TBCD_ARATH
ID TBCD_ARATH Reviewed; 1254 AA.
AC Q8L5R3; Q9LZY9;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Tubulin-folding cofactor D;
DE Short=AtTFCD;
DE AltName: Full=Protein CHAMPIGNON;
DE AltName: Full=Protein EMBRYO DEFECTIVE 133;
DE AltName: Full=Protein TITAN 1;
GN Name=TFCD; Synonyms=CHO, EMB133, TBCD, TTN1; OrderedLocusNames=At3g60740;
GN ORFNames=T4C21.150;
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=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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9807824; DOI=10.1046/j.1365-313x.1998.00268.x;
RA Liu C.M., Meinke D.W.;
RT "The titan mutants of Arabidopsis are disrupted in mitosis and cell cycle
RT control during seed development.";
RL Plant J. 16:21-31(1998).
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, AND DISRUPTION PHENOTYPE.
RX PubMed=11788751; DOI=10.1104/pp.010911;
RA Tzafrir I., McElver J.A., Liu C.-M., Yang L.J., Wu J.Q., Martinez A.,
RA Patton D.A., Meinke D.W.;
RT "Diversity of TITAN functions in Arabidopsis seed development.";
RL Plant Physiol. 128:38-51(2002).
CC -!- FUNCTION: Regulates microtubule function in seed development. Required
CC for development of both embryo and endosperm tissue. Not essential for
CC cell viability. Probably involved in the binding of beta-tubulin in the
CC multimeric supercomplex. {ECO:0000269|PubMed:10099932,
CC ECO:0000269|PubMed:11788751, ECO:0000269|PubMed:11959844,
CC ECO:0000269|PubMed:9807824}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality. Embryo development limited to
CC the formation of a few giant cells lacking microtubules but not actin
CC filaments, each with one to several nuclei. Failure to localize KNOLLE
CC in mitotic cells. Presence of abnormal endosperm with giant polyploid
CC nuclei. {ECO:0000269|PubMed:11788751, ECO:0000269|PubMed:11959844,
CC ECO:0000269|PubMed:9807824}.
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 TBCD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB82678.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF486851; AAM22960.1; -; mRNA.
DR EMBL; AL162295; CAB82678.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80102.1; -; Genomic_DNA.
DR PIR; T47885; T47885.
DR RefSeq; NP_191633.3; NM_115938.6.
DR AlphaFoldDB; Q8L5R3; -.
DR STRING; 3702.AT3G60740.1; -.
DR iPTMnet; Q8L5R3; -.
DR PaxDb; Q8L5R3; -.
DR PRIDE; Q8L5R3; -.
DR EnsemblPlants; AT3G60740.1; AT3G60740.1; AT3G60740.
DR GeneID; 825245; -.
DR Gramene; AT3G60740.1; AT3G60740.1; AT3G60740.
DR KEGG; ath:AT3G60740; -.
DR Araport; AT3G60740; -.
DR TAIR; locus:2101856; AT3G60740.
DR eggNOG; KOG1943; Eukaryota.
DR HOGENOM; CLU_003043_0_0_1; -.
DR InParanoid; Q8L5R3; -.
DR OrthoDB; 79003at2759; -.
DR PhylomeDB; Q8L5R3; -.
DR PRO; PR:Q8L5R3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8L5R3; baseline and differential.
DR Genevisible; Q8L5R3; AT.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0048487; F:beta-tubulin binding; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0015631; F:tubulin binding; ISS:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IMP:TAIR.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; ISS:TAIR.
DR GO; GO:0007021; P:tubulin complex assembly; ISS:TAIR.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033162; TBCD.
DR InterPro; IPR022577; Tubulin_specific_chaperoneD_C.
DR PANTHER; PTHR12658; PTHR12658; 1.
DR Pfam; PF12612; TFCD_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 2: Evidence at transcript level;
KW Chaperone; Reference proteome.
FT CHAIN 1..1254
FT /note="Tubulin-folding cofactor D"
FT /id="PRO_0000423500"
FT CONFLICT 237
FT /note="G -> R (in Ref. 2; CAB82678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1254 AA; 139916 MW; 206629B3E55B79BE CRC64;
MASRAEEMSP TKIEIETAVK IEEEEDDEHD SKERVLQRYF LQEWKLVKSL LDDIVSNGRV
VDPTSVHKIR SIMDKYQEQG QLVEPYLESI VSPLMFIIRS KTVDLEAKPD EILEIIKPIS
IIIYALVTVC GYKAVIKFFP HQVSDLELAV LLLEKCHSTN SVSALRQEST GEMEAKCVTL
LWLSILVLVP FDISSVDTSI ADDKTFGVDD LAPLVLKILG FCKDYLCSAG PMRRISGLLL
SKLLTRPDMG KAFSSFFEWT YEVLSCKEDS VTNHFRLLGV MEALSAIFKT ASRKVLLDVL
PIVLNDVTVL SKSNAAAKSS LLRKYLIKLT QRIGLVCLPH RSPSWRYVAQ TASLSENMST
SSSQRLAPDH TVTAILQPES LDDQEDEDMD VPEILEEIIE MLLSGLRDTD TVVRWSAAKG
IGRVTSRLTS VLSDEVLSSV LELFSPGEGD GSWHGGCLAL AELARRGLLL PRSFPLVVPV
IVKALHYDVR RGPHSVGSHV RDAAAYVCWA FGRAYSHKDM KNVLDQLAPD LLIVGSFDRE
VNCRRAAAAA FQENVGRQGN YPHGIDIVSI ADYFSLSSRV NSYLQVAVSI AQYEGYLYPF
VDELLYNKIC HWDKSLRELA AEALAPLVKY EPKHFANYVL EKLIPCTLST DLCMRHGATL
AAGEVVLALH QCGYVLSADS QKRMAGIVPS IEKARLYRGK GGEIMRLAVS RFIECISLSH
VTLAERTERI LLDTLTENLR HPNSQIQNAA VSAVKQLVQS YLVGNDKKSV DLILKHLKHL
TDPNVAVRRG SALALGVLPY ELLTAKWKDI VLKLCSACKI EVNPEDRDAE ARVNAVKGLT
SVCETLTQKR ASDPGNDDLS LFLLIKTEVM DTLLKALDDY SVDNRGDVGS WVREAAVHGL
EKCTYILCKK METYSEGDYN DDTSSLFDSN LATRLIGGML KQGVEKMDKL RETAAKVLQR
ILYHKSVSVP HVPYREKLEE ILPNKANLQW AVPAFSFPRF VQLLKLRCYS KEVMSGLVIS
IGGLQDSLRK ASLVALLEYM REGEAKDPKE QQSRESALGD DILWILQEYK KCDRVMVPCL
QTIEILFSSK IFLNQESYTF SFYAGVMDSL AIELRASKDF TKLKAGLAIL GYIASVSHFI
STKAFSQLLS FLGHRYPMIR KAAAEQVYLA LLQNGILVTE EKMEKVIEII SESCWEADME
TTKTQRLELC ELAGLDHEVV FKTRNRLVIK DIAGNKSAAD ENASYSSLVD SSGF
