Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein farnesyltransferase subunit beta

Gene

FTB

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X (CaaX). The beta subunit is responsible for peptide-binding.1 Publication

Catalytic activityi

Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Kineticsi

Kcat is 49.1 h(-1), 28.8 h(-1), 12.8 h(-1) and 3.7 h(-1) for CVIQ, CVIM, CVII and CVIL substrates, respectively.

  1. KM=5.4 µM for CVIM substrate1 Publication
  2. KM=5.5 µM for CVIQ substrate1 Publication
  3. KM=6.9 µM for CVII substrate1 Publication
  4. KM=7.0 µM for CVIL substrate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei110 – 1101Important for selectivity against geranylgeranyl diphosphateBy similarity
    Metal bindingi304 – 3041Zinc; catalyticBy similarity
    Metal bindingi306 – 3061Zinc; catalyticBy similarity
    Metal bindingi421 – 4211Zinc; via tele nitrogen; catalyticBy similarity

    GO - Molecular functioni

    • farnesyltranstransferase activity Source: TAIR
    • protein farnesyltransferase activity Source: UniProtKB
    • zinc ion binding Source: UniProtKB

    GO - Biological processi

    • negative regulation of abscisic acid-activated signaling pathway Source: TAIR
    • protein farnesylation Source: UniProtKB
    • protein prenylation Source: TAIR
    • regulation of cell proliferation Source: InterPro
    • regulation of meristem structural organization Source: TAIR
    • response to abscisic acid Source: TAIR
    • response to water deprivation Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Prenyltransferase, Transferase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciARA:AT5G40280-MONOMER.
    MetaCyc:AT5G40280-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein farnesyltransferase subunit beta (EC:2.5.1.58)
    Short name:
    FTase-beta
    Alternative name(s):
    CAAX farnesyltransferase subunit beta
    Enhanced response to abscisic acid 1
    Ras proteins prenyltransferase subunit beta
    Gene namesi
    Name:FTB
    Synonyms:ERA1, WIGGUM
    Ordered Locus Names:At5g40280
    ORF Names:MSN9.20
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 5

    Organism-specific databases

    TAIRiAT5G40280.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Disruption phenotypei

    Plants show an increase in floral organ number, particularly in the sepals and petals, correlating with an increase in the width of young floral meristems.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 482482Protein farnesyltransferase subunit betaPRO_0000119764Add
    BLAST

    Proteomic databases

    PaxDbiQ38920.
    PRIDEiQ38920.

    Expressioni

    Gene expression databases

    GenevisibleiQ38920. AT.

    Interactioni

    Subunit structurei

    Heterodimer of FTA and FTB (farnesyltransferase). Heterodimer of an alpha and a beta subunit.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FTAQ9LX334EBI-1553332,EBI-1553317

    Protein-protein interaction databases

    BioGridi19277. 1 interaction.
    IntActiQ38920. 1 interaction.
    STRINGi3702.AT5G40280.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ38920.
    SMRiQ38920. Positions 33-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati131 – 17242PFTB 1Add
    BLAST
    Repeati182 – 22342PFTB 2Add
    BLAST
    Repeati230 – 27142PFTB 3Add
    BLAST
    Repeati278 – 31942PFTB 4Add
    BLAST
    Repeati391 – 43343PFTB 5Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni256 – 2594Farnesyl diphosphate bindingBy similarity
    Regioni298 – 3014Farnesyl diphosphate bindingBy similarity
    Regioni307 – 3104Farnesyl diphosphate bindingBy similarity

    Sequence similaritiesi

    Contains 5 PFTB repeats.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiKOG0365. Eukaryota.
    COG5029. LUCA.
    HOGENOMiHOG000190594.
    InParanoidiQ38920.
    KOiK05954.
    OMAiRPWIFYW.

    Family and domain databases

    Gene3Di1.50.10.20. 2 hits.
    InterProiIPR026872. FTB.
    IPR001330. PFTB_repeat.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view]
    PANTHERiPTHR11774:SF6. PTHR11774:SF6. 2 hits.
    PfamiPF00432. Prenyltrans. 5 hits.
    [Graphical view]
    SUPFAMiSSF48239. SSF48239. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q38920-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPVVTRLIRL KCVGLRLDRS GLNRRICHGG HGESTRRRVM EELSSLTVSQ
    60 70 80 90 100
    REQFLVENDV FGIYNYFDAS DVSTQKYMME IQRDKQLDYL MKGLRQLGPQ
    110 120 130 140 150
    FSSLDANRPW LCYWILHSIA LLGETVDDEL ESNAIDFLGR CQGSEGGYGG
    160 170 180 190 200
    GPGQLPHLAT TYAAVNALVT LGGDKALSSI NREKMSCFLR RMKDTSGGFR
    210 220 230 240 250
    MHDMGEMDVR ACYTAISVAS ILNIMDDELT QGLGDYILSC QTYEGGIGGE
    260 270 280 290 300
    PGSEAHGGYT YCGLAAMILI NEVDRLNLDS LMNWAVHRQG VEMGFQGRTN
    310 320 330 340 350
    KLVDGCYTFW QAAPCVLLQR LYSTNDHDVH GSSHISEGTN EEHHAHDEDD
    360 370 380 390 400
    LEDSDDDDDS DEDNDEDSVN GHRIHHTSTY INRRMQLVFD SLGLQRYVLL
    410 420 430 440 450
    CSKIPDGGFR DKPRKPRDFY HTCYCLSGLS VAQHAWLKDE DTPPLTRDIM
    460 470 480
    GGYSNLLEPV QLLHNIVMDQ YNEAIEFFFK AA
    Length:482
    Mass (Da):54,216
    Last modified:May 31, 2011 - v3
    Checksum:i4A557EB53567C83B
    GO

