SPC3/YLR066W Summary Help

Standard Name SPC3
Systematic Name YLR066W
Feature Type ORF, Verified
Description Subunit of signal peptidase complex (Spc1p, Spc2p, Spc3p, Sec11p), which catalyzes cleavage of N-terminal signal sequences of proteins targeted to the secretory pathway; homologous to mammalian SPC22/23 (1, 2 and see Summary Paragraph)
Name Description Signal Peptidase Complex 2
Chromosomal Location
ChrXII:267169 to 267723 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All SPC3 GO evidence and references
  View Computational GO annotations for SPC3
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant phenotypes All SPC3 Phenotype evidence and references
Large-scale survey
null
overexpression
reduction of function
repressible
Resources
interactions All SPC3 Interaction evidence and references
17 total interaction(s) for 14 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 7
  • Affinity Capture-RNA: 2
  • PCA: 2
Genetic Interactions
  • Dosage Rescue: 1
  • Positive Genetic: 1
  • Synthetic Lethality: 4
Resources
Expression Summary
histogram
Resources
Protein Information All SPC3 Protein evidence and references
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXII:267169 to 267723 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..555 267169..267723 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004056
SUMMARY PARAGRAPH for SPC3

SPC3 encodes a subunit of the signal peptidase complex (SPC), which cleaves the signal sequence from proteins targeted to the endoplasmic reticulum (ER) (1, 2). Signal peptide cleavage occurs concomitantly with translocation through the translocon pore into the ER. In yeast, translocation can occur cotranslationally or posttranslationally, whereas in mammals translocation is always cotranslational. The process of protein translocation into the ER is reviewed in references 3 and 4.

The yeast SPC comprises four proteins, Spc1p, Spc2p, Spc3p, and Sec11p (5, 6). Spc3p is homologous to the mammalian signal peptidase subunit SPC22/23 (1, 2). SPC3 is essential for viability and for signal peptidase activity (1, 2). Depletion of Spc3p causes loss of signal peptidase activity and reduces levels of the other SPC proteins (2). Overexpression of SPC3 suppresses a temperature-sensitive mutation in SEC11, which encodes the catalytic SPC subunit (1), and Spc3p and Sec11p can be coimmunoprecipitated (7).

Last updated: 2000-12-08

References cited on this page View Complete Literature Guide for SPC3
1) Fang H, et al.  (1997) In addition to SEC11, a newly identified gene, SPC3, is essential for signal peptidase activity in the yeast endoplasmic reticulum. J Biol Chem 272(20):13152-8
2) Meyer HA and Hartmann E  (1997) The yeast SPC22/23 homolog Spc3p is essential for signal peptidase activity. J Biol Chem 272(20):13159-64
3) Rapoport TA, et al.  (1996) Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu Rev Biochem 65:271-303
4) Johnson AE and van Waes MA  (1999) The translocon: a dynamic gateway at the ER membrane. Annu Rev Cell Dev Biol 15:799-842
5) YaDeau JT, et al.  (1991) Yeast signal peptidase contains a glycoprotein and the Sec11 gene product. Proc Natl Acad Sci U S A 88(2):517-21
6) Antonin W, et al.  (2000) Interactions between Spc2p and other components of the endoplasmic reticulum translocation sites of the yeast Saccharomyces cerevisiae. J Biol Chem 275(44):34068-72
7) VanValkenburgh C, et al.  (1999) The catalytic mechanism of endoplasmic reticulum signal peptidase appears to be distinct from most eubacterial signal peptidases. J Biol Chem 274(17):11519-25