FOLK_ARATH
ID FOLK_ARATH Reviewed; 307 AA.
AC Q67ZM7; Q67ZA1; Q8LAW9; Q9LV00;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Farnesol kinase, chloroplastic {ECO:0000303|PubMed:21395888};
DE EC=2.7.1.216 {ECO:0000269|PubMed:21395888};
DE Flags: Precursor;
GN Name=FOLK {ECO:0000303|PubMed:21395888};
GN OrderedLocusNames=At5g58560 {ECO:0000312|Araport:AT5G58560};
GN ORFNames=MZN1.8 {ECO:0000312|EMBL:BAA97326.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION.
RX PubMed=16361393; DOI=10.1105/tpc.105.037077;
RA Valentin H.E., Lincoln K., Moshiri F., Jensen P.K., Qi Q., Venkatesh T.V.,
RA Karunanandaa B., Baszis S.R., Norris S.R., Savidge B., Gruys K.J.,
RA Last R.L.;
RT "The Arabidopsis vitamin E pathway gene5-1 mutant reveals a critical role
RT for phytol kinase in seed tocopherol biosynthesis.";
RL Plant Cell 18:212-224(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND INDUCTION BY ABSCISIC ACID.
RC STRAIN=cv. Columbia;
RX PubMed=21395888; DOI=10.1111/j.1365-313x.2011.04572.x;
RA Fitzpatrick A.H., Bhandari J., Crowell D.N.;
RT "Farnesol kinase is involved in farnesol metabolism, ABA signaling and
RT flower development in Arabidopsis.";
RL Plant J. 66:1078-1088(2011).
CC -!- FUNCTION: Kinase involved in negative regulation of abscisic acid (ABA)
CC signaling. Substrate preference is farnesol > geraniol >
CC geranylgeraniol, but has no activity with farnesyl phosphate. Can use
CC CTP > ATP > GTP = UTP as phosphoryl donor.
CC {ECO:0000269|PubMed:21395888}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesol + CTP = (2E,6E)-farnesyl phosphate + CDP +
CC H(+); Xref=Rhea:RHEA:51680, ChEBI:CHEBI:15378, ChEBI:CHEBI:16619,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:58069, ChEBI:CHEBI:88226;
CC EC=2.7.1.216; Evidence={ECO:0000269|PubMed:21395888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51681;
CC Evidence={ECO:0000269|PubMed:21395888};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesol + ATP = (2E,6E)-farnesyl phosphate + ADP +
CC H(+); Xref=Rhea:RHEA:61656, ChEBI:CHEBI:15378, ChEBI:CHEBI:16619,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:88226, ChEBI:CHEBI:456216;
CC EC=2.7.1.216; Evidence={ECO:0000269|PubMed:21395888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61657;
CC Evidence={ECO:0000269|PubMed:21395888};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geraniol + ATP = (2E)-geranyl phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:61660, ChEBI:CHEBI:15378, ChEBI:CHEBI:17447,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:88107, ChEBI:CHEBI:456216;
CC EC=2.7.1.216; Evidence={ECO:0000269|PubMed:21395888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61661;
CC Evidence={ECO:0000269|PubMed:21395888};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeraniol + ATP = (2E,6E,10E)-geranylgeranyl
CC phosphate + ADP + H(+); Xref=Rhea:RHEA:61664, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:46762, ChEBI:CHEBI:144936,
CC ChEBI:CHEBI:456216; EC=2.7.1.216;
CC Evidence={ECO:0000269|PubMed:21395888};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61665;
CC Evidence={ECO:0000269|PubMed:21395888};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- INDUCTION: Down-regulated by abscisic acid.
CC {ECO:0000269|PubMed:21395888}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to abscisic acid.
CC {ECO:0000269|PubMed:21395888}.
CC -!- SIMILARITY: Belongs to the polyprenol kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97326.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB020755; BAA97326.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97069.1; -; Genomic_DNA.
DR EMBL; AY087555; AAM65097.1; -; mRNA.
DR EMBL; AK176090; BAD43853.1; -; mRNA.
DR EMBL; AK176217; BAD43980.1; -; mRNA.
DR RefSeq; NP_200664.1; NM_125242.4.
DR AlphaFoldDB; Q67ZM7; -.
DR BioGRID; 21213; 54.
DR IntAct; Q67ZM7; 54.
DR STRING; 3702.AT5G58560.1; -.
DR PaxDb; Q67ZM7; -.
DR PRIDE; Q67ZM7; -.
DR ProteomicsDB; 230557; -.
DR EnsemblPlants; AT5G58560.1; AT5G58560.1; AT5G58560.
DR GeneID; 835969; -.
DR Gramene; AT5G58560.1; AT5G58560.1; AT5G58560.
DR KEGG; ath:AT5G58560; -.
DR Araport; AT5G58560; -.
DR TAIR; locus:2178768; AT5G58560.
DR eggNOG; KOG4453; Eukaryota.
DR HOGENOM; CLU_058561_3_0_1; -.
DR OMA; QIWILNT; -.
DR OrthoDB; 1323987at2759; -.
DR PhylomeDB; Q67ZM7; -.
DR BioCyc; ARA:AT5G58560-MON; -.
DR BioCyc; MetaCyc:AT5G58560-MON; -.
DR BRENDA; 2.7.1.216; 399.
DR PRO; PR:Q67ZM7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q67ZM7; baseline and differential.
DR Genevisible; Q67ZM7; AT.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102237; F:ATP:farnesol kinase activity; IEA:RHEA.
DR GO; GO:0102243; F:ATP:geranylgeraniol phosphotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052668; F:CTP:farnesol kinase activity; IDA:TAIR.
DR GO; GO:0052672; F:CTP:geranylgeraniol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0052670; F:geraniol kinase activity; IDA:TAIR.
DR GO; GO:0052671; F:geranylgeraniol kinase activity; IDA:TAIR.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0048440; P:carpel development; IMP:TAIR.
DR GO; GO:0016487; P:farnesol metabolic process; IMP:TAIR.
DR GO; GO:0006720; P:isoprenoid metabolic process; IDA:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR InterPro; IPR039606; Phytol/farnesol_kinase.
DR PANTHER; PTHR32523; PTHR32523; 2.
PE 1: Evidence at protein level;
KW Chloroplast; Kinase; Membrane; Plastid; Reference proteome; Transferase;
KW Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..65
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 66..307
FT /note="Farnesol kinase, chloroplastic"
FT /id="PRO_0000226592"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 190
FT /note="I -> V (in Ref. 4; BAD43853)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="A -> G (in Ref. 3; AAM65097)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 307 AA; 33218 MW; F98BB457D44D1079 CRC64;
MATTSTTTKL SVLCCSFISS PLVDSPPSLA FFSPIPRFLT VRIATSFRSS SRFPATKIRK
SSLAAVMFPE NSVLSDVCAF GVTSIVAFSC LGFWGEIGKR GIFDQKLIRK LVHINIGLVF
MLCWPLFSSG IQGALFASLV PGLNIVRMLL LGLGVYHDEG TIKSMSRHGD RRELLKGPLY
YVLSITSACI YYWKSSPIAI AVICNLCAGD GMADIVGRRF GTEKLPYNKN KSFAGSIGMA
TAGFLASVAY MYYFASFGYI EDSGGMILRF LVISIASALV ESLPISTDID DNLTISLTSA
LAGFLLF
