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RIP1

Gene
rip1
Protein
Zinc metalloprotease Rip1
Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Length
406 amino acids
Function
Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal (possibly oxidative stress) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein (includes anti-sigma factors RskA, RslA, RsmA, and PbpB) is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this entry), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein (ECF sigma factors SigK, SigL and SigM).
Similarity
Belongs to the peptidase M50B family.
Mass
42.91 kDa
Sequence
MMFGIGIVLFALAILVSVALHECGHMWVARATGMKVRRYFVGFGPTLWSTRRANRLGSTEYGIKAIPLGGFCDIAGMTSVDEIAPEDRPYAMYKQKVWKRVAVLFAGPAMNFVIGLVLIYGIAIVWGLPNLHQPTTAIVGETGCVAPQITLEEMGECTGPGPAALAGIQAGDEIVKVGDTEVKDFAGMAAAVRKLDGPTRIEFKRDGRVMDTVVDVTPTQRFTSADASAPSTVGAIGVSAVPVQPPAQYNPITAVPATFAFTGDLAVELGKSLAKIPTKIGALVEAIGGGERDKETPISVVGASIIGGETVDAGLWVAFWFFLAQLNFVLGAINLVPLLPFDGGHIAVATYEKIRNMIRSARGMVAAGPVNYLKLMPATYVVLAVVAGYMLLTVTADLVNPLSIFQ

Gene
rip1
Protein
Zinc metalloprotease Rip1
Organism
Mycobacterium bovis (strain BCG / Pasteur 1173P2)
Length
404 amino acids
Function
Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal (possibly oxidative stress) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein (includes anti-sigma factors RskA, RslA, RsmA, and PbpB in M.tuberculosis) is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this entry), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein (ECF sigma factors SigK, SigL and SigM) (Probable).
Similarity
Belongs to the peptidase M50B family.
Mass
42.912 kDa
Sequence
MMFVTGIVLFALAILISVALHECGHMWVARRTGMKVRRYFVGFGPTLWSTRRGETEYGVKAVPLGGFCDIAGMTPVEELDPDERDRAMYKQATWKRVAVLFAGPGMNLAICLVLIYAIALVWGLPNLHPPTRAVIGETGCVAQEVSQGKLEQCTGPGPAALAGIRSGDVVVKVGDTPVSSFDEMAAAVRKSHGSVPIVVERDGTAIVTYVDIESTQRWIPNGQGGELQPATVGAIGVGAARVGPVRYGVFSAMPATFAFTGDLTVEVGKALAALPTKVGALVRAIGGGQRDPQTPISVVGASIIGGDTVDHGLWVAFWFFLAQLNLILATINLLPLLPFDGGHIAVAVFERIRNMVRSARGKVAAAPVNYLKLLPATYVVLVLVVGYMLLTVTADLVNPIRLFQ

Gene
rip1
Protein
Zinc metalloprotease Rip1
Organism
Mycobacterium leprae (strain TN)
Length
404 amino acids
Function
A probable intramembrane site-2 protease (S2P) that cleaves type-2 transmembrane proteins within their membrane-spanning domains. Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal (possibly oxidative stress) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this entry), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein.
Similarity
Belongs to the peptidase M50B family.
Mass
42.875 kDa
Sequence
MMFALGIVLFAIAILISVALHECGHLWVACATGMKVRRYFVGFGPTLWSTRRGETQYGIKAVPLGGFCDIVGMTSVEKLEPDESDRAMYKQATWKRVAVLFAGPAMNFVICLVLIYGIALVWGLPNLHMPTRAVIGETACVASELDQGKLGNCTGPGPAALAGLRAGDVVVKIGDTTVSTFDDMAAVVRKLHGTVPIVFERDGTAITSYVDITPTQRYMSKGKGSQLEPATVGAIGVGAHHLLPTHYGVFSALPATAAFAGDLTVEVGKALVTIPTKLGALVHAIGGGQRDPQTPMSVVGASIIGGDTVDHGLWVAFWFFLAQLNLILGAINLVPLLPFDGGHIAIAVFERIRNLIRSARGVVVAAPVNYLKLMPATYVVLVFVVGYVLLTVTADLVNPIRLFQ

Gene
rip1
Protein
Zinc metalloprotease Rip1
Organism
Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
Length
404 amino acids
Function
Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal (possibly oxidative stress) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein (includes anti-sigma factors RskA, RslA, RsmA, and PbpB) is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this entry), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein (ECF sigma factors SigK, SigL and SigM).
Similarity
Belongs to the peptidase M50B family.
Mass
42.834 kDa
Sequence
MMFVTGIVLFALAILISVALHECGHMWVARRTGMKVRRYFVGFGPTLWSTRRGETEYGVKAVPLGGFCDIAGMTPVEELDPDERDRAMYKQATWKRVAVLFAGPGMNLAICLVLIYAIALVWGLPNLHPPTRAVIGETGCVAQEVSQGKLEQCTGPGPAALAGIRSGDVVVKVGDTPVSSFDEMAAAVRKSHGSVPIVVERDGTAIVTYVDIESTQRWIPNGQGGELQPATVGAIGVGAARVGPVRYGVFSAMPATFAVTGDLTVEVGKALAALPTKVGALVRAIGGGQRDPQTPISVVGASIIGGDTVDHGLWVAFWFFLAQLNLILAAINLLPLLPFDGGHIAVAVFERIRNMVRSARGKVAAAPVNYLKLLPATYVVLVLVVGYMLLTVTADLVNPIRLFQ

