KTI12_ARATH
ID KTI12_ARATH Reviewed; 302 AA.
AC Q9LMH0; Q8H2D4;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Protein KTI12 homolog {ECO:0000303|PubMed:20836892};
DE Short=AtKTI12 {ECO:0000303|PubMed:20836892};
DE AltName: Full=At1g13870;
DE AltName: Full=Protein DEFORMED ROOTS AND LEAVES 1 {ECO:0000303|PubMed:8392411};
DE Short=AtDRL1 {ECO:0000303|PubMed:8392411};
DE AltName: Full=Protein ELONGATA4 {ECO:0000303|PubMed:10353913};
GN Name=KTI12 {ECO:0000303|PubMed:20836892};
GN Synonyms=DRL1 {ECO:0000303|PubMed:8392411},
GN ELO4 {ECO:0000303|PubMed:10353913};
GN OrderedLocusNames=At1g13870 {ECO:0000312|Araport:AT1G13870};
GN ORFNames=F16A14.8 {ECO:0000312|EMBL:AAF79415.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP INTERACTION WITH CALMODULIN, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12615938; DOI=10.1105/tpc.007062;
RA Nelissen H., Clarke J.H., De Block M., De Block S., Vanderhaeghen R.,
RA Zielinski R.E., Dyer T., Lust S., Inze D., Van Lijsebettens M.;
RT "DRL1, a homolog of the yeast TOT4/KTI12 protein, has a function in
RT meristem activity and organ growth in plants.";
RL Plant Cell 15:639-654(2003).
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=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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8392411; DOI=10.2307/3869806;
RA Bancroft I., Jones J.D.G., Dean C.;
RT "Heterologous transposon tagging of the DRL1 locus in Arabidopsis.";
RL Plant Cell 5:631-638(1993).
RN [6]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=10353913; DOI=10.1093/genetics/152.2.729;
RA Berna G., Robles P., Micol J.L.;
RT "A mutational analysis of leaf morphogenesis in Arabidopsis thaliana.";
RL Genetics 152:729-742(1999).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11589569; DOI=10.1007/s004380100535;
RA Robles P., Micol J.L.;
RT "Genome-wide linkage analysis of Arabidopsis genes required for leaf
RT development.";
RL Mol. Genet. Genomics 266:12-19(2001).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=15894610; DOI=10.1073/pnas.0502600102;
RA Nelissen H., Fleury D., Bruno L., Robles P., de Veylder L., Traas J.,
RA Micol J., Van Montagu M., Inze D., Van Lijsebettens M.;
RT "The elongata mutants identify a functional Elongator complex in plants
RT with a role in cell proliferation during organ growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7754-7759(2005).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20836892; DOI=10.1186/1471-2229-10-201;
RA Chen P., Jaeger G., Zheng B.;
RT "Transfer RNA modifications and genes for modifying enzymes in Arabidopsis
RT thaliana.";
RL BMC Plant Biol. 10:201-201(2010).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25518926; DOI=10.14348/molcells.2015.2297;
RA Jun S.E., Cho K.-H., Hwang J.-Y., Abdel-Fattah W., Hammermeister A.,
RA Schaffrath R., Bowman J.L., Kim G.-T.;
RT "Comparative analysis of the conserved functions of Arabidopsis DRL1 and
RT yeast KTI12.";
RL Mol. Cells 38:243-250(2015).
CC -!- FUNCTION: Elongator complex-associated factor that is not a structural
CC subunit but rather transiently contacts the complex (PubMed:25518926).
CC Regulates both meristem activity and organ growth; acts as a positive
CC regulator of adaxial leaf patterning by modulating both cell division
CC and differentiation (PubMed:12615938, PubMed:8392411, PubMed:11589569,
CC PubMed:15894610, PubMed:25518926). Required for an early step in
CC synthesis of 5-carbamoylmethyl (ncm5) groups present on uridines
CC (ncm5U) at the wobble position in tRNA (PubMed:20836892).
CC {ECO:0000250|UniProtKB:P34253, ECO:0000269|PubMed:11589569,
CC ECO:0000269|PubMed:12615938, ECO:0000269|PubMed:15894610,
CC ECO:0000269|PubMed:20836892, ECO:0000269|PubMed:25518926,
CC ECO:0000269|PubMed:8392411}.
CC -!- SUBUNIT: Interacts with the elongator complex (By similarity). Binds to
CC calmodulin in a calcium-dependent manner (PubMed:12615938).
CC {ECO:0000250|UniProtKB:P34253, ECO:0000269|PubMed:12615938}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P34253}. Nucleus
CC {ECO:0000250|UniProtKB:P34253}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, hypocotyls, cotyledons, shoot
CC apices, stems, inflorescence apices, leaves and flowers.
CC {ECO:0000269|PubMed:12615938}.
