TBCB_ARATH
ID TBCB_ARATH Reviewed; 243 AA.
AC Q67Z52; Q67XW4; Q8L5R5; Q9SS34;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Tubulin-folding cofactor B;
DE Short=AtTFCB;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2804;
GN Name=TFCB; Synonyms=EMB2804, TBCB; OrderedLocusNames=At3g10220;
GN ORFNames=F14P13.18;
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].
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH TUBA6.
RX PubMed=16928693; DOI=10.1093/pcp/pcl001;
RA Dhonukshe P., Bargmann B.O., Gadella T.W. Jr.;
RT "Arabidopsis tubulin folding cofactor B interacts with alpha-tubulin in
RT vivo.";
RL Plant Cell Physiol. 47:1406-1411(2006).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20036919; DOI=10.2741/e135;
RA Du Y., Cui M., Qian D., Zhu L., Wei C., Yuan M., Zhang Z., Li Y.;
RT "AtTFC B is involved in control of cell division.";
RL Front. Biosci. 2:752-763(2010).
RN [7]
RP STRUCTURE BY NMR OF 10-96.
RA Mani R., Swapna G.V.T., Shastry R., Foote E., Ciccosanti C., Jiang M.,
RA Xiao R., Nair R., Everett J., Huang Y.J., Acton T., Rost B.,
RA Montelione G.T.;
RT "NMR Solution Structure of Tbulin folding Cofactor B obtained from
RT Arabidopsis thaliana: Northeast.";
RL Submitted (MAY-2009) to the PDB data bank.
CC -!- FUNCTION: Involved in control of cell division. Regulates probably the
CC availability of alpha-tubulin for dimerization of alpha-/beta-tubulin,
CC which is required for proper microtubule biogenesis. Decreased
CC expression of TFCB results in enlarged mesophyll cells and leaf
CC epidermal cells with bulged nuclei, increased ploidy and increased
CC numbers of spindles and phragmoplasts. {ECO:0000269|PubMed:20036919}.
CC -!- SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D
CC 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 TUBA6. {ECO:0000269|PubMed:16928693}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16928693}. Note=Not
CC associated with microtubular arrays.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:16928693, ECO:0000269|PubMed:20036919}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality. {ECO:0000269|PubMed:20036919}.
CC -!- SIMILARITY: Belongs to the TBCB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF02820.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF486849; AAM22958.1; -; mRNA.
DR EMBL; AC009400; AAF02820.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74873.1; -; Genomic_DNA.
DR EMBL; AK176183; BAD43946.1; -; mRNA.
DR EMBL; AK176266; BAD44029.1; -; mRNA.
DR EMBL; AK176704; BAD44467.1; -; mRNA.
DR RefSeq; NP_187633.2; NM_111857.5.
DR PDB; 2KJ6; NMR; -; A=10-96.
DR PDBsum; 2KJ6; -.
DR AlphaFoldDB; Q67Z52; -.
DR BMRB; Q67Z52; -.
DR SMR; Q67Z52; -.
DR STRING; 3702.AT3G10220.1; -.
DR PaxDb; Q67Z52; -.
DR PRIDE; Q67Z52; -.
DR ProteomicsDB; 233015; -.
DR EnsemblPlants; AT3G10220.1; AT3G10220.1; AT3G10220.
DR GeneID; 820184; -.
DR Gramene; AT3G10220.1; AT3G10220.1; AT3G10220.
DR KEGG; ath:AT3G10220; -.
DR Araport; AT3G10220; -.
DR TAIR; locus:2076224; AT3G10220.
DR eggNOG; KOG3206; Eukaryota.
DR HOGENOM; CLU_067577_3_0_1; -.
DR InParanoid; Q67Z52; -.
DR OMA; IGVKYDE; -.
DR OrthoDB; 1550378at2759; -.
DR PhylomeDB; Q67Z52; -.
DR EvolutionaryTrace; Q67Z52; -.
DR PRO; PR:Q67Z52; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q67Z52; baseline and differential.
DR Genevisible; Q67Z52; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; HDA:TAIR.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR CDD; cd01789; Ubl_TBCB; 1.
DR Gene3D; 2.30.30.190; -; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR045172; TBCB_N_Ubl.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF14560; Ubiquitin_2; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..243
FT /note="Tubulin-folding cofactor B"
FT /id="PRO_0000423499"
FT DOMAIN 181..223
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT CONFLICT 43
FT /note="E -> G (in Ref. 4; BAD44467)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="S -> F (in Ref. 1; AAM22958)"
FT /evidence="ECO:0000305"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:2KJ6"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:2KJ6"
FT HELIX 38..49
FT /evidence="ECO:0007829|PDB:2KJ6"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:2KJ6"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2KJ6"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:2KJ6"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:2KJ6"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:2KJ6"
SQ SEQUENCE 243 AA; 27331 MW; E4685B37CFD9DC16 CRC64;
MATSRLQLEG DDSVHLHITH ANLKSFSADA RFSPQMSVEA VKEKLWKKCG TSVNSMALEL
YDDSGSKVAV LSDDSRPLGF FSPFDGFRLH IIDLDPSSVT TGGWLEDTSL VEKYNISEED
YAKRTDSFRK FKEKRVSQNP VAAEAKTKEN YMEDLCANIK VGDRCQVEPG EKRGMVKYVG
RAESLGPGYW VGIQYDEPLG KHDGMVKGTR FFECPRLQGG MVRPDKVKVG DYPERDPFEE
DEI
