Cloned (Comment) | Organism |
---|---|
recombinant expression of His-tagged chimeric enzyme constructs in Escherichia coli strain BL21 (DE3) | Mus musculus |
recombinant expression of His-tagged chimeric enzyme constructs in Escherichia coli strain BL21(DE3) | Homo sapiens |
recombinant expression of His-tagged chimeric enzyme constructs in Escherichia coli strain BL21(DE3) | Thermochaetoides thermophila |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of a bi-cistronic construct containing human SRalpha subunit and murine SRbeta subunit lacking the transmembrane domain and cloning in the pET16b vector. Linker deletion variants of SR are created using the same construct | Homo sapiens |
additional information | construction of a bi-cistronic construct containing human SRalpha subunit and murine SRbeta subunit lacking the transmembrane domain and cloning in the pET16b vector. Linker deletion variants of SR are created using the same construct | Mus musculus |
additional information | while CtSRalpha complexed with SRbetaDELTAN can bind ribosomes, both CtSRbetaDELTAN alone and the minimal CtSRalpha138/SRbetaDELTAN complex are unable to bind ribosomes. Full-length CtSRalpha alone readily binds to the ribosomes in a sedimentation assay, as well as to canine ribosomes | Thermochaetoides thermophila |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
endoplasmic reticulum membrane | - |
Homo sapiens | 5789 | - |
endoplasmic reticulum membrane | - |
Mus musculus | 5789 | - |
endoplasmic reticulum membrane | - |
Thermochaetoides thermophila | 5789 | - |
membrane | peripheral membrane protein subunit SRalpha, which is anchored to the membrane by the 30 kDa subunit SRbeta, that has a single N-terminal transmembrane domain and short luminal domain | Homo sapiens | 16020 | - |
membrane | peripheral membrane protein subunit SRalpha, which is anchored to the membrane by the 30 kDa subunit SRbeta, that has a single N-terminal transmembrane domain and short luminal domain | Mus musculus | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Homo sapiens | |
Mg2+ | required | Mus musculus | |
Mg2+ | required | Thermochaetoides thermophila |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
GTP + H2O | Homo sapiens | - |
GDP + phosphate | - |
? | |
GTP + H2O | Mus musculus | - |
GDP + phosphate | - |
? | |
GTP + H2O | Thermochaetoides thermophila | - |
GDP + phosphate | - |
? | |
GTP + H2O | Thermochaetoides thermophila IMI 039719 | - |
GDP + phosphate | - |
? | |
GTP + H2O | Thermochaetoides thermophila DSM 1495 | - |
GDP + phosphate | - |
? | |
GTP + H2O | Thermochaetoides thermophila CBS 144.50 | - |
GDP + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P08240 AND Q9Y5M8 | subunits SRalpha and SRbeta | - |
Mus musculus | Q9DBG7 AND P47758 | subunits SRalpha and SRbeta | - |
Thermochaetoides thermophila | G0SD15 | signal recognition particle 54 kDa protein subunit with GTPase activity | - |
Thermochaetoides thermophila CBS 144.50 | G0SD15 | signal recognition particle 54 kDa protein subunit with GTPase activity | - |
Thermochaetoides thermophila DSM 1495 | G0SD15 | signal recognition particle 54 kDa protein subunit with GTPase activity | - |
Thermochaetoides thermophila IMI 039719 | G0SD15 | signal recognition particle 54 kDa protein subunit with GTPase activity | - |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged chimeric enzyme constructs from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography,anion exchange chromatography, and cation exchange chromatography, followed by gel filtration | Mus musculus |
recombinant His-tagged chimeric enzyme constructs from Escherichia coli strain BL21(DE3) | Thermochaetoides thermophila |
recombinant His-tagged chimeric enzyme constructs from Escherichia coli strain BL21(DE3) by nickel affinity chromatography,anion exchange chromatography, and cation exchange chromatography, followed by gel filtration | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
