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Protein

Tubulin-folding cofactor A

Gene

TFCA

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

Functioni

Tubulin-folding protein involved in the control of the alpha-/beta-tubulin monomer balance. Function as a reservoir of bound and non-toxic beta-tubulin. Required in the developing embryo.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin-folding cofactor A
Short name:
AtTFCA
Short name:
CFA
Alternative name(s):
Protein KIESEL
TCP1-chaperonin cofactor A
Tubulin-specific chaperone A
Gene namesi
Name:TFCA
Synonyms:KIS
Ordered Locus Names:At2g30410
ORF Names:T06B20.22, T09D09.22
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G30410.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi5 – 51R → A: No effect on beta-tubulin binding. 1 Publication
Mutagenesisi9 – 91I → A: No effect on beta-tubulin binding. 1 Publication
Mutagenesisi16 – 161R → A: No effect on beta-tubulin binding. 1 Publication
Mutagenesisi20 – 201E → A: Loss of beta-tubulin binding. 1 Publication
Mutagenesisi20 – 201E → Q: Slight decrease of beta-tubulin binding. 1 Publication
Mutagenesisi22 – 221H → A: Decreased beta-tubulin binding; when associated with A-23. 1 Publication
Mutagenesisi23 – 231S → A: Decreased beta-tubulin binding; when associated with A-22. 1 Publication
Mutagenesisi24 – 241Y → A: Loss of beta-tubulin binding. 1 Publication
Mutagenesisi24 – 241Y → F: Slight decrease of beta-tubulin binding. 1 Publication
Mutagenesisi25 – 251E → A: No effect on beta-tubulin binding; when associated with A-26. 1 Publication
Mutagenesisi26 – 261K → A: No effect on beta-tubulin binding; when associated with A-25. 1 Publication
Mutagenesisi29 – 291E → A: Decreased beta-tubulin binding; when associated with A-30. 1 Publication
Mutagenesisi30 – 301R → A: Decreased beta-tubulin binding; when associated with A-29. 1 Publication
Mutagenesisi49 – 491K → A: Decreased beta-tubulin binding; when associated with A-50. 1 Publication
Mutagenesisi50 – 501Q → A: Decreased beta-tubulin binding; when associated with A-49. 1 Publication
Mutagenesisi53 – 531N → A: No effect on beta-tubulin binding. 1 Publication
Mutagenesisi54 – 541V → A: No effect on beta-tubulin binding. 1 Publication
Mutagenesisi57 – 571E → A: Loss of beta-tubulin binding.
Mutagenesisi59 – 591R → A: No effect on beta-tubulin binding. 1 Publication
Mutagenesisi64 – 641D → A: Decreased beta-tubulin binding. 1 Publication
Mutagenesisi65 – 651C → A: Increased beta-tubulin binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 113113Tubulin-folding cofactor APRO_0000080043Add
BLAST

Proteomic databases

PaxDbiO04350.
PRIDEiO04350.

Expressioni

Tissue specificityi

Expressed in leaves, roots, flowers and stems.1 Publication

Gene expression databases

GenevisibleiO04350. AT.

Interactioni

Subunit structurei

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 TUBB9.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TUBB9P295175EBI-1999365,EBI-2000198

Protein-protein interaction databases

BioGridi2941. 2 interactions.
IntActiO04350. 2 interactions.
MINTiMINT-7968859.
STRINGi3702.AT2G30410.1.

Structurei

Secondary structure

113
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 4040Combined sources
Helixi45 – 8440Combined sources
Helixi92 – 10514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MXZX-ray1.60A1-113[»]
ProteinModelPortaliO04350.
SMRiO04350. Positions 1-107.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO04350.

Family & Domainsi

Sequence similaritiesi

Belongs to the TBCA family.Curated

Phylogenomic databases

eggNOGiKOG3470. Eukaryota.
ENOG4111Y9A. LUCA.
HOGENOMiHOG000213817.
InParanoidiO04350.
KOiK17292.
OMAiKTGTCKR.
OrthoDBiEOG09360VTN.
PhylomeDBiO04350.

