CAAX prenyl protease 1 (P47154)

Identification
NameCAAX prenyl protease 1
Synonyms
  • A-factor-converting enzyme
  • Prenyl protein-specific endoprotease 1
  • PPSEP 1
Gene NameSTE24
Enzyme Class
Biological Properties
General FunctionPosttranslational modification, protein turnover, chaperones
Specific FunctionProteolytically removes the C-terminal three residues of farnesylated A-factor mating pheromone. Also acts to cleave the N- terminal extension of the pheromone. Does not act on Ras
Cellular LocationEndoplasmic reticulum membrane; Multi-pass membrane protein
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG Reactions
protein ↔ conjugated protein
Metabolites
YMDB IDNameView
GO Classification
Component
cell part
membrane
Function
catalytic activity
hydrolase activity
peptidase activity
peptidase activity, acting on L-amino acid peptides
endopeptidase activity
metalloendopeptidase activity
Process
metabolic process
macromolecule metabolic process
protein metabolic process
proteolysis
Gene Properties
Chromosome LocationNot Available
Locus
Gene Sequence>1362 bp ATGTTTGATCTTAAGACGATTCTCGACCATCCTAATATCCCGTGGAAATTAATCATTTCT GGGTTCTCGATTGCCCAATTTTCTTTCGAATCTTACTTGACGTACAGACAGTACCAGAAG CTATCTGAAACAAAGTTGCCACCTGTGCTGGAAGACGAAATTGATGATGAAACTTTTCAT AAATCAAGGAACTACTCCCGGGCCAAGGCCAAGTTCTCCATTTTCGGTGACGTCTATAAC CTAGCCCAAAAGCTAGTTTTCATCAAATACGACCTCTTCCCTAAAATCTGGCACATGGCC GTTTCTTTATTGAATGCAGTCCTGCCAGTCAGATTTCATATGGTCTCCACTGTCGCACAG AGTTTATGCTTCTTGGGTCTCTTATCCAGTTTGTCTACCTTGGTTGATTTGCCACTCTCT TACTATAGCCATTTTGTCCTGGAAGAAAAATTTGGTTTCAATAAATTGACCGTCCAACTA TGGATCACCGATATGATCAAGAGTCTGACTTTGGCGTATGCTATTGGTGGCCCAATCCTT TACCTGTTCCTTAAGATCTTTGATAAATTCCCTACTGATTTCCTTTGGTACATTATGGTC TTCTTGTTCGTTGTCCAAATCTTAGCCATGACAATCATTCCAGTCTTCATCATGCCCATG TTTAATAAGTTCACTCCATTGGAGGACGGTGAACTGAAAAAATCTATTGAAAGTTTGGCC GATAGAGTTGGGTTCCCTCTAGATAAGATTTTTGTCATTGACGGCTCAAAAAGATCTTCT CATTCAAACGCATATTTCACAGGTTTGCCATTCACCTCCAAGAGAATTGTTTTGTTCGAC ACTTTAGTGAACAGTAATTCTACTGATGAAATTACGGCTGTTTTGGCCCATGAAATCGGT CACTGGCAAAAAAACCACATCGTTAATATGGTCATCTTTAGTCAATTGCACACCTTCCTC ATTTTCTCCCTTTTCACCAGCATCTACAGAAATACATCATTTTACAACACCTTCGGCTTT TTCTTAGAGAAGTCCACTGGCAGTTTTGTTGATCCCGTTATCACTAAGGAATTCCCCATT ATCATTGGATTTATGTTATTTAACGACTTATTAACTCCACTCGAATGTGCCATGCAATTC GTGATGAGTTTAATTTCCAGAACTCATGAATATCAAGCTGATGCTTATGCTAAAAAATTG GGCTACAAGCAAAATCTATGTAGGGCTCTAATTGATCTACAAATCAAAAACCTTTCCACC ATGAATGTAGATCCTCTGTATTCTAGCTATCATTATTCCCATCCAACTCTAGCTGAAAGA TTGACCGCTCTAGACTATGTTAGTGAAAAGAAGAAAAACTAA
Protein Properties
Pfam Domain Function
Protein Residues453
Protein Molecular Weight52323.60156
Protein Theoretical pI8.09
Signalling Regions
  • None
Transmembrane Regions
  • 13-33
  • 90-110
  • 122-142
  • 168-188
  • 198-218
  • 307-327
