Q9LFR0 · GMAN2_ARATH
- ProteinAlpha-mannosidase 2
- GeneGMII
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1173 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway. Converts GlcNAcMan5GlcNAc2 (Man5Gn) into GlcNAcMan3GlcNAc2 (MGn) by sequential removal of two alpha1,6- and alpha1,3-linked mannose residues from the alpha1,6-mannose branch of the substrate. To a lesser extent, also able to cleave beta1,2-xylosylated Man5Gn-glycopeptide (Man5GnX-GP) and pyridylaminated substrates Man5Gn-PA and Man5GnX-PA, but not active toward Man5-glycopeptide (PubMed:16460512, PubMed:21478158).
Required for resistance to salt stress (PubMed:18408158).
Required for resistance to salt stress (PubMed:18408158).
Catalytic activity
- 2 H2O + N4-{beta-D-GlcNAc-(1->2)-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] = 2 alpha-D-mannopyranose + N4-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein]
Cofactor
Note: Binds 1 zinc ion per subunit. Not sensitive to EDTA and not significantly stimulated by cations such as Ca2+, Co2+, Mn2+, Ni2+ or Zn2+ (PubMed:16460512).
Activity regulation
Inhibited by 1 mM Cu2+ and by the class II alpha-mannosidase inhibitor swainsonine.
Pathway
Protein modification; protein glycosylation.
Features
Showing features for binding site, active 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 | carbohydrate binding | |
Molecular Function | mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity | |
Molecular Function | metal ion binding | |
Biological Process | hyperosmotic salinity response | |
Biological Process | mannose metabolic process | |
Biological Process | protein N-linked glycosylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAlpha-mannosidase 2
- EC number
- 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 accessionQ9LFR0
- 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 | 1-50 | Cytoplasmic | ||||
Sequence: MPFSSYIGNSRRSSTGGGTGGWGQSLLPTALSKSKLAINRKPRKRTLVVN | ||||||
Transmembrane | 51-71 | Helical; Signal-anchor | ||||
Sequence: FIFANFFVIALTVSLLFFLLT | ||||||
Topological domain | 72-1173 | Lumenal | ||||
Sequence: LFHFGVPGPISSRFLTSRSNRIVKPRKNINRRPLNDSNSGAVVDITTKDLYDRIEFLDTDGGPWKQGWRVTYKDDEWEKEKLKIFVVPHSHNDPGWKLTVEEYYQRQSRHILDTIVETLSKDSRRKFIWEEMSYLERWWRDASPNKQEALTKLVKDGQLEIVGGGWVMNDEANSHYFAIIEQIAEGNMWLNDTIGVIPKNSWAIDPFGYSSTMAYLLRRMGFENMLIQRTHYELKKDLAQHKNLEYIWRQSWDAMETTDIFVHMMPFYSYDIPHTCGPEPAICCQFDFARMRGFKYELCPWGKHPVETTLENVQERALKLLDQYRKKSTLYRTNTLLIPLGDDFRYISIDEAEAQFRNYQMLFDHINSNPSLNAEAKFGTLEDYFRTVREEADRVNYSRPGEVGSGQVVGFPSLSGDFFTYADRQQDYWSGYYVSRPFFKAVDRVLEHTLRGAEIMMSFLLGYCHRIQCEKFPTSFTYKLTAARRNLALFQHHDGVTGTAKDYVVQDYGTRMHTSLQDLQIFMSKAIEVLLGIRHEKEKSDQSPSFFEAEQMRSKYDARPVHKPIAAREGNSHTVILFNPSEQTREEVVTVVVNRAEISVLDSNWTCVPSQISPEVQHDDTKLFTGRHRLYWKASIPALGLRTYFIANGNVECEKATPSKLKYASEFDPFPCPPPYSCSKLDNDVTEIRNEHQTLVFDVKNGSLRKIVHRNGSETVVGEEIGMYSSPESGAYLFKPDGEAQPIVQPDGHVVTSEGLLVQEVFSYPKTKWEKSPLSQKTRLYTGGNTLQDQVVEIEYHVELLGNDFDDRELIVRYKTDVDNKKVFYSDLNGFQMSRRETYDKIPLQGNYYPMPSLAFIQGSNGQRFSVHSRQSLGVASLKEGWLEIMLDRRLVRDDGRGLGQGVMDNRAMTVVFHLLAESNISQADPASNTNPRNPSLLSHLIGAHLNYPINTFIAKKPQDISVRVPQYGSFAPLAKPLPCDLHIVNFKVPRPSKYSQQLEEDKPRFALILNRRAWDSAYCHKGRQVNCTSMANEPVNFSDMFKDLAASKVKPTSLNLLQEDMEILGYDDQELPRDSSQPREGRVSISPMEIRAYKLELRPHK |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Predominant presence of unprocessed hybrid N-glycans (PubMed:16460512).