Family and domain databases

InterProiIPR004226. TBCA.
[Graphical view]
PANTHERiPTHR21500:SF0. PTHR21500:SF0. 1 hit.
PfamiPF02970. TBCA. 1 hit.
[Graphical view]
ProDomiPD010430. CofA_tubulin_bd. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46988. SSF46988. 1 hit.

Sequencei

Sequence statusi: Complete.

O04350-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATIRNLKIK TSTCKRIVKE LHSYEKEVER EAAKTADMKD KGADPYDLKQ
60 70 80 90 100
QENVLGESRM MIPDCHKRLE SALADLKSTL AELEETDEKE GPEIEDAKKT
110
VADVEKQFPT EDA
Length:113
Mass (Da):12,824
Last modified:June 20, 2002 - v2
Checksum:iD29B73FEA6E352DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF486848 mRNA. Translation: AAM22957.1.
AC002338 Genomic DNA. Translation: AAM14821.1.
U93215 Genomic DNA. Translation: AAB63093.2.
CP002685 Genomic DNA. Translation: AEC08383.1.
CP002685 Genomic DNA. Translation: AEC08384.1.
AY050952 mRNA. Translation: AAK93629.1.
AY091344 mRNA. Translation: AAM14283.1.
AY085814 mRNA. Translation: AAM63030.1.
PIRiB84708.
RefSeqiNP_001189640.1. NM_001202711.1.
NP_565699.1. NM_128594.3.
UniGeneiAt.23965.

Genome annotation databases

EnsemblPlantsiAT2G30410.1; AT2G30410.1; AT2G30410.
AT2G30410.2; AT2G30410.2; AT2G30410.
GeneIDi817592.
GrameneiAT2G30410.1; AT2G30410.1; AT2G30410.
AT2G30410.2; AT2G30410.2; AT2G30410.
KEGGiath:AT2G30410.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF486848 mRNA. Translation: AAM22957.1.
AC002338 Genomic DNA. Translation: AAM14821.1.
U93215 Genomic DNA. Translation: AAB63093.2.
CP002685 Genomic DNA. Translation: AEC08383.1.
CP002685 Genomic DNA. Translation: AEC08384.1.
AY050952 mRNA. Translation: AAK93629.1.
AY091344 mRNA. Translation: AAM14283.1.
AY085814 mRNA. Translation: AAM63030.1.
PIRiB84708.
RefSeqiNP_001189640.1. NM_001202711.1.
NP_565699.1. NM_128594.3.
UniGeneiAt.23965.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MXZX-ray1.60A1-113[»]
ProteinModelPortaliO04350.
SMRiO04350. Positions 1-107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi2941. 2 interactions.
IntActiO04350. 2 interactions.
MINTiMINT-7968859.
STRINGi3702.AT2G30410.1.

Proteomic databases

PaxDbiO04350.
PRIDEiO04350.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G30410.1; AT2G30410.1; AT2G30410.
AT2G30410.2; AT2G30410.2; AT2G30410.
GeneIDi817592.
GrameneiAT2G30410.1; AT2G30410.1; AT2G30410.
AT2G30410.2; AT2G30410.2; AT2G30410.
KEGGiath:AT2G30410.

Organism-specific databases

TAIRiAT2G30410.

Phylogenomic databases

eggNOGiKOG3470. Eukaryota.
ENOG4111Y9A. LUCA.
HOGENOMiHOG000213817.
InParanoidiO04350.
KOiK17292.
OMAiKTGTCKR.
OrthoDBiEOG09360VTN.
PhylomeDBiO04350.

Miscellaneous databases

EvolutionaryTraceiO04350.
PROiO04350.

Gene expression databases

GenevisibleiO04350. AT.

Family and domain databases

InterProiIPR004226. TBCA.
[Graphical view]
PANTHERiPTHR21500:SF0. PTHR21500:SF0. 1 hit.
PfamiPF02970. TBCA. 1 hit.
[Graphical view]
ProDomiPD010430. CofA_tubulin_bd. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF46988. SSF46988. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTBCA_ARATH
AccessioniPrimary (citable) accession number: O04350
Secondary accession number(s): Q547H3, Q949R2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 20, 2002
Last modified: September 7, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.