TBCE_ARATH
ID TBCE_ARATH Reviewed; 531 AA.
AC Q8GRL7; Q8L405; Q9C9I1;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Tubulin-folding cofactor E;
DE Short=AtTFCE;
DE AltName: Full=Protein PFIFFERLING;
GN Name=TFCE; Synonyms=PFI, TBCE; OrderedLocusNames=At1g71440;
GN ORFNames=F26A9.18;
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], 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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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 [6]
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 [7]
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).
CC -!- FUNCTION: Essential tubulin-folding protein involved in the tubulin
CC folding pathway. Not essential for cell viability. Probably involved in
CC the binding of alpha-tubulin in the multimeric supercomplex.
CC {ECO:0000269|PubMed:10099932, ECO:0000269|PubMed:11959844}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethality. Embryo development limited to
CC the formation of a few giant cells lacking microtubules but not actin
CC filaments. Failure to localize KNOLLE in mitotic cells.
CC {ECO:0000269|PubMed:11959844}.
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 TBCE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG51824.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF486853; AAM22962.1; -; mRNA.
DR EMBL; AC016163; AAG51824.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35201.1; -; Genomic_DNA.
DR EMBL; AK118835; BAC43424.1; -; mRNA.
DR EMBL; BT002403; AAO00763.1; -; mRNA.
DR EMBL; BT008888; AAP68327.1; -; mRNA.
DR EMBL; AY085930; AAM63142.1; -; mRNA.
DR RefSeq; NP_565017.1; NM_105813.4.
DR AlphaFoldDB; Q8GRL7; -.
DR SMR; Q8GRL7; -.
DR STRING; 3702.AT1G71440.1; -.
DR PaxDb; Q8GRL7; -.
DR PRIDE; Q8GRL7; -.
DR ProteomicsDB; 234160; -.
DR DNASU; 843485; -.
DR EnsemblPlants; AT1G71440.1; AT1G71440.1; AT1G71440.
DR GeneID; 843485; -.
DR Gramene; AT1G71440.1; AT1G71440.1; AT1G71440.
DR KEGG; ath:AT1G71440; -.
DR Araport; AT1G71440; -.
DR TAIR; locus:2825339; AT1G71440.
DR eggNOG; KOG2982; Eukaryota.
DR HOGENOM; CLU_017716_5_0_1; -.
DR InParanoid; Q8GRL7; -.
DR OMA; KKYALDW; -.
DR OrthoDB; 249920at2759; -.
DR PhylomeDB; Q8GRL7; -.
DR PRO; PR:Q8GRL7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GRL7; baseline and differential.
DR Genevisible; Q8GRL7; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043014; F:alpha-tubulin binding; IBA:GO_Central.
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:0007023; P:post-chaperonin tubulin folding pathway; IBA:GO_Central.
DR GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR CDD; cd17044; Ubl_TBCE; 1.
DR Gene3D; 2.30.30.190; -; 1.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR044994; TBCE.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR044079; Ubl_TBCE.
DR PANTHER; PTHR15140; PTHR15140; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
DR PROSITE; PS51450; LRR; 6.
PE 2: Evidence at transcript level;
KW Chaperone; Cytoplasm; Leucine-rich repeat; Reference proteome; Repeat.
FT CHAIN 1..531
FT /note="Tubulin-folding cofactor E"
FT /id="PRO_0000423501"
FT DOMAIN 32..76
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REPEAT 84..109
FT /note="LRR 1"
FT REPEAT 159..183
FT /note="LRR 2"
FT REPEAT 185..213
FT /note="LRR 3"
FT REPEAT 233..256
FT /note="LRR 4"
FT REPEAT 260..284
FT /note="LRR 5"
FT REPEAT 285..308
FT /note="LRR 6"
FT REPEAT 318..342
FT /note="LRR 7"
FT REPEAT 344..366
FT /note="LRR 8"
FT REPEAT 474..497
FT /note="LRR 9"
FT CONFLICT 207
FT /note="Q -> E (in Ref. 1; AAM22962 and 6; AAM63142)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="V -> L (in Ref. 1; AAM22962 and 6; AAM63142)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 531 AA; 58242 MW; DFED24FF5946B9CF CRC64;
MKAESSNESF IIGQRVHSLN DSRRVGTVKY VGDVEGYSGT WIGVDWDQDG DGKHNGSVNG
VFYFNGRSQS SASFVRSQNL SRGITLLQAL ELRYRTISTK DEEDEMYVLS AGNRRVSIQL
LGGDKIQDKL SRFEELTSAS LSYLGVSSLG VSSDLGSILP NLKLLDLTGN LISDWEEIGA
LCEQLPALTT LNLSCNSLSS DIKSLPQLKN IRVLVLNNSG LSWTQVEILR RSLPGIEELH
LMGNMISTIT STSSSDDQAF NSLRLLNLDD NCISDWSEVL KLSQLPCLEQ LYLNKNKLSR
IFQSVNGTES SEKGSDPFPS LSCLLLGANN IGDLASVDAL NGFPQLVDIR LSENPISDPV
RGGVPRFVLV ARLTKVQVLN GSEVRAREKK DSEIRYVRMV MSKLNDKSGE IELLHPRFYE
LKKLHGIEDE RASAENSGPK NIASGLISIT LKCVGPSMGE KPHLTKKLPG SITVGKLKIL
SENFFKLKSI KPRLFLQEEG SPFPTALDDE TATLLDVGIC DGSTLLVDEE S
