P31755 · OCH1_YEAST
- ProteinInitiation-specific alpha-1,6-mannosyltransferase
- GeneOCH1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids480 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mannosyltransferase involved in outer chain elongation of asparagine-linked oligosaccharides of the type Man9GlcNAc2. Adds the first alpha-1,6-mannose to the Man8GlcNAc2 and Man9GlcNAc2, but not Man5GlcNAc2, endoplasmic reticulum intermediates. Represents the first enzymatic event required for synthesis of outer chain mannose linkages on yeast secretory proteins. Has also the potential to transfer a second alpha-1,6-mannose to the Man8GlcNAc2 core oligosaccharide.
Miscellaneous
Present with 9490 molecules/cell in log phase SD medium.
Catalytic activity
Cofactor
pH Dependence
Optimum pH is 7.5.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | Golgi cis cisterna | |
Cellular Component | mannan polymerase complex | |
Molecular Function | alpha-1,6-mannosyltransferase activity | |
Molecular Function | glycolipid 1,6-alpha-mannosyltransferase activity | |
Biological Process | protein N-linked glycosylation |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameInitiation-specific alpha-1,6-mannosyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP31755
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Single-pass type II membrane protein
Golgi apparatus membrane ; Single-pass type II membrane protein
Note: Is recycled between the trans-Golgi network and a late compartment of the endoplasmic reticulum.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-15 | Cytoplasmic | ||||
Sequence: MSRKLSHLIATRKSK | ||||||
Transmembrane | 16-30 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: TIVVTVLLIYSLLTF | ||||||
Topological domain | 31-480 | Lumenal | ||||
Sequence: HLSNKRLLSQFYPSKDDFKQTLLPTTSHSQDINLKKQITVNKKKNQLHNLRDQLSFAFPYDSQAPIPQRVWQTWKVGADDKNFPSSFRTYQKTWSGSYSPDYQYSLISDDSIIPFLENLYAPVPIVIQAFKLMPGNILKADFLRYLLLFARGGIYSDMDTMLLKPIDSWPSQNKSWLNNIIDLNKPIPYKNSKPSLLSSDEISHQPGLVIGIEADPDRDDWSEWYARRIQFCQWTIQAKPGHPILRELILNITATTLASVQNPGVPVSEMIDPRFEEDYNVNYRHKRRHDETYKHSELKNNKNVDGSDIMNWTGPGIFSDIIFEYMNNVLRYNSDILLINPNLNKNDEEGSESATTPAKDVDNDTLSKSTRKFYKKISESLQSSNSMPWEFFSFLKEPVIVDDVMVLPITSFSPDVGQMGAQSSDDKMAFVKHMFSGSWKEDADKNAGHK |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Stops growing at the early stage of bud formation and rapidly loses viability at the non-permissive temperature. Exhibits a defect in the initiation of the mannose outer chain. Leads to accumulation of free forms of oligosaccharides (fOSs).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 187 | Loss of mannosyltransferase activity. | ||||
Sequence: D → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 6 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_0000080563 | 1-480 | Initiation-specific alpha-1,6-mannosyltransferase | |||
Sequence: MSRKLSHLIATRKSKTIVVTVLLIYSLLTFHLSNKRLLSQFYPSKDDFKQTLLPTTSHSQDINLKKQITVNKKKNQLHNLRDQLSFAFPYDSQAPIPQRVWQTWKVGADDKNFPSSFRTYQKTWSGSYSPDYQYSLISDDSIIPFLENLYAPVPIVIQAFKLMPGNILKADFLRYLLLFARGGIYSDMDTMLLKPIDSWPSQNKSWLNNIIDLNKPIPYKNSKPSLLSSDEISHQPGLVIGIEADPDRDDWSEWYARRIQFCQWTIQAKPGHPILRELILNITATTLASVQNPGVPVSEMIDPRFEEDYNVNYRHKRRHDETYKHSELKNNKNVDGSDIMNWTGPGIFSDIIFEYMNNVLRYNSDILLINPNLNKNDEEGSESATTPAKDVDNDTLSKSTRKFYKKISESLQSSNSMPWEFFSFLKEPVIVDDVMVLPITSFSPDVGQMGAQSSDDKMAFVKHMFSGSWKEDADKNAGHK | ||||||
Glycosylation | 203 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 281 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 341 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 393 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Expression is regulated by SKN7, SLN1, and CDC4.
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 187-189 | DXD motif | ||||
Sequence: DMD |
Domain
The conserved DXD motif is involved in enzyme activity.
Sequence similarities
Belongs to the glycosyltransferase 32 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length480
- Mass (Da)55,156
- Last updated1993-07-01 v1
- Checksum6B0ACA09A9B17E72
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D11095 EMBL· GenBank· DDBJ | BAA01869.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z72560 EMBL· GenBank· DDBJ | CAA96740.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY692749 EMBL· GenBank· DDBJ | AAT92768.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006941 EMBL· GenBank· DDBJ | DAA08062.1 EMBL· GenBank· DDBJ | Genomic DNA |