Gene Ontology annotation through association of InterPro records with GO terms
Use of the ND evidence code for Gene Ontology (GO) terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotations Inferred by Curator (IC) using at least one Inferred by Sequence Similarity (ISS) annotation to support the inference
A sensitive predictor for potential GPI lipid modification sites in fungal protein sequences and its application to genome-wide studies for Aspergillus nidulans, Candida albicans, Neurospora crassa, Saccharomyces cerevisiae and Schizosaccharomyces pombe.
ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.
UniProtKB O94380: curated sequence, features and source attribution
Falcon deep-research report for fission-yeast gpi16
The GPI transamidase complex of Saccharomyces cerevisiae contains Gaa1p, Gpi8p, and Gpi16p.
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Budding-yeast affinity purification establishes Gpi16 as a GPI-transamidase component, providing direct ortholog evidence.
"These complexes can be affinity purified
and are shown to consist of Gaa1p, Gpi8p, and Gpi16p (YHR188c)."
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Budding-yeast Gpi16 is a type-I ER membrane glycoprotein whose bulk faces the lumen.
"Its bulk resides on the
lumenal side of the ER, and it has a single C-terminal transmembrane domain"
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Depleting Gpi16 blocks attachment of the anchor to protein but not synthesis of the GPI lipid.
"Depletion of Gpi16p results in the accumulation of the complete GPI lipid CP2 and of
unprocessed GPI precursor proteins."
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Gpi16 and Gpi8 stabilise each other.
"Gpi8p and Gpi16p are unstable if either of them is removed by depletion."
PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8.
Structure of human glycosylphosphatidylinositol transamidase.
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The human structure and mutational study identifies PIGK, not PIGT, as the catalytic component.
"The PIGK subunit
functions as the catalytic component"
Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge.
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In mammalian cells PIG-T is disulfide-linked to GPI8; the bond is required for full transamidase activity but not essential, and the five-subunit complex holds substrate proteins.
"The formation of this disulfide bond is not essential but"