MGAT1_RABIT
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 03-AUG-2022, entry version 127.
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}.
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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 CAZy; GT13; Glycosyltransferase Family 13.
DR PRIDE; P27115; -.
DR Ensembl; ENSOCUT00000006540; ENSOCUP00000037416; ENSOCUG00000006544.
DR GeneID; 100009521; -.
DR KEGG; ocu:100009521; -.
DR CTD; 4245; -.
DR GeneTree; ENSGT00530000063632; -.
DR InParanoid; P27115; -.
DR OrthoDB; 1324622at2759; -.
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 tissues.
DR GO; GO:0005797; C:Golgi medial cisterna; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004139; Glyco_trans_13.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF03071; GNT-I; 1.
DR SUPFAM; SSF53448; SSF53448; 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
