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Q9XGM8

- MGAT1_ARATH

UniProt

Q9XGM8 - MGAT1_ARATH

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Protein
Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
Gene
GNTI, CGL1, At4g38240, F20D10.360, F22I13.10
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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

Manganese. 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-GlcNAc

Vmax=3.42 µmol/min/mg enzyme toward Man(5)-glycopeptide

Vmax=0.09 µmol/min/mg enzyme toward Man(3)-octyl

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei115 – 1151Substrate By similarity
Binding sitei144 – 1441Substrate By similarity
Binding sitei188 – 1881Substrate By similarity
Binding sitei210 – 2101Substrate By similarity
Metal bindingi211 – 2111Manganese By similarity
Active sitei287 – 2871Proton acceptor Reviewed prediction
Binding sitei318 – 3181Substrate By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. N-glycan processing Source: TAIR
  2. hyperosmotic response Source: TAIR
  3. 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_187828. 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: Chromosome 4

Organism-specific databases

TAIRiAT4G38240.

Subcellular locationi

Golgi apparatus membrane; Single-pass type II membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66Cytoplasmic Reviewed prediction
Transmembranei7 – 2418Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini25 – 444420Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: TAIR
  2. Golgi membrane Source: UniProtKB-SubCell
  3. endosome Source: TAIR
  4. integral component of membrane Source: UniProtKB-KW
  5. 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-acetylglucosaminyltransferase
PRO_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

GenevestigatoriQ9XGM8.

Structurei

3D structure databases

ProteinModelPortaliQ9XGM8.
SMRiQ9XGM8. Positions 105-435.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili61 – 9232 Reviewed prediction
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG148227.
HOGENOMiHOG000247055.
InParanoidiQ9XGM8.
KOiK00726.
OMAiHEETAQV.
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. Align

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

MARISCDLRF LLIPAAFMFI YIQMRLFQTQ SQYADRLSSA IESENHCTSQ    50
MRGLIDEVSI KQSRIVALED MKNRQDEELV QLKDLIQTFE KKGIAKLTQG 100
GQMPVAAVVV MACSRADYLE RTVKSVLTYQ TPVASKYPLF ISQDGSDQAV 150
KSKSLSYNQL TYMQHLDFEP VVTERPGELT AYYKIARHYK WALDQLFYKH 200
KFSRVIILED DMEIAPDFFD YFEAAASLMD RDKTIMAASS WNDNGQKQFV 250
HDPYALYRSD FFPGLGWMLK RSTWDELSPK WPKAYWDDWL RLKENHKGRQ 300
FIRPEVCRTY NFGEHGSSLG QFFSQYLEPI KLNDVTVDWK AKDLGYLTEG 350
NYTKYFSGLV RQARPIQGSD LVLKAQNIKD DVRIRYKDQV EFERIAGEFG 400
IFEEWKDGVP RTAYKGVVVF RIQTTRRVFL VGPDSVMQLG IRNS 444
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.
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti303 – 3031R → A in CAC80700. 1 Publication
Sequence conflicti382 – 3821V → D in CAC80700. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi JC7084.
T05651.
RefSeqi NP_195537.2. NM_119986.3. [Q9XGM8-1 ]
NP_849517.1. NM_179186.1. [Q9XGM8-1 ]
UniGenei At.22245.

3D structure databases

ProteinModelPortali Q9XGM8.
SMRi Q9XGM8. Positions 105-435.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GT13. Glycosyltransferase Family 13.

Proteomic databases

PaxDbi Q9XGM8.
PRIDEi Q9XGM8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G38240.1 ; AT4G38240.1 ; AT4G38240 . [Q9XGM8-1 ]
AT4G38240.2 ; AT4G38240.2 ; AT4G38240 . [Q9XGM8-1 ]
GeneIDi 829981.
KEGGi ath:AT4G38240.

Organism-specific databases

TAIRi AT4G38240.

Phylogenomic databases

eggNOGi NOG148227.
HOGENOMi HOG000247055.
InParanoidi Q9XGM8.
KOi K00726.
OMAi HEETAQV.
PhylomeDBi Q9XGM8.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BioCyci ARA:AT4G38240-MONOMER.
ARA:GQT-355-MONOMER.
ARA:GQT-506-MONOMER.
Reactomei REACT_187828. N-glycan trimming and elongation in the cis-Golgi.

Miscellaneous databases

PROi Q9XGM8.

Gene expression databases

Genevestigatori Q9XGM8.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR004139. Glyco_trans_13.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
PANTHERi PTHR10468. PTHR10468. 1 hit.
Pfami PF03071. GNT-I. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 82 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

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