P27614 · CBPS_YEAST

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

  • Release of a C-terminal amino acid from a peptide in which glycine is the penultimate amino acid, e.g. Z-Gly-|-Leu.
    EC:3.4.17.4 (UniProtKB | ENZYME | Rhea)

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Features

Showing features for binding site, active site.

157650100150200250300350400450500550
TypeIDPosition(s)Description
Binding site168Zn2+ 2 (UniProtKB | ChEBI)
Active site170
Binding site205Zn2+ 1 (UniProtKB | ChEBI)
Binding site205Zn2+ 2 (UniProtKB | ChEBI)
Active site239Proton acceptor
Binding site240Zn2+ 1 (UniProtKB | ChEBI)
Binding site268Zn2+ 2 (UniProtKB | ChEBI)
Binding site547Zn2+ 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentfungal-type vacuole
Cellular Componentfungal-type vacuole lumen
Cellular Componentvacuolar lumen
Cellular Componentvacuolar membrane
Molecular Functioncarboxypeptidase activity
Molecular Functionmetal ion binding
Molecular Functionmetallocarboxypeptidase activity
Biological Processproteolysis involved in protein catabolic process

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Carboxypeptidase S
  • EC number
  • Alternative names
    • GLY-X carboxypeptidase
    • YSCS

Gene names

    • Name
      CPS1
    • Synonyms
      CPS
    • ORF names
      J0510
    • Ordered locus names
      YJL172W

Organism names

Accessions

  • Primary accession
    P27614
  • Secondary accessions
    • D6VW16

Proteomes

Organism-specific databases

Subcellular Location

Vacuole membrane
; Single-pass membrane protein
Note: Lysosome-like vacuoles.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-19Cytoplasmic
Transmembrane20-40Helical
Topological domain41-576Lumenal

Keywords

PTM/Processing

Features

Showing features for chain, cross-link, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00001852711-576Carboxypeptidase S
Cross-link8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Glycosylation88N-linked (GlcNAc...) asparagine
Glycosylation176N-linked (GlcNAc...) asparagine
Glycosylation228N-linked (GlcNAc...) asparagine
Glycosylation381N-linked (GlcNAc...) asparagine
Glycosylation525N-linked (GlcNAc...) asparagine

Post-translational modification

Glycosylated.
Ubiquitinated. Ubiquitination mediates sorting into internal vesicles in late endosomes. TUL1 is required for ubiquitination.

Keywords

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.

TypeIDPosition(s)Description
Region44-65Disordered

Domain

The transmembrane domain contains polar residues that mediate the recognition by TUL1.

Sequence similarities

Belongs to the peptidase M20A family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    576
  • Mass (Da)
    64,597
  • Last updated
    1995-11-01 v2
  • Checksum
    5CBB536D421B5F70
MIALPVEKAPRKSLWQRHRAFISGIVALIIIGTFFLTSGLHPAPPHEAKRPHHGKGPMHSPKCEKIEPLSPSFKHSVDTILHDPAFRNSSIEKLSNAVRIPTVVQDKNPNPADDPDFYKHFYELHDYFEKTFPNIHKHLKLEKVNELGLLYTWEGSDPDLKPLLLMAHQDVVPVNNETLSSWKFPPFSGHYDPETDFVWGRGSNDCKNLLIAEFEAIEQLLIDGFKPNRTIVMSLGFDEEASGTLGAASLASFLHERYGDDGIYSIIDEGEGIMEVDKDVFVATPINAEKGYVDFEVSILGHGGHSSVPPDHTTIGIASELITEFEANPFDYEFEFDNPIYGLLTCAAEHSKSLSKDVKKTILGAPFCPRRKDKLVEYISNQSHLRSLIRTTQAVDIINGGVKANALPETTRFLINHRINLHSSVAEVFERNIEYAKKIAEKYGYGLSKNGDDYIIPETELGHIDITLLRELEPAPLSPSSGPVWDILAGTIQDVFENGVLQNNEEFYVTTGLFSGNTDTKYYWNLSKNIYRFVGSIIDIDLLKTLHSVNEHVDVPGHLSAIAFVYEYIVNVNEYA

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict387in Ref. 2; CAA40571

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp