MGAT1_ARATH
ID MGAT1_ARATH Reviewed; 444 AA.
AC Q9XGM8; Q8VWR5; Q9SVG1; Q9SZM4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase {ECO:0000305};
DE EC=2.4.1.101 {ECO:0000269|PubMed:15537386};
DE AltName: Full=N-acetylglucosaminyltransferase I {ECO:0000303|PubMed:10889259};
DE Short=GlcNAcT-I {ECO:0000303|PubMed:10889259};
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I {ECO:0000305};
DE AltName: Full=Protein COMPLEX GLYCAN LESS 1 {ECO:0000303|PubMed:15537386};
GN Name=GNTI {ECO:0000303|PubMed:10889259};
GN Synonyms=CGL1 {ECO:0000303|PubMed:15537386};
GN OrderedLocusNames=At4g38240 {ECO:0000312|Araport:AT4G38240};
GN ORFNames=F20D10.360 {ECO:0000312|EMBL:CAB37564.1},
GN F22I13.10 {ECO:0000312|EMBL:CAB37480.1};
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], AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10441510; DOI=10.1006/bbrc.1999.1117;
RA Bakker H., Lommen A., Jordi W., Stiekema W., Bosch D.;
RT "An Arabidopsis thaliana cDNA complements the N-
RT acetylglucosaminyltransferase I deficiency of CHO Lec1 cells.";
RL Biochem. Biophys. Res. Commun. 261:829-832(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10889259; DOI=10.1104/pp.123.3.1097;
RA Wenderoth I., von Schaewen A.;
RT "Isolation and characterization of plant N-acetyl glucosaminyltransferase I
RT (GntI) cDNA sequences. Functional analyses in the Arabidopsis cgl mutant
RT and in antisense plants.";
RL Plant Physiol. 123:1097-1108(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8278542; DOI=10.1104/pp.102.4.1109;
RA von Schaewen A., Sturm A., O'Neill J., Chrispeels M.J.;
RT "Isolation of a mutant Arabidopsis plant that lacks N-acetyl glucosaminyl
RT transferase I and is unable to synthesize Golgi-modified complex N-linked
RT glycans.";
RL Plant Physiol. 102:1109-1118(1993).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8127889; DOI=10.1073/pnas.91.5.1829;
RA Gomez L., Chrispeels M.J.;
RT "Complementation of an Arabidopsis thaliana mutant that lacks complex
RT asparagine-linked glycans with the human cDNA encoding N-
RT acetylglucosaminyltransferase I.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1829-1833(1994).
RN [8]
RP MUTANT CGL1 C5, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15537386; DOI=10.1042/bj20041686;
RA Strasser R., Stadlmann J., Svoboda B., Altmann F., Gloessl J., Mach L.;
RT "Molecular basis of N-acetylglucosaminyltransferase I deficiency in
RT Arabidopsis thaliana plants lacking complex N-glycans.";
RL Biochem. J. 387:385-391(2005).
RN [9]
RP FUNCTION.
RX PubMed=18408158; DOI=10.1073/pnas.0800237105;
RA Kang J.S., Frank J., Kang C.H., Kajiura H., Vikram M., Ueda A., Kim S.,
RA Bahk J.D., Triplett B., Fujiyama K., Lee S.Y., von Schaewen A., Koiwa H.;
RT "Salt tolerance of Arabidopsis thaliana requires maturation of N-
RT glycosylated proteins in the Golgi apparatus.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5933-5938(2008).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-353, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18768906; DOI=10.1104/pp.108.127027;
RA Frank J., Kaulfuerst-Soboll H., Rips S., Koiwa H., von Schaewen A.;
RT "Comparative analyses of arabidopsis complex glycan1 mutants and genetic
RT interaction with staurosporin and temperature sensitive3a.";
RL Plant Physiol. 148:1354-1367(2008).
CC -!- FUNCTION: Initiates complex N-linked carbohydrate formation. Essential
CC for the conversion of high-mannose to hybrid and complex N-glycans.
CC Required for normal root growth and morphology.
CC {ECO:0000269|PubMed:10441510, ECO:0000269|PubMed:18408158,
CC ECO:0000269|PubMed:18768906, ECO:0000269|PubMed:8127889,
CC ECO:0000269|PubMed:8278542}.
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:15537386};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P27115};
CC Note=The cofactor is mostly bound to the substrate.
CC {ECO:0000250|UniProtKB:P27115};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for Man(5)-glycopeptide {ECO:0000269|PubMed:15537386};
CC KM=0.05 mM for UDP-GlcNAc {ECO:0000269|PubMed:15537386};
CC Vmax=3.42 umol/min/mg enzyme toward Man(5)-glycopeptide
CC {ECO:0000269|PubMed:15537386};
CC Vmax=0.09 umol/min/mg enzyme toward Man(3)-octyl
CC {ECO:0000269|PubMed:15537386};
CC Note=the apparent KM is >3.0 mM for Man(3)-octyl.;
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:18768906, ECO:0000269|PubMed:8127889}; Single-pass
CC type II membrane protein {ECO:0000269|PubMed:18768906,
CC ECO:0000269|PubMed:8127889}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9XGM8-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers.
CC {ECO:0000269|PubMed:10889259}.
CC -!- PTM: Glycosylated.
