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Protein

CAAX prenyl protease 1

Gene

STE24

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Proteolytically 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.5 Publications

Catalytic activityi

The peptide bond hydrolyzed can be designated -C-|-A-A-X in which C is an S-isoprenylated cysteine residue, A is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi297 – 2971Zinc; catalyticPROSITE-ProRule annotation
Active sitei298 – 2981PROSITE-ProRule annotation
Metal bindingi301 – 3011Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi390 – 3901Zinc; catalyticPROSITE-ProRule annotation
Active sitei394 – 3941Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • metalloendopeptidase activity Source: SGD

GO - Biological processi

  • CAAX-box protein processing Source: SGD
  • peptide mating pheromone maturation involved in conjugation with cellular fusion Source: SGD
  • response to pheromone Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Pheromone response

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:YJR117W-MONOMER.
YEAST:YJR117W-MONOMER.
BRENDAi3.4.24.84. 984.

Protein family/group databases

MEROPSiM48.001.
TCDBi9.B.1.1.3. the integral membrane caax protease (caax protease) family.

Names & Taxonomyi

Protein namesi
Recommended name:
CAAX prenyl protease 1 (EC:3.4.24.84)
Alternative name(s):
A-factor-converting enzyme
Prenyl protein-specific endoprotease 1
Short name:
PPSEP 1
Gene namesi
Name:STE24
Synonyms:AFC1
Ordered Locus Names:YJR117W
ORF Names:J2032
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR117W.
SGDiS000003878. STE24.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212LumenalSequence analysisAdd
BLAST
Transmembranei13 – 3321HelicalSequence analysisAdd
BLAST
Topological domaini34 – 8956CytoplasmicSequence analysisAdd
BLAST
Transmembranei90 – 11021HelicalSequence analysisAdd
BLAST
Topological domaini111 – 12111LumenalSequence analysisAdd
BLAST
Transmembranei122 – 14221HelicalSequence analysisAdd
BLAST
Topological domaini143 – 16725CytoplasmicSequence analysisAdd
BLAST
Transmembranei168 – 18821HelicalSequence analysisAdd
BLAST
Topological domaini189 – 1979LumenalSequence analysis
Transmembranei198 – 21821HelicalSequence analysisAdd
BLAST
Topological domaini219 – 30688CytoplasmicSequence analysisAdd
BLAST
Transmembranei307 – 32721HelicalSequence analysisAdd
BLAST
Topological domaini328 – 35730LumenalSequence analysisAdd
BLAST
Transmembranei358 – 37821HelicalSequence analysisAdd
BLAST
Topological domaini379 – 45375CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of endoplasmic reticulum membrane Source: SGD
  • nuclear inner membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1741185.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453CAAX prenyl protease 1PRO_0000138846Add
BLAST

Proteomic databases

MaxQBiP47154.
PeptideAtlasiP47154.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
AGP1P253761EBI-18298,EBI-2357
CAB3P360761EBI-18298,EBI-26778
CHO1P084561EBI-18298,EBI-14055
EMC2P471331EBI-18298,EBI-25568
ERG11P106141EBI-18298,EBI-5127
ERP1Q053591EBI-18298,EBI-6581
KRE27P405401EBI-18298,EBI-24977
NCP1P166031EBI-18298,EBI-11940
OST1P415431EBI-18298,EBI-12651
PHO84P252971EBI-18298,EBI-13320
PHO88P382641EBI-18298,EBI-13350
PMP2P409751EBI-18298,EBI-2043041
PPZ1P265701EBI-18298,EBI-13807
RTN1Q049471EBI-18298,EBI-38020
SAC1P323681EBI-18298,EBI-16210
SEC63P149061EBI-18298,EBI-16636
SPF1P399861EBI-18298,EBI-3128
SSA2P105921EBI-18298,EBI-8603
YET1P357231EBI-18298,EBI-26730

Protein-protein interaction databases

BioGridi33873. 233 interactions.
DIPiDIP-1390N.
IntActiP47154. 21 interactions.
MINTiMINT-410624.

Structurei

3D structure databases

ProteinModelPortaliP47154.
SMRiP47154. Positions 11-446.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M48A family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000002053.
HOGENOMiHOG000257874.
InParanoidiP47154.
KOiK06013.
OMAiKKQGCNN.
OrthoDBiEOG74N5S9.

