FNTA_ARATH
ID FNTA_ARATH Reviewed; 326 AA.
AC Q9LX33; O65346;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha;
DE EC=2.5.1.58;
DE EC=2.5.1.59;
DE AltName: Full=CAAX farnesyltransferase subunit alpha;
DE AltName: Full=FTase-alpha;
DE AltName: Full=Ras proteins prenyltransferase subunit alpha;
DE AltName: Full=Type I protein geranyl-geranyltransferase subunit alpha;
DE Short=GGTase-I-alpha;
GN Name=FTA; OrderedLocusNames=At3g59380; ORFNames=F25L23.240;
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].
RC STRAIN=cv. Columbia;
RA Belbahri L., Villaroel R., Inze D., Thomas D., Thomasset B.;
RT "Nucleotide sequence of a putative protein farnesyltransferase subunit A
RT from Arabidopsis.";
RL (er) Plant Gene Register PGR98-134(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11500541; DOI=10.1104/pp.126.4.1416;
RA Caldelari D., Sternberg H., Rodriguez-Concepcion M., Gruissem W.,
RA Yalovsky S.;
RT "Efficient prenylation by a plant geranylgeranyltransferase-I requires a
RT functional CaaL box motif and a proximal polybasic domain.";
RL Plant Physiol. 126:1416-1429(2001).
RN [5]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
CC -!- FUNCTION: Essential subunit of both the farnesyltransferase and the
CC geranylgeranyltransferase complex. Contributes to the transfer of a
CC farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl
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. {ECO:0000269|PubMed:11500541,
CC ECO:0000269|PubMed:20565889}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] =
CC diphosphate + S-geranylgeranyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533,
CC ChEBI:CHEBI:86021; EC=2.5.1.59;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P29703};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.4 uM for CVIM substrate and for farnesyl transferase activity
CC {ECO:0000269|PubMed:11500541, ECO:0000269|PubMed:20565889};
CC KM=5.5 uM for CVIQ substrate and for farnesyl transferase activity
CC {ECO:0000269|PubMed:11500541, ECO:0000269|PubMed:20565889};
CC KM=6.9 uM for CVII substrate and for farnesyl transferase activity
CC {ECO:0000269|PubMed:11500541, ECO:0000269|PubMed:20565889};
CC KM=7.0 uM for CVIL substrate and for farnesyl transferase activity
CC {ECO:0000269|PubMed:11500541, ECO:0000269|PubMed:20565889};
CC KM=5.8 uM for CVIM substrate and for geranylgeranyl transferase
CC activity {ECO:0000269|PubMed:11500541, ECO:0000269|PubMed:20565889};
CC KM=3.5 uM for CVIQ substrate and for geranylgeranyl transferase
CC activity {ECO:0000269|PubMed:11500541, ECO:0000269|PubMed:20565889};
CC KM=19.0 uM for CVII substrate and for geranylgeranyl transferase
CC activity {ECO:0000269|PubMed:11500541, ECO:0000269|PubMed:20565889};
CC KM=17.2 uM for CVIL substrate and for geranylgeranyl transferase
CC activity {ECO:0000269|PubMed:11500541, ECO:0000269|PubMed:20565889};
CC pH dependence:
CC Optimum pH is 7.9-8.5 for CTIL substrate and geranylgeranyl
CC transferase activity. {ECO:0000269|PubMed:11500541,
CC ECO:0000269|PubMed:20565889};
CC Temperature dependence:
CC Optimum temperature is 30-37 degrees Celsius for CTIL substrate and
CC geranylgeranyl transferase activity. {ECO:0000269|PubMed:11500541,
CC ECO:0000269|PubMed:20565889};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC -!- INTERACTION:
CC Q9LX33; Q38920: FTB; NbExp=4; IntAct=EBI-1553317, EBI-1553332;
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB91608.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF064542; AAC61853.1; -; mRNA.
