Q12563 · MNS1B_ASPPH
- ProteinMannosyl-oligosaccharide alpha-1,2-mannosidase 1B
- Genemns1B
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids513 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Involved in the maturation of Asn-linked oligosaccharides. Progressively trims alpha-1,2-linked mannose residues from Man9GlcNAc2 to produce Man5GlcNAc2.
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)
Cofactor
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )
Note: Ca2+. Can also use Mg2+, but with lower efficiency.
Pathway
Protein modification; protein glycosylation.
Features
Showing features for active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic vesicle lumen | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | membrane | |
Molecular Function | calcium ion binding | |
Molecular Function | mannosyl-oligosaccharide 1,2-alpha-mannosidase activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | ERAD pathway | |
Biological Process | protein glycosylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMannosyl-oligosaccharide alpha-1,2-mannosidase 1B
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus
Accessions
- Primary accessionQ12563
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MHLPSLSLSLTALAIASPSAA | ||||||
Chain | PRO_0000394821 | 22-513 | Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B | |||
Sequence: YPHFGSSQPVLHSSSDTTQSRADAIKAAFSHAWDGYLQYAFPHDELHPVSNGYGDSRNGWGASAVDALSTAVIMRNATIVNQILDHVGKIDYSKTNTTVSLFETTIRYLGGMLSGYDLLKGPVSDLVQNSSKIDVLLTQSKNLADVLKFAFDTPSGVPYNNLNITSGGNDGAKTNGLAVTGTLALEWTRLSDLTGDTTYADLSQKAESYLLNPQPKSAEPFPGLVGSNINISNGQFTDAQVSWNGGDDSYYEYLIKMYVYDPKRFGLYKDRWVAAAQSTMQHLASHPSSRPDLTFLASYNNGTLGLSSQHLTCFDGGSFLLGGTVLNRTDFINFGLDLVSGCHDTYNSTLTGIGPESFSWDTSDIPSSQQSLYEKAGFYITSGAYILRPEVIESFYYAWRVTGQETYRDWIWSAFSAVNDYCRTSSGFSGLTDVNAANGGSRYDNQESFLFAEVMKYSYMAFAEDAAWQVQPGSGNQFVFNTEAHPVRVSST | ||||||
Glycosylation | 97 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 117 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 150 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 184 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 251 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 322 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 334↔363 | |||||
Sequence: CFDGGSFLLGGTVLNRTDFINFGLDLVSGC | ||||||
Glycosylation | 348 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 368 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Interaction
Subunit
Monomer.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length513
- Mass (Da)55,875
- Last updated1996-11-01 v1
- Checksum0FDAB2CB27E93724