Reviewed, UniProtKB/Swiss-Prot Q9XGM8 (MGAT1_ARATH)

Names and origin

Protein names

Recommended name:
    Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
    EC=2.4.1.101
Alternative name(s):
    N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I
    N-acetylglucosaminyltransferase I
      Short name=GlcNAcT-I
    Protein COMPLEX GLYCAN LESS 1

Gene names

Name:	GNTI
Synonyms:	CGL1
Ordered Locus Names:	At4g38240
ORF Names:	F20D10.360, F22I13.10

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	444 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans. Required for normal root growth and morphology. Ref.1 Ref.5 Ref.6 Ref.8 Ref.9
Catalytic activity	UDP-N-acetyl-D-glucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 3-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein. Ref.6 Ref.9
Tissue specificity	Expressed in roots, stems, leaves and flowers. Ref.2
Post-translational modification	Glycosylated.
Disruption phenotype	Plants have an increased salt-sensitivity resulting in growth inhibition, aberrant root-tip morphology and callose accumulation. Ref.5 Ref.9
Miscellaneous	Creation of a second N-glycosylation site in mutant cgl1 C5/cgl1-1 interferes with protein folding and sequesters the protein for degradation in the endoplasmic reticulum.
Sequence similarities	Belongs to the glycosyltransferase 13 family.
Biophysicochemical properties	Kinetic parameters: the apparent KM is >3.0 mM for Man(3)-octyl. KM=0.14 mM for Man(5)-glycopeptide KM=0.05 mM for UDP-GlcNAc Vmax=3.42 µmol/min/mg enzyme toward Man(5)-glycopeptide Vmax=0.09 µmol/min/mg enzyme toward Man(3)-octyl
Sequence caution	The sequence CAB37480.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB37564.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAB80489.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Coiled coil Signal-anchor Transmembrane
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	N-glycan processing Ref.9 Inferred from mutant phenotype. Source: TAIR hyperosmotic response Ref.8 Inferred from mutant phenotype. Source: TAIR
Cellular component	Golgi membrane Inferred from electronic annotation. Source: InterPro integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Ref.7 Inferred from direct assay. Source: TAIR protein N-acetylglucosaminyltransferase activity Ref.5 Inferred from mutant phenotype. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 444	444	Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase		PRO_0000356191
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 24	18	Signal-anchor for type II membrane protein Potential
	Topological domain	25 – 444	420	Lumenal Potential
	Coiled coil	61 – 92	32	Potential
Amino acid modifications
	Glycosylation	351	1	N-linked (GlcNAc...)
Experimental info
	Mutagenesis	144	1	D → N in cgl1 C5/cgl1-1; loss of activity due to drgradation in the reticulum endoplasmic.
	Mutagenesis	353	1	T → V: Loss of glycosylation. No effect on localization and stability. Ref.9
	Sequence conflict	303	1	R → A in CAC80700. Ref.2
	Sequence conflict	382	1	V → D in CAC80700. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9XGM8-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: B3DDCF221C526336	FASTA	444	51,634
	10 20 30 40 50 60 MARISCDLRF LLIPAAFMFI YIQMRLFQTQ SQYADRLSSA IESENHCTSQ MRGLIDEVSI 70 80 90 100 110 120 KQSRIVALED MKNRQDEELV QLKDLIQTFE KKGIAKLTQG GQMPVAAVVV MACSRADYLE 130 140 150 160 170 180 RTVKSVLTYQ TPVASKYPLF ISQDGSDQAV KSKSLSYNQL TYMQHLDFEP VVTERPGELT 190 200 210 220 230 240 AYYKIARHYK WALDQLFYKH KFSRVIILED DMEIAPDFFD YFEAAASLMD RDKTIMAASS 250 260 270 280 290 300 WNDNGQKQFV HDPYALYRSD FFPGLGWMLK RSTWDELSPK WPKAYWDDWL RLKENHKGRQ 310 320 330 340 350 360 FIRPEVCRTY NFGEHGSSLG QFFSQYLEPI KLNDVTVDWK AKDLGYLTEG NYTKYFSGLV 370 380 390 400 410 420 RQARPIQGSD LVLKAQNIKD DVRIRYKDQV EFERIAGEFG IFEEWKDGVP RTAYKGVVVF 430 440 RIQTTRRVFL VGPDSVMQLG IRNS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An Arabidopsis thaliana cDNA complements the N-acetylglucosaminyltransferase I deficiency of CHO Lec1 cells." Bakker H., Lommen A., Jordi W., Stiekema W., Bosch D. Biochem. Biophys. Res. Commun. 261:829-832(1999) [PubMed: 10441510] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Strain: cv. Columbia.
