TBCC_ARATH
ID TBCC_ARATH Reviewed; 345 AA.
AC Q9SMR2; Q8L5R4;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Tubulin-folding cofactor C;
DE Short=AtTFCC;
DE Short=TFC C;
DE AltName: Full=Protein PORCINO;
GN Name=TFCC; Synonyms=POR; OrderedLocusNames=At4g39920; ORFNames=T5J17.90;
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, DISRUPTION PHENOTYPE, MUTAGENESIS OF
RP SER-238, SUBUNIT, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=10099932; DOI=10.1016/s0171-9335(99)80011-9;
RA Mayer U., Herzog U., Berger F., Inze D., Juergens G.;
RT "Mutations in the pilz group genes disrupt the microtubule cytoskeleton and
RT uncouple cell cycle progression from cell division in Arabidopsis embryo
RT and endosperm.";
RL Eur. J. Cell Biol. 78:100-108(1999).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12225668; DOI=10.1016/s0960-9822(02)01109-0;
RA Kirik V., Mathur J., Grini P.E., Klinkhammer I., Adler K., Bechtold N.,
RA Herzog M., Bonneville J.-M., Huelskamp M.;
RT "Functional analysis of the tubulin-folding cofactor C in Arabidopsis
RT thaliana.";
RL Curr. Biol. 12:1519-1523(2002).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Essential tubulin-folding protein involved in the final step
CC of the tubulin folding pathway. Required for continuous microtubule
CC cytoskeleton organization, mitotic division, cytokinesis, and to couple
CC cell cycle progression to cell division in embryos and endosperms. Not
CC essential for cell viability. Binds probably to the multimeric
CC supercomplex, stimulating GTP hydrolysis by the bound beta-tubulin and
CC the release of the alpha-/beta-tubulin heterodimer.
CC {ECO:0000269|PubMed:10099932, ECO:0000269|PubMed:11959844,
CC ECO:0000269|PubMed:12225668}.
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.
CC {ECO:0000269|PubMed:11959844}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11959844,
CC ECO:0000269|PubMed:12225668}. Note=Not associated with microtubular
CC arrays.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). Present
CC in leaves, roots, flowers, and stems. {ECO:0000269|PubMed:11959844,
CC ECO:0000269|PubMed:12225668}.
CC -!- DISRUPTION PHENOTYPE: Disturbed microtubule organization. Lethal
CC embryos that consist of one or a few grossly enlarged cells that lack
CC microtubules but not actin filaments. Failure to localize KNOLLE in
CC mitotic cells. Cortical microtubules-free interphase cells and mitotic
CC nuclei missing spindles. Reduced trichome size with fewer branches.
CC {ECO:0000269|PubMed:11959844, ECO:0000269|PubMed:12225668}.
CC -!- MISCELLANEOUS: Belongs to the PILZ group of genes that disrupt, when
CC mutated, the microtubule cytoskeleton and produce mushroom-shaped
CC ('pilz' in German) embryos.
CC -!- SIMILARITY: Belongs to the TBCC family. {ECO:0000305}.
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DR EMBL; AF486850; AAM22959.1; -; mRNA.
DR EMBL; AL035708; CAB38905.1; -; Genomic_DNA.
DR EMBL; AL161596; CAB80655.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87138.1; -; Genomic_DNA.
DR EMBL; BT024735; ABD59073.1; -; mRNA.
DR PIR; T06098; T06098.
DR RefSeq; NP_195702.1; NM_120155.4.
DR AlphaFoldDB; Q9SMR2; -.
DR SMR; Q9SMR2; -.
DR STRING; 3702.AT4G39920.1; -.
DR iPTMnet; Q9SMR2; -.
DR PaxDb; Q9SMR2; -.
DR PRIDE; Q9SMR2; -.
DR ProteomicsDB; 234193; -.
DR EnsemblPlants; AT4G39920.1; AT4G39920.1; AT4G39920.
DR GeneID; 830151; -.
DR Gramene; AT4G39920.1; AT4G39920.1; AT4G39920.
DR KEGG; ath:AT4G39920; -.
DR Araport; AT4G39920; -.
DR TAIR; locus:2140089; AT4G39920.
DR eggNOG; KOG2512; Eukaryota.
DR HOGENOM; CLU_032612_2_0_1; -.
DR InParanoid; Q9SMR2; -.
DR OMA; CQQLRLH; -.
DR OrthoDB; 1618114at2759; -.
DR PhylomeDB; Q9SMR2; -.
DR PRO; PR:Q9SMR2; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SMR2; baseline and differential.
DR Genevisible; Q9SMR2; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
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; ISS:TAIR.
DR Gene3D; 1.20.58.1250; -; 1.
DR Gene3D; 2.160.20.70; -; 1.
DR InterPro; IPR017901; C-CAP_CF_C-like.
DR InterPro; IPR016098; CAP/MinC_C.
DR InterPro; IPR006599; CARP_motif.
DR InterPro; IPR027684; TBCC.
DR InterPro; IPR031925; TBCC_N.
DR InterPro; IPR038397; TBCC_N_sf.
DR InterPro; IPR012945; Tubulin-bd_cofactor_C_dom.
DR PANTHER; PTHR15139; PTHR15139; 1.
DR Pfam; PF07986; TBCC; 1.
DR Pfam; PF16752; TBCC_N; 1.
DR SMART; SM00673; CARP; 2.
DR PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..345
FT /note="Tubulin-folding cofactor C"
FT /id="PRO_0000420263"
FT DOMAIN 169..318
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 238
FT /note="S->L: Embryo lethal. Cortical microtubules-free
FT interphase cells and mitotic nuclei without spindles."
FT /evidence="ECO:0000269|PubMed:11959844"
FT CONFLICT 154..158
FT /note="Missing (in Ref. 1; AAM22959)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 345 AA; 38309 MW; 74C9A612473FF295 CRC64;
MEDDGQSSVA ETLDPALQKK HHDMLERLSA RHQARKSDSP DSSSSSSSTL ESTSSFLAKF
SDSKRSIESR IAESRLASSS TDSSKLKSDL AEISVAIDNL EKLLAENSYF LPSYEVRSSL
KIVSDLKQSL DILSGELVPK KKFSFKSKST TKKPESKLPE IQKPDVVLPP KLVPVRDSPG
LRNKHGETLV KSFEGSSIGE FTLSDLDSCQ VKLTGTVNAL FLHRLKKCSV YTGPVIGSIL
IDDVEDCVLV LASHQIRIHC ARKSDFYLRV RSRPIIEDSN GVRFAPYCLD YKGIDEDLKT
AGLEEETNNW ANVDDFRWLR AVQSPNWSLL PEEERVSLLT ISGDS
