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Q9XEE9

- ALG11_ARATH

UniProt

Q9XEE9 - ALG11_ARATH

Protein

GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase

Gene

ALG11

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 66 (01 Oct 2014)
      Sequence version 2 (21 Sep 2011)
      Previous versions | rss
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    Functioni

    Required for N-linked oligosaccharide assembly. Has a role in the last step of the synthesis of the Man5GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum.1 Publication

    Catalytic activityi

    2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = 2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. mannosylation Source: GOC
    2. oligosaccharide-lipid intermediate biosynthetic process Source: UniProtKB
    3. plant-type cell wall biogenesis Source: TAIR
    4. protein N-linked glycosylation Source: TAIR
    5. response to abscisic acid Source: TAIR
    6. response to osmotic stress Source: TAIR

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT4. Glycosyltransferase Family 4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase (EC:2.4.1.131)
    Alternative name(s):
    Alpha-1,2-mannosyltransferase ALG11
    Asparagine-linked glycosylation protein 11
    Protein LEAF WILTING 3
    Gene namesi
    Name:ALG11
    Synonyms:LEW3
    Ordered Locus Names:At2g40190
    ORF Names:T07M07.7
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 2

    Organism-specific databases

    TAIRiAT2G40190.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum membrane Source: TAIR
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Lethality.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi148 – 1481G → E in lew3; deficiency in N-glycosylation leading to dwarf phenotype, reduced fertility and impaired cellulose synthesis. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 463463GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferasePRO_0000412585Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi227 – 2271N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi314 – 3141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi423 – 4231N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRIDEiQ9XEE9.

    Expressioni

    Tissue specificityi

    Expressed in shoots, leaves, sepals, filaments, siliques, stems, roots and guard cells.1 Publication

    Gene expression databases

    GenevestigatoriQ9XEE9.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT2G40190.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9XEE9.
    SMRiQ9XEE9. Positions 272-442.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei3 – 2321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei204 – 22623HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi46 – 494Poly-Gly

    Sequence similaritiesi

    Belongs to the glycosyltransferase 4 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0438.
    HOGENOMiHOG000209670.
    InParanoidiQ0WT32.
    KOiK03844.
    OMAiGTVILAH.

    Family and domain databases

    InterProiIPR001296. Glyco_trans_1.
    [Graphical view]
    PfamiPF00534. Glycos_transf_1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9XEE9-1) [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

    MAIYFILYTL LTIIFAVSLS LFLSVINARK SRKRAVGFFH PYTNDGGGGE    50
    RVLWCAVKAI QEENPDLDCV IFTGDHDSSS DSLARRAVDR FGVHLQSPPK 100
    VIHLNKRKWI EESTYPHFTM IGQSLGSVYL AWEALRMFTP LYFLDTSGYA 150
    FTYPLARIFG CKVVCYTHYP TISLDMISRV RQRNSMYNND ASIAKSNWLS 200
    TCKLVYYRAF SWMYGMVGSC THLAMVNSSW TKSHIEVLWR IPERITRVYP 250
    PCDTSGLQAF PLERSSDPPK IISVAQFRPE KAHMLQLEAF SLALEKLDAD 300
    VPRPKLQFVG SCRNNSDEER LQKLKDRAVE LKVDGDVQFY KNAMYRELVE 350
    LLGNAVAGLH GMIDEHFGIS VVEYMAAGAI PIAHNSAGPK MDIVLEEDGQ 400
    KTGFLAETVE EYAEAILEIV KMNETERLKM AESARKRAAR FSEQRFCEDF 450
    KTAIRPIFTG PLK 463
    Length:463
    Mass (Da):52,573
    Last modified:September 21, 2011 - v2
    Checksum:i7092C34149CD4AE1
    GO
    Isoform 2 (identifier: Q9XEE9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-212: Missing.

    Show »
    Length:251
    Mass (Da):28,261
    Checksum:iCFB26F285390374C
    GO

    Sequence cautioni

    The sequence AAD25934.1 differs from that shown. Reason: Erroneous gene model prediction.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 212212Missing in isoform 2. 1 PublicationVSP_041714Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF085279 Genomic DNA. Translation: AAD25934.1. Sequence problems.
    CP002685 Genomic DNA. Translation: AEC09794.1.
    AK227731 mRNA. Translation: BAE99716.1.
    BT009712 mRNA. Translation: AAP88346.1.
    PIRiD84826.
    RefSeqiNP_181548.2. NM_129577.4. [Q9XEE9-1]
    UniGeneiAt.21597.

    Genome annotation databases

    EnsemblPlantsiAT2G40190.1; AT2G40190.1; AT2G40190. [Q9XEE9-1]
    GeneIDi818610.
    KEGGiath:AT2G40190.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF085279 Genomic DNA. Translation: AAD25934.1 . Sequence problems.
    CP002685 Genomic DNA. Translation: AEC09794.1 .
    AK227731 mRNA. Translation: BAE99716.1 .
    BT009712 mRNA. Translation: AAP88346.1 .
    PIRi D84826.
    RefSeqi NP_181548.2. NM_129577.4. [Q9XEE9-1 ]
    UniGenei At.21597.

    3D structure databases

    ProteinModelPortali Q9XEE9.
    SMRi Q9XEE9. Positions 272-442.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT2G40190.1-P.

    Protein family/group databases

    CAZyi GT4. Glycosyltransferase Family 4.

    Proteomic databases

    PRIDEi Q9XEE9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G40190.1 ; AT2G40190.1 ; AT2G40190 . [Q9XEE9-1 ]
    GeneIDi 818610.
    KEGGi ath:AT2G40190.

    Organism-specific databases

    TAIRi AT2G40190.

    Phylogenomic databases

    eggNOGi COG0438.
    HOGENOMi HOG000209670.
    InParanoidi Q0WT32.
    KOi K03844.
    OMAi GTVILAH.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    PROi Q9XEE9.

    Gene expression databases

    Genevestigatori Q9XEE9.

    Family and domain databases

    InterProi IPR001296. Glyco_trans_1.
    [Graphical view ]
    Pfami PF00534. Glycos_transf_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A cluster of ABA-regulated genes on Arabidopsis thaliana BAC T07M07."
      Wang M.L., Belmonte S., Kim U., Dolan M., Morris J.W., Goodman H.M.
      Genome Res. 9:325-333(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Morosawa T., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K.
      , Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-463.
    6. "LEW3, encoding a putative alpha-1,2-mannosyltransferase (ALG11) in N-linked glycoprotein, plays vital roles in cell-wall biosynthesis and the abiotic stress response in Arabidopsis thaliana."
      Zhang M., Henquet M., Chen Z., Zhang H., Zhang Y., Ren X., van der Krol S., Gonneau M., Bosch D., Gong Z.
      Plant J. 60:983-999(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-148, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiALG11_ARATH
    AccessioniPrimary (citable) accession number: Q9XEE9
    Secondary accession number(s): F4IH01, Q0WT32, Q7DNH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 66 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In the absence of ALG11 activity, no N-glycans are produced and transferred to proteins.

    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