Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9C512

- MNS1_ARATH

UniProt

Q9C512 - MNS1_ARATH

Protein

Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1

Gene

MNS1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 6.0. Stable from pH 4.5 to 6.5.1 Publication

    Temperature dependencei

    Optimum temperature is 25 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei179 – 1791Proton donorBy similarity
    Active sitei312 – 3121By similarity
    Active sitei445 – 4451By 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:AT1G51590-MONOMER.
    ARA:GQT-893-MONOMER.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGH47. Glycoside Hydrolase Family 47.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1 (EC:3.2.1.113)
    Short name:
    AtMANIb
    Alternative name(s):
    Alpha-mannosidase IB
    Gene namesi
    Name:MNS1
    Synonyms:MANIB
    Ordered Locus Names:At1g51590
    ORF Names:F19C24.18, F5D21.1
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G51590.

    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 MNS2. 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 – 560560Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1PRO_0000397933Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi377 ↔ 409By similarity
    Glycosylationi459 – 4591N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9C512.
    PRIDEiQ9C512.

    Expressioni

    Tissue specificityi

    Expressed in flowers, siliques, stems, leaves, roots, pollen grains, shoot apical meristems, hypocotyls and upper region of the root.2 Publications

    Gene expression databases

    GenevestigatoriQ9C512.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT1G51590.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9C512.
    SMRiQ9C512. Positions 97-536.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2727CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini48 – 560513LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei28 – 4720Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili47 – 8034Sequence 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.
    InParanoidiQ9C512.
    KOiK01230.
    OMAiLHAWSSY.
    PhylomeDBiQ9C512.

    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.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9C512-1) [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

    MARSRSISGY GIWKYLNPAY YLRRPRRLAL LFIVFVSVSM LVWDRINLAR    50
    EHEVEVFKLN EEVSRLEQML EELNGGVGNK PLKTLKDAPE DPVDKQRRQK 100
    VKEAMIHAWS SYEKYAWGKD ELQPRTKDGT DSFGGLGATM VDSLDTLYIM 150
    GLDEQFQKAR EWVASSLDFD KDYDASMFET TIRVVGGLLS AYDLSGDKMF 200
    LEKAKDIADR LLPAWNTPTG IPYNIINLRN GNAHNPSWAA GGDSILADSG 250
    TEQLEFIALS QRTGDPKYQQ KVEKVITELN KNFPADGLLP IYINPDNANP 300
    SYSTTTFGAM GDSFYEYLLK VWVQGNKTSA VKPYRDMWEK SMKGLLSLVK 350
    KSTPSSFTYI CEKNGNNLID KMDELACFAP GMLALGASGY GPDEEKKFLS 400
    LAGELAWTCY NFYQSTPTKL AGENYFFTAG QDMSVGTSWN ILRPETVESL 450
    FYLWRLTGNK TYQEWGWNIF QAFEKNSRVE SGYVGLKDVN TGAKDNKMQS 500
    FFLAETLKYL YLLFSPSSVI SLDEWVFNTE AHPLKIVARN DPRKPTIALR 550
    QRKFGHQINV 560
    Length:560
    Mass (Da):63,532
    Last modified:June 1, 2001 - v1
    Checksum:iBCC20CB9E63020B9
    GO
    Isoform 2 (identifier: Q9C512-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-104: Missing.

    Note: Derived from EST data. No experimental confirmation available.

    Show »
    Length:456
    Mass (Da):51,349
    Checksum:i16E3C4590FAFCDFC
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 104104Missing in isoform 2. CuratedVSP_039724Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC024261 Genomic DNA. Translation: AAG52623.1.
    AC025294 Genomic DNA. Translation: AAG50876.1.
    CP002684 Genomic DNA. Translation: AEE32686.1.
    CP002684 Genomic DNA. Translation: AEE32687.1.
    AY081353 mRNA. Translation: AAL91242.1.
    AY128845 mRNA. Translation: AAM91245.1.
    PIRiE96554.
    RefSeqiNP_001031171.1. NM_001036094.1. [Q9C512-2]
    NP_175570.1. NM_104037.4. [Q9C512-1]
    UniGeneiAt.26180.
    At.37784.
    At.66909.

    Genome annotation databases

    EnsemblPlantsiAT1G51590.1; AT1G51590.1; AT1G51590. [Q9C512-1]
    GeneIDi841584.
    KEGGiath:AT1G51590.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC024261 Genomic DNA. Translation: AAG52623.1 .
    AC025294 Genomic DNA. Translation: AAG50876.1 .
    CP002684 Genomic DNA. Translation: AEE32686.1 .
    CP002684 Genomic DNA. Translation: AEE32687.1 .
    AY081353 mRNA. Translation: AAL91242.1 .
    AY128845 mRNA. Translation: AAM91245.1 .
    PIRi E96554.
    RefSeqi NP_001031171.1. NM_001036094.1. [Q9C512-2 ]
    NP_175570.1. NM_104037.4. [Q9C512-1 ]
    UniGenei At.26180.
    At.37784.
    At.66909.

    3D structure databases

    ProteinModelPortali Q9C512.
    SMRi Q9C512. Positions 97-536.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 3702.AT1G51590.1-P.

    Protein family/group databases

    CAZyi GH47. Glycoside Hydrolase Family 47.

    Proteomic databases

    PaxDbi Q9C512.
    PRIDEi Q9C512.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G51590.1 ; AT1G51590.1 ; AT1G51590 . [Q9C512-1 ]
    GeneIDi 841584.
    KEGGi ath:AT1G51590.

    Organism-specific databases

    TAIRi AT1G51590.

    Phylogenomic databases

    eggNOGi NOG300315.
    HOGENOMi HOG000181987.
    InParanoidi Q9C512.
    KOi K01230.
    OMAi LHAWSSY.
    PhylomeDBi Q9C512.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BioCyci ARA:AT1G51590-MONOMER.
    ARA:GQT-893-MONOMER.

    Miscellaneous databases

    PROi Q9C512.

    Gene expression databases

    Genevestigatori Q9C512.

    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. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "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.
    4. "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.
    5. "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 nameiMNS1_ARATH
    AccessioniPrimary (citable) accession number: Q9C512
    Secondary accession number(s): Q2V4H4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 86 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