DR EMBL; AL356014; CAB91608.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE79914.1; -; Genomic_DNA.
DR PIR; T49006; T49006.
DR PIR; T51811; T51811.
DR RefSeq; NP_567084.1; NM_115800.6.
DR AlphaFoldDB; Q9LX33; -.
DR SMR; Q9LX33; -.
DR BioGRID; 10422; 7.
DR IntAct; Q9LX33; 1.
DR STRING; 3702.AT3G59380.1; -.
DR PaxDb; Q9LX33; -.
DR PRIDE; Q9LX33; -.
DR ProteomicsDB; 230607; -.
DR EnsemblPlants; AT3G59380.1; AT3G59380.1; AT3G59380.
DR GeneID; 825107; -.
DR Gramene; AT3G59380.1; AT3G59380.1; AT3G59380.
DR KEGG; ath:AT3G59380; -.
DR Araport; AT3G59380; -.
DR TAIR; locus:2081177; AT3G59380.
DR eggNOG; KOG0530; Eukaryota.
DR HOGENOM; CLU_026582_1_1_1; -.
DR InParanoid; Q9LX33; -.
DR OMA; RRKYWQY; -.
DR OrthoDB; 1527547at2759; -.
DR BioCyc; MetaCyc:AT3G59380-MON; -.
DR PRO; PR:Q9LX33; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LX33; baseline and differential.
DR Genevisible; Q9LX33; AT.
DR GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005965; C:protein farnesyltransferase complex; IBA:GO_Central.
DR GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004311; F:farnesyltranstransferase activity; TAS:TAIR.
DR GO; GO:0004660; F:protein farnesyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004661; F:protein geranylgeranyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:TAIR.
DR GO; GO:0008318; F:protein prenyltransferase activity; IDA:TAIR.
DR GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0018343; P:protein farnesylation; ISS:UniProtKB.
DR GO; GO:0018344; P:protein geranylgeranylation; IDA:TAIR.
DR GO; GO:0018342; P:protein prenylation; IDA:TAIR.
DR GO; GO:0008360; P:regulation of cell shape; IMP:TAIR.
DR GO; GO:0048509; P:regulation of meristem development; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR InterPro; IPR002088; Prenyl_trans_a.
DR Pfam; PF01239; PPTA; 4.
DR PROSITE; PS51147; PFTA; 5.
PE 1: Evidence at protein level;
KW Magnesium; Prenyltransferase; Reference proteome; Repeat; Transferase.
FT CHAIN 1..326
FT /note="Protein
FT farnesyltransferase/geranylgeranyltransferase type-1
FT subunit alpha"
FT /id="PRO_0000119749"
FT REPEAT 55..89
FT /note="PFTA 1"
FT REPEAT 90..124
FT /note="PFTA 2"
FT REPEAT 126..160
FT /note="PFTA 3"
FT REPEAT 161..194
FT /note="PFTA 4"
FT REPEAT 201..235
FT /note="PFTA 5"
FT CONFLICT 309
FT /note="V -> I (in Ref. 1; AAC61853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 37985 MW; 78146021EAFC785A CRC64;
MNFDETVPLS QRLEWSDVVP LTQDDGPNPV VPIAYKEEFR ETMDYFRAIY FSDERSPRAL
RLTEETLLLN SGNYTVWHFR RLVLEALNHD LFEELEFIER IAEDNSKNYQ LWHHRRWVAE
KLGPDVAGRE LEFTRRVLSL DAKHYHAWSH RQWTLRALGG WEDELDYCHE LLEADVFNNS
AWNQRYYVIT QSPLLGGLEA MRESEVSYTI KAILTNPANE SSWRYLKALY KDDKESWISD
PSVSSVCLNV LSRTDCFHGF ALSTLLDLLC DGLRPTNEHK DSVRALANEE PETNLANLVC
TILGRVDPVR ANYWAWRKSK ITVAAI
