MGAT2_ARATH
ID MGAT2_ARATH Reviewed; 430 AA.
AC Q9FT88; Q9SJ30;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase {ECO:0000305};
DE EC=2.4.1.143 {ECO:0000269|PubMed:11229321};
DE AltName: Full=Beta-1,2-N-acetylglucosaminyltransferase II {ECO:0000303|PubMed:11229321};
DE AltName: Full=GlcNAc-T II {ECO:0000303|PubMed:11229321};
DE Short=GNT-II {ECO:0000303|PubMed:11229321};
DE AltName: Full=Mannoside acetylglucosaminyltransferase 2 {ECO:0000305};
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II {ECO:0000303|PubMed:11229321};
GN Name=GNT2 {ECO:0000303|PubMed:11229321};
GN OrderedLocusNames=At2g05320 {ECO:0000312|Araport:AT2G05320};
GN ORFNames=F5G3.22 {ECO:0000312|EMBL:AAD29068.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Columbia;
RX PubMed=11229321; DOI=10.1023/a:1007127815012;
RA Strasser R., Steinkellner H., Boren M., Altmann F., Mach L., Gloessl J.,
RA Mucha J.;
RT "Molecular cloning of cDNA encoding N-acetylglucosaminyltransferase II from
RT Arabidopsis thaliana.";
RL Glycoconj. J. 16:787-791(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=24905498; DOI=10.1111/tpj.12577;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: Catalyzes an essential step in the conversion of oligo-
CC mannose and hybrid to complex N-glycans. {ECO:0000269|PubMed:11229321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-
CC asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) +
CC N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-
CC alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-
CC GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:12941,
CC Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:14369, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60615,
CC ChEBI:CHEBI:60651; EC=2.4.1.143;
CC Evidence={ECO:0000269|PubMed:11229321};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q10469};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:11229321}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 16 (GT16) protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD29068.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=The Arabidopsis glycosyltransferase collection;
CC Note=E7 GT16;
CC URL="http://gt.jbei.org/arabidopsis.html";
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DR EMBL; AJ249274; CAC08806.1; -; mRNA.
DR EMBL; KJ138918; AHL38858.1; -; mRNA.
DR EMBL; AC007018; AAD29068.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC05916.1; -; Genomic_DNA.
DR PIR; B84467; B84467.
DR RefSeq; NP_178601.2; NM_126556.3.
DR AlphaFoldDB; Q9FT88; -.
DR SMR; Q9FT88; -.
DR STRING; 3702.AT2G05320.1; -.
DR CAZy; GT16; Glycosyltransferase Family 16.
DR SwissPalm; Q9FT88; -.
DR PaxDb; Q9FT88; -.
DR PRIDE; Q9FT88; -.
DR ProteomicsDB; 238289; -.
DR EnsemblPlants; AT2G05320.1; AT2G05320.1; AT2G05320.
DR GeneID; 815080; -.
DR Gramene; AT2G05320.1; AT2G05320.1; AT2G05320.
DR KEGG; ath:AT2G05320; -.
DR Araport; AT2G05320; -.
DR TAIR; locus:2051279; AT2G05320.
DR eggNOG; KOG2791; Eukaryota.
DR HOGENOM; CLU_032753_1_0_1; -.
DR InParanoid; Q9FT88; -.
DR OMA; MHHKKTC; -.
DR OrthoDB; 647764at2759; -.
DR PhylomeDB; Q9FT88; -.
DR BioCyc; MetaCyc:MON-20298; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9FT88; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9FT88; baseline and differential.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0005795; C:Golgi stack; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008455; F:alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR007754; GlcNAc_II.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR12871; PTHR12871; 1.
DR Pfam; PF05060; MGAT2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Manganese; Membrane; Metal-binding; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..430
FT /note="Alpha-1,6-mannosyl-glycoprotein 2-beta-N-
FT acetylglucosaminyltransferase"
FT /id="PRO_0000439832"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 13..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..430
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT BINDING 104..108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 205..209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 237
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT BINDING 345
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 177..188
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT DISULFID 259..262
FT /evidence="ECO:0000250|UniProtKB:Q10469"
FT DISULFID 310..414
FT /evidence="ECO:0000250|UniProtKB:Q10469"
SQ SEQUENCE 430 AA; 48947 MW; 4CFF491AD490199D CRC64;
MANLWKKQRL RDTGLCRLGI LFAVTLSIVL MLVSVPRTAL NGSSIDDDLD GLDKDLEAKL
NASLLSVARG NRMSLRLHRR NHFSPRNTDL FPDLAKDRVV IVLYVHNRAQ YFRVTVESLS
KVKGISETLL IVSHDGYFEE MNRIVESIKF CQVKQIFSPY SPHIYRTSFP GVTLNDCKNK
GDEAKGHCEG NPDQYGNHRS PKIVSLKHHW WWMMNTVWDG LEETKGHEGH ILFIEEDHFL
FPNAYRNIQT LTRLKPAKCP DCFAANLAPS DVKSRGEGLE SLVAERMGNV GYSFNRSVWE
NIHQKAREFC FFDDYNWDIT MWATVFPSFG SPVYTLRGPR TSAVHFGKCG LHQGRGDEGD
CIDNGVVNIE VKETDKVVNI KEGWGVRVYK HQAGYKAGFE GWGGWGDDRD RHLCLDFATM
YRYSSSSASP