GTP + H2O | - |
Homo sapiens | GDP + phosphate | - |
? | |
GTP + H2O | - |
Mus musculus | GDP + phosphate | - |
? | |
GTP + H2O | - |
Thermochaetoides thermophila | GDP + phosphate | - |
? | |
GTP + H2O | - |
Thermochaetoides thermophila IMI 039719 | GDP + phosphate | - |
? | |
GTP + H2O | - |
Thermochaetoides thermophila DSM 1495 | GDP + phosphate | - |
? | |
GTP + H2O | - |
Thermochaetoides thermophila CBS 144.50 | GDP + phosphate | - |
? | |
additional information | both SRalpha and SRbeta are GTPases | Homo sapiens | ? | - |
- |
|
additional information | both SRalpha and SRbeta are GTPases | Mus musculus | ? | - |
- |
|
additional information | both SRalpha and SRbeta are GTPases | Thermochaetoides thermophila | ? | - |
- |
|
additional information | both SRalpha and SRbeta are GTPases | Thermochaetoides thermophila IMI 039719 | ? | - |
- |
|
additional information | both SRalpha and SRbeta are GTPases | Thermochaetoides thermophila DSM 1495 | ? | - |
- |
|
additional information | both SRalpha and SRbeta are GTPases | Thermochaetoides thermophila CBS 144.50 | ? | - |
- |
Subunits | Comment | Organism |
---|---|---|
heterodimer | 1 * 70000, subunit SRalpha, + 1 * 30000, subunit SRbeta, SDS-PAGE | Homo sapiens |
heterodimer | 1 * 70000, subunit SRalpha, + 1 * 30000, subunit SRbeta, SDS-PAGE | Mus musculus |
More | in eukaryotes, SR is composed of two subunits, the 70 kDa peripheral membrane protein SRalpha, which is anchored to the membrane by the 30 kDa SRbeta, which has a single N-terminal transmembrane (TM) domain and short luminal domain. Both SRalpha and SRbeta are GTPases | Homo sapiens |
More | in eukaryotes, SR is composed of two subunits, the 70 kDa peripheral membrane protein SRalpha, which is anchored to the membrane by the 30 kDa SRbeta, which has a single N-terminal transmembrane (TM) domain and short luminal domain. Both SRalpha and SRbeta are GTPases | Mus musculus |
Synonyms | Comment | Organism |
---|---|---|
CtSR | - |
Thermochaetoides thermophila |
GTPase | - |
Homo sapiens |
GTPase | - |
Mus musculus |
GTPase | - |
Thermochaetoides thermophila |
signal recognition particle receptor subunit alpha | - |
Homo sapiens |
signal recognition particle receptor subunit alpha | - |
Mus musculus |
signal recognition particle receptor subunit beta | - |
Homo sapiens |
signal recognition particle receptor subunit beta | - |
Mus musculus |
SRalpha | - |
Homo sapiens |
SRalpha | - |
Mus musculus |
SRPRA | gene name, subunit SRalpha | Homo sapiens |
SRPRA | gene name, subunit SRalpha | Mus musculus |
SRPRB | gene name, subunit SRbeta | Homo sapiens |
SRPRB | gene name, subunit SRbeta | Mus musculus |
General Information | Comment | Organism |
---|---|---|
evolution | SR ribosome binding is evolutionarily conserved | Homo sapiens |
evolution | SR ribosome binding is evolutionarily conserved | Mus musculus |
evolution | SR ribosome binding is evolutionarily conserved. Unlike the ribosome-binding activity of human SRalpha, CtSRalpha is unable to destabilize the interaction between protein translocase subunit Sec61beta and the Sec translocase-associated endoplasmic reticulum membrane protein Sec62, suggesting that this interaction is specific to higher eukaryotes | Thermochaetoides thermophila |
malfunction | in contrast to the Sec61beta-SRalpha cross-link species, which increase in abundance when SR is added to EKRMs (membranes stripped of ribosomes with EDTA and high salt), most other Sec61beta-derived cross-linked adducts are reduced, in particular, the cross-link between Sec61beta and Sec62. A mutant SRP receptor, which contains only the SRX domain of SRalpha (SRalpha126/betaDN), shows a much weaker reduction in Sec61beta-Sec62 crosslinking | Homo sapiens |
