RCE1_METMP
ID RCE1_METMP Reviewed; 271 AA.
AC Q6LZY8;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=CAAX prenyl protease 2 {ECO:0000305|PubMed:24291792};
DE EC=3.4.-.- {ECO:0000269|PubMed:24291792};
DE AltName: Full=Intramembrane protease Rce1 {ECO:0000303|PubMed:24291792};
DE Short=IMP Rce1 {ECO:0000303|PubMed:24291792};
DE AltName: Full=Prenyl protein-specific endoprotease 2 {ECO:0000305|PubMed:24291792};
DE AltName: Full=Ras and a-factor-converting enzyme 1 {ECO:0000303|PubMed:24291792};
GN Name=rce1 {ECO:0000303|PubMed:24291792};
GN OrderedLocusNames=MMP0485 {ECO:0000312|EMBL:CAF30041.1};
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377 {ECO:0000312|Proteomes:UP000000590};
RN [1] {ECO:0000312|EMBL:CAF30041.1, ECO:0000312|Proteomes:UP000000590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL {ECO:0000312|Proteomes:UP000000590};
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
RN [2] {ECO:0007744|PDB:4CAD}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH MONOCLONAL ANTIBODY
RP FAB FRAGMENT, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TOPOLOGY, CIRCULAR
RP DICHROISM ANALYSIS, REACTION MECHANISM, ACTIVE SITES, SITES, AND
RP MUTAGENESIS OF LEU-45; LEU-132; GLU-140; GLU-141; HIS-173; HIS-227 AND
RP ASN-231.
RX PubMed=24291792; DOI=10.1038/nature12754;
RA Manolaridis I., Kulkarni K., Dodd R.B., Ogasawara S., Zhang Z., Bineva G.,
RA O'Reilly N., Hanrahan S.J., Thompson A.J., Cronin N., Iwata S., Barford D.;
RT "Mechanism of farnesylated CAAX protein processing by the intramembrane
RT protease Rce1.";
RL Nature 504:301-305(2013).
CC -!- FUNCTION: Endopeptidase which proteolytically removes the C-terminal
CC three residues of farnesylated peptides containing the CAAX motif where
CC C is cysteine, A is an aliphatic amino acid and X is any amino acid.
CC Cleaves the CAAX motif C-terminal to both P1 and P1' positions.
CC Hydrolysis depends on a farnesylated cysteine residue and no activity
CC is shown towards geranylgeranylated peptides.
CC {ECO:0000269|PubMed:24291792}.
CC -!- ACTIVITY REGULATION: Activity is unaffected by metalloprotease
CC inhibitors 5 mM EDTA and 5 mM Zn(2+). Activity partially inhibited by
CC 1,10-phenanthroline and 1,7-phenanthroline.
CC {ECO:0000269|PubMed:24291792}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=19.7 uM for peptide substrate DABCYL-ARSGAKASGC(farnesyl)LVS-EDANS
CC where EDANS is 5-[(2-aminoethyl)amino]naphthalene-1-sulphonic acid
CC fluorophore and DABCYL is 4-{[4-(dimethylamino)phenyl]azo}benzoic
CC acid quencher {ECO:0000269|PubMed:24291792};
CC Note=kcat is 0.175 sec(-1) for peptide substrate DABCYL-
CC ARSGAKASGC(farnesyl)LVS-EDANS. {ECO:0000269|PubMed:24291792};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24291792};
CC Multi-pass membrane protein {ECO:0000269|PubMed:24291792}.
CC -!- SIMILARITY: Belongs to the peptidase U48 family. {ECO:0000305}.
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DR EMBL; BX950229; CAF30041.1; -; Genomic_DNA.
DR RefSeq; WP_011170429.1; NC_005791.1.
DR PDB; 4CAD; X-ray; 2.50 A; C/F/I/L=1-271.
DR PDBsum; 4CAD; -.
DR AlphaFoldDB; Q6LZY8; -.
DR SMR; Q6LZY8; -.
DR STRING; 267377.MMP0485; -.
DR MEROPS; G05.004; -.
DR ABCD; Q6LZY8; 1 sequenced antibody.
DR EnsemblBacteria; CAF30041; CAF30041; MMP0485.
DR GeneID; 2761751; -.
DR KEGG; mmp:MMP0485; -.
DR PATRIC; fig|267377.15.peg.491; -.
DR eggNOG; arCOG02768; Archaea.
DR HOGENOM; CLU_064706_2_0_2; -.
DR OMA; LWALWHL; -.
DR OrthoDB; 59035at2157; -.
DR BioCyc; MMAR267377:MMP_RS02575-MON; -.
