FNTB_ARATH
ID FNTB_ARATH Reviewed; 482 AA.
AC Q38920; A4VCL6; Q38916; Q8LPK8; Q9LLE9;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Protein farnesyltransferase subunit beta {ECO:0000303|PubMed:20565889};
DE Short=FTase-beta {ECO:0000303|PubMed:20565889};
DE EC=2.5.1.58 {ECO:0000269|PubMed:20565889};
DE AltName: Full=CAAX farnesyltransferase subunit beta {ECO:0000303|PubMed:20565889};
DE AltName: Full=Enhanced response to abscisic acid 1 {ECO:0000303|PubMed:10840062};
DE AltName: Full=Ras proteins prenyltransferase subunit beta {ECO:0000303|PubMed:20565889};
GN Name=FTB;
GN Synonyms=ERA1 {ECO:0000303|PubMed:10840062},
GN WIGGUM {ECO:0000303|PubMed:10840062};
GN OrderedLocusNames=At5g40280 {ECO:0000312|Araport:AT5G40280};
GN ORFNames=MSN9.20 {ECO:0000312|EMBL:BAB10909.1};
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], AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10840062; DOI=10.1073/pnas.130189397;
RA Ziegelhoffer E.C., Medrano L.J., Meyerowitz E.M.;
RT "Cloning of the Arabidopsis WIGGUM gene identifies a role for farnesylation
RT in meristem development.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:7633-7638(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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;
RA Bautista-Mercan V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C.,
RA Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-482.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 79-482.
RA Cutler S.R., Ghassemian M., Bonetta D., Cooney S.E., Mccourt P.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, COFACTOR, AND
RP SUBUNIT.
RX PubMed=20565889; DOI=10.1186/1471-2229-10-118;
RA Andrews M., Huizinga D.H., Crowell D.N.;
RT "The CaaX specificities of Arabidopsis protein prenyltransferases explain
RT era1 and ggb phenotypes.";
RL BMC Plant Biol. 10:118-118(2010).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=26147561; DOI=10.1111/pce.12605;
RA Dutilleul C., Ribeiro I., Blanc N., Nezames C.D., Deng X.W., Zglobicki P.,
RA Palacio Barrera A.M., Atehortua L., Courtois M., Labas V.,
RA Giglioli-Guivarc'h N., Ducos E.;
RT "ASG2 is a farnesylated DWD protein that acts as ABA negative regulator in
RT Arabidopsis.";
RL Plant Cell Environ. 39:185-198(2016).
CC -!- FUNCTION: Catalyzes the transfer of a farnesyl moiety from farnesyl
CC diphosphate to a cysteine at the fourth position from the C-terminus of
CC several proteins having the C-terminal sequence Cys-aliphatic-
CC aliphatic-X (CaaX) (PubMed:20565889). The beta subunit is responsible
CC for peptide-binding (PubMed:20565889). Acts as an abscisic acid (ABA)
CC negative regulator by mediating ASG2 farnesylation and consequently
CC monitoring its subcellular localization (PubMed:26147561). Involved in
CC responses to salt (NaCl) and osmotic (e.g. in response to mannitol and
CC PEG) stresses (PubMed:26147561). {ECO:0000269|PubMed:20565889,
CC ECO:0000269|PubMed:26147561}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] =
CC diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:13345, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11535,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:86019,
CC ChEBI:CHEBI:175763; EC=2.5.1.58;
CC Evidence={ECO:0000269|PubMed:20565889};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:20565889};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:20565889};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.4 uM for CVIM substrate {ECO:0000269|PubMed:20565889};
CC KM=5.5 uM for CVIQ substrate {ECO:0000269|PubMed:20565889};
CC KM=6.9 uM for CVII substrate {ECO:0000269|PubMed:20565889};
CC KM=7.0 uM for CVIL substrate {ECO:0000269|PubMed:20565889};
CC Note=kcat is 49.1 h(-1), 28.8 h(-1), 12.8 h(-1) and 3.7 h(-1) for
CC CVIQ, CVIM, CVII and CVIL substrates, respectively.;
CC -!- SUBUNIT: Heterodimer of FTA and FTB (farnesyltransferase). Heterodimer
CC of an alpha and a beta subunit. {ECO:0000269|PubMed:20565889}.
CC -!- INTERACTION:
CC Q38920; Q9LX33: FTA; NbExp=4; IntAct=EBI-1553332, EBI-1553317;
CC -!- DISRUPTION PHENOTYPE: Plants show an increase in floral organ number,
CC particularly in the sepals and petals, correlating with an increase in
CC the width of young floral meristems (PubMed:10840062). Increased
CC sensitivity to abscisic acid (ABA) as well as salt (NaCl) and osmotic
CC (e.g. in response to mannitol and PEG) stresses in term of seed
CC germination and roots elongation (PubMed:26147561).
CC {ECO:0000269|PubMed:10840062, ECO:0000269|PubMed:26147561}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM20474.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB10909.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF214106; AAF74564.1; -; mRNA.