malfunction | in contrast to the Sec61beta-SRalpha cross-link species, which increase in abundance when SR is added to EKRMs (membranes stripped of ribosomes with EDTA and high salt), most other Sec61beta-derived cross-linked adducts are reduced, in particular, the cross-link between Sec61beta and Sec62. A mutant SRP receptor, which contains only the SRX domain of SRalpha (SRalpha126/betaDN), shows a much weaker reduction in Sec61beta-Sec62 crosslinking | Mus musculus |
metabolism | two distinct pathways deliver secretory proteins to the Sec61 protein translocase in the endoplasmic reticulum (ER) membrane. The canonical pathway requires the signal recognition particle (SRP) and its cognate receptor (SR), and targets ribosome-associated proteins to the Sec translocase. The SRP-independent pathway requires the Sec translocase-associated ER membrane protein Sec62 and can be uncoupled from translation. SR switches translocons to SRP-dependent translocation by displacing Sec62. This activity localizes to the charged linker region between the longin and GTPase domains of SRalpha. A second pathway promotes ribosome binding and is conserved between all eukaryotes. These specific regions in SRalpha reprogramme the Sec translocon and facilitate recruitment of ribosome-nascent chain complexes | Homo sapiens |
metabolism | two distinct pathways deliver secretory proteins to the Sec61 protein translocase in the endoplasmic reticulum (ER) membrane. The canonical pathway requires the signal recognition particle (SRP) and its cognate receptor (SR), and targets ribosome-associated proteins to the Sec translocase. The SRP-independent pathway requires the Sec translocase-associated ER membrane protein Sec62 and can be uncoupled from translation. SR switches translocons to SRP-dependent translocation by displacing Sec62. This activity localizes to the charged linker region between the longin and GTPase domains of SRalpha. A second pathway promotes ribosome binding and is conserved between all eukaryotes. These specific regions in SRalpha reprogramme the Sec translocon and facilitate recruitment of ribosome-nascent chain complexes | Mus musculus |
additional information | binding of SR to Sec61 positions SRalpha close to Sec61beta | Homo sapiens |
additional information | binding of SR to Sec61 positions SRalpha close to Sec61beta | Mus musculus |
physiological function | two distinct pathways deliver secretory proteins to the Sec61 protein translocase in the endoplasmic reticulum (ER) membrane. The canonical pathway requires the signal recognition particle (SRP) and its cognate receptor (SR), and targets ribosome-associated proteins to the Sec translocase. The SRP-independent pathway requires the Sec translocase-associated ER membrane protein Sec62 and can be uncoupled from translation. SR switches translocons to SRP-dependent translocation by displacing Sec62. This activity localizes to the charged linker region between the longin and GTPase domains of SRalpha. Both SRalpha and SRbeta are GTPases. SR inhibits translocation of Sec62-dependent substrates | Homo sapiens |
physiological function | two distinct pathways deliver secretory proteins to the Sec61 protein translocase in the endoplasmic reticulum (ER) membrane. The canonical pathway requires the signal recognition particle (SRP) and its cognate receptor (SR), and targets ribosome-associated proteins to the Sec translocase. The SRP-independent pathway requires the Sec translocase-associated ER membrane protein Sec62 and can be uncoupled from translation. SR switches translocons to SRP-dependent translocation by displacing Sec62. This activity localizes to the charged linker region between the longin and GTPase domains of SRalpha. Both SRalpha and SRbeta are GTPases. SR inhibits translocation of Sec62-dependent substrates | Mus musculus |