STE24_YEAST
ID STE24_YEAST Reviewed; 453 AA.
AC P47154; D6VWT6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=CAAX prenyl protease 1;
DE EC=3.4.24.84;
DE AltName: Full=A-factor-converting enzyme;
DE AltName: Full=Prenyl protein-specific endoprotease 1;
DE Short=PPSEP 1;
GN Name=STE24; Synonyms=AFC1; OrderedLocusNames=YJR117W; ORFNames=J2032;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9015299; DOI=10.1083/jcb.136.2.271;
RA Fujimura-Kamada K., Nouvet F.J., Michaelis S.;
RT "A novel membrane-associated metalloprotease, Ste24p, is required for the
RT first step of NH2-terminal processing of the yeast a-factor precursor.";
RL J. Cell Biol. 136:271-285(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=9065405; DOI=10.1126/science.275.5307.1796;
RA Boyartchuk V.L., Ashby M.N., Rine J.;
RT "Modulation of Ras and a-factor function by carboxyl-terminal
RT proteolysis.";
RL Science 275:1796-1800(1997).
RN [5]
RP FUNCTION.
RX PubMed=9700155; DOI=10.1083/jcb.142.3.635;
RA Tam A., Nouvet F.J., Fujimura-Kamada K., Slunt H., Sisodia S.S.,
RA Michaelis S.;
RT "Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal
RT proteolysis and COOH-terminal CAAX processing.";
RL J. Cell Biol. 142:635-649(1998).
RN [6]
RP FUNCTION.
RX PubMed=9725832; DOI=10.1093/genetics/150.1.95;
RA Boyartchuk V.L., Rine J.;
RT "Roles of prenyl protein proteases in maturation of Saccharomyces
RT cerevisiae a-factor.";
RL Genetics 150:95-101(1998).
RN [7]
RP FUNCTION.
RX PubMed=10692417; DOI=10.1074/jbc.275.9.6227;
RA Schmidt W.K., Tam A., Michaelis S.;
RT "Reconstitution of the Ste24p-dependent N-terminal proteolytic step in
RT yeast a-Factor biogenesis.";
RL J. Biol. Chem. 275:6227-6233(2000).
RN [8]
RP CHARACTERIZATION.
RX PubMed=10825201; DOI=10.1128/mcb.20.12.4381-4392.2000;
RA Trueblood C.E., Boyartchuk V.L., Picologlou E.A., Rozema D., Poulter C.D.,
RA Rine J.;
RT "The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct
RT substrate specificities.";
RL Mol. Cell. Biol. 20:4381-4392(2000).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=9736709; DOI=10.1073/pnas.95.19.11175;
RA Schmidt W.K., Tam A., Fujimura-Kamada K., Michaelis S.;
RT "Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast
RT proteases involved in carboxyl-terminal CAAX protein processing and amino-
RT terminal a-factor cleavage.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11175-11180(1998).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Proteolytically removes the C-terminal three residues of
CC farnesylated A-factor mating pheromone. Also acts to cleave the N-
CC terminal extension of the pheromone. Does not act on Ras.
CC {ECO:0000269|PubMed:10692417, ECO:0000269|PubMed:9015299,
CC ECO:0000269|PubMed:9065405, ECO:0000269|PubMed:9700155,
CC ECO:0000269|PubMed:9725832}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The peptide bond hydrolyzed can be designated -C-|-A-A-X in
CC which C is an S-isoprenylated cysteine residue, A is usually
CC aliphatic and X is the C-terminal residue of the substrate protein,
CC and may be any of several amino acids.; EC=3.4.24.84;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:9736709}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9736709}.
CC -!- MISCELLANEOUS: Present with 19600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M48A family. {ECO:0000305}.
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DR EMBL; U77137; AAB38271.1; -; Genomic_DNA.
DR EMBL; Z49617; CAA89647.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08902.1; -; Genomic_DNA.
DR PIR; S57140; S57140.
DR RefSeq; NP_012651.1; NM_001181775.1.
DR AlphaFoldDB; P47154; -.
DR SMR; P47154; -.
DR BioGRID; 33873; 370.
DR DIP; DIP-1390N; -.
DR IntAct; P47154; 21.
DR MINT; P47154; -.
DR STRING; 4932.YJR117W; -.
DR ChEMBL; CHEMBL1741185; -.
DR DrugCentral; P47154; -.
DR MEROPS; M48.001; -.
DR TCDB; 9.B.1.1.3; the integral membrane caax protease (caax protease) family.
DR MaxQB; P47154; -.
DR PaxDb; P47154; -.
DR PRIDE; P47154; -.
DR DNASU; 853581; -.
DR EnsemblFungi; YJR117W_mRNA; YJR117W; YJR117W.
DR GeneID; 853581; -.
DR KEGG; sce:YJR117W; -.
DR SGD; S000003878; STE24.
DR VEuPathDB; FungiDB:YJR117W; -.
DR eggNOG; KOG2719; Eukaryota.
DR GeneTree; ENSGT00390000002053; -.
DR HOGENOM; CLU_025947_3_3_1; -.
DR InParanoid; P47154; -.
DR OMA; LPFKIYK; -.
DR BioCyc; MetaCyc:YJR117W-MON; -.
DR BioCyc; YEAST:YJR117W-MON; -.
DR BRENDA; 3.4.24.84; 984.
DR PRO; PR:P47154; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47154; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005637; C:nuclear inner membrane; IMP:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:SGD.
DR GO; GO:0071586; P:CAAX-box protein processing; IMP:SGD.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IMP:SGD.
DR GO; GO:0120236; P:negative regulation of post-translational protein targeting to membrane, translocation; IMP:SGD.
DR GO; GO:0071432; P:peptide mating pheromone maturation involved in positive regulation of conjugation with cellular fusion; IDA:SGD.
DR GO; GO:0016485; P:protein processing; IDA:SGD.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR CDD; cd07343; M48A_Zmpste24p_like; 1.
DR InterPro; IPR027057; CAXX_Prtase_1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR032456; Peptidase_M48_N.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF16491; Peptidase_M48_N; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Pheromone response; Protease; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..453
FT /note="CAAX prenyl protease 1"
FT /id="PRO_0000138846"
FT TOPO_DOM 1..12
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..121
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..197
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..357
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 394
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 297
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 453 AA; 52324 MW; 331CC9AE2D7C99DA CRC64;
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