CC -!- DEVELOPMENTAL STAGE: Detected in globular-, heart-, and torpedo-stage
CC embryos, in the outer integuments of ovules and in the funiculi. Also
CC expressed in the peripheral zone of the shoot apical meristem (SAM)
CC corresponding to the central zone. In elongating tissues, restricted at
CC the periphery of the vascular bundle. In shoot and inflorescence
CC apices, mostly present in the L2 layer, and, at lower levels, in the L1
CC layer, but absent of the L3 layer. In young leaf primordia, localized
CC in the basal part of the dorsal side. In older leaf primordia, detected
CC in vascular bundles and in the mesophyll between the vascular bundles.
CC In expanding leaves, confined to stomatal guard cells, and individual
CC palisade and spongy mesophyll parenchyma cells. In general, present
CC around the vascular bundles. Expressed in young flower organs but not
CC in mature sepals and petals. Gradient accumulation in the stamens and
CC carpels, with the highest activity at the tip of the organs. Present in
CC the meristematic and elongation zones of the primary root and in the
CC vascular bundle of the differentiation zone.
CC {ECO:0000269|PubMed:12615938}.
CC -!- DISRUPTION PHENOTYPE: Defective organ formation due to disorganized
CC shoot, inflorescence, flower, and root meristems leading to stunted
CC roots, few root hairs, lanceolate leaves, and a highly enlarged,
CC disorganized shoot apex that does not produce an inflorescence
CC (PubMed:12615938, PubMed:8392411, PubMed:10353913, PubMed:11589569,
CC PubMed:15894610, PubMed:25518926). Altered cell division and cell
CC differentiation in leaves (PubMed:25518926). No detectable 5-
CC carbamoylmethyluridine (ncm5U) modified nucleosides (PubMed:20836892).
CC {ECO:0000269|PubMed:10353913, ECO:0000269|PubMed:11589569,
CC ECO:0000269|PubMed:12615938, ECO:0000269|PubMed:15894610,
CC ECO:0000269|PubMed:20836892, ECO:0000269|PubMed:25518926,
CC ECO:0000269|PubMed:8392411}.
CC -!- SIMILARITY: Belongs to the KTI12 family. {ECO:0000305}.
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DR EMBL; AJ428870; CAD21832.1; -; Genomic_DNA.
DR EMBL; AC068197; AAF79415.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29078.1; -; Genomic_DNA.
DR EMBL; BT004091; AAO42118.1; -; mRNA.
DR EMBL; BT005095; AAO50628.1; -; mRNA.
DR PIR; H86271; H86271.
DR RefSeq; NP_172840.1; NM_101253.3.
DR AlphaFoldDB; Q9LMH0; -.
DR SMR; Q9LMH0; -.
DR STRING; 3702.AT1G13870.1; -.
DR PaxDb; Q9LMH0; -.
DR PRIDE; Q9LMH0; -.
DR ProteomicsDB; 237117; -.
DR EnsemblPlants; AT1G13870.1; AT1G13870.1; AT1G13870.
DR GeneID; 837946; -.
DR Gramene; AT1G13870.1; AT1G13870.1; AT1G13870.
DR KEGG; ath:AT1G13870; -.
DR Araport; AT1G13870; -.
DR TAIR; locus:2014804; AT1G13870.
DR eggNOG; KOG3062; Eukaryota.
DR HOGENOM; CLU_027147_1_0_1; -.
DR InParanoid; Q9LMH0; -.
DR OMA; LYCEAKA; -.
DR OrthoDB; 1300128at2759; -.
DR PhylomeDB; Q9LMH0; -.
DR PRO; PR:Q9LMH0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMH0; baseline and differential.
DR Genevisible; Q9LMH0; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033588; C:elongator holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
DR GO; GO:0080178; P:5-carbamoylmethyl uridine residue modification; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0009933; P:meristem structural organization; IMP:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0010449; P:root meristem growth; IMP:CACAO.
DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045106; Kti12.
DR InterPro; IPR013641; KTI12/PSTK.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR12435; PTHR12435; 1.
DR Pfam; PF08433; KTI12; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; tRNA processing.
FT CHAIN 1..302
FT /note="Protein KTI12 homolog"
FT /id="PRO_0000432190"
FT REGION 260..273
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT CONFLICT 232
FT /note="A -> G (in Ref. 1; CAD21832)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 34064 MW; 825FF5E7EA3DCC65 CRC64;
MALVVICGQP CSGKSIAAVT LAETLKESET KQSVRIIDEA SFHLDRNQNY ANMPAEKNLR
GKLRSDVDRS VSTGEIVIVD SLNSIKGYRY ELWCIARAAG IRYCVVYCDV DEAHCRQWNK
ERSDRGEDGY DDGIFEDLVR RFEKPERRNR WDSPLFELYP SREVIDKSSP VILEAVTYLT
KTVDSKTQDV RILQPSIATQ AARFSEANSL YELDRATQEI INAIVEQQSL GAAISRVTLG
NELPPIEICR PIGLPELRRL RRTFVKLMGQ SSLSGPPLPT DADSAKRRFV DYLNREFGGN
NA
