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Q9XGM8

- MGAT1_ARATH

UniProt

Q9XGM8 - MGAT1_ARATH

Protein

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

Gene

GNTI

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    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.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

    Vmax=3.42 µmol/min/mg enzyme toward Man(5)-glycopeptide1 Publication

    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

    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. hyperosmotic response Source: TAIR
    2. N-glycan processing Source: TAIR
    3. protein glycosylation Source: TAIR

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

    GO - Cellular componenti

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

    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

    GenevestigatoriQ9XGM8.

    Structurei

    3D structure databases

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

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini25 – 444420LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2418Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    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.
    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.

    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:
    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

    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: October 1, 2014
    This is version 83 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