  • 358-378
Protein Sequence>CAAX prenyl protease 1 MFDLKTILDHPNIPWKLIISGFSIAQFSFESYLTYRQYQKLSETKLPPVLEDEIDDETFH KSRNYSRAKAKFSIFGDVYNLAQKLVFIKYDLFPKIWHMAVSLLNAVLPVRFHMVSTVAQ SLCFLGLLSSLSTLVDLPLSYYSHFVLEEKFGFNKLTVQLWITDMIKSLTLAYAIGGPIL YLFLKIFDKFPTDFLWYIMVFLFVVQILAMTIIPVFIMPMFNKFTPLEDGELKKSIESLA DRVGFPLDKIFVIDGSKRSSHSNAYFTGLPFTSKRIVLFDTLVNSNSTDEITAVLAHEIG HWQKNHIVNMVIFSQLHTFLIFSLFTSIYRNTSFYNTFGFFLEKSTGSFVDPVITKEFPI IIGFMLFNDLLTPLECAMQFVMSLISRTHEYQADAYAKKLGYKQNLCRALIDLQIKNLST MNVDPLYSSYHYSHPTLAERLTALDYVSEKKKN
References
External Links
ResourceLink
Saccharomyces Genome Database STE24
Uniprot IDP47154
Uniprot NameSTE24_YEAST
GenBank Gene IDU77137
Genebank Protein ID1679741
General Reference
  • Fujimura-Kamada, K., Nouvet, F. J., Michaelis, S. (1997). "A novel membrane-associated metalloprotease, Ste24p, is required for the first step of NH2-terminal processing of the yeast a-factor precursor." J Cell Biol 136:271-285.9015299
  • Galibert, F., Alexandraki, D., Baur, A., Boles, E., Chalwatzis, N., Chuat, J. C., Coster, F., Cziepluch, C., De Haan, M., Domdey, H., Durand, P., Entian, K. D., Gatius, M., Goffeau, A., Grivell, L. A., Hennemann, A., Herbert, C. J., Heumann, K., Hilger, F., Hollenberg, C. P., Huang, M. E., Jacq, C., Jauniaux, J. C., Katsoulou, C., Karpfinger-Hartl, L., et, a. l. .. (1996). "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." EMBO J 15:2031-2049.8641269
  • Boyartchuk, V. L., Ashby, M. N., Rine, J. (1997). "Modulation of Ras and a-factor function by carboxyl-terminal proteolysis." Science 275:1796-1800.9065405
  • Tam, A., Nouvet, F. J., Fujimura-Kamada, K., Slunt, H., Sisodia, S. S., Michaelis, S. (1998). "Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processing." J Cell Biol 142:635-649.9700155
  • Boyartchuk, V. L., Rine, J. (1998). "Roles of prenyl protein proteases in maturation of Saccharomyces cerevisiae a-factor." Genetics 150:95-101.9725832
  • Schmidt, W. K., Tam, A., Michaelis, S. (2000). "Reconstitution of the Ste24p-dependent N-terminal proteolytic step in yeast a-factor biogenesis." J Biol Chem 275:6227-6233.10692417
  • Trueblood, C. E., Boyartchuk, V. L., Picologlou, E. A., Rozema, D., Poulter, C. D., Rine, J. (2000). "The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities." Mol Cell Biol 20:4381-4392.10825201
  • Schmidt, W. K., Tam, A., Fujimura-Kamada, K., Michaelis, S. (1998). "Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage." Proc Natl Acad Sci U S A 95:11175-11180.9736709
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Kim, H., Melen, K., Osterberg, M., von Heijne, G. (2006). "A global topology map of the Saccharomyces cerevisiae membrane proteome." Proc Natl Acad Sci U S A 103:11142-11147.16847258