DR Proteomes; UP000000590; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0071586; P:CAAX-box protein processing; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR InterPro; IPR042150; MmRce1-like.
DR InterPro; IPR003675; Rce1-like.
DR PANTHER; PTHR35797; PTHR35797; 1.
DR Pfam; PF02517; Rce1-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Hydrolase; Membrane; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..271
FT /note="CAAX prenyl protease 2"
FT /id="PRO_0000433642"
FT TOPO_DOM 1..9
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24291792"
FT TRANSMEM 10..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:24291792"
FT TOPO_DOM 31..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24291792"
FT TRANSMEM 39..59
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:24291792"
FT TOPO_DOM 60..82
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24291792"
FT TRANSMEM 83..105
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:24291792"
FT TOPO_DOM 106..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24291792"
FT TRANSMEM 126..149
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:24291792"
FT TOPO_DOM 150..159
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24291792"
FT TRANSMEM 160..179
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:24291792"
FT TOPO_DOM 180..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24291792"
FT TRANSMEM 193..213
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:24291792"
FT TOPO_DOM 214..219
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24291792"
FT TRANSMEM 220..237
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:24291792"
FT TOPO_DOM 238..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:24291792"
FT TRANSMEM 244..263
FT /note="Helical; Name=8"
FT /evidence="ECO:0000269|PubMed:24291792"
FT TOPO_DOM 264..271
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:24291792"
FT ACT_SITE 140
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:24291792"
FT ACT_SITE 173
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:24291792"
FT SITE 227
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000269|PubMed:24291792"
FT SITE 231
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000269|PubMed:24291792"
FT MUTAGEN 45
FT /note="L->W: Decreased enzymatic activity to about 25
FT percent relative to wild-type."
FT /evidence="ECO:0000269|PubMed:24291792"
FT MUTAGEN 132
FT /note="L->W: Decreased enzymatic activity to about 20
FT percent relative to wild-type."
FT /evidence="ECO:0000269|PubMed:24291792"
FT MUTAGEN 140
FT /note="E->A,Q: Nearly loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24291792"
FT MUTAGEN 141
FT /note="E->A: Decreased enzymatic activity to about 15
FT percent relative to wild-type."
FT /evidence="ECO:0000269|PubMed:24291792"
FT MUTAGEN 173
FT /note="H->A: Strongly decreased enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24291792"
FT MUTAGEN 227
FT /note="H->A: Decreased enzymatic activity to about 20
FT percent relative to wild-type."
FT /evidence="ECO:0000269|PubMed:24291792"
FT MUTAGEN 231
FT /note="N->A: Nearly loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:24291792"
FT MUTAGEN 231
FT /note="N->D: Decreased enzymatic activity to 40 percent
FT relative to wild-type. At higher pH 8.0 nearly loss of
FT enzymatic activity whereas the activity of the wild-type is
FT unchanged."
FT /evidence="ECO:0000269|PubMed:24291792"
FT HELIX 9..30
FT /evidence="ECO:0007829|PDB:4CAD"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:4CAD"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:4CAD"
FT HELIX 41..60
FT /evidence="ECO:0007829|PDB:4CAD"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:4CAD"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4CAD"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:4CAD"
FT HELIX 86..104
FT /evidence="ECO:0007829|PDB:4CAD"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4CAD"
FT HELIX 126..144
FT /evidence="ECO:0007829|PDB:4CAD"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:4CAD"
FT HELIX 158..172
FT /evidence="ECO:0007829|PDB:4CAD"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:4CAD"
FT HELIX 183..190
FT /evidence="ECO:0007829|PDB:4CAD"
FT HELIX 192..215
FT /evidence="ECO:0007829|PDB:4CAD"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:4CAD"
FT HELIX 220..236
FT /evidence="ECO:0007829|PDB:4CAD"
FT HELIX 241..261
FT /evidence="ECO:0007829|PDB:4CAD"
FT HELIX 263..267
FT /evidence="ECO:0007829|PDB:4CAD"
SQ SEQUENCE 271 AA; 31197 MW; 199EA975C25C7B9F CRC64;
MISSYKYNPK LYFLSTFVVT YILWFTGAYL SFSSTYSGIY MLIMLPGLMA PFIISTILIA
KSKNNELKKD FINRLFNLKL INLKTIPVVF LLMPAVILLS ILLSIPFGGS ISQFQFSGGF
SFSTDFVPVL FLLLLAATFE ELGWRGYAFD SLQSRYSLFK ASILFGIFWS LWHFPLIFVN
NSYQYEIFNQ SIWYGLNFFL SILPMGIIIT WMCLKNRKSI ILAIIFHFLI NLNQELLAIT
QDTKIIETGV LFLVAAAIIL YDKKMFFEKL G
