TCTP1_ARATH
ID TCTP1_ARATH Reviewed; 168 AA.
AC P31265; Q8L973; Q9LUS0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=Translationally-controlled tumor protein 1 {ECO:0000303|Ref.1};
DE Short=TCTP1 {ECO:0000303|Ref.1};
GN Name=TCTP1 {ECO:0000303|Ref.1}; Synonyms=TXTP;
GN OrderedLocusNames=At3g16640 {ECO:0000312|Araport:AT3G16640};
GN ORFNames=MGL6.10 {ECO:0000312|EMBL:BAB02755.1};
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].
RA Kang J.-G., Park C.-M.;
RT "Isolation of cDNA clone encoding a putative translationally controlled
RT tumor protein homolog in Arabidopsis thaliana.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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=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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-53.
RC STRAIN=cv. C24; TISSUE=Flower bud;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=16902407; DOI=10.1038/sj.emboj.7601270;
RA Szecsi J., Joly C., Bordji K., Varaud E., Cock J.M., Dumas C.,
RA Bendahmane M.;
RT "BIGPETALp, a bHLH transcription factor is involved in the control of
RT Arabidopsis petal size.";
RL EMBO J. 25:3912-3920(2006).
RN [8]
RP FUNCTION, 3D-STRUCTURE MODELING, TISSUE SPECIFICITY, INDUCTION BY LIGHT,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19060111; DOI=10.1105/tpc.108.061010;
RA Berkowitz O., Jost R., Pollmann S., Masle J.;
RT "Characterization of TCTP, the translationally controlled tumor protein,
RT from Arabidopsis thaliana.";
RL Plant Cell 20:3430-3447(2008).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, MUTAGENESIS OF GLU-12, AND
RP INTERACTION WITH RABA4A; RABA4B; RABF1 AND RABF2B.
RX PubMed=20736351; DOI=10.1073/pnas.1007926107;
RA Brioudes F., Thierry A.M., Chambrier P., Mollereau B., Bendahmane M.;
RT "Translationally controlled tumor protein is a conserved mitotic growth
RT integrator in animals and plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:16384-16389(2010).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY ABSCISIC ACID, AND INTERACTION
RP WITH MICROTUBULES.
RX PubMed=22610367; DOI=10.1007/s10059-012-0080-8;
RA Kim Y.M., Han Y.J., Hwang O.J., Lee S.S., Shin A.Y., Kim S.Y., Kim J.I.;
RT "Overexpression of Arabidopsis translationally controlled tumor protein
RT gene AtTCTP enhances drought tolerance with rapid ABA-induced stomatal
RT closure.";
RL Mol. Cells 33:617-626(2012).
RN [11]
RP FUNCTION, CALCIUM-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=24040826; DOI=10.1186/1471-2229-13-135;
RA Hoepflinger M.C., Reitsamer J., Geretschlaeger A.M., Mehlmer N.,
RA Tenhaken R.;
RT "The effect of translationally controlled tumour protein (TCTP) on
RT programmed cell death in plants.";
RL BMC Plant Biol. 13:135-135(2013).
RN [12]
RP GENE FAMILY, AND 3D-STRUCTURE MODELING.
RX PubMed=25120549; DOI=10.3389/fpls.2014.00361;
RA Gutierrez-Galeano D.F., Toscano-Morales R., Calderon-Perez B.,
RA Xoconostle-Cazares B., Ruiz-Medrano R.;
RT "Structural divergence of plant TCTPs.";
RL Front. Plant Sci. 5:361-361(2014).
RN [13]
RP MUTAGENESIS OF 35-TRP--ALA-47, AND 3D-STRUCTURE MODELING.
RC STRAIN=cv. Columbia;
RX PubMed=26191065; DOI=10.3389/fpls.2015.00468;
RA Toscano-Morales R., Xoconostle-Cazares B., Cabrera-Ponce J.L.,
RA Hinojosa-Moya J., Ruiz-Salas J.L., Galvan-Gordillo S.V.,
RA Guevara-Gonzalez R.G., Ruiz-Medrano R.;
RT "AtTCTP2, an Arabidopsis thaliana homolog of Translationally Controlled
RT Tumor Protein, enhances in vitro plant regeneration.";
RL Front. Plant Sci. 6:468-468(2015).
