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SPC3 protein (Saccharomyces cerevisiae) - STRING interaction network
"SPC3" - Subunit of signal peptidase complex (Spc1p, Spc2p, Spc3p, Sec11p), which catalyzes cleavage of N-terminal signal sequences of proteins targeted to the secretory pathway in Saccharomyces cerevisiae
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Predicted Interactions
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protein homology
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SPC3Subunit 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; Component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post- translationally) through the translocon pore into the endoplasmic reticulum. SPC3 is required for signal peptidase activity and is essential for [...] (184 aa)    
Predicted Functional Partners:
SEC11
18kDa catalytic subunit of the Signal Peptidase Complex (SPC; Spc1p, Spc2p, Spc3p, and Sec11p) which cleaves the signal sequence of proteins targeted to the endoplasmic reticulum; Catalytic component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum (167 aa)
     
  0.999
SPC1
Subunit of the signal peptidase complex (SPC), which cleaves the signal sequence from proteins targeted to the endoplasmic reticulum (ER), homolog of the SPC12 subunit of mammalian signal peptidase complex; Nonessential component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum. SPC3 is not required for signal peptidase activity (94 aa)
     
  0.982
SPC2
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 SPC25; Nonessential component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum. SPC2 enhances the enzymatic activity of SPC and facilitate [...] (178 aa)
     
  0.979
OST2
Epsilon subunit of the oligosaccharyltransferase complex of the ER lumen, which catalyzes asparagine-linked glycosylation of newly synthesized proteins; Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation a [...] (130 aa)
     
      0.795
KAR2
ATPase involved in protein import into the ER, also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis (682 aa)
     
 
  0.784
IMP1
Catalytic subunit of the mitochondrial inner membrane peptidase complex, required for maturation of mitochondrial proteins of the intermembrane space; complex contains Imp1p and Imp2p (both catalytic subunits), and Som1p; Catalytic component of the mitochondrial inner membrane peptidase (IMP) complex. IMP catalyzes the removal of signal peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter- membrane space. The two catalytic IMP subunits seem to have non- overlapping substrate specificities. IMP1 substrates include nucle [...] (190 aa)
     
   
  0.732
YMR035W
Catalytic subunit of the mitochondrial inner membrane peptidase complex, required for maturation of mitochondrial proteins of the intermembrane space; complex contains Imp1p and Imp2p (both catalytic subunits), and Som1p; Catalytic component of the mitochondrial inner membrane peptidase (IMP) complex. IMP catalyzes the removal of signal peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter- membrane space. The two catalytic IMP subunits seem to have non- overlapping substrate specificities. IMP2 substrates include nucle [...] (177 aa)
     
   
  0.732
OLE1
Delta(9) fatty acid desaturase, required for monounsaturated fatty acid synthesis and for normal distribution of mitochondria; Stearyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed-1978720, PubMed-7947684). Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed-1978720). Required for the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (PubMed-1978720, Pu [...] (510 aa)
     
      0.697
PET309
Specific translational activator for the COX1 mRNA, also influences stability of intron-containing COX1 primary transcripts; localizes to the mitochondrial inner membrane; contains seven pentatricopeptide repeats (PPRs); Required for initiation of translation of the COX1 coding region. Also involved in the stability of the intron containing transcript of COX1 (965 aa)
           
  0.572
ERD2
HDEL receptor, an integral membrane protein that binds to the HDEL motif in proteins destined for retention in the endoplasmic reticulum; has a role in maintenance of normal levels of ER-resident proteins; Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi. This receptor strongly recognizes H-D- E-L and weakly recognizes D-D-E-L and K-D-E-L (219 aa)
     
 
  0.512
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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