[2]	"Isolation and characterization of plant N-acetyl glucosaminyltransferase I (GntI) cDNA sequences. Functional analyses in the Arabidopsis cgl mutant and in antisense plants." Wenderoth I., von Schaewen A. Plant Physiol. 123:1097-1108(2000) [PubMed: 10889259] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: cv. Columbia.
[3]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Isolation of a mutant Arabidopsis plant that lacks N-acetyl glucosaminyl transferase I and is unable to synthesize Golgi-modified complex N-linked glycans." von Schaewen A., Sturm A., O'Neill J., Chrispeels M.J. Plant Physiol. 102:1109-1118(1993) [PubMed: 8278542] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]	"Complementation of an Arabidopsis thaliana mutant that lacks complex asparagine-linked glycans with the human cDNA encoding N-acetylglucosaminyltransferase I." Gomez L., Chrispeels M.J. Proc. Natl. Acad. Sci. U.S.A. 91:1829-1833(1994) [PubMed: 8127889] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"Molecular basis of N-acetylglucosaminyltransferase I deficiency in Arabidopsis thaliana plants lacking complex N-glycans." Strasser R., Stadlmann J., Svoboda B., Altmann F., Gloessl J., Mach L. Biochem. J. 387:385-391(2005) [PubMed: 15537386] [Abstract] Cited for: MUTANT CGL1 C5, BIOPHYSICOCHEMICAL PROPERTIES.
[8]	"Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus." Kang J.S., Frank J., Kang C.H., Kajiura H., Vikram M., Ueda A., Kim S., Bahk J.D., Triplett B., Fujiyama K., Lee S.Y., von Schaewen A., Koiwa H. Proc. Natl. Acad. Sci. U.S.A. 105:5933-5938(2008) [PubMed: 18408158] [Abstract] Cited for: FUNCTION.
[9]	"Comparative analyses of arabidopsis complex glycan1 mutants and genetic interaction with staurosporin and temperature sensitive3a." Frank J., Kaulfuerst-Soboll H., Rips S., Koiwa H., von Schaewen A. Plant Physiol. 148:1354-1367(2008) [PubMed: 18768906] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-353, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ243198 mRNA. Translation: CAB45521.1. AJ249881 mRNA. Translation: CAC80700.1. AL035538 Genomic DNA. Translation: CAB37564.1. Sequence problems. AL035539 Genomic DNA. Translation: CAB37480.1. Sequence problems. AL161593 Genomic DNA. Translation: CAB80489.1. Sequence problems. AY099838 mRNA. Translation: AAM20689.1. BT000334 mRNA. Translation: AAN15653.1.
IPI	IPI00545584.
PIR	JC7084. T05651.
RefSeq	NP_195537.2. NP_849517.1.
UniGene	At.22245
3D structure databases
HSSP	HSSP built from PDB template 1FO8 based on UniProtKB P27115.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9XGM8.
Protein family/group databases
CAZy	GT13. Glycosyltransferase Family 13.
Proteomic databases
PRIDE	Q9XGM8.
Genome annotation databases
GeneID	829981.
GenomeReviews	Gene locus AT4G38240 in contig CT486007_GR.
KEGG	ath:AT4G38240.
NMPDR	fig|3702.1.peg.21943.
Organism-specific databases
TAIR	At4g38240.
Phylogenomic databases
OMA	PPDHRKF.
Gene expression databases
Genevestigator	Q9XGM8.
Family and domain databases
InterPro	IPR004139. Glyco_trans_13. [Graphical view]
PANTHER	PTHR10468. Glyco_trans_13. 1 hit.
Pfam	PF03071. GNT-I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MGAT1_ARATH

Accession

Primary (citable) accession number: Q9XGM8
Secondary accession number(s): Q8VWR5, Q9SVG1, Q9SZM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	November 1, 1999
Last modified:	November 3, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)