Reduced levels of glycoprotein N-glycans (PubMed:21478158).
Increased sensitivity to salt stress (PubMed:18408158).
Reduced levels of glycoprotein N-glycans (PubMed:21478158).
Increased sensitivity to salt stress (PubMed:18408158).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 68 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000432115 | 1-1173 | Alpha-mannosidase 2 | |||
Sequence: MPFSSYIGNSRRSSTGGGTGGWGQSLLPTALSKSKLAINRKPRKRTLVVNFIFANFFVIALTVSLLFFLLTLFHFGVPGPISSRFLTSRSNRIVKPRKNINRRPLNDSNSGAVVDITTKDLYDRIEFLDTDGGPWKQGWRVTYKDDEWEKEKLKIFVVPHSHNDPGWKLTVEEYYQRQSRHILDTIVETLSKDSRRKFIWEEMSYLERWWRDASPNKQEALTKLVKDGQLEIVGGGWVMNDEANSHYFAIIEQIAEGNMWLNDTIGVIPKNSWAIDPFGYSSTMAYLLRRMGFENMLIQRTHYELKKDLAQHKNLEYIWRQSWDAMETTDIFVHMMPFYSYDIPHTCGPEPAICCQFDFARMRGFKYELCPWGKHPVETTLENVQERALKLLDQYRKKSTLYRTNTLLIPLGDDFRYISIDEAEAQFRNYQMLFDHINSNPSLNAEAKFGTLEDYFRTVREEADRVNYSRPGEVGSGQVVGFPSLSGDFFTYADRQQDYWSGYYVSRPFFKAVDRVLEHTLRGAEIMMSFLLGYCHRIQCEKFPTSFTYKLTAARRNLALFQHHDGVTGTAKDYVVQDYGTRMHTSLQDLQIFMSKAIEVLLGIRHEKEKSDQSPSFFEAEQMRSKYDARPVHKPIAAREGNSHTVILFNPSEQTREEVVTVVVNRAEISVLDSNWTCVPSQISPEVQHDDTKLFTGRHRLYWKASIPALGLRTYFIANGNVECEKATPSKLKYASEFDPFPCPPPYSCSKLDNDVTEIRNEHQTLVFDVKNGSLRKIVHRNGSETVVGEEIGMYSSPESGAYLFKPDGEAQPIVQPDGHVVTSEGLLVQEVFSYPKTKWEKSPLSQKTRLYTGGNTLQDQVVEIEYHVELLGNDFDDRELIVRYKTDVDNKKVFYSDLNGFQMSRRETYDKIPLQGNYYPMPSLAFIQGSNGQRFSVHSRQSLGVASLKEGWLEIMLDRRLVRDDGRGLGQGVMDNRAMTVVFHLLAESNISQADPASNTNPRNPSLLSHLIGAHLNYPINTFIAKKPQDISVRVPQYGSFAPLAKPLPCDLHIVNFKVPRPSKYSQQLEEDKPRFALILNRRAWDSAYCHKGRQVNCTSMANEPVNFSDMFKDLAASKVKPTSLNLLQEDMEILGYDDQELPRDSSQPREGRVSISPMEIRAYKLELRPHK | ||||||
Glycosylation | 106 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 262 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 467 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 675 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 772 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 782 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 991 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1098 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1108 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MPFSSYIGNSRRSSTGGGTGG |
Sequence similarities
Belongs to the glycosyl hydrolase 38 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,173
- Mass (Da)134,726
- Last updated2000-10-01 v1
- ChecksumC13CD004D8DE49F9
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ029214 EMBL· GenBank· DDBJ | AAY90120.1 EMBL· GenBank· DDBJ | mRNA | ||
AL391146 EMBL· GenBank· DDBJ | CAC01814.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED92095.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY052707 EMBL· GenBank· DDBJ | AAK96611.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF446883 EMBL· GenBank· DDBJ | AAL38616.1 EMBL· GenBank· DDBJ | mRNA |