DR EMBL; AB010699; BAB10909.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94529.1; -; Genomic_DNA.
DR EMBL; BT030457; ABP88111.1; -; mRNA.
DR EMBL; AY099623; AAM20474.1; ALT_INIT; mRNA.
DR EMBL; U46574; AAA87585.1; -; Genomic_DNA.
DR EMBL; U44849; AAA86658.1; -; mRNA.
DR RefSeq; NP_198844.1; NM_123392.2.
DR AlphaFoldDB; Q38920; -.
DR SMR; Q38920; -.
DR BioGRID; 19277; 1.
DR IntAct; Q38920; 1.
DR STRING; 3702.AT5G40280.1; -.
DR PaxDb; Q38920; -.
DR PRIDE; Q38920; -.
DR EnsemblPlants; AT5G40280.1; AT5G40280.1; AT5G40280.
DR GeneID; 834026; -.
DR Gramene; AT5G40280.1; AT5G40280.1; AT5G40280.
DR KEGG; ath:AT5G40280; -.
DR Araport; AT5G40280; -.
DR TAIR; locus:2173802; AT5G40280.
DR eggNOG; KOG0365; Eukaryota.
DR HOGENOM; CLU_028946_0_1_1; -.
DR InParanoid; Q38920; -.
DR OMA; WCIYWIL; -.
DR BioCyc; ARA:AT5G40280-MON; -.
DR BioCyc; MetaCyc:AT5G40280-MON; -.
DR BRENDA; 2.5.1.58; 399.
DR PRO; PR:Q38920; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q38920; baseline and differential.
DR Genevisible; Q38920; AT.
DR GO; GO:0005965; C:protein farnesyltransferase complex; ISS:UniProtKB.
DR GO; GO:0004311; F:farnesyltranstransferase activity; ISS:TAIR.
DR GO; GO:0004660; F:protein farnesyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0042335; P:cuticle development; IMP:TAIR.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0018343; P:protein farnesylation; ISS:UniProtKB.
DR GO; GO:0018342; P:protein prenylation; IMP:TAIR.
DR GO; GO:0009934; P:regulation of meristem structural organization; IMP:TAIR.
DR GO; GO:0047484; P:regulation of response to osmotic stress; IMP:UniProtKB.
DR GO; GO:1901000; P:regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009620; P:response to fungus; IGI:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:1990069; P:stomatal opening; IMP:TAIR.
DR CDD; cd02893; FTase; 1.
DR InterPro; IPR026872; FTB.
DR InterPro; IPR001330; PFTB_repeat.
DR InterPro; IPR045089; PGGT1B-like.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11774; PTHR11774; 1.
DR Pfam; PF00432; Prenyltrans; 5.
DR SUPFAM; SSF48239; SSF48239; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Prenyltransferase; Reference proteome; Repeat; Transferase;
KW Zinc.
FT CHAIN 1..482
FT /note="Protein farnesyltransferase subunit beta"
FT /id="PRO_0000119764"
FT REPEAT 131..172
FT /note="PFTB 1"
FT REPEAT 182..223
FT /note="PFTB 2"
FT REPEAT 230..271
FT /note="PFTB 3"
FT REPEAT 278..319
FT /note="PFTB 4"
FT REPEAT 391..433
FT /note="PFTB 5"
FT REGION 329..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..365
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 256..259
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 298..301
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 307..310
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT BINDING 421
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT SITE 110
FT /note="Important for selectivity against geranylgeranyl
FT diphosphate"
FT /evidence="ECO:0000250|UniProtKB:P49356"
FT CONFLICT 129
FT /note="E -> K (in Ref. 5; AAM20474)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="M -> I (in Ref. 6; AAA86658/AAA87585)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 482 AA; 54216 MW; 4A557EB53567C83B CRC64;
MPVVTRLIRL KCVGLRLDRS GLNRRICHGG HGESTRRRVM EELSSLTVSQ REQFLVENDV
FGIYNYFDAS DVSTQKYMME IQRDKQLDYL MKGLRQLGPQ FSSLDANRPW LCYWILHSIA
LLGETVDDEL ESNAIDFLGR CQGSEGGYGG GPGQLPHLAT TYAAVNALVT LGGDKALSSI
NREKMSCFLR RMKDTSGGFR MHDMGEMDVR ACYTAISVAS ILNIMDDELT QGLGDYILSC
QTYEGGIGGE PGSEAHGGYT YCGLAAMILI NEVDRLNLDS LMNWAVHRQG VEMGFQGRTN
KLVDGCYTFW QAAPCVLLQR LYSTNDHDVH GSSHISEGTN EEHHAHDEDD LEDSDDDDDS
DEDNDEDSVN GHRIHHTSTY INRRMQLVFD SLGLQRYVLL CSKIPDGGFR DKPRKPRDFY
HTCYCLSGLS VAQHAWLKDE DTPPLTRDIM GGYSNLLEPV QLLHNIVMDQ YNEAIEFFFK
AA