RN [14]
RP INDUCTION BY MOMILACTONE B.
RX PubMed=26058145;
RA Kato-Noguchi H., Kitajima S.;
RT "Momilactone sensitive proteins in Arabidopsis thaliana.";
RL Nat. Prod. Commun. 10:729-732(2015).
CC -!- FUNCTION: General regulator required for the development of the entire
CC plant. Regulates the duration of cell cycle (PubMed:20736351). Probable
CC activator of Rab GTPases and upstream regulator of the cell growth-
CC regulating TOR (target of rapamycin) network (PubMed:19060111,
CC PubMed:20736351). Might also control spatial growth in pollen tubes or
CC root hairs via the TORC2 signaling branch (PubMed:19060111). Involved
CC in the regulation of abscisic acid- and calcium-mediated stomatal
CC closure, but not in light or H(+)-pumping induced stomatal opening. May
CC regulate microtubules depolymerization (PubMed:22610367). Binds calcium
CC and has a cytoprotective function (PubMed:24040826).
CC {ECO:0000269|PubMed:19060111, ECO:0000269|PubMed:20736351,
CC ECO:0000269|PubMed:22610367, ECO:0000269|PubMed:24040826}.
CC -!- SUBUNIT: Homodimer. Interacts with the Rab GTPases RABA4A, RABA4B,
CC RABF1 and RABF2B (PubMed:20736351). Interacts with microtubules and
CC heterodimers of alpha- and beta-tubulins. Cytosolic calcium positively
CC regulates this interaction (PubMed:22610367).
CC {ECO:0000269|PubMed:20736351, ECO:0000269|PubMed:22610367}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24040826}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers, leaves and stems
CC (PubMed:16902407, PubMed:19060111). Expressed in roots and siliques.
CC Detected in seeds. Highest expression in actively dividing and
CC differentiating cell types, such as the meristematic and division zones
CC of the root, the embryo or the elongating tube of germinating pollen
CC (PubMed:19060111). Expressed in cotyledons, leaves, hypocotyls and
CC roots. Detected in mitotically active tissues such as shoot apical
CC meristems, root tips, lateral root initiation regions and anthers, and
CC in guard cells (PubMed:22610367). {ECO:0000269|PubMed:16902407,
CC ECO:0000269|PubMed:19060111, ECO:0000269|PubMed:22610367}.
CC -!- INDUCTION: Up-regulated by momilactone B (PubMed:26058145). Not
CC regulated by light (PubMed:19060111). Up-regulated by abscisic acid
CC (PubMed:22610367). {ECO:0000269|PubMed:19060111,
CC ECO:0000269|PubMed:22610367, ECO:0000269|PubMed:26058145}.
CC -!- DISRUPTION PHENOTYPE: Male gametophytic phenotype with normal pollen
CC formation and germination but impaired pollen tube growth
CC (PubMed:19060111). Embryonic lethality when homozygous due to a
CC retarded development of the embryos that eventually collapse at the
CC silique dehiscence stage (PubMed:20736351).
CC {ECO:0000269|PubMed:19060111, ECO:0000269|PubMed:20736351}.
CC -!- MISCELLANEOUS: Knockdown mutants have retarded growth due to decreased
CC cell size. {ECO:0000269|PubMed:19060111}.
CC -!- SIMILARITY: Belongs to the TCTP family. {ECO:0000255|PROSITE-
CC ProRule:PRU01133}.
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DR EMBL; AF215897; AAG44002.1; -; mRNA.
DR EMBL; AB022217; BAB02755.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75847.1; -; Genomic_DNA.
DR EMBL; AF361815; AAK32828.1; -; mRNA.
DR EMBL; AY045802; AAK76476.1; -; mRNA.
DR EMBL; AY056065; AAL06965.1; -; mRNA.
