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Q9XGM8 (MGAT1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase

EC=2.4.1.101
Alternative name(s):
N-acetylglucosaminyltransferase I
Short name=GlcNAcT-I
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I
Protein COMPLEX GLYCAN LESS 1
Gene names
Name:GNTI
Synonyms:CGL1
Ordered Locus Names:At4g38240
ORF Names:F20D10.360, F22I13.10
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Protein existenceEvidence 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.6 Ref.7 Ref.9 Ref.10

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.

Cofactor

Manganese. The cofactor is mostly bound to the substrate By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein Ref.7 Ref.10.

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.6 Ref.10

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 Ref.8

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.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9XGM8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
PRO_0000356191

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2418Helical; Signal-anchor for type II membrane protein; Potential
Topological domain25 – 444420Lumenal Potential
Coiled coil61 – 9232 Potential

Sites

Active site2871Proton acceptor Potential
Metal binding2111Manganese By similarity
Binding site1151Substrate By similarity
Binding site1441Substrate By similarity
Binding site1881Substrate By similarity
Binding site2101Substrate By similarity
Binding site3181Substrate By similarity

Amino acid modifications

Glycosylation3511N-linked (GlcNAc...)

Experimental info

Mutagenesis1441D → N in cgl1 C5/cgl1-1; loss of activity due to drgradation in the reticulum endoplasmic.
Mutagenesis3531T → V: Loss of glycosylation. No effect on localization and stability. Ref.10
Sequence conflict3031R → A in CAC80700. Ref.2
Sequence conflict3821V → D in CAC80700. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: B3DDCF221C526336

FASTA44451,634
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"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] [Europe PMC] [Abstract]
Cited for: MUTANT CGL1 C5, BIOPHYSICOCHEMICAL PROPERTIES.
[9]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-353, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CP002687 Genomic DNA. Translation: AEE86902.1.
CP002687 Genomic DNA. Translation: AEE86903.1.
AY099838 mRNA. Translation: AAM20689.1.
BT000334 mRNA. Translation: AAN15653.1.
PIRJC7084.
T05651.
RefSeqNP_195537.2. NM_119986.3.
NP_849517.1. NM_179186.1.
UniGeneAt.22245.

3D structure databases

ProteinModelPortalQ9XGM8.
SMRQ9XGM8. Positions 105-435.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT13. Glycosyltransferase Family 13.

Proteomic databases

PaxDbQ9XGM8.
PRIDEQ9XGM8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G38240.1; AT4G38240.1; AT4G38240. [Q9XGM8-1]
AT4G38240.2; AT4G38240.2; AT4G38240. [Q9XGM8-1]
GeneID829981.
KEGGath:AT4G38240.

Organism-specific databases

TAIRAT4G38240.

Phylogenomic databases

eggNOGNOG148227.
HOGENOMHOG000247055.
InParanoidQ9XGM8.
KOK00726.
OMAHEETAQV.
PhylomeDBQ9XGM8.
ProtClustDBCLSN2680320.

Enzyme and pathway databases

BioCycARA:AT4G38240-MONOMER.
ARA:GQT-355-MONOMER.
ARA:GQT-506-MONOMER.
UniPathwayUPA00378.

Gene expression databases

GenevestigatorQ9XGM8.

Family and domain databases

InterProIPR004139. Glyco_trans_13.
[Graphical view]
PANTHERPTHR10468. PTHR10468. 1 hit.
PfamPF03071. GNT-I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9XGM8.

Entry information

Entry nameMGAT1_ARATH
AccessionPrimary (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: April 16, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names