Use of the ND evidence code for Gene Ontology (GO) terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
The nucleotide sequence of a third cyclophilin-homologous gene from Saccharomyces cerevisiae.
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CPR4/SCC3 encodes a cyclophilin-homologous protein with two hydrophobic regions — an N-terminal signal peptide and a C-terminal transmembrane-like helix — making it a likely secretory or membrane protein.
"Its putative protein product (Scc3) contains two hydrophobic cores, one at the amino terminal, 20 amino acids long, which could serve as a signal peptide, and the other one at the carboxyl end with a structure similar to a transmembrane helix."
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The only cyclophilin with the same dual topology is Drosophila NinaA, a secretory-pathway transmembrane cyclophilin implicated in rhodopsin folding, suggesting an analogous foldase role for CPR4 on different, unidentified target proteins.
"The only cyclophilin with similar structure to that of Scc3 is ninaA from Drosophila melanogaster, a transmembrane protein which seems to be implicated in the correct folding and/or intercalation of rhodopsin in the endoplasmic reticulum of the fly photoreceptors"
All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae.
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CPR4 is the secretory-pathway cyclophilin of S. cerevisiae; CPR8 is its homolog. None of the eight yeast cyclophilins is essential, and a strain lacking all 12 immunophilins is viable, with little evidence of functional overlap.
"Cpr8, a homolog of the secretory pathway cyclophilin Cpr4"
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The physiological functions of yeast immunophilins are largely unknown; each is proposed to act on a small set of unique, as-yet-unidentified partner proteins.
"the physiological functions of these proteins are largely unknown"
The cyclophilins.
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Cpr4 and Cpr8 each contain a single cyclophilin-like domain plus a long N-terminal signal peptide and are localized to vacuoles.
"Cpr4 and Cpr8 contain a single CLD domain plus a long amino-terminal signal peptide and are located in vacuoles"
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None of the eight individual yeast cyclophilins is essential, and an octuple mutant lacking all eight is viable with little or no evidence of functional redundancy.
"an octuplet mutant lacking all eight cyclophilins was viable and that there was little or no evidence for functional redundancy"
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Drosophila NinaA, the structural analog of Cpr4, is an ortholog of mammalian CypC and is crucial for folding of rhodopsin isoforms.
"NinaA (an ortholog of mammal CypC), is crucial for the folding of rhodopsin isoforms"
Prolyl isomerases in yeast.
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Comprehensive review of the S. cerevisiae prolyl isomerase repertoire (cyclophilins, FKBPs, parvulins), providing family-level context for Cpr4 among Cpr1-Cpr8.
"Prolyl isomerases in yeast."
One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy.
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Genome-wide N-terminal GFP tagging (SWAT) of endomembrane proteins assigned many proteins to the ER, punctate structures and the vacuole; CPR4 received its high-throughput vacuole localization from this class of systematic screen.
"most new localization assignments were to the ER, punctate structures and vacuole"
Falcon deep research report for CPR4 (Edison Scientific Literature)
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The tryptophan equivalent to human cyclophilin A W121 (a key cyclosporin A contact) is replaced by glutamate in CPR4/Scc3, predicting reduced cyclosporin A binding while leaving catalytic PPIase features intact.
"the conserved cyclophilin residue equivalent to W121, important for cyclosporin A binding in other cyclophilins, is replaced by glutamate in Scc3/CPR4"
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No direct biochemical measurement of CPR4 PPIase catalytic activity, substrate specificity, or kinetics has been reported, and its precise cellular function is unresolved.
"direct biochemical measurement of Cpr4's PPIase catalytic activity, substrate specificity, or kinetic parameters has not been reported"