DR EMBL; AY072337; AAL61944.1; -; mRNA.
DR EMBL; AY079333; AAL85064.1; -; mRNA.
DR EMBL; AY114601; AAM47920.1; -; mRNA.
DR EMBL; AY088605; AAM66134.1; -; mRNA.
DR EMBL; Z18387; CAA79177.1; -; mRNA.
DR RefSeq; NP_188286.1; NM_112537.4.
DR AlphaFoldDB; P31265; -.
DR SMR; P31265; -.
DR BioGRID; 6250; 4.
DR IntAct; P31265; 4.
DR STRING; 3702.AT3G16640.1; -.
DR iPTMnet; P31265; -.
DR PaxDb; P31265; -.
DR PRIDE; P31265; -.
DR ProteomicsDB; 234209; -.
DR EnsemblPlants; AT3G16640.1; AT3G16640.1; AT3G16640.
DR GeneID; 820916; -.
DR Gramene; AT3G16640.1; AT3G16640.1; AT3G16640.
DR KEGG; ath:AT3G16640; -.
DR Araport; AT3G16640; -.
DR TAIR; locus:2089378; AT3G16640.
DR eggNOG; KOG1727; Eukaryota.
DR HOGENOM; CLU_095877_1_1_1; -.
DR InParanoid; P31265; -.
DR OMA; TPYMISF; -.
DR OrthoDB; 1439384at2759; -.
DR PhylomeDB; P31265; -.
DR PRO; PR:P31265; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P31265; baseline and differential.
DR Genevisible; P31265; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0010252; P:auxin homeostasis; IMP:TAIR.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0009819; P:drought recovery; IMP:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0048527; P:lateral root development; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:0031117; P:positive regulation of microtubule depolymerization; IMP:TAIR.
DR GO; GO:0009791; P:post-embryonic development; IMP:TAIR.
DR GO; GO:0001558; P:regulation of cell growth; IMP:TAIR.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:TAIR.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:TAIR.
DR GO; GO:0090333; P:regulation of stomatal closure; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
DR GO; GO:0048768; P:root hair cell tip growth; IMP:TAIR.
DR Gene3D; 2.170.150.10; -; 1.
DR InterPro; IPR011057; Mss4-like_sf.
DR InterPro; IPR011323; Mss4/transl-control_tumour.
DR InterPro; IPR034737; TCTP.
DR InterPro; IPR018103; Translation_control_tumour_CS.
DR InterPro; IPR018105; Translational_control_tumour_p.
DR PANTHER; PTHR11991; PTHR11991; 1.
DR Pfam; PF00838; TCTP; 1.
DR PRINTS; PR01653; TCTPROTEIN.
DR SUPFAM; SSF51316; SSF51316; 1.
DR PROSITE; PS01002; TCTP_1; 1.
DR PROSITE; PS01003; TCTP_2; 1.
DR PROSITE; PS51797; TCTP_3; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Reference proteome.
FT CHAIN 1..168
FT /note="Translationally-controlled tumor protein 1"
FT /id="PRO_0000211297"
FT DOMAIN 1..168
FT /note="TCTP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01133"
FT MUTAGEN 12
FT /note="E->V: Loss of function."
FT /evidence="ECO:0000269|PubMed:20736351"
FT MUTAGEN 35..47
FT /note="Missing: Gain of regeneration capacity."
FT /evidence="ECO:0000269|PubMed:26191065"
FT CONFLICT 64
FT /note="T -> A (in Ref. 5; AAM66134)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 168 AA; 18910 MW; 3A86AB8DFEBBE166 CRC64;
MLVYQDLLTG DELLSDSFPY KEIENGILWE VEGKWVTVGA VDVNIGANPS AEEGGEDEGV
DDSTQKVVDI VDTFRLQEQP TYDKKGFIAY IKKYIKLLTP KLSEEDQAVF KKGIEGATKF
LLPRLSDFQF FVGEGMHDDS TLVFAYYKEG STNPTFLYFA HGLKEVKC
