TBCA_ARATH
ID TBCA_ARATH Reviewed; 113 AA.
AC O04350; Q547H3; Q949R2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Tubulin-folding cofactor A;
DE Short=AtTFCA;
DE Short=CFA;
DE AltName: Full=Protein KIESEL;
DE AltName: Full=TCP1-chaperonin cofactor A;
DE AltName: Full=Tubulin-specific chaperone A;
GN Name=TFCA; Synonyms=KIS; OrderedLocusNames=At2g30410;
GN ORFNames=T06B20.22, T09D09.22;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta, and cv. Wassilewskija; TISSUE=Flower;
RX PubMed=11959844; DOI=10.1101/gad.221702;
RA Steinborn K., Maulbetsch C., Priester B., Trautmann S., Pacher T.,
RA Geiges B., Kuettner F., Lepiniec L., Stierhof Y.-D., Schwarz H.,
RA Juergens G., Mayer U.;
RT "The Arabidopsis PILZ group genes encode tubulin-folding cofactor orthologs
RT required for cell division but not cell growth.";
RL Genes Dev. 16:959-971(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12215519; DOI=10.1105/tpc.003020;
RA Kirik V., Grini P.E., Mathur J., Klinkhammer I., Adler K., Bechtold N.,
RA Herzog M., Bonneville J.M., Huelskamp M.;
RT "The Arabidopsis TUBULIN-FOLDING COFACTOR A gene is involved in the control
RT of the alpha/beta-tubulin monomer balance.";
RL Plant Cell 14:2265-2276(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), SUBUNIT, INTERACTION WITH TUBB9,
RP AND MUTAGENESIS OF ARG-5; ILE-9; ARG-16; GLU-20; HIS-22; SER-23; TYR-24;
RP GLU-25; LYS-26; GLU-29; ARG-30; LYS-49; GLN-50; ASN-53; VAL-54; ARG-59;
RP ASP-64 AND CYS-65.
RX PubMed=20638386; DOI=10.1016/j.febslet.2010.07.017;
RA Lu L., Nan J., Mi W., Li L.F., Wei C.H., Su X.D., Li Y.;
RT "Crystal structure of tubulin folding cofactor A from Arabidopsis thaliana
RT and its beta-tubulin binding characterization.";
RL FEBS Lett. 584:3533-3539(2010).
CC -!- FUNCTION: Tubulin-folding protein involved in the control of the
CC alpha-/beta-tubulin monomer balance. Functions as a reservoir of bound
CC and non-toxic beta-tubulin. Required in the developing embryo.
CC {ECO:0000269|PubMed:11959844, ECO:0000269|PubMed:12215519}.
CC -!- SUBUNIT: Monomer. Supercomplex made of cofactors A to E. Cofactors A
CC and D function by capturing and stabilizing tubulin in a quasi-native
CC conformation. Cofactor E binds to the cofactor D-tubulin complex;
CC interaction with cofactor C then causes the release of tubulin
CC polypeptides that are committed to the native state. Interacts with
CC TUBB9. {ECO:0000269|PubMed:20638386}.
CC -!- INTERACTION:
CC O04350; P29517: TUBB9; NbExp=5; IntAct=EBI-1999365, EBI-2000198;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, flowers and stems.
CC {ECO:0000269|PubMed:12215519}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality. Embryos consisting of variably
CC enlarged cells with cell-wall stubs. Abnormal microtubule organization.
CC Endosperm indistinguishable from wild-type endosperm in regard to
CC nuclear multiplication and subsequent cellularization. Cells undergoing
CC cytokinesis divide abnormally although they display pheragmoplast
CC microtubules and accumulate KNOLLE in the forming cell plate.
CC {ECO:0000269|PubMed:11959844}.
CC -!- SIMILARITY: Belongs to the TBCA family. {ECO:0000305}.
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DR EMBL; AF486848; AAM22957.1; -; mRNA.
DR EMBL; AC002338; AAM14821.1; -; Genomic_DNA.
DR EMBL; U93215; AAB63093.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC08383.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08384.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61960.1; -; Genomic_DNA.
DR EMBL; AY050952; AAK93629.1; -; mRNA.
DR EMBL; AY091344; AAM14283.1; -; mRNA.
DR EMBL; AY085814; AAM63030.1; -; mRNA.
DR PIR; B84708; B84708.
DR RefSeq; NP_001189640.1; NM_001202711.2.
DR RefSeq; NP_001318319.1; NM_001336255.1.
DR RefSeq; NP_565699.1; NM_128594.4.
DR PDB; 3MXZ; X-ray; 1.60 A; A=1-113.
DR PDBsum; 3MXZ; -.
DR AlphaFoldDB; O04350; -.
DR SMR; O04350; -.
DR BioGRID; 2941; 2.
DR IntAct; O04350; 2.
DR MINT; O04350; -.
DR STRING; 3702.AT2G30410.2; -.
DR PaxDb; O04350; -.
DR PRIDE; O04350; -.
DR ProteomicsDB; 246453; -.
DR EnsemblPlants; AT2G30410.1; AT2G30410.1; AT2G30410.
DR EnsemblPlants; AT2G30410.2; AT2G30410.2; AT2G30410.
DR EnsemblPlants; AT2G30410.3; AT2G30410.3; AT2G30410.
DR GeneID; 817592; -.
DR Gramene; AT2G30410.1; AT2G30410.1; AT2G30410.
DR Gramene; AT2G30410.2; AT2G30410.2; AT2G30410.
DR Gramene; AT2G30410.3; AT2G30410.3; AT2G30410.
DR KEGG; ath:AT2G30410; -.
DR Araport; AT2G30410; -.
DR TAIR; locus:2064367; AT2G30410.
DR eggNOG; KOG3470; Eukaryota.
DR HOGENOM; CLU_130569_1_2_1; -.
DR InParanoid; O04350; -.
DR OMA; IMMVPDS; -.
DR OrthoDB; 1471374at2759; -.
DR PhylomeDB; O04350; -.
DR EvolutionaryTrace; O04350; -.
DR PRO; PR:O04350; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O04350; baseline and differential.
DR Genevisible; O04350; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0048487; F:beta-tubulin binding; IEA:InterPro.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR InterPro; IPR004226; TBCA.
DR InterPro; IPR036126; TBCA_sf.
DR PANTHER; PTHR21500; PTHR21500; 1.
DR Pfam; PF02970; TBCA; 1.
DR SUPFAM; SSF46988; SSF46988; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Reference proteome.
FT CHAIN 1..113
FT /note="Tubulin-folding cofactor A"
FT /id="PRO_0000080043"
FT REGION 83..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 5
FT /note="R->A: No effect on beta-tubulin binding."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 9
FT /note="I->A: No effect on beta-tubulin binding."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 16
FT /note="R->A: No effect on beta-tubulin binding."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 20
FT /note="E->A: Loss of beta-tubulin binding."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 20
FT /note="E->Q: Slight decrease of beta-tubulin binding."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 22
FT /note="H->A: Decreased beta-tubulin binding; when
FT associated with A-23."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 23
FT /note="S->A: Decreased beta-tubulin binding; when
FT associated with A-22."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 24
FT /note="Y->A: Loss of beta-tubulin binding."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 24
FT /note="Y->F: Slight decrease of beta-tubulin binding."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 25
FT /note="E->A: No effect on beta-tubulin binding; when
FT associated with A-26."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 26
FT /note="K->A: No effect on beta-tubulin binding; when
FT associated with A-25."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 29
FT /note="E->A: Decreased beta-tubulin binding; when
FT associated with A-30."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 30
FT /note="R->A: Decreased beta-tubulin binding; when
FT associated with A-29."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 49
FT /note="K->A: Decreased beta-tubulin binding; when
FT associated with A-50."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 50
FT /note="Q->A: Decreased beta-tubulin binding; when
FT associated with A-49."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 53
FT /note="N->A: No effect on beta-tubulin binding."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 54
FT /note="V->A: No effect on beta-tubulin binding."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 57
FT /note="E->A: Loss of beta-tubulin binding."
FT MUTAGEN 59
FT /note="R->A: No effect on beta-tubulin binding."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 64
FT /note="D->A: Decreased beta-tubulin binding."
FT /evidence="ECO:0000269|PubMed:20638386"
FT MUTAGEN 65
FT /note="C->A: Increased beta-tubulin binding."
FT /evidence="ECO:0000269|PubMed:20638386"
FT HELIX 1..40
FT /evidence="ECO:0007829|PDB:3MXZ"
FT HELIX 45..84
FT /evidence="ECO:0007829|PDB:3MXZ"
FT HELIX 92..105
FT /evidence="ECO:0007829|PDB:3MXZ"
SQ SEQUENCE 113 AA; 12824 MW; D29B73FEA6E352DC CRC64;
MATIRNLKIK TSTCKRIVKE LHSYEKEVER EAAKTADMKD KGADPYDLKQ QENVLGESRM
MIPDCHKRLE SALADLKSTL AELEETDEKE GPEIEDAKKT VADVEKQFPT EDA