CC -!- DISRUPTION PHENOTYPE: Plants have an increased salt-sensitivity
CC resulting in growth inhibition, aberrant root-tip morphology and
CC callose accumulation. {ECO:0000269|PubMed:18768906,
CC ECO:0000269|PubMed:8278542}.
CC -!- MISCELLANEOUS: Creation of a second N-glycosylation site in mutant cgl1
CC C5/cgl1-1 interferes with protein folding and sequesters the protein
CC for degradation in the endoplasmic reticulum.
CC {ECO:0000269|PubMed:15537386}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 13 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB37480.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB37564.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80489.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ243198; CAB45521.1; -; mRNA.
DR EMBL; AJ249881; CAC80700.1; -; mRNA.
DR EMBL; AL035538; CAB37564.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL035539; CAB37480.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161593; CAB80489.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86902.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86903.1; -; Genomic_DNA.
DR EMBL; AY099838; AAM20689.1; -; mRNA.
DR EMBL; BT000334; AAN15653.1; -; mRNA.
DR PIR; JC7084; JC7084.
DR PIR; T05651; T05651.
DR RefSeq; NP_195537.2; NM_119986.3. [Q9XGM8-1]
DR RefSeq; NP_849517.1; NM_179186.1. [Q9XGM8-1]
DR AlphaFoldDB; Q9XGM8; -.
DR SMR; Q9XGM8; -.
DR BioGRID; 15261; 2.
DR STRING; 3702.AT4G38240.2; -.
DR CAZy; GT13; Glycosyltransferase Family 13.
DR SwissPalm; Q9XGM8; -.
DR PaxDb; Q9XGM8; -.
DR PRIDE; Q9XGM8; -.
DR EnsemblPlants; AT4G38240.1; AT4G38240.1; AT4G38240. [Q9XGM8-1]
DR EnsemblPlants; AT4G38240.2; AT4G38240.2; AT4G38240. [Q9XGM8-1]
DR GeneID; 829981; -.
DR Gramene; AT4G38240.1; AT4G38240.1; AT4G38240. [Q9XGM8-1]
DR Gramene; AT4G38240.2; AT4G38240.2; AT4G38240. [Q9XGM8-1]
DR KEGG; ath:AT4G38240; -.
DR Araport; AT4G38240; -.
DR TAIR; locus:2120993; AT4G38240.
DR eggNOG; KOG1413; Eukaryota.
DR HOGENOM; CLU_022150_1_1_1; -.
DR InParanoid; Q9XGM8; -.
DR OMA; KGYDLSW; -.
DR PhylomeDB; Q9XGM8; -.
DR BioCyc; MetaCyc:AT4G38240-MON; -.
DR BRENDA; 2.4.1.101; 399.
DR SABIO-RK; Q9XGM8; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9XGM8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9XGM8; baseline and differential.
DR Genevisible; Q9XGM8; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0005797; C:Golgi medial cisterna; HDA:TAIR.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0003827; F:alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity; IDA:TAIR.
DR GO; GO:0016757; F:glycosyltransferase activity; IMP:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; IMP:TAIR.
DR GO; GO:0006972; P:hyperosmotic response; IMP:TAIR.
DR GO; GO:0006491; P:N-glycan processing; IMP:TAIR.
DR GO; GO:0006486; P:protein glycosylation; IMP:TAIR.
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 Alternative splicing; Coiled coil; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..444
FT /note="Alpha-1,3-mannosyl-glycoprotein 2-beta-N-
FT acetylglucosaminyltransferase"
FT /id="PRO_0000356191"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..444
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT COILED 61..92
FT /evidence="ECO:0000255"
FT ACT_SITE 287
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P27115"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 144
FT /note="D->N: In cgl1 C5/cgl1-1; loss of activity due to
FT degradation in the reticulum endoplasmic."
FT MUTAGEN 353
FT /note="T->V: Loss of glycosylation. No effect on
FT localization and stability."
FT /evidence="ECO:0000269|PubMed:18768906"
FT CONFLICT 303
FT /note="R -> A (in Ref. 2; CAC80700)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="V -> D (in Ref. 2; CAC80700)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 51634 MW; B3DDCF221C526336 CRC64;
MARISCDLRF LLIPAAFMFI YIQMRLFQTQ SQYADRLSSA IESENHCTSQ MRGLIDEVSI
KQSRIVALED MKNRQDEELV QLKDLIQTFE KKGIAKLTQG GQMPVAAVVV MACSRADYLE
RTVKSVLTYQ TPVASKYPLF ISQDGSDQAV KSKSLSYNQL TYMQHLDFEP VVTERPGELT
AYYKIARHYK WALDQLFYKH KFSRVIILED DMEIAPDFFD YFEAAASLMD RDKTIMAASS
WNDNGQKQFV HDPYALYRSD FFPGLGWMLK RSTWDELSPK WPKAYWDDWL RLKENHKGRQ
FIRPEVCRTY NFGEHGSSLG QFFSQYLEPI KLNDVTVDWK AKDLGYLTEG NYTKYFSGLV
RQARPIQGSD LVLKAQNIKD DVRIRYKDQV EFERIAGEFG IFEEWKDGVP RTAYKGVVVF
RIQTTRRVFL VGPDSVMQLG IRNS