    Sequence cautioni

    The sequence BAB10909.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti207 – 2071M → I in AAA86658 (Ref. 5) Curated
    Sequence conflicti207 – 2071M → I in AAA87585 (Ref. 5) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF214106 mRNA. Translation: AAF74564.1.
    AB010699 Genomic DNA. Translation: BAB10909.1. Sequence problems.
    CP002688 Genomic DNA. Translation: AED94529.1.
    BT030457 mRNA. Translation: ABP88111.1.
    U46574 Genomic DNA. Translation: AAA87585.1.
    U44849 mRNA. Translation: AAA86658.1.
    RefSeqiNP_198844.1. NM_123392.1.
    UniGeneiAt.9205.

    Genome annotation databases

    EnsemblPlantsiAT5G40280.1; AT5G40280.1; AT5G40280.
    GeneIDi834026.
    GrameneiAT5G40280.1; AT5G40280.1; AT5G40280.
    KEGGiath:AT5G40280.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF214106 mRNA. Translation: AAF74564.1.
    AB010699 Genomic DNA. Translation: BAB10909.1. Sequence problems.
    CP002688 Genomic DNA. Translation: AED94529.1.
    BT030457 mRNA. Translation: ABP88111.1.
    U46574 Genomic DNA. Translation: AAA87585.1.
    U44849 mRNA. Translation: AAA86658.1.
    RefSeqiNP_198844.1. NM_123392.1.
    UniGeneiAt.9205.

    3D structure databases

    ProteinModelPortaliQ38920.
    SMRiQ38920. Positions 33-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi19277. 1 interaction.
    IntActiQ38920. 1 interaction.
    STRINGi3702.AT5G40280.1.

    Proteomic databases

    PaxDbiQ38920.
    PRIDEiQ38920.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT5G40280.1; AT5G40280.1; AT5G40280.
    GeneIDi834026.
    GrameneiAT5G40280.1; AT5G40280.1; AT5G40280.
    KEGGiath:AT5G40280.

    Organism-specific databases

    TAIRiAT5G40280.

    Phylogenomic databases

    eggNOGiKOG0365. Eukaryota.
    COG5029. LUCA.
    HOGENOMiHOG000190594.
    InParanoidiQ38920.
    KOiK05954.
    OMAiRPWIFYW.

    Enzyme and pathway databases

    BioCyciARA:AT5G40280-MONOMER.
    MetaCyc:AT5G40280-MONOMER.

    Miscellaneous databases

    PROiQ38920.

    Gene expression databases

    GenevisibleiQ38920. AT.

    Family and domain databases

    Gene3Di1.50.10.20. 2 hits.
    InterProiIPR026872. FTB.
    IPR001330. PFTB_repeat.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    [Graphical view]
    PANTHERiPTHR11774:SF6. PTHR11774:SF6. 2 hits.
    PfamiPF00432. Prenyltrans. 5 hits.
    [Graphical view]
    SUPFAMiSSF48239. SSF48239. 2 hits.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning of the Arabidopsis WIGGUM gene identifies a role for farnesylation in meristem development."
      Ziegelhoffer E.C., Medrano L.J., Meyerowitz E.M.
      Proc. Natl. Acad. Sci. U.S.A. 97:7633-7638(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE.
      Strain: cv. Landsberg erecta.
    2. "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones."
      Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., Tabata S.
      DNA Res. 5:131-145(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Arabidopsis ORF clones."
      Bautista-Mercan V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.
      Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. Cutler S.R., Ghassemian M., Bonetta D., Cooney S.E., Mccourt P.
      Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 79-482.
    6. "The CaaX specificities of Arabidopsis protein prenyltransferases explain era1 and ggb phenotypes."
      Andrews M., Huizinga D.H., Crowell D.N.
      BMC Plant Biol. 10:118-118(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.

    Entry informationi

    Entry nameiFNTB_ARATH
    AccessioniPrimary (citable) accession number: Q38920
    Secondary accession number(s): A4VCL6, Q38916, Q9LLE9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: May 31, 2011
    Last modified: February 17, 2016
    This is version 115 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.