RCE1_YEAST
ID RCE1_YEAST Reviewed; 315 AA.
AC Q03530; D6W0A1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=CAAX prenyl protease 2;
DE EC=3.4.-.-;
DE AltName: Full=Prenyl protein-specific endoprotease 2;
DE Short=PPSEP 2;
DE AltName: Full=Ras and A-factor-converting enzyme;
DE Short=RACE;
GN Name=RCE1; OrderedLocusNames=YMR274C; ORFNames=YM8156.16C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
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 [3]
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 [4]
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 [5]
RP CHARACTERIZATION, AND FUNCTION.
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 [6]
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 proteins, including the a-factor mating pheromone and RAS.
CC {ECO:0000269|PubMed:10825201, ECO:0000269|PubMed:9065405}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:9736709}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9736709}.
CC -!- SIMILARITY: Belongs to the peptidase U48 family. {ECO:0000305}.
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DR EMBL; Z49260; CAA89257.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10175.1; -; Genomic_DNA.
DR PIR; S54486; S54486.
DR RefSeq; NP_014001.1; NM_001182781.1.
DR AlphaFoldDB; Q03530; -.
DR BioGRID; 35453; 175.
DR DIP; DIP-7636N; -.
DR STRING; 4932.YMR274C; -.
DR ChEMBL; CHEMBL1250413; -.
DR DrugCentral; Q03530; -.
DR MEROPS; G05.001; -.
DR TCDB; 9.B.1.2.1; the integral membrane caax protease (caax protease) family.
DR PaxDb; Q03530; -.
DR DNASU; 855317; -.
DR EnsemblFungi; YMR274C_mRNA; YMR274C; YMR274C.
DR GeneID; 855317; -.
DR KEGG; sce:YMR274C; -.
DR SGD; S000004887; RCE1.
DR VEuPathDB; FungiDB:YMR274C; -.
DR eggNOG; KOG4130; Eukaryota.
DR GeneTree; ENSGT00390000004124; -.
DR HOGENOM; CLU_049909_1_0_1; -.
DR InParanoid; Q03530; -.
DR OMA; HSFCNWC; -.
DR BioCyc; YEAST:G3O-32945-MON; -.
DR BRENDA; 3.4.99.B1; 984.
DR PRO; PR:Q03530; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03530; 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:0004222; F:metalloendopeptidase activity; IDA:SGD.
DR GO; GO:0071586; P:CAAX-box protein processing; IMP:SGD.
DR GO; GO:0071432; P:peptide mating pheromone maturation involved in positive regulation of conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR InterPro; IPR039731; Rce1.
DR InterPro; IPR003675; Rce1-like.
DR PANTHER; PTHR13046; PTHR13046; 1.
DR Pfam; PF02517; Rce1-like; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Membrane; Pheromone response; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..315
FT /note="CAAX prenyl protease 2"
FT /id="PRO_0000194834"
FT TOPO_DOM 1..3
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..74
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..148
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..237
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..315
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 156
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT ACT_SITE 194
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT SITE 248
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT SITE 252
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
SQ SEQUENCE 315 AA; 35911 MW; D151F4790F066081 CRC64;
MLQFSTFLVL LYISISYVLP LYATSQPEGS KRDNPRTIKS RMQKLTIMLI SNLFLVPFLQ
SQLSSTTSHI SFKDAFLGLG IIPGYYAALP NPWQFSQFVK DLTKCVAMLL TLYCGPVLDF
VLYHLLNPKS SILEDFYHEF LNIWSFRNFI FAPITEEIFY TSMLLTTYLN LIPHSQLSYQ
QLFWQPSLFF GLAHAHHAYE QLQEGSMTTV SILLTTCFQI LYTTLFGGLT KFVFVRTGGN
LWCCIILHAL CNIMGFPGPS RLNLHFTVVD KKAGRISKLV SIWNKCYFAL LVLGLISLKD
TLQTLVGTPG YRITL
