Basic Information
Name | CAAX prenyl protease 1 (EC 3.4.24.84) (A-factor-converting enzyme) (Prenyl protein-specific endoprotease 1) (PPSEP 1) |
Uniprot ID | P47154 |
Systematic gene name | YJR117W |
Standard gene name | STE24 |
Gene names | STE24 AFC1 YJR117W J2032 |
Description from SGD | YJR117W STE24 SGDID:S000003878, Chr X from 642007-643368, Genome Release 64-3-1, Verified ORF, "Highly conserved zinc metalloprotease; component of the ER quality control mechanism that removes faulty proteins clogging translocation channels; inhibits SRP-independent translocation into the ER; has two roles in a-factor maturation, C-terminal CAAX proteolysis and the first step of N-terminal proteolytic processing; cleaves isoprenylated and non-prenylated oligopeptides; human homolog ZMPSTE24 implicated in mandibuloacral dysplasia (MAD), and complements the null mutant" |
Protein length | 453 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MFDLKTILDH PNIPWKLIIS GFSIAQFSFE SYLTYRQYQK LSETKLPPVL
EDEIDDETFH KSRNYSRAKA KFSIFGDVYN LAQKLVFIKY DLFPKIWHMA
VSLLNAVLPV RFHMVSTVAQ SLCFLGLLSS LSTLVDLPLS YYSHFVLEEK
FGFNKLTVQL WITDMIKSLT LAYAIGGPIL YLFLKIFDKF PTDFLWYIMV
FLFVVQILAM TIIPVFIMPM FNKFTPLEDG ELKKSIESLA DRVGFPLDKI
FVIDGSKRSS HSNAYFTGLP FTSKRIVLFD TLVNSNSTDE ITAVLAHEIG
HWQKNHIVNM VIFSQLHTFL IFSLFTSIYR NTSFYNTFGF FLEKSTGSFV
DPVITKEFPI IIGFMLFNDL LTPLECAMQF VMSLISRTHE YQADAYAKKL
GYKQNLCRAL IDLQIKNLST MNVDPLYSSY HYSHPTLAER LTALDYVSEK
KKN
EDEIDDETFH KSRNYSRAKA KFSIFGDVYN LAQKLVFIKY DLFPKIWHMA
VSLLNAVLPV RFHMVSTVAQ SLCFLGLLSS LSTLVDLPLS YYSHFVLEEK
FGFNKLTVQL WITDMIKSLT LAYAIGGPIL YLFLKIFDKF PTDFLWYIMV
FLFVVQILAM TIIPVFIMPM FNKFTPLEDG ELKKSIESLA DRVGFPLDKI
FVIDGSKRSS HSNAYFTGLP FTSKRIVLFD TLVNSNSTDE ITAVLAHEIG
HWQKNHIVNM VIFSQLHTFL IFSLFTSIYR NTSFYNTFGF FLEKSTGSFV
DPVITKEFPI IIGFMLFNDL LTPLECAMQF VMSLISRTHE YQADAYAKKL
GYKQNLCRAL IDLQIKNLST MNVDPLYSSY HYSHPTLAER LTALDYVSEK
KKN
Legend
- X K-acetylation
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[398, K-acetyl] | Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications) |
[419, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[420, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |