Q38920 · FNTB_ARATH
- ProteinProtein farnesyltransferase subunit beta
- GeneFTB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids482 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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) (PubMed:20565889).
The beta subunit is responsible for peptide-binding (PubMed:20565889).
Acts as an abscisic acid (ABA) negative regulator by mediating ASG2 farnesylation and consequently monitoring its subcellular localization (PubMed:26147561).
Involved in responses to salt (NaCl) and osmotic (e.g. in response to mannitol and PEG) stresses (PubMed:26147561).
The beta subunit is responsible for peptide-binding (PubMed:20565889).
Acts as an abscisic acid (ABA) negative regulator by mediating ASG2 farnesylation and consequently monitoring its subcellular localization (PubMed:26147561).
Involved in responses to salt (NaCl) and osmotic (e.g. in response to mannitol and PEG) stresses (PubMed:26147561).
Catalytic activity
- (2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein]
Cofactor
Note: Binds 1 zinc ion per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
5.4 μM | CVIM substrate | |||||
5.5 μM | CVIQ substrate | |||||
6.9 μM | CVII substrate | |||||
7 μM | CVIL substrate |
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.
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 110 | Important for selectivity against geranylgeranyl diphosphate | ||||
Sequence: W | ||||||
Binding site | 256-259 | (2E,6E)-farnesyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: HGGY | ||||||
Binding site | 298-301 | (2E,6E)-farnesyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: RTNK | ||||||
Binding site | 304 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 306 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 307-310 | (2E,6E)-farnesyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: YTFW | ||||||
Binding site | 421 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | protein farnesyltransferase complex | |
Molecular Function | farnesyltranstransferase activity | |
Molecular Function | protein farnesyltransferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | cuticle development | |
Biological Process | negative regulation of abscisic acid-activated signaling pathway | |
Biological Process | protein farnesylation | |
Biological Process | protein prenylation | |
Biological Process | regulation of meristem structural organization | |
Biological Process | regulation of response to osmotic stress | |
Biological Process | regulation of response to salt stress | |
Biological Process | response to abscisic acid | |
Biological Process | response to fungus | |
Biological Process | response to water deprivation | |
Biological Process | stomatal opening |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein farnesyltransferase subunit beta
- EC number
- Short namesFTase-beta
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ38920
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
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 (PubMed:10840062).
Increased sensitivity to abscisic acid (ABA) as well as salt (NaCl) and osmotic (e.g. in response to mannitol and PEG) stresses in term of seed germination and roots elongation (PubMed:26147561).
Increased sensitivity to abscisic acid (ABA) as well as salt (NaCl) and osmotic (e.g. in response to mannitol and PEG) stresses in term of seed germination and roots elongation (PubMed:26147561).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 69 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000119764 | 1-482 | Protein farnesyltransferase subunit beta | |||
Sequence: MPVVTRLIRLKCVGLRLDRSGLNRRICHGGHGESTRRRVMEELSSLTVSQREQFLVENDVFGIYNYFDASDVSTQKYMMEIQRDKQLDYLMKGLRQLGPQFSSLDANRPWLCYWILHSIALLGETVDDELESNAIDFLGRCQGSEGGYGGGPGQLPHLATTYAAVNALVTLGGDKALSSINREKMSCFLRRMKDTSGGFRMHDMGEMDVRACYTAISVASILNIMDDELTQGLGDYILSCQTYEGGIGGEPGSEAHGGYTYCGLAAMILINEVDRLNLDSLMNWAVHRQGVEMGFQGRTNKLVDGCYTFWQAAPCVLLQRLYSTNDHDVHGSSHISEGTNEEHHAHDEDDLEDSDDDDDSDEDNDEDSVNGHRIHHTSTYINRRMQLVFDSLGLQRYVLLCSKIPDGGFRDKPRKPRDFYHTCYCLSGLSVAQHAWLKDEDTPPLTRDIMGGYSNLLEPVQLLHNIVMDQYNEAIEFFFKAA |
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Heterodimer of FTA and FTB (farnesyltransferase). Heterodimer of an alpha and a beta subunit.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q38920 | FTA Q9LX33 | 4 | EBI-1553332, EBI-1553317 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for repeat, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 131-172 | PFTB 1 | ||||
Sequence: ESNAIDFLGRCQGSEGGYGGGPGQLPHLATTYAAVNALVTLG | ||||||
Repeat | 182-223 | PFTB 2 | ||||
Sequence: REKMSCFLRRMKDTSGGFRMHDMGEMDVRACYTAISVASILN | ||||||
Repeat | 230-271 | PFTB 3 | ||||
Sequence: TQGLGDYILSCQTYEGGIGGEPGSEAHGGYTYCGLAAMILIN | ||||||
Repeat | 278-319 | PFTB 4 | ||||
Sequence: LDSLMNWAVHRQGVEMGFQGRTNKLVDGCYTFWQAAPCVLLQ | ||||||
Region | 329-372 | Disordered | ||||
Sequence: VHGSSHISEGTNEEHHAHDEDDLEDSDDDDDSDEDNDEDSVNGH | ||||||
Compositional bias | 330-347 | Basic and acidic residues | ||||
Sequence: HGSSHISEGTNEEHHAHD | ||||||
Compositional bias | 348-365 | Acidic residues | ||||
Sequence: EDDLEDSDDDDDSDEDND | ||||||
Repeat | 391-433 | PFTB 5 | ||||
Sequence: SLGLQRYVLLCSKIPDGGFRDKPRKPRDFYHTCYCLSGLSVAQ |
Sequence similarities
Belongs to the protein prenyltransferase subunit beta family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length482
- Mass (Da)54,216
- Last updated2011-05-31 v3
- Checksum4A557EB53567C83B
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1P8BE65 | A0A1P8BE65_ARATH | ERA1 | 514 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 129 | in Ref. 5; AAM20474 | ||||
Sequence: E → K | ||||||
Sequence conflict | 207 | in Ref. 6; AAA86658/AAA87585 | ||||
Sequence: M → I | ||||||
Compositional bias | 330-347 | Basic and acidic residues | ||||
Sequence: HGSSHISEGTNEEHHAHD | ||||||
Compositional bias | 348-365 | Acidic residues | ||||
Sequence: EDDLEDSDDDDDSDEDND |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF214106 EMBL· GenBank· DDBJ | AAF74564.1 EMBL· GenBank· DDBJ | mRNA | ||
AB010699 EMBL· GenBank· DDBJ | BAB10909.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002688 EMBL· GenBank· DDBJ | AED94529.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT030457 EMBL· GenBank· DDBJ | ABP88111.1 EMBL· GenBank· DDBJ | mRNA | ||
AY099623 EMBL· GenBank· DDBJ | AAM20474.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
U46574 EMBL· GenBank· DDBJ | AAA87585.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U44849 EMBL· GenBank· DDBJ | AAA86658.1 EMBL· GenBank· DDBJ | mRNA |