Family and domain databases

InterProiIPR027057. CAXX_Prtase_1.
IPR001915. Peptidase_M48.
IPR032456. Peptidase_M48_N.
[Graphical view]
PANTHERiPTHR10120:SF24. PTHR10120:SF24. 1 hit.
PfamiPF01435. Peptidase_M48. 1 hit.
PF16491. Peptidase_M48_N. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47154-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFDLKTILDH PNIPWKLIIS GFSIAQFSFE SYLTYRQYQK LSETKLPPVL
60 70 80 90 100
EDEIDDETFH KSRNYSRAKA KFSIFGDVYN LAQKLVFIKY DLFPKIWHMA
110 120 130 140 150
VSLLNAVLPV RFHMVSTVAQ SLCFLGLLSS LSTLVDLPLS YYSHFVLEEK
160 170 180 190 200
FGFNKLTVQL WITDMIKSLT LAYAIGGPIL YLFLKIFDKF PTDFLWYIMV
210 220 230 240 250
FLFVVQILAM TIIPVFIMPM FNKFTPLEDG ELKKSIESLA DRVGFPLDKI
260 270 280 290 300
FVIDGSKRSS HSNAYFTGLP FTSKRIVLFD TLVNSNSTDE ITAVLAHEIG
310 320 330 340 350
HWQKNHIVNM VIFSQLHTFL IFSLFTSIYR NTSFYNTFGF FLEKSTGSFV
360 370 380 390 400
DPVITKEFPI IIGFMLFNDL LTPLECAMQF VMSLISRTHE YQADAYAKKL
410 420 430 440 450
GYKQNLCRAL IDLQIKNLST MNVDPLYSSY HYSHPTLAER LTALDYVSEK

KKN
Length:453
Mass (Da):52,324
Last modified:February 1, 1996 - v1
Checksum:i331CC9AE2D7C99DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77137 Genomic DNA. Translation: AAB38271.1.
Z49617 Genomic DNA. Translation: CAA89647.1.
BK006943 Genomic DNA. Translation: DAA08902.1.
PIRiS57140.
RefSeqiNP_012651.1. NM_001181775.1.

Genome annotation databases

EnsemblFungiiYJR117W; YJR117W; YJR117W.
GeneIDi853581.
KEGGisce:YJR117W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77137 Genomic DNA. Translation: AAB38271.1.
Z49617 Genomic DNA. Translation: CAA89647.1.
BK006943 Genomic DNA. Translation: DAA08902.1.
PIRiS57140.
RefSeqiNP_012651.1. NM_001181775.1.

3D structure databases

ProteinModelPortaliP47154.
SMRiP47154. Positions 11-446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33873. 233 interactions.
DIPiDIP-1390N.
IntActiP47154. 21 interactions.
MINTiMINT-410624.

Chemistry

ChEMBLiCHEMBL1741185.

Protein family/group databases

MEROPSiM48.001.
TCDBi9.B.1.1.3. the integral membrane caax protease (caax protease) family.

Proteomic databases

MaxQBiP47154.
PeptideAtlasiP47154.

Protocols and materials databases

DNASUi853581.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJR117W; YJR117W; YJR117W.
GeneIDi853581.
KEGGisce:YJR117W.

Organism-specific databases

EuPathDBiFungiDB:YJR117W.
SGDiS000003878. STE24.

Phylogenomic databases

GeneTreeiENSGT00390000002053.
HOGENOMiHOG000257874.
InParanoidiP47154.
KOiK06013.
OMAiKKQGCNN.
OrthoDBiEOG74N5S9.

Enzyme and pathway databases

BioCyciMetaCyc:YJR117W-MONOMER.
YEAST:YJR117W-MONOMER.
BRENDAi3.4.24.84. 984.

Miscellaneous databases

PROiP47154.

Family and domain databases

InterProiIPR027057. CAXX_Prtase_1.
IPR001915. Peptidase_M48.
IPR032456. Peptidase_M48_N.
[Graphical view]
PANTHERiPTHR10120:SF24. PTHR10120:SF24. 1 hit.
PfamiPF01435. Peptidase_M48. 1 hit.
PF16491. Peptidase_M48_N. 1 hit.
[Graphical view]
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel membrane-associated metalloprotease, Ste24p, is required for the first step of NH2-terminal processing of the yeast a-factor precursor."
    Fujimura-Kamada K., Nouvet F.J., Michaelis S.
    J. Cell Biol. 136:271-285(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    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., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Modulation of Ras and a-factor function by carboxyl-terminal proteolysis."
    Boyartchuk V.L., Ashby M.N., Rine J.
    Science 275:1796-1800(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Dual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processing."
    Tam A., Nouvet F.J., Fujimura-Kamada K., Slunt H., Sisodia S.S., Michaelis S.
    J. Cell Biol. 142:635-649(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Roles of prenyl protein proteases in maturation of Saccharomyces cerevisiae a-factor."
    Boyartchuk V.L., Rine J.
    Genetics 150:95-101(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Reconstitution of the Ste24p-dependent N-terminal proteolytic step in yeast a-Factor biogenesis."
    Schmidt W.K., Tam A., Michaelis S.
    J. Biol. Chem. 275:6227-6233(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities."
    Trueblood C.E., Boyartchuk V.L., Picologlou E.A., Rozema D., Poulter C.D., Rine J.
    Mol. Cell. Biol. 20:4381-4392(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. "Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage."
    Schmidt W.K., Tam A., Fujimura-Kamada K., Michaelis S.
    Proc. Natl. Acad. Sci. U.S.A. 95:11175-11180(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.

Entry informationi

Entry nameiSTE24_YEAST
AccessioniPrimary (citable) accession number: P47154
Secondary accession number(s): D6VWT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 8, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 19600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.