P27614 · CBPS_YEAST
- ProteinCarboxypeptidase S
- GeneCPS1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids576 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Necessary for use of certain peptides as sole nitrogen source. May also cleave intracellularly generated peptides to recycle amino acids for protein synthesis.
Miscellaneous
Present with 721 molecules/cell in log phase SD medium.
Catalytic activity
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 168 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 170 | |||||
Sequence: D | ||||||
Binding site | 205 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 205 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 239 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 240 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 268 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 547 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | fungal-type vacuole | |
Cellular Component | fungal-type vacuole lumen | |
Cellular Component | vacuolar lumen | |
Cellular Component | vacuolar membrane | |
Molecular Function | carboxypeptidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | metallocarboxypeptidase activity | |
Biological Process | proteolysis involved in protein catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCarboxypeptidase S
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP27614
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Vacuole membrane ; Single-pass membrane protein
Note: Lysosome-like vacuoles.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-19 | Cytoplasmic | ||||
Sequence: MIALPVEKAPRKSLWQRHR | ||||||
Transmembrane | 20-40 | Helical | ||||
Sequence: AFISGIVALIIIGTFFLTSGL | ||||||
Topological domain | 41-576 | Lumenal | ||||
Sequence: HPAPPHEAKRPHHGKGPMHSPKCEKIEPLSPSFKHSVDTILHDPAFRNSSIEKLSNAVRIPTVVQDKNPNPADDPDFYKHFYELHDYFEKTFPNIHKHLKLEKVNELGLLYTWEGSDPDLKPLLLMAHQDVVPVNNETLSSWKFPPFSGHYDPETDFVWGRGSNDCKNLLIAEFEAIEQLLIDGFKPNRTIVMSLGFDEEASGTLGAASLASFLHERYGDDGIYSIIDEGEGIMEVDKDVFVATPINAEKGYVDFEVSILGHGGHSSVPPDHTTIGIASELITEFEANPFDYEFEFDNPIYGLLTCAAEHSKSLSKDVKKTILGAPFCPRRKDKLVEYISNQSHLRSLIRTTQAVDIINGGVKANALPETTRFLINHRINLHSSVAEVFERNIEYAKKIAEKYGYGLSKNGDDYIIPETELGHIDITLLRELEPAPLSPSSGPVWDILAGTIQDVFENGVLQNNEEFYVTTGLFSGNTDTKYYWNLSKNIYRFVGSIIDIDLLKTLHSVNEHVDVPGHLSAIAFVYEYIVNVNEYA |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, cross-link, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000185271 | 1-576 | Carboxypeptidase S | |||
Sequence: MIALPVEKAPRKSLWQRHRAFISGIVALIIIGTFFLTSGLHPAPPHEAKRPHHGKGPMHSPKCEKIEPLSPSFKHSVDTILHDPAFRNSSIEKLSNAVRIPTVVQDKNPNPADDPDFYKHFYELHDYFEKTFPNIHKHLKLEKVNELGLLYTWEGSDPDLKPLLLMAHQDVVPVNNETLSSWKFPPFSGHYDPETDFVWGRGSNDCKNLLIAEFEAIEQLLIDGFKPNRTIVMSLGFDEEASGTLGAASLASFLHERYGDDGIYSIIDEGEGIMEVDKDVFVATPINAEKGYVDFEVSILGHGGHSSVPPDHTTIGIASELITEFEANPFDYEFEFDNPIYGLLTCAAEHSKSLSKDVKKTILGAPFCPRRKDKLVEYISNQSHLRSLIRTTQAVDIINGGVKANALPETTRFLINHRINLHSSVAEVFERNIEYAKKIAEKYGYGLSKNGDDYIIPETELGHIDITLLRELEPAPLSPSSGPVWDILAGTIQDVFENGVLQNNEEFYVTTGLFSGNTDTKYYWNLSKNIYRFVGSIIDIDLLKTLHSVNEHVDVPGHLSAIAFVYEYIVNVNEYA | ||||||
Cross-link | 8 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | ||||||
Glycosylation | 88 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 176 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 228 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 381 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 525 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Glycosylated.
Ubiquitinated. Ubiquitination mediates sorting into internal vesicles in late endosomes. TUL1 is required for ubiquitination.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
yscS is synthesized as one polypeptide chain precursor which after carbohydrate modification in the secretory pathway yields two active precursor molecules. The proteolytically unprocessed forms are associated with the membrane, whereas the mature forms of the enzyme are soluble.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 44-65 | Disordered | ||||
Sequence: PPHEAKRPHHGKGPMHSPKCEK |
Domain
The transmembrane domain contains polar residues that mediate the recognition by TUL1.
Sequence similarities
Belongs to the peptidase M20A family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length576
- Mass (Da)64,597
- Last updated1995-11-01 v2
- Checksum5CBB536D421B5F70
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 387 | in Ref. 2; CAA40571 | ||||
Sequence: S → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X57316 EMBL· GenBank· DDBJ | CAA40571.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X63068 EMBL· GenBank· DDBJ | CAA44790.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z49447 EMBL· GenBank· DDBJ | CAA89467.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006943 EMBL· GenBank· DDBJ | DAA08632.1 EMBL· GenBank· DDBJ | Genomic DNA |