binding; KW Reference proteome; Signal-anchor; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..447 FT /note="Alpha-1,3-mannosyl-glycoprotein 2-beta-N- FT acetylglucosaminyltransferase" FT /id="PRO_0000191387" 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:0000269|PubMed:11032794, FT ECO:0000269|PubMed:16769084, ECO:0007744|PDB:1FOA, FT ECO:0007744|PDB:2AM3, ECO:0007744|PDB:2AM4, FT ECO:0007744|PDB:2AM5, ECO:0007744|PDB:2APC" FT BINDING 144 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:11032794, FT ECO:0000269|PubMed:16769084, ECO:0007744|PDB:1FOA, FT ECO:0007744|PDB:2AM3, ECO:0007744|PDB:2AM4, FT ECO:0007744|PDB:2AM5, ECO:0007744|PDB:2APC" FT BINDING 190 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:11032794, FT ECO:0000269|PubMed:16769084, ECO:0007744|PDB:1FOA, FT ECO:0007744|PDB:2AM3, ECO:0007744|PDB:2AM4, FT ECO:0007744|PDB:2AM5, ECO:0007744|PDB:2APC" FT BINDING 212 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:11032794, FT ECO:0000269|PubMed:16769084, ECO:0007744|PDB:1FOA, FT ECO:0007744|PDB:2AM3, ECO:0007744|PDB:2AM4, FT ECO:0007744|PDB:2AM5, ECO:0007744|PDB:2APC" FT BINDING 213 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000269|PubMed:11032794, FT ECO:0007744|PDB:1FOA" FT BINDING 322 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:11032794, FT ECO:0000269|PubMed:16769084, ECO:0007744|PDB:1FOA, FT ECO:0007744|PDB:2AM3, ECO:0007744|PDB:2AM4, FT ECO:0007744|PDB:2AM5" FT DISULFID 115..145 FT /evidence="ECO:0000269|PubMed:11032794, FT ECO:0000269|PubMed:16769084, ECO:0007744|PDB:1FO8, FT ECO:0007744|PDB:1FO9, ECO:0007744|PDB:1FOA, FT ECO:0007744|PDB:2AM3, ECO:0007744|PDB:2AM4, FT ECO:0007744|PDB:2AM5, ECO:0007744|PDB:2APC" FT DISULFID 239..305 FT /evidence="ECO:0000269|PubMed:11032794, FT ECO:0000269|PubMed:16769084, ECO:0007744|PDB:1FO8, FT ECO:0007744|PDB:1FO9, ECO:0007744|PDB:1FOA, FT ECO:0007744|PDB:2AM3, ECO:0007744|PDB:2AM4, FT ECO:0007744|PDB:2AM5, ECO:0007744|PDB:2APC" FT STRAND 110..116 FT /evidence="ECO:0007829|PDB:1FO8" FT HELIX 120..130 FT /evidence="ECO:0007829|PDB:1FO8" FT TURN 134..136 FT /evidence="ECO:0007829|PDB:1FO8" FT STRAND 139..143 FT /evidence="ECO:0007829|PDB:1FO8" FT HELIX 148..155 FT /evidence="ECO:0007829|PDB:1FO8" FT HELIX 156..160 FT /evidence="ECO:0007829|PDB:1FO8" FT STRAND 161..165 FT /evidence="ECO:0007829|PDB:1FO8" FT HELIX 179..181 FT /evidence="ECO:0007829|PDB:1FO8" FT HELIX 182..199 FT /evidence="ECO:0007829|PDB:1FO8" FT STRAND 205..211 FT /evidence="ECO:0007829|PDB:1FO8" FT STRAND 214..216 FT /evidence="ECO:0007829|PDB:1FO8" FT HELIX 220..233 FT /evidence="ECO:0007829|PDB:1FO8" FT STRAND 237..242 FT /evidence="ECO:0007829|PDB:1FO8" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:1FO8" FT STRAND 260..265 FT /evidence="ECO:0007829|PDB:1FO8" FT STRAND 269..274 FT /evidence="ECO:0007829|PDB:1FO8" FT HELIX 275..281 FT /evidence="ECO:0007829|PDB:1FO8" FT HELIX 282..284 FT /evidence="ECO:0007829|PDB:1FO8" FT HELIX 290..294 FT /evidence="ECO:0007829|PDB:1FO8" FT HELIX 297..300 FT /evidence="ECO:0007829|PDB:1FO8" FT STRAND 304..315 FT /evidence="ECO:0007829|PDB:1FO8" FT STRAND 318..322 FT /evidence="ECO:0007829|PDB:2APC" FT HELIX 325..329 FT /evidence="ECO:0007829|PDB:2APC" FT HELIX 331..333 FT /evidence="ECO:0007829|PDB:2APC" FT HELIX 343..345 FT /evidence="ECO:0007829|PDB:1FO8" FT HELIX 349..351 FT /evidence="ECO:0007829|PDB:1FO8" FT HELIX 353..366 FT /evidence="ECO:0007829|PDB:1FO8" FT HELIX 372..376 FT /evidence="ECO:0007829|PDB:1FO8" FT STRAND 384..389 FT /evidence="ECO:0007829|PDB:1FO8" FT HELIX 393..402 FT /evidence="ECO:0007829|PDB:1FO8" FT STRAND 421..426 FT /evidence="ECO:0007829|PDB:1FO8" FT STRAND 429..434 FT /evidence="ECO:0007829|PDB:1FO8" SQ SEQUENCE 447 AA; 51540 MW; 18AC90994F0EB435 CRC64; MLKKQSAGLV LWGAILFVAW NALLLLFFWT RPVPSRLPSD NALDDDPASL TREVIRLAQD AEVELERQRG LLQQIREHHA LWSQRWKVPT AAPPAQPHVP VTPPPAVIPI LVIACDRSTV RRCLDKLLHY RPSAELFPII VSQDCGHEET AQVIASYGSA VTHIRQPDLS NIAVQPDHRK FQGYYKIARH YRWALGQIFH NFNYPAAVVV EDDLEVAPDF FEYFQATYPL LKADPSLWCV SAWNDNGKEQ MVDSSKPELL YRTDFFPGLG WLLLAELWAE LEPKWPKAFW DDWMRRPEQR KGRACVRPEI SRTMTFGRKG VSHGQFFDQH LKFIKLNQQF VPFTQLDLSY LQQEAYDRDF LARVYGAPQL QVEKVRTNDR KELGEVRVQY TGRDSFKAFA KALGVMDDLK SGVPRAGYRG IVTFLFRGRR VHLAPPQTWD GYDPSWT //