O04350 · TBCA_ARATH
- ProteinTubulin-folding cofactor A
- GeneTFCA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids113 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Tubulin-folding protein involved in the control of the alpha-/beta-tubulin monomer balance. Functions as a reservoir of bound and non-toxic beta-tubulin. Required in the developing embryo.
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | peroxisome | |
Molecular Function | beta-tubulin binding | |
Biological Process | post-chaperonin tubulin folding pathway | |
Biological Process | tubulin complex assembly |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameTubulin-folding cofactor A
- Short namesAtTFCA; CFA
- 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 accessionO04350
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Embryo lethality. Embryos consisting of variably enlarged cells with cell-wall stubs. Abnormal microtubule organization. Endosperm indistinguishable from wild-type endosperm in regard to nuclear multiplication and subsequent cellularization. Cells undergoing cytokinesis divide abnormally although they display pheragmoplast microtubules and accumulate KNOLLE in the forming cell plate.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 5 | No effect on beta-tubulin binding. | ||||
Sequence: R → A | ||||||
Mutagenesis | 9 | No effect on beta-tubulin binding. | ||||
Sequence: I → A | ||||||
Mutagenesis | 16 | No effect on beta-tubulin binding. | ||||
Sequence: R → A | ||||||
Mutagenesis | 20 | Loss of beta-tubulin binding. | ||||
Sequence: E → A | ||||||
Mutagenesis | 20 | Slight decrease of beta-tubulin binding. | ||||
Sequence: E → Q | ||||||
Mutagenesis | 22 | Decreased beta-tubulin binding; when associated with A-23. | ||||
Sequence: H → A | ||||||
Mutagenesis | 23 | Decreased beta-tubulin binding; when associated with A-22. | ||||
Sequence: S → A | ||||||
Mutagenesis | 24 | Loss of beta-tubulin binding. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 24 | Slight decrease of beta-tubulin binding. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 25 | No effect on beta-tubulin binding; when associated with A-26. | ||||
Sequence: E → A | ||||||
Mutagenesis | 26 | No effect on beta-tubulin binding; when associated with A-25. | ||||
Sequence: K → A | ||||||
Mutagenesis | 29 | Decreased beta-tubulin binding; when associated with A-30. | ||||
Sequence: E → A | ||||||
Mutagenesis | 30 | Decreased beta-tubulin binding; when associated with A-29. | ||||
Sequence: R → A | ||||||
Mutagenesis | 49 | Decreased beta-tubulin binding; when associated with A-50. | ||||
Sequence: K → A | ||||||
Mutagenesis | 50 | Decreased beta-tubulin binding; when associated with A-49. | ||||
Sequence: Q → A | ||||||
Mutagenesis | 53 | No effect on beta-tubulin binding. | ||||
Sequence: N → A | ||||||
Mutagenesis | 54 | No effect on beta-tubulin binding. | ||||
Sequence: V → A | ||||||
Mutagenesis | 57 | Loss of beta-tubulin binding. | ||||
Sequence: E → A | ||||||
Mutagenesis | 59 | No effect on beta-tubulin binding. | ||||
Sequence: R → A | ||||||
Mutagenesis | 64 | Decreased beta-tubulin binding. | ||||
Sequence: D → A | ||||||
Mutagenesis | 65 | Increased beta-tubulin binding. | ||||
Sequence: C → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 5 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_0000080043 | 1-113 | Tubulin-folding cofactor A | |||
Sequence: MATIRNLKIKTSTCKRIVKELHSYEKEVEREAAKTADMKDKGADPYDLKQQENVLGESRMMIPDCHKRLESALADLKSTLAELEETDEKEGPEIEDAKKTVADVEKQFPTEDA |
Proteomic databases
Expression
Tissue specificity
Expressed in leaves, roots, flowers and stems.
Gene expression databases
Interaction
Subunit
Monomer. Supercomplex made of cofactors A to E. Cofactors A and D function by capturing and stabilizing tubulin in a quasi-native conformation. Cofactor E binds to the cofactor D-tubulin complex; interaction with cofactor C then causes the release of tubulin polypeptides that are committed to the native state. Interacts with TUBB9.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O04350 | TUBB9 P29517 | 5 | EBI-1999365, EBI-2000198 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 83-113 | Disordered | ||||
Sequence: LEETDEKEGPEIEDAKKTVADVEKQFPTEDA | ||||||
Compositional bias | 92-113 | Basic and acidic residues | ||||
Sequence: PEIEDAKKTVADVEKQFPTEDA |
Sequence similarities
Belongs to the TBCA family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length113
- Mass (Da)12,824
- Last updated2002-06-20 v2
- ChecksumD29B73FEA6E352DC
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 92-113 | Basic and acidic residues | ||||
Sequence: PEIEDAKKTVADVEKQFPTEDA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF486848 EMBL· GenBank· DDBJ | AAM22957.1 EMBL· GenBank· DDBJ | mRNA | ||
AC002338 EMBL· GenBank· DDBJ | AAM14821.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U93215 EMBL· GenBank· DDBJ | AAB63093.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC08383.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC08384.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | ANM61960.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY050952 EMBL· GenBank· DDBJ | AAK93629.1 EMBL· GenBank· DDBJ | mRNA | ||
AY091344 EMBL· GenBank· DDBJ | AAM14283.1 EMBL· GenBank· DDBJ | mRNA | ||
AY085814 EMBL· GenBank· DDBJ | AAM63030.1 EMBL· GenBank· DDBJ | mRNA |