ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.
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SPAC24C9.08 localizes to the fungal-type vacuole based on YFP tagging in high-throughput study
"we determined the localization of 4,431 proteins, corresponding to approximately 90% of the fission yeast proteome, by tagging each ORF with the yellow fluorescent protein"
The Secreted Enzyme PM20D1 Regulates Lipidated Amino Acid Uncouplers of Mitochondria
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PM20D1 is a bidirectional N-fatty-acyl-amino acid synthase/hydrolase that has diverged from classical carboxypeptidase function
"We demonstrate that PM20D1 is a bidirectional enzyme in vitro, catalyzing both the condensation of fatty acids and amino acids to generate N-acyl amino acids and also the reverse hydrolytic reaction"
Carboxypeptidase yscS: gene structure and function of the vacuolar enzyme.
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S. cerevisiae CPS1 is a vacuolar carboxypeptidase with Gly-Xaa specificity
"Chromosomal disruption of the CPS1 gene completely abolishes carboxypeptidase yscS activity"
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CPS1 enables growth on Cbz-Gly-Leu as sole leucine source
"The cloned CPS1 gene, which again enabled a leucine auxotrophic cps1-3 mutant to grow on the modified dipeptide Cbz-Gly-Leu (Cbz, benzyloxycarbonyl) as sole leucine source"
Biogenesis of the yeast vacuole (lysosome). The precursor forms of the soluble hydrolase carboxypeptidase yscS are associated with the vacuolar membrane.
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Carboxypeptidase yscS precursor is membrane-associated, mature enzyme is soluble in vacuolar lumen
"The mature forms of carboxypeptidase yscS appeared soluble in the vacuolar lumen, while the precursor proteins accumulated tightly associated with the vacuolar membrane"
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Carboxypeptidase yscS is synthesized as type II transmembrane precursor (77 and 74 kDa glycoforms)
"After assembly into the vacuolar membrane, proteinase yscB presumably cleaves the precursor molecules to release soluble carboxypeptidase yscS forms into the lumen of the vacuole"
Gene Ontology annotation through association of InterPro records with GO terms.
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping.
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods.
Deep research on SPAC24C9.08 vacuolar carboxypeptidase (Perplexity)
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SPAC24C9.08 is annotated as a vacuolar carboxypeptidase S belonging to the M20A family, but this is based on sequence homology rather than direct biochemical characterization.
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The gene symbol "cps1" in S. pombe is ambiguous - it also refers to bgs1 (SPBC19G7.05c), which encodes a completely different enzyme (1,3-beta-glucan synthase).
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The M20 family employs a co-catalytic mechanism involving two zinc ions per monomer at the active site center.
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Based on S. cerevisiae CPS1 (which HAS been characterized), the enzyme would exhibit preference for glycine and leucine residues at the P1 site and contribute approximately 60% of vacuolar activity for hydrolyzing specific synthetic dipeptides.
Deep research on SPAC24C9.08 vacuolar carboxypeptidase (Cyberian)
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SpCPS belongs to the M20A subfamily of metallopeptidases, part of the larger M20 family within clan MH.
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The protein contains the peptidase M20 catalytic domain (IPR002933), the peptidase M20 dimer domain (IPR011650), the bacterial exopeptidase dimerization domain (IPR036264), and the M20A-specific domain (IPR047177).
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SpCPS has four lysine residues (K16, K19, K32, and K33) in its putative N-terminal cytoplasmic domain, which are potential sites for ubiquitination required for MVB sorting.
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The precise substrate specificity profile of SpCPS has not been systematically characterized. Several aspects of SpCPS biology remain incompletely understood.
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No experimental structure of SpCPS or the S. cerevisiae ortholog CPS1 is currently available.
Deep research on SPAC24C9.08 M20A metallopeptidase (Falcon)
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The gene symbol "cps1" is ambiguous - in S. pombe it commonly denotes a different, well-studied membrane glucan synthase (Bgs1), while SPAC24C9.08 is an M20A metallopeptidase.
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M20A subfamily members prominently include aminoacylases (Acy1-like) that hydrolyze non-peptidic amide bonds in N-acyl-L-amino acids, not peptide bonds in proteins.
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M20A enzymes are zinc-dependent metallopeptidases with a Zn2+-bound water nucleophile and conserved metal coordination involving two histidines and two glutamates.
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Eukaryotic M20A members include Acy1 and PM20D1; the family shows remarkable functional divergence from classical carboxypeptidase activity to aminoacylase activity.
Essential roles of class E Vps proteins for sorting into multivesicular bodies in Schizosaccharomyces pombe.
UniProt O13968 (SPAC24C9.08) target record