Q9C512 · MNS1_ARATH
- ProteinMannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1
- GeneMNS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids560 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Class I alpha-mannosidase essential for early N-glycan processing. Progressively trims alpha-1,2-linked mannose residues. Produces Man5GlcNAc2 from Man8GlcNAc2, but only Man6GlcNAc2 from Man9GlcNAc2. Has difficulty acting on the terminal mannose of the b-branch. Involved in root development and cell wall biosynthesis.
Catalytic activity
- 4 H2O + N4-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N4-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)
- 3 H2O + N4-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) = 3 beta-D-mannose + N4-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)
- H2O + N4-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = beta-D-mannose + N4-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3)
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )
Note: Ca2+ or Mn2+. Mg2+ can be used to a lesser extent.
Activity regulation
Inhibited by kifunensine and 1-deoxymannojirimycin, but not by swainsonine.
pH Dependence
Optimum pH is 6.0. Stable from pH 4.5 to 6.5.
Temperature Dependence
Optimum temperature is 25 degrees Celsius.
Pathway
Protein modification; protein glycosylation.
Features
Showing features for active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endosome | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi cis cisterna | |
Cellular Component | Golgi membrane | |
Cellular Component | trans-Golgi network | |
Molecular Function | alpha-mannosidase activity | |
Molecular Function | calcium ion binding | |
Molecular Function | mannosyl-oligosaccharide 1,2-alpha-mannosidase activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | N-glycan processing | |
Biological Process | protein glycosylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1
- EC number
- Short namesAtMANIb
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9C512
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-27 | Cytoplasmic | ||||
Sequence: MARSRSISGYGIWKYLNPAYYLRRPRR | ||||||
Transmembrane | 28-47 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: LALLFIVFVSVSMLVWDRIN | ||||||
Topological domain | 48-560 | Lumenal | ||||
Sequence: LAREHEVEVFKLNEEVSRLEQMLEELNGGVGNKPLKTLKDAPEDPVDKQRRQKVKEAMIHAWSSYEKYAWGKDELQPRTKDGTDSFGGLGATMVDSLDTLYIMGLDEQFQKAREWVASSLDFDKDYDASMFETTIRVVGGLLSAYDLSGDKMFLEKAKDIADRLLPAWNTPTGIPYNIINLRNGNAHNPSWAAGGDSILADSGTEQLEFIALSQRTGDPKYQQKVEKVITELNKNFPADGLLPIYINPDNANPSYSTTTFGAMGDSFYEYLLKVWVQGNKTSAVKPYRDMWEKSMKGLLSLVKKSTPSSFTYICEKNGNNLIDKMDELACFAPGMLALGASGYGPDEEKKFLSLAGELAWTCYNFYQSTPTKLAGENYFFTAGQDMSVGTSWNILRPETVESLFYLWRLTGNKTYQEWGWNIFQAFEKNSRVESGYVGLKDVNTGAKDNKMQSFFLAETLKYLYLLFSPSSVISLDEWVFNTEAHPLKIVARNDPRKPTIALRQRKFGHQINV |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
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.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 21 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000397933 | 1-560 | Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1 | |||
Sequence: MARSRSISGYGIWKYLNPAYYLRRPRRLALLFIVFVSVSMLVWDRINLAREHEVEVFKLNEEVSRLEQMLEELNGGVGNKPLKTLKDAPEDPVDKQRRQKVKEAMIHAWSSYEKYAWGKDELQPRTKDGTDSFGGLGATMVDSLDTLYIMGLDEQFQKAREWVASSLDFDKDYDASMFETTIRVVGGLLSAYDLSGDKMFLEKAKDIADRLLPAWNTPTGIPYNIINLRNGNAHNPSWAAGGDSILADSGTEQLEFIALSQRTGDPKYQQKVEKVITELNKNFPADGLLPIYINPDNANPSYSTTTFGAMGDSFYEYLLKVWVQGNKTSAVKPYRDMWEKSMKGLLSLVKKSTPSSFTYICEKNGNNLIDKMDELACFAPGMLALGASGYGPDEEKKFLSLAGELAWTCYNFYQSTPTKLAGENYFFTAGQDMSVGTSWNILRPETVESLFYLWRLTGNKTYQEWGWNIFQAFEKNSRVESGYVGLKDVNTGAKDNKMQSFFLAETLKYLYLLFSPSSVISLDEWVFNTEAHPLKIVARNDPRKPTIALRQRKFGHQINV | ||||||
Glycosylation | 326 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 377↔409 | |||||
Sequence: CFAPGMLALGASGYGPDEEKKFLSLAGELAWTC | ||||||
Glycosylation | 459 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in flowers, siliques, stems, leaves, roots, pollen grains, shoot apical meristems, hypocotyls and upper region of the root.
Gene expression databases
Structure
Family & Domains
Features
Showing features for coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 47-80 | |||||
Sequence: NLAREHEVEVFKLNEEVSRLEQMLEELNGGVGNK |
Sequence similarities
Belongs to the glycosyl hydrolase 47 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9C512-1
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.
- Name1
- Length560
- Mass (Da)63,532
- Last updated2001-06-01 v1
- ChecksumBCC20CB9E63020B9
Q9C512-2
- Name2
- Differences from canonical
- 1-104: Missing
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_039724 | 1-104 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC024261 EMBL· GenBank· DDBJ | AAG52623.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC025294 EMBL· GenBank· DDBJ | AAG50876.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE32686.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE32687.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY081353 EMBL· GenBank· DDBJ | AAL91242.1 EMBL· GenBank· DDBJ | mRNA | ||
AY128845 EMBL· GenBank· DDBJ | AAM91245.1 EMBL· GenBank· DDBJ | mRNA |