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9.B.1.1.3
The CAAX integral membrane zinc prenyl metaloprotease, CAAX PP or Ste24p of 453 aas and 7 TMSs, found in every kingdom of eukaryotes. It's 3-D structure has been solved (Goblirsch and Wiener 2020). It is a factor responsible for processing the yeast mating a-factor pheromone. In animals, Ste24 processes prelamin, a component of the nuclear lamina; mutations in the human ortholog of Ste24 diminish its activity, giving rise to genetic diseases of accelerated aging (progerias). Additionally, lipodystrophy, acquired from the standard highly active antiretroviral therapy (HAART) used to treat AIDS patients, likely results from off-target interactions of HIV (aspartyl) protease inhibitor drugs with Ste24. Ste24 possesses a novel "α-barrel" structure, consisting of a ring of seven transmembrane α-helices enclosing a large (> 12,000 Å3) interior volume that contains the active-site and substrate-binding region; this "membrane-interior reaction chamber" is unprecedented in integral membrane protein structures. Additionally, the surface of the membrane-interior reaction chamber possesses a strikingly large negative electrostatic surface potential. Ste24p may be a key factor in several endoplasmic reticulum (ER) processes, including the unfolded protein response, a cellular stress response of the ER, and removal of misfolded proteins from the translocon. Ste24p is thus a "translocon unclogger". Goblirsch and Wiener 2020 have reviewed the sturcture and functions of Ste24 structure.

Accession Number:P47154
Protein Name:CAAX prenyl protease 1
Length:453
Molecular Weight:52324.00
Species:Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [559292]
Number of TMSs:5
Location1 / Topology2 / Orientation3: Endoplasmic reticulum membrane1 / Multi-pass membrane protein2
Substrate prenyl

Cross database links:

Structure:
4il3     

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FASTA formatted sequence
1:	MFDLKTILDH PNIPWKLIIS GFSIAQFSFE SYLTYRQYQK LSETKLPPVL EDEIDDETFH 
61:	KSRNYSRAKA KFSIFGDVYN LAQKLVFIKY DLFPKIWHMA VSLLNAVLPV RFHMVSTVAQ 
121:	SLCFLGLLSS LSTLVDLPLS YYSHFVLEEK FGFNKLTVQL WITDMIKSLT LAYAIGGPIL 
181:	YLFLKIFDKF PTDFLWYIMV FLFVVQILAM TIIPVFIMPM FNKFTPLEDG ELKKSIESLA 
241:	DRVGFPLDKI FVIDGSKRSS HSNAYFTGLP FTSKRIVLFD TLVNSNSTDE ITAVLAHEIG 
301:	HWQKNHIVNM VIFSQLHTFL IFSLFTSIYR NTSFYNTFGF FLEKSTGSFV DPVITKEFPI 
361:	IIGFMLFNDL LTPLECAMQF VMSLISRTHE YQADAYAKKL GYKQNLCRAL IDLQIKNLST 
421:	MNVDPLYSSY HYSHPTLAER LTALDYVSEK KKN