Gene
rip1
Protein
Zinc metalloprotease Rip1
Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Length
404 amino acids
Function
Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal (possibly oxidative stress) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein (includes anti-sigma factors RskA, RslA, RsmA, and PbpB in M.tuberculosis) is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this entry), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein (ECF sigma factors SigK, SigL and SigM) (By similarity).
Similarity
Belongs to the peptidase M50B family.
Mass
42.834 kDa
Sequence
MMFVTGIVLFALAILISVALHECGHMWVARRTGMKVRRYFVGFGPTLWSTRRGETEYGVKAVPLGGFCDIAGMTPVEELDPDERDRAMYKQATWKRVAVLFAGPGMNLAICLVLIYAIALVWGLPNLHPPTRAVIGETGCVAQEVSQGKLEQCTGPGPAALAGIRSGDVVVKVGDTPVSSFDEMAAAVRKSHGSVPIVVERDGTAIVTYVDIESTQRWIPNGQGGELQPATVGAIGVGAARVGPVRYGVFSAMPATFAVTGDLTVEVGKALAALPTKVGALVRAIGGGQRDPQTPISVVGASIIGGDTVDHGLWVAFWFFLAQLNLILAAINLLPLLPFDGGHIAVAVFERIRNMVRSARGKVAAAPVNYLKLLPATYVVLVLVVGYMLLTVTADLVNPIRLFQ

Gene
rip1
Protein
Zinc metalloprotease Rip1
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Length
404 amino acids
Function
Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal (possibly oxidative stress) triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. The membrane-spanning regulatory substrate protein (includes anti-sigma factors RskA, RslA, RsmA, and PbpB in M.tuberculosis) is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this entry), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein (ECF sigma factors SigK, SigL and SigM).
Similarity
Belongs to the peptidase M50B family.
Mass
42.834 kDa
Sequence
MMFVTGIVLFALAILISVALHECGHMWVARRTGMKVRRYFVGFGPTLWSTRRGETEYGVKAVPLGGFCDIAGMTPVEELDPDERDRAMYKQATWKRVAVLFAGPGMNLAICLVLIYAIALVWGLPNLHPPTRAVIGETGCVAQEVSQGKLEQCTGPGPAALAGIRSGDVVVKVGDTPVSSFDEMAAAVRKSHGSVPIVVERDGTAIVTYVDIESTQRWIPNGQGGELQPATVGAIGVGAARVGPVRYGVFSAMPATFAVTGDLTVEVGKALAALPTKVGALVRAIGGGQRDPQTPISVVGASIIGGDTVDHGLWVAFWFFLAQLNLILAAINLLPLLPFDGGHIAVAVFERIRNMVRSARGKVAAAPVNYLKLLPATYVVLVLVVGYMLLTVTADLVNPIRLFQ

Gene
RIP1
Protein
Heterotepalin-4
Organism
Phytolacca heterotepala
Length
312 amino acids
Function
Inhibits protein synthesis in vitro.
Similarity
Belongs to the ribosome-inactivating protein family. Type 1 RIP subfamily.
Mass
35.153 kDa
Sequence
MKSMLVVTISVWLILAPTSTWAVNTIIYNVGSTTISKYATFLDDLRNEAKDPNLKCYGIPMLPNTNSNPKYVLVELQGSNKKTITLMLRRNNLYVMGYSDPFDTSKCRYHIFNDISGTERQDVETTLCPNSNSRVSKNINYDSRYPTLESKVGVKSRSQVQLGIQILDSDIGKISGVTSFSEKTEAEFLLVAIQISEAARFKYIENQVKTNFNRAFNPNPKVLNLEETWGKISTAIHDAKNGVLPKPLELVDASGAKWIVLRVDEIKPDVALLNYVSGSCQTTYNQNAMFPQLIMSTYYNYMANLGDLFEEF

Gene
rip1
Protein
Cytochrome b-c1 complex subunit Rieske, mitochondrial
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Length
228 amino acids
Function
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
Mass
24.74 kDa
Sequence
MLAKQFISKSLASSLRRLLPVSSTASSLKGSMMTIPKFTSIRTYTDSPEMPDFSEYQTKSTGDRSRVISYAMVGTMGALTAAGAQATVHDFLASWSASADVLAMSKAEVDLSKIPEGKNLVVKWQGKPVFIRHRTPEEIQEANSVDISTLRDPQADSDRVQKPEWLVMIGVCTHLGCVPIGEAGDYGGWFCPCHGSHYDISGRIRRGPAPLNLAIPAYTFEGSKIIIG

Gene
RIP1
Protein
Cytochrome b-c1 complex subunit Rieske, mitochondrial
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
215 amino acids
Function
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c.
Mass
23.365 kDa
Sequence
MLGIRSSVKTCFKPMSLTSKRLISQSLLASKSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAGAKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDPQWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGDKVIVG