FACE1_ARATH
ID FACE1_ARATH Reviewed; 424 AA.
AC Q8RX88; O04602; Q93ZV9; Q94FS8; Q9M139;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=CAAX prenyl protease 1 homolog;
DE EC=3.4.24.84;
DE AltName: Full=Farnesylated proteins-converting enzyme 1;
DE Short=AtFACE-1;
DE Short=FACE-1;
DE AltName: Full=Prenyl protein-specific endoprotease 1;
DE AltName: Full=Zinc metalloproteinase Ste24 homolog;
DE Short=AtSTE24;
GN Name=FACE1; Synonyms=STE24; OrderedLocusNames=At4g01320;
GN ORFNames=A_IG002N01.21, F2N1.21;
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, MUTAGENESIS OF HIS-284, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12039957; DOI=10.1074/jbc.m202916200;
RA Bracha K., Lavy M., Yalovsky S.;
RT "The Arabidopsis AtSTE24 is a CAAX protease with broad substrate
RT specificity.";
RL J. Biol. Chem. 277:29856-29864(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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=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 [5]
RP SUBSTRATE SPECIFICITY.
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 [6]
RP 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 proteins. The substrate specificity is only partially
CC overlapping with that of FACE2. {ECO:0000269|PubMed:12039957}.
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:12039957, ECO:0000269|PubMed:18641086}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12039957,
CC ECO:0000269|PubMed:18641086}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers.
CC {ECO:0000269|PubMed:12039957}.
CC -!- SIMILARITY: Belongs to the peptidase M48A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB61028.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80941.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF353722; AAK39514.1; -; mRNA.
DR EMBL; AF007269; AAB61028.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161491; CAB80941.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82008.1; -; Genomic_DNA.
DR EMBL; AY056235; AAL07084.1; -; mRNA.
DR EMBL; AY090232; AAL90896.1; -; mRNA.
DR EMBL; BT006355; AAP21163.1; -; mRNA.
DR PIR; C85017; C85017.
DR PIR; T01712; T01712.
DR RefSeq; NP_567212.1; NM_116362.3.
DR AlphaFoldDB; Q8RX88; -.
DR SMR; Q8RX88; -.
DR STRING; 3702.AT4G01320.1; -.
DR TCDB; 9.B.1.1.2; the integral membrane caax protease (caax protease) family.
DR PaxDb; Q8RX88; -.
DR PRIDE; Q8RX88; -.
DR ProteomicsDB; 230844; -.
DR EnsemblPlants; AT4G01320.1; AT4G01320.1; AT4G01320.
DR GeneID; 828209; -.
DR Gramene; AT4G01320.1; AT4G01320.1; AT4G01320.
DR KEGG; ath:AT4G01320; -.
DR Araport; AT4G01320; -.
DR TAIR; locus:2124983; AT4G01320.
DR eggNOG; KOG2719; Eukaryota.
DR HOGENOM; CLU_025947_3_3_1; -.
DR InParanoid; Q8RX88; -.
DR OMA; LPFKIYK; -.
DR OrthoDB; 878143at2759; -.
DR PhylomeDB; Q8RX88; -.
DR BRENDA; 3.4.24.84; 399.
DR PRO; PR:Q8RX88; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8RX88; baseline and differential.
DR Genevisible; Q8RX88; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0004175; F:endopeptidase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISS:TAIR.
DR GO; GO:0080120; P:CAAX-box protein maturation; IDA:TAIR.
DR GO; GO:0071586; P:CAAX-box protein processing; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IDA:TAIR.
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.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..424
FT /note="CAAX prenyl protease 1 homolog"
FT /id="PRO_0000356240"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 285
FT /evidence="ECO:0000250"
FT ACT_SITE 366
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MUTAGEN 284
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12039957"
FT CONFLICT 81
FT /note="G -> W (in Ref. 4; AAL07084)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="D -> G (in Ref. 4; AAL07084)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="Y -> H (in Ref. 1; AAK39514)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 48482 MW; B894AE17C8044857 CRC64;
MAIPFMETVV GFMIVMYIFE TYLDLRQLTA LKLPTLPKTL VGVISQEKFE KSRAYSLDKS
YFHFVHEFVT ILMDSAILFF GILPWFWKMS GAVLPRLGLD PENEILHTLS FLAGVMTWSQ
ITDLPFSLYS TFVIESRHGF NKQTIWMFIR DMIKGTFLSV ILGPPIVAAI IFIVQKGGPY
LAIYLWAFMF ILSLVMMTIY PVLIAPLFNK FTPLPDGDLR EKIEKLASSL KFPLKKLFVV
DGSTRSSHSN AYMYGFFKNK RIVLYDTLIQ QCKNEDEIVA VIAHELGHWK LNHTTYSFIA
VQILAFLQFG GYTLVRNSTD LFRSFGFDTQ PVLIGLIIFQ HTVIPLQHLV SFGLNLVSRA
FEFQADAFAV KLGYAKDLRP ALVKLQEENL SAMNTDPLYS AYHYSHPPLV ERLRAIDGED
KKTD
