FACE2_ARATH
ID FACE2_ARATH Reviewed; 311 AA.
AC Q8GW19; Q70VU9;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=CAAX prenyl protease 2;
DE EC=3.4.-.-;
DE AltName: Full=Farnesylated proteins-converting enzyme 2;
DE Short=AtFACE-2;
DE AltName: Full=Prenyl protein-specific endoprotease 2;
DE AltName: Full=Protein RAS-CONVERTING ENZYME 1;
DE Short=AtRCE1;
GN Name=FACE2; Synonyms=RCE1; OrderedLocusNames=At2g36305; ORFNames=F2H17;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND ACTIVITY
RP REGULATION.
RX PubMed=12928436; DOI=10.1074/jbc.m306700200;
RA Cadinanos J., Varela I., Mandel D.A., Schmidt W.K., Diaz-Perales A.,
RA Lopez-Otin C., Freije J.M.;
RT "AtFACE-2, a functional prenylated protein protease from Arabidopsis
RT thaliana related to mammalian Ras-converting enzymes.";
RL J. Biol. Chem. 278:42091-42097(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18641086; DOI=10.1104/pp.108.120477;
RA Bracha-Drori K., Shichrur K., Lubetzky T.C., Yalovsky S.;
RT "Functional analysis of Arabidopsis postprenylation CaaX processing enzymes
RT and their function in subcellular protein targeting.";
RL Plant Physiol. 148:119-131(2008).
CC -!- FUNCTION: Proteolytically removes the C-terminal three residues of
CC farnesylated and geranylated proteins. The substrate specificity is
CC only partially overlapping with that of FACE1.
CC {ECO:0000269|PubMed:12928436, ECO:0000269|PubMed:18641086}.
CC -!- ACTIVITY REGULATION: Inhibited by L-1-tosylamido-2-phenylethyl
CC chloromethyl ketone (TPCK) and N-ethylmaleimide, but not by EDTA.
CC {ECO:0000269|PubMed:12928436}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18641086}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18641086}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds, stems, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:12928436}.
CC -!- SIMILARITY: Belongs to the peptidase U48 family. {ECO:0000305}.
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DR EMBL; AJ534971; CAD59227.1; -; mRNA.
DR EMBL; AC006921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002685; AEC09230.1; -; Genomic_DNA.
DR EMBL; BT005303; AAO63367.1; -; mRNA.
DR EMBL; AK119135; BAC43705.1; -; mRNA.
DR RefSeq; NP_850262.2; NM_179931.4.
DR AlphaFoldDB; Q8GW19; -.
DR BioGRID; 3547; 46.
DR IntAct; Q8GW19; 46.
DR STRING; 3702.AT2G36305.1; -.
DR MEROPS; G05.002; -.
DR TCDB; 9.B.1.2.5; the integral membrane caax protease (caax protease) family.
DR PaxDb; Q8GW19; -.
DR PRIDE; Q8GW19; -.
DR ProteomicsDB; 230633; -.
DR EnsemblPlants; AT2G36305.1; AT2G36305.1; AT2G36305.
DR GeneID; 818203; -.
DR Gramene; AT2G36305.1; AT2G36305.1; AT2G36305.
DR KEGG; ath:AT2G36305; -.
DR Araport; AT2G36305; -.
DR TAIR; locus:504956028; AT2G36305.
DR eggNOG; KOG4130; Eukaryota.
DR HOGENOM; CLU_049909_2_0_1; -.
DR InParanoid; Q8GW19; -.
DR OMA; ASHFHHI; -.
DR OrthoDB; 1607650at2759; -.
DR PRO; PR:Q8GW19; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GW19; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IDA:TAIR.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0080120; P:CAAX-box protein maturation; IGI:TAIR.
DR GO; GO:0071586; P:CAAX-box protein processing; IBA:GO_Central.
DR GO; GO:0016485; P:protein processing; IDA:TAIR.
DR InterPro; IPR039731; Rce1.
DR InterPro; IPR003675; Rce1-like.
DR PANTHER; PTHR13046; PTHR13046; 1.
DR Pfam; PF02517; Rce1-like; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Hydrolase; Membrane; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..311
FT /note="CAAX prenyl protease 2"
FT /id="PRO_0000356239"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 164
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT ACT_SITE 198
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT SITE 251
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT SITE 255
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q6LZY8"
FT CONFLICT 256
FT /note="Y -> C (in Ref. 4; AAO63367 and 5; BAC43705)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 34548 MW; 52B83032F3EF6456 CRC64;
MATDGESISM SLAVATCVAM ALFYVLILYV PTVILRLPSA SSYTEFMIRR FICAAICTVA
SLVFTAFILP IKSWEASYIL GVYGIRKDHL WQGVVYPLLL TSLVYAGSLV LKLFTLLESW
KENGGGCSSF NYIRSFFQTI PASVLTSASN VSVWRNFIVA PVTEELVFRS CMIPLLLCAG
FRINTAIFLC PVLFSLAHLN HFREMYIRHN RSYLRASLIV GLQLGYTVIF GAYASFLFIR
TGHLAAPLFA HIFCNYMGLP VLYANGKGLV SAAFLGGVVG FVLLLFPLTK PLMYNDSTND
CPCWLGYCLW N
