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Q8H116

- MNS2_ARATH

UniProt

Q8H116 - MNS2_ARATH

Protein

Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2

Gene

MNS2

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 70 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Class I alpha-mannosidase essential for early N-glycan processing. Progressively trim alpha-1,2-linked mannose residues. Produces Man5GlcNAc2 from Man8GlcNAc2, but only Man6GlcNAc2 from Man9GlcNAc2. Have difficulty acting on the terminal mannose of the b-branch. Involved in root development and cell wall biosynthesis.2 Publications

    Catalytic activityi

    Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2.1 Publication

    Cofactori

    Calcium or manganese. Magnesium can be used to a lesser extent.

    Enzyme regulationi

    Inhibited by kifunensine and 1-deoxymannojirimycin, but not by swainsonine.2 Publications

    pH dependencei

    Optimum pH is 7.0. Stable from pH 5.0 to 10.0.1 Publication

    Temperature dependencei

    Optimum temperature is 25 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei180 – 1801Proton donorBy similarity
    Active sitei312 – 3121By similarity
    Active sitei446 – 4461By similarity

    GO - Molecular functioni

    1. alpha-mannosidase activity Source: TAIR
    2. calcium ion binding Source: InterPro
    3. mannosyl-oligosaccharide 1,2-alpha-mannosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. N-glycan processing Source: TAIR
    2. root development Source: TAIR

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Calcium, Magnesium, Manganese

    Enzyme and pathway databases

    BioCyciARA:AT3G21160-MONOMER.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGH47. Glycoside Hydrolase Family 47.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2 (EC:3.2.1.113)
    Short name:
    AtMANIa
    Alternative name(s):
    Alpha-mannosidase IA
    Gene namesi
    Name:MNS2
    Synonyms:MANIA
    Ordered Locus Names:At3g21160
    ORF Names:MSA6.31
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G21160.

    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

    No visible phenotype; due the redundancy with MNS1. Lack of complex N-glycans, shorter roots and increased lateral root formation in mns1 and mns2 double mutants.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 572572Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2PRO_0000397934Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi377 ↔ 410By similarity
    Glycosylationi460 – 4601N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ8H116.
    PRIDEiQ8H116.

    Expressioni

    Tissue specificityi

    Expressed in flowers, siliques, stems, leaves, roots, pollen grains and shoot apical meristems.2 Publications

    Gene expression databases

    GenevestigatoriQ8H116.

    Interactioni

    Protein-protein interaction databases

    BioGridi7000. 1 interaction.
    IntActiQ8H116. 1 interaction.
    STRINGi3702.AT3G21160.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8H116.
    SMRiQ8H116. Positions 98-537.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2727CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini46 – 572527LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei28 – 4518Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili51 – 8131Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 47 family.Curated

    Keywords - Domaini

    Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG300315.
    HOGENOMiHOG000181987.
    InParanoidiQ8H116.
    KOiK01230.
    OMAiTSAVKHY.
    PhylomeDBiQ8H116.

    Family and domain databases

    Gene3Di1.50.10.50. 1 hit.
    InterProiIPR001382. Glyco_hydro_47.
    [Graphical view]
    PANTHERiPTHR11742. PTHR11742. 1 hit.
    PfamiPF01532. Glyco_hydro_47. 1 hit.
    [Graphical view]
    PRINTSiPR00747. GLYHDRLASE47.
    SUPFAMiSSF48225. SSF48225. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q8H116-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARNKLVSGS HGIWKYFNPA FYLRRPRRLA LLIILFVSVS MVVWDRQSLS    50
    RDYQFEVSKL NEEVLRLQQM LEEIKSVTED VSVNSLKDVQ EDPVDAQRMQ 100
    RVKEAMVHAW SSYEKYAWGQ DELQPQTKDG VDSFGGLGAT MIDALDTLYI 150
    MGLDEQFQKA REWVASSLDF DKDYAASMFE TTIRVVGGLL SAYDLSGDKI 200
    FLEKAMDIAD RLLPAWDTQS GIPYNIINLK HGNAHNPTWA GGDSILADSG 250
    TEQLEFIALS QRTGDPKYQQ KVEKVISVLN KNFPADGLLP IYINPDTANP 300
    SQSTITFGAM GDSFYEYLLK VWVFGNKTSA VKHYRDMWEK SMNGLLSLVK 350
    KSTPLSFTYI CEKSGNSLID KMDELACFAP GMLALGASGY SDPAEGKKFL 400
    TLAEELAWTC YNFYQSTPTK LAGENYFFNS GSDMSVGTSW NILRPETVES 450
    LFYLWRLTGN KTYQEWGWNI FEAFEKNSRI ESGYVGLKDV NTGVKDNKMQ 500
    SFFLAETLKY LYLLFSPTTV IPLDEWVFNT EAHPLKIKSR NDQVNLKQSN 550
    KVLLRKPAFR IRQRHYGRIT KK 572
    Length:572
    Mass (Da):65,136
    Last modified:March 1, 2003 - v1
    Checksum:i14614DD4525F9499
    GO

