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Protein

Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase

Gene

GNTI

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

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.

Cofactori

Mn2+By similarityNote: The cofactor is mostly bound to the substrate.By similarity

Kineticsi

the apparent KM is >3.0 mM for Man(3)-octyl.

  1. KM=0.14 mM for Man(5)-glycopeptide1 Publication
  2. KM=0.05 mM for UDP-GlcNAc1 Publication
  1. Vmax=3.42 µmol/min/mg enzyme toward Man(5)-glycopeptide1 Publication
  2. Vmax=0.09 µmol/min/mg enzyme toward Man(3)-octyl1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei115 – 1151SubstrateBy similarity
Binding sitei144 – 1441SubstrateBy similarity
Binding sitei188 – 1881SubstrateBy similarity
Binding sitei210 – 2101SubstrateBy similarity
Metal bindingi211 – 2111ManganeseBy similarity
Active sitei287 – 2871Proton acceptorSequence Analysis
Binding sitei318 – 3181SubstrateBy similarity

GO - Molecular functioni

  • alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Source: TAIR
  • metal ion binding Source: UniProtKB-KW
  • protein N-acetylglucosaminyltransferase activity Source: TAIR
  • transferase activity, transferring glycosyl groups Source: TAIR

GO - Biological processi

  • hyperosmotic response Source: TAIR
  • N-glycan processing Source: TAIR
  • protein glycosylation Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT4G38240-MONOMER.
ARA:GQT-355-MONOMER.
ARA:GQT-506-MONOMER.
ReactomeiREACT_349178. N-glycan trimming and elongation in the cis-Golgi.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT13. Glycosyltransferase Family 13.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:GNTI
Synonyms:CGL1
Ordered Locus Names:At4g38240
ORF Names:F20D10.360, F22I13.10
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G38240.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Transmembranei7 – 2418Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini25 – 444420LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • endosome Source: TAIR
  • Golgi apparatus Source: TAIR
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • trans-Golgi network Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Plants have an increased salt-sensitivity resulting in growth inhibition, aberrant root-tip morphology and callose accumulation.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi144 – 1441D → N in cgl1 C5/cgl1-1; loss of activity due to drgradation in the reticulum endoplasmic.
Mutagenesisi353 – 3531T → V: Loss of glycosylation. No effect on localization and stability. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 444444Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferasePRO_0000356191Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi351 – 3511N-linked (GlcNAc...)

Post-translational modificationi

Glycosylated.

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9XGM8.
PRIDEiQ9XGM8.

Expressioni

Tissue specificityi

Expressed in roots, stems, leaves and flowers.1 Publication

Gene expression databases

ExpressionAtlasiQ9XGM8. baseline and differential.
GenevestigatoriQ9XGM8.

Structurei

3D structure databases

ProteinModelPortaliQ9XGM8.
SMRiQ9XGM8. Positions 105-435.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili61 – 9232Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 13 family.Curated

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG148227.
HOGENOMiHOG000247055.
InParanoidiQ9XGM8.
KOiK00726.
OMAiWIELSPK.
PhylomeDBiQ9XGM8.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR004139. Glyco_trans_13.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10468. PTHR10468. 1 hit.
PfamiPF03071. GNT-I. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q9XGM8-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MARISCDLRF LLIPAAFMFI YIQMRLFQTQ SQYADRLSSA IESENHCTSQ
60 70 80 90 100
MRGLIDEVSI KQSRIVALED MKNRQDEELV QLKDLIQTFE KKGIAKLTQG
110 120 130 140 150
GQMPVAAVVV MACSRADYLE RTVKSVLTYQ TPVASKYPLF ISQDGSDQAV
160 170 180 190 200
KSKSLSYNQL TYMQHLDFEP VVTERPGELT AYYKIARHYK WALDQLFYKH
210 220 230 240 250
KFSRVIILED DMEIAPDFFD YFEAAASLMD RDKTIMAASS WNDNGQKQFV
260 270 280 290 300
HDPYALYRSD FFPGLGWMLK RSTWDELSPK WPKAYWDDWL RLKENHKGRQ
310 320 330 340 350
FIRPEVCRTY NFGEHGSSLG QFFSQYLEPI KLNDVTVDWK AKDLGYLTEG
360 370 380 390 400
NYTKYFSGLV RQARPIQGSD LVLKAQNIKD DVRIRYKDQV EFERIAGEFG
410 420 430 440
IFEEWKDGVP RTAYKGVVVF RIQTTRRVFL VGPDSVMQLG IRNS
Length:444
Mass (Da):51,634
Last modified:November 1, 1999 - v1
Checksum:iB3DDCF221C526336
GO

Sequence cautioni

The sequence CAB37480.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB37564.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB80489.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti303 – 3031R → A in CAC80700 (PubMed:10889259).Curated
Sequence conflicti382 – 3821V → D in CAC80700 (PubMed:10889259).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJC7084.
T05651.
RefSeqiNP_195537.2. NM_119986.3. [Q9XGM8-1]
NP_849517.1. NM_179186.1. [Q9XGM8-1]
UniGeneiAt.22245.

Genome annotation databases

EnsemblPlantsiAT4G38240.1; AT4G38240.1; AT4G38240. [Q9XGM8-1]
AT4G38240.2; AT4G38240.2; AT4G38240. [Q9XGM8-1]
GeneIDi829981.
KEGGiath:AT4G38240.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJC7084.
T05651.
RefSeqiNP_195537.2. NM_119986.3. [Q9XGM8-1]
NP_849517.1. NM_179186.1. [Q9XGM8-1]
UniGeneiAt.22245.

3D structure databases

ProteinModelPortaliQ9XGM8.
SMRiQ9XGM8. Positions 105-435.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGT13. Glycosyltransferase Family 13.

Proteomic databases

PaxDbiQ9XGM8.
PRIDEiQ9XGM8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G38240.1; AT4G38240.1; AT4G38240. [Q9XGM8-1]
AT4G38240.2; AT4G38240.2; AT4G38240. [Q9XGM8-1]
GeneIDi829981.
KEGGiath:AT4G38240.

Organism-specific databases

TAIRiAT4G38240.

Phylogenomic databases

eggNOGiNOG148227.
HOGENOMiHOG000247055.
InParanoidiQ9XGM8.
KOiK00726.
OMAiWIELSPK.
PhylomeDBiQ9XGM8.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciARA:AT4G38240-MONOMER.
ARA:GQT-355-MONOMER.
ARA:GQT-506-MONOMER.
ReactomeiREACT_349178. N-glycan trimming and elongation in the cis-Golgi.

Miscellaneous databases

PROiQ9XGM8.

Gene expression databases

ExpressionAtlasiQ9XGM8. baseline and differential.
GenevestigatoriQ9XGM8.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR004139. Glyco_trans_13.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR10468. PTHR10468. 1 hit.
PfamiPF03071. GNT-I. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiMGAT1_ARATH
AccessioniPrimary (citable) accession number: Q9XGM8
Secondary accession number(s): Q8VWR5, Q9SVG1, Q9SZM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: November 1, 1999
Last modified: April 1, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.