Q8H116 (MNS2_ARATH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 61.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2 Short name=AtMANIa EC=3.2.1.113 Alternative name(s): Alpha-mannosidase IA | ||||||||
| Gene names |
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| Organism | Arabidopsis thaliana (Mouse-ear cress) [Reference proteome] | ||||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis![]() |
Protein attributes
| Sequence length | 572 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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. Ref.5 Ref.6 |
| Catalytic activity | Hydrolysis of the terminal (1->2)-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man9(GlcNAc)2. Ref.6 |
| Cofactor | Calcium or manganese. Magnesium can be used to a lesser extent. |
| Enzyme regulation | Inhibited by kifunensine and 1-deoxymannojirimycin, but not by swainsonine. Ref.5 Ref.6 |
| Pathway | |
| Subcellular location | Golgi apparatus membrane; Single-pass type II membrane protein Ref.5 Ref.6. |
| Tissue specificity | Expressed in flowers, siliques, stems, leaves, roots, pollen grains and shoot apical meristems. Ref.5 Ref.6 |
| Disruption phenotype | No visible phenotype, due the redundancy with MNS1. Lack of complex N-glycans, shorter roots and increased lateral root formation in double mutants mns1 mns2. Ref.5 Ref.6 |
| Sequence similarities | Belongs to the glycosyl hydrolase 47 family. |
| Biophysicochemical properties | pH dependence: Optimum pH is 7.0. Stable from pH 5.0 to 10.0. Ref.6 Temperature dependence: Optimum temperature is 25 degrees Celsius. |
| Sequence caution | The sequence BAB01459.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 572 | 572 | Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2 | PRO_0000397934 | |||||||
Regions | |||||||||||
| Topological domain | 1 – 27 | 27 | Cytoplasmic Potential | ||||||||
| Transmembrane | 28 – 45 | 18 | Helical; Signal-anchor for type II membrane protein; Potential | ||||||||
| Topological domain | 46 – 572 | 527 | Lumenal Potential | ||||||||
| Coiled coil | 51 – 81 | 31 | Potential | ||||||||
Sites | |||||||||||
| Active site | 180 | 1 | Proton donor By similarity | ||||||||
| Active site | 312 | 1 | By similarity | ||||||||
| Active site | 446 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 326 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 460 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 377 ↔ 410 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 113 | 1 | Y → H in AAK92711. Ref.4 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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. 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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | 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. |
| IPI | IPI00534039. |
| RefSeq | NP_566675.1. NM_113010.2. |
| UniGene | At.25787. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FMI based on UniProtKB Q9UKM7. |
| ProteinModelPortal | Q8H116. |
| SMR | Q8H116. Positions 98-537. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q8H116. 1 interaction. |
| STRING | 3702.AT3G21160.1-P. |
Protein family/group databases | |
| CAZy | GH47. Glycoside Hydrolase Family 47. |
Proteomic databases | |
| PaxDb | Q8H116. |
| PRIDE | Q8H116. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblPlants | AT3G21160.1; AT3G21160.1; AT3G21160. |
| GeneID | 821668. |
| KEGG | ath:AT3G21160. |
Organism-specific databases | |
| TAIR | At3g21160. |
Phylogenomic databases | |
| eggNOG | NOG300315. |
| HOGENOM | HOG000181987. |
| InParanoid | Q8H116. |
| KO | K01230. |
| OMA | ENYFFHT. |
| PhylomeDB | Q8H116. |
| ProtClustDB | CLSN2914679. |
Enzyme and pathway databases | |
| UniPathway | UPA00378. |
Gene expression databases | |
| ArrayExpress | Q8H116. |
| Genevestigator | Q8H116. |
Family and domain databases | |
| Gene3D | 1.50.10.50. 1 hit. |
| InterPro | IPR001382. Glyco_hydro_47. [Graphical view] |
| PANTHER | PTHR11742. PTHR11742. 1 hit. |
| Pfam | PF01532. Glyco_hydro_47. 1 hit. [Graphical view] |
| PRINTS | PR00747. GLYHDRLASE47. |
| SUPFAM | SSF48225. Glyco_hydro_47. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | MNS2_ARATH | ||||||||
| Accession | Primary (citable) accession number: Q8H116 Secondary accession number(s): Q94A04, Q9LJB6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
