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Protein

Tubulin-folding cofactor A

Gene

TFCA

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -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 - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone

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

AraportiAT2G30410
TAIRilocus:2064367 AT2G30410

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
Mutagenesisi5R → A: No effect on beta-tubulin binding. 1 Publication1
Mutagenesisi9I → A: No effect on beta-tubulin binding. 1 Publication1
Mutagenesisi16R → A: No effect on beta-tubulin binding. 1 Publication1
Mutagenesisi20E → A: Loss of beta-tubulin binding. 1 Publication1
Mutagenesisi20E → Q: Slight decrease of beta-tubulin binding. 1 Publication1
Mutagenesisi22H → A: Decreased beta-tubulin binding; when associated with A-23. 1 Publication1
Mutagenesisi23S → A: Decreased beta-tubulin binding; when associated with A-22. 1 Publication1
Mutagenesisi24Y → A: Loss of beta-tubulin binding. 1 Publication1
Mutagenesisi24Y → F: Slight decrease of beta-tubulin binding. 1 Publication1
Mutagenesisi25E → A: No effect on beta-tubulin binding; when associated with A-26. 1 Publication1
Mutagenesisi26K → A: No effect on beta-tubulin binding; when associated with A-25. 1 Publication1
Mutagenesisi29E → A: Decreased beta-tubulin binding; when associated with A-30. 1 Publication1
Mutagenesisi30R → A: Decreased beta-tubulin binding; when associated with A-29. 1 Publication1
Mutagenesisi49K → A: Decreased beta-tubulin binding; when associated with A-50. 1 Publication1
Mutagenesisi50Q → A: Decreased beta-tubulin binding; when associated with A-49. 1 Publication1
Mutagenesisi53N → A: No effect on beta-tubulin binding. 1 Publication1
Mutagenesisi54V → A: No effect on beta-tubulin binding. 1 Publication1
Mutagenesisi57E → A: Loss of beta-tubulin binding. 1
Mutagenesisi59R → A: No effect on beta-tubulin binding. 1 Publication1
Mutagenesisi64D → A: Decreased beta-tubulin binding. 1 Publication1
Mutagenesisi65C → A: Increased beta-tubulin binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000800431 – 113Tubulin-folding cofactor AAdd BLAST113

Proteomic databases

PaxDbiO04350

Expressioni

Tissue specificityi

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

Gene expression databases

ExpressionAtlasiO04350 baseline and differential
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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi2941, 2 interactors
IntActiO04350, 2 interactors
MINTiO04350
STRINGi3702.AT2G30410.1

Structurei

Secondary structure

1113
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 40Combined sources40
Helixi45 – 84Combined sources40
Helixi92 – 105Combined sources14

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO04350

Family & Domainsi

Sequence similaritiesi

Belongs to the TBCA family.Curated

Phylogenomic databases

eggNOGiKOG3470 Eukaryota
ENOG4111Y9A LUCA
HOGENOMiHOG000213817
InParanoidiO04350
KOiK17292
OMAiIMMVPDS
OrthoDBiEOG09360VTN
PhylomeDBiO04350

Family and domain databases

InterProiView protein in InterPro
IPR004226 TBCA
IPR036126 TBCA_sf
PANTHERiPTHR21500 PTHR21500, 1 hit
PfamiView protein in Pfam
PF02970 TBCA, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD010430 CofA_tubulin_bd, 1 hit
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
CP002685 Genomic DNA Translation: ANM61960.1
AY050952 mRNA Translation: AAK93629.1
AY091344 mRNA Translation: AAM14283.1
AY085814 mRNA Translation: AAM63030.1
PIRiB84708
RefSeqiNP_001189640.1, NM_001202711.2
NP_001318319.1, NM_001336255.1
NP_565699.1, NM_128594.4
UniGeneiAt.23965

Genome annotation databases

EnsemblPlantsiAT2G30410.1; AT2G30410.1; AT2G30410
AT2G30410.2; AT2G30410.2; AT2G30410
AT2G30410.3; AT2G30410.3; AT2G30410
GeneIDi817592
GrameneiAT2G30410.1; AT2G30410.1; AT2G30410
AT2G30410.2; AT2G30410.2; AT2G30410
AT2G30410.3; AT2G30410.3; AT2G30410
KEGGiath:AT2G30410

Similar proteinsi

Entry informationi

Entry nameiTBCA_ARATH
AccessioniPrimary (citable) accession number: O04350
Secondary accession number(s): Q547H3, Q949R2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 20, 2002
Last modified: April 25, 2018
This is version 131 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health