Structurally related Spc1p and Spc2p of yeast signal peptidase complex are functionally distinct.

doi:10.1074/jbc.271.46.29094

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Article

Structurally related Spc1p and Spc2p of yeast signal peptidase complex are functionally distinct.

The Journal of biological chemistry - 15 Nov 1996

Mullins C, Meyer H A, Hartmann E, Green N, Fang H

Abstract excerpt

Two subunits of the mammalian signal peptidase complex, SPC12 and SPC25, share similar membrane topologies with the majority of each protein oriented toward the cytoplasm. Such similarities may suggest that these proteins perform redundant functions in signal peptidase activity. In the present st...

Topics

Amino Acid Sequence
Animals
Calcium-Calmodulin-Dependent Protein Kinases
Cloning, Molecular
Dogs
Fungal Proteins
Hot Temperature
Membrane Proteins
Mitogen-Activated Protein Kinases
Molecular Sequence Data
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Precursors

Saccharomyces cerevisiae

Saccharomyces cerevisiae Proteins

Schizosaccharomyces pombe Proteins

Sequence Homology, Amino Acid

Serine Endopeptidases

Source

Open in PubMed

Identifiers

PMID: 8910564
DOI: 10.1074/jbc.271.46.29094

Genes

SPC25

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8910564-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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