TSL_ARATH
ID TSL_ARATH Reviewed; 688 AA.
AC Q39238; Q8LPL1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Serine/threonine-protein kinase TOUSLED;
DE EC=2.7.11.1;
GN Name=TOUSLED; Synonyms=TSL; OrderedLocusNames=At5g20930;
GN ORFNames=F22D1.100;
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], MUTAGENESIS OF VAL-355, FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Wassilewskija; TISSUE=Flower;
RX PubMed=8252629; DOI=10.1016/0092-8674(93)90537-z;
RA Roe J.L., Rivin C.J., Sessions R.A.L., Feldmann K.A., Zambryski P.C.;
RT "The TOUSLED gene in Arabidopsis thaliana encodes a protein kinase
RT homologue that is required for leaf and flower development.";
RL Cell 75:939-950(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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] OF 218-688.
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 CHARACTERIZATION, MUTAGENESIS OF LYS-438, SUBUNIT, PHOSPHORYLATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9038200; DOI=10.1074/jbc.272.9.5838;
RA Roe J.L., Durfee T., Zupan J.R., Repetti P.P., McLean B.G., Zambryski P.C.;
RT "TOUSLED is a nuclear serine/threonine protein kinase that requires a
RT coiled-coil region for oligomerization and catalytic activity.";
RL J. Biol. Chem. 272:5838-5845(1997).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND INTERACTION WITH TKI1 AND ASF1B/SGA1.
RX PubMed=15047893; DOI=10.1104/pp.103.038117;
RA Ehsan H., Reichheld J.-P., Durfee T., Roe J.L.;
RT "TOUSLED kinase activity oscillates during the cell cycle and interacts
RT with chromatin regulators.";
RL Plant Physiol. 134:1488-1499(2004).
CC -!- FUNCTION: Required for correct initiation of floral organ primordia and
CC for proper development of organ primordia. Phosphorylates in vitro
CC ASF1B/SGA1, the C-terminal part of TKI1 and histone H3.
CC {ECO:0000269|PubMed:15047893, ECO:0000269|PubMed:8252629}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- ACTIVITY REGULATION: Oligomerization is required for activity. May be
CC activated by trans-autophosphorylation. Higher activity during G2/M
CC phase and G1 phase compared to S phase.
CC -!- SUBUNIT: Homooligomer. Interacts with TKI1 and ASF1B/SGA1.
CC {ECO:0000269|PubMed:15047893, ECO:0000269|PubMed:9038200}.
CC -!- INTERACTION:
CC Q39238; Q9LS09: ASF1B; NbExp=2; IntAct=EBI-2325484, EBI-2366572;
CC Q39238; Q8LJT8: TKI1; NbExp=4; IntAct=EBI-2325484, EBI-2366507;
CC Q39238; Q39238: TOUSLED; NbExp=2; IntAct=EBI-2325484, EBI-2325484;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9038200}.
CC -!- TISSUE SPECIFICITY: Most abundant in developing floral meristem. Also
CC expressed in maturing flowers, developing seeds, mature leaves and
CC roots. Barely detected in stems. {ECO:0000269|PubMed:8252629}.
CC -!- DEVELOPMENTAL STAGE: Expressed at constant level during the cell cycle.
CC {ECO:0000269|PubMed:15047893}.
CC -!- DOMAIN: The first coiled coil domain is essential for oligomerization.
CC -!- PTM: Autophosphorylation on both phosphoserine and phosphothreonine.
CC {ECO:0000269|PubMed:9038200}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM20455.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L23985; AAA32874.1; -; mRNA.
DR EMBL; AF296834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92907.1; -; Genomic_DNA.
DR EMBL; AY099604; AAM20455.1; ALT_INIT; mRNA.
DR EMBL; BT000260; AAN15579.1; -; mRNA.
DR PIR; A49318; A49318.
DR RefSeq; NP_568405.1; NM_122101.2.
DR AlphaFoldDB; Q39238; -.
DR SMR; Q39238; -.
DR BioGRID; 17492; 3.
DR IntAct; Q39238; 2.
DR STRING; 3702.AT5G20930.1; -.
DR iPTMnet; Q39238; -.
DR PaxDb; Q39238; -.
DR PRIDE; Q39238; -.
DR ProteomicsDB; 234594; -.
DR EnsemblPlants; AT5G20930.1; AT5G20930.1; AT5G20930.
DR GeneID; 832217; -.
DR Gramene; AT5G20930.1; AT5G20930.1; AT5G20930.
DR KEGG; ath:AT5G20930; -.
DR Araport; AT5G20930; -.
DR TAIR; locus:2147087; AT5G20930.
DR eggNOG; KOG1151; Eukaryota.
DR HOGENOM; CLU_000288_85_0_1; -.
DR InParanoid; Q39238; -.
DR OMA; YKHACRE; -.
DR OrthoDB; 693214at2759; -.
DR PhylomeDB; Q39238; -.
DR PRO; PR:Q39238; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39238; baseline and differential.
DR Genevisible; Q39238; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:1900368; P:regulation of post-transcriptional gene silencing by RNA; IMP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..688
FT /note="Serine/threonine-protein kinase TOUSLED"
FT /id="PRO_0000270795"
FT DOMAIN 409..683
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 194..253
FT /evidence="ECO:0000255"
FT COILED 298..332
FT /evidence="ECO:0000255"
FT MOTIF 97..100
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 123..139
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 389..392
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 539
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 415..423
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 355
FT /note="V->D: In tsl-2; loss of activity resulting in an
FT aberrant floral development."
FT /evidence="ECO:0000269|PubMed:8252629"
FT MUTAGEN 438
FT /note="K->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9038200"
SQ SEQUENCE 688 AA; 78149 MW; 2B14F0E677D78C9B CRC64;
MSDDMVLHFS SNSSNQSDHS LPDKIAKLEA RLTGKTPSSA KPPQQQQQQQ QQVSLWSSAS
AAVKVVTSTP PGLSETSISD SDDENTGDFL IRANTKKRQK VQESNNFSVV DHVEPQEAAY
DGRKNDAESK TGLDVSKKKQ GRGRASSTGR GRGSKTNNDV TKSQFVVAPV SAASQLDASD
QKDFRPDGQL RNGECSLQDE DLKSLRAKIA MLEEELRKSR QDSSEYHHLV RNLENEVKDL
KDQEQQGKQK TTKVISDLLI SVSKTERQEA RTKVRNESLR LGSVGVLRTG TIIAETWEDG
QMLKDLNAQL RQLLETKEAI ERQRKLLKKR QNGDKNDGTD TESGAQEEDI IPDEVYKSRL
TSIKREEEAV LRERERYTLE KGLLMREMKR IRDEDGSRFN HFPVLNSRYA LLNLLGKGGF
SEVYKAYDLV DHRYVACKLH GLNAQWSEEK KQSYIRHANR ECEIHKSLVH HHIVRLWDKF
HIDMHTFCTV LEYCSGKDLD AVLKATSNLP EKEARIIIVQ IVQGLVYLNK KSQKIIHYDL
KPGNVLFDEF GVAKVTDFGL SKIVEDNVGS QGMELTSQGA GTYWYLPPEC FELNKTPMIS
SKVDVWSVGV LFYQMLFGKR PFGHDQSQER ILREDTIIKA KKVEFPVTRP AISNEAKDLI
RRCLTYNQED RPDVLTMAQD PYLAYSKK