    Sequence cautioni

    The sequence BAB01459.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti113 – 1131Y → H in AAK92711. (PubMed:14593172)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP000604, AB023045 Genomic DNA. Translation: BAB01459.1. Sequence problems.
    CP002686 Genomic DNA. Translation: AEE76468.1.
    AY050776 mRNA. Translation: AAK92711.1.
    BT000893 mRNA. Translation: AAN41293.1.
    RefSeqiNP_566675.1. NM_113010.2.
    UniGeneiAt.25787.

    Genome annotation databases

    EnsemblPlantsiAT3G21160.1; AT3G21160.1; AT3G21160.
    GeneIDi821668.
    KEGGiath:AT3G21160.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP000604 , AB023045 Genomic DNA. Translation: BAB01459.1 . Sequence problems.
    CP002686 Genomic DNA. Translation: AEE76468.1 .
    AY050776 mRNA. Translation: AAK92711.1 .
    BT000893 mRNA. Translation: AAN41293.1 .
    RefSeqi NP_566675.1. NM_113010.2.
    UniGenei At.25787.

    3D structure databases

    ProteinModelPortali Q8H116.
    SMRi Q8H116. Positions 98-537.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 7000. 1 interaction.
    IntActi Q8H116. 1 interaction.
    STRINGi 3702.AT3G21160.1-P.

    Protein family/group databases

    CAZyi GH47. Glycoside Hydrolase Family 47.

    Proteomic databases

    PaxDbi Q8H116.
    PRIDEi Q8H116.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G21160.1 ; AT3G21160.1 ; AT3G21160 .
    GeneIDi 821668.
    KEGGi ath:AT3G21160.

    Organism-specific databases

    TAIRi AT3G21160.

    Phylogenomic databases

    eggNOGi NOG300315.
    HOGENOMi HOG000181987.
    InParanoidi Q8H116.
    KOi K01230.
    OMAi TSAVKHY.
    PhylomeDBi Q8H116.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BioCyci ARA:AT3G21160-MONOMER.

    Gene expression databases

    Genevestigatori Q8H116.

    Family and domain databases

    Gene3Di 1.50.10.50. 1 hit.
    InterProi IPR001382. Glyco_hydro_47.
    [Graphical view ]
    PANTHERi PTHR11742. PTHR11742. 1 hit.
    Pfami PF01532. Glyco_hydro_47. 1 hit.
    [Graphical view ]
    PRINTSi PR00747. GLYHDRLASE47.
    SUPFAMi SSF48225. SSF48225. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones."
      Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.
      DNA Res. 7:217-221(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
      Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
      DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
      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. "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.
    5. "Class I alpha-mannosidases are required for N-glycan processing and root development in Arabidopsis thaliana."
      Liebminger E., Huttner S., Vavra U., Fischl R., Schoberer J., Grass J., Blaukopf C., Seifert G.J., Altmann F., Mach L., Strasser R.
      Plant Cell 21:3850-3867(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ENZYME REGULATION, DISRUPTION PHENOTYPE.
    6. "Two Arabidopsis thaliana Golgi alpha-mannosidase I enzymes are responsible for plant N-glycan maturation."
      Kajiura H., Koiwa H., Nakazawa Y., Okazawa A., Kobayashi A., Seki T., Fujiyama K.
      Glycobiology 20:235-247(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiMNS2_ARATH
    AccessioniPrimary (citable) accession number: Q8H116
    Secondary accession number(s): Q94A04, Q9LJB6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 70 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3