TIO_ARATH
ID TIO_ARATH Reviewed; 1322 AA.
AC Q2QAV0; Q2QB51; Q9SX42;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Serine/threonine-protein kinase TIO;
DE EC=2.7.11.1;
DE AltName: Full=Fused homolog;
DE Short=AtFUSED;
DE AltName: Full=Protein TWO-IN-ONE;
DE Short=AtTIO;
GN Name=TIO; Synonyms=FU; OrderedLocusNames=At1g50240; ORFNames=F14I3.15;
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 [GENOMIC DNA / MRNA], FUNCTION, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=16332535; DOI=10.1016/j.cub.2005.10.044;
RA Oh S.A., Johnson A., Smertenko A., Rahman D., Park S.K., Hussey P.J.,
RA Twell D.;
RT "A divergent cellular role for the FUSED kinase family in the plant-
RT specific cytokinetic phragmoplast.";
RL Curr. Biol. 15:2107-2111(2005).
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 FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, INTERACTION WITH KIN12A AND KIN12B,
RP AND MUTAGENESIS OF LYS-35; ASP-127 AND ASN-132.
RX PubMed=22709276; DOI=10.1111/j.1365-313x.2012.05077.x;
RA Oh S.A., Allen T., Kim G.J., Sidorova A., Borg M., Park S.K., Twell D.;
RT "Arabidopsis Fused kinase and the Kinesin-12 subfamily constitute a
RT signalling module required for phragmoplast expansion.";
RL Plant J. 72:308-319(2012).
RN [5]
RP INTERACTION WITH KIN7B/NACK2.
RX PubMed=24146312; DOI=10.1007/s00497-013-0235-6;
RA Oh S.A., Bourdon V., Dickinson H.G., Twell D., Park S.K.;
RT "Arabidopsis Fused kinase TWO-IN-ONE dominantly inhibits male meiotic
RT cytokinesis.";
RL Plant Reprod. 27:7-17(2014).
CC -!- FUNCTION: Plays a role in conventional modes of cytokinesis in
CC meristems and during male gametogenesis but also acts in
CC nonconventional modes of cytokinesis (cellularization) during female
CC gametogenesis. Constitutes a signaling module in association with
CC Kinesin-12 members that is required to support phragmoplast expansion
CC and cell-plate growth in plant cells. {ECO:0000269|PubMed:16332535,
CC ECO:0000269|PubMed:22709276}.
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 -!- SUBUNIT: Interacts with Kinesin-12 members KIN12A/PAKRP1 and
CC KIN12B/PAKRP1L (PubMed:22709276). Interacts with KIN7B/NACK2
CC (PubMed:24146312). {ECO:0000269|PubMed:22709276,
CC ECO:0000269|PubMed:24146312}.
CC -!- INTERACTION:
CC Q2QAV0; Q9LDN0: KIN12A; NbExp=3; IntAct=EBI-6280536, EBI-6280428;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:16332535}. Note=Localized to the midline of the
CC nascent phragmoplast and remains associated with the expanding
CC phragmoplast ring.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16332535}.
CC -!- DOMAIN: The ARM-repeat containing C-terminal region is required for the
CC binding to the Kinesin-12 members. {ECO:0000269|PubMed:22709276}.
CC -!- DISRUPTION PHENOTYPE: Cytokinesis-defective leading to aberrant pollen
CC and embryo sacs. {ECO:0000269|PubMed:16332535,
CC ECO:0000269|PubMed:22709276}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD50043.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ149983; AAZ66047.1; -; mRNA.
DR EMBL; DQ153170; AAZ66048.1; -; Genomic_DNA.
DR EMBL; AC007980; AAD50043.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32527.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58830.1; -; Genomic_DNA.
DR PIR; F96538; F96538.
DR RefSeq; NP_001319189.1; NM_001333427.1.
DR RefSeq; NP_001321239.1; NM_001333428.1.
DR AlphaFoldDB; Q2QAV0; -.
DR SMR; Q2QAV0; -.
DR BioGRID; 26671; 3.
DR IntAct; Q2QAV0; 2.
DR STRING; 3702.AT1G50240.2; -.
DR iPTMnet; Q2QAV0; -.
DR PaxDb; Q2QAV0; -.
DR PRIDE; Q2QAV0; -.
DR ProteomicsDB; 234317; -.
DR EnsemblPlants; AT1G50240.2; AT1G50240.2; AT1G50240.
DR EnsemblPlants; AT1G50240.3; AT1G50240.3; AT1G50240.
DR GeneID; 841446; -.
DR Gramene; AT1G50240.2; AT1G50240.2; AT1G50240.
DR Gramene; AT1G50240.3; AT1G50240.3; AT1G50240.
DR KEGG; ath:AT1G50240; -.
DR Araport; AT1G50240; -.
DR TAIR; locus:2011927; AT1G50240.
DR eggNOG; KOG0597; Eukaryota.
DR HOGENOM; CLU_002453_1_1_1; -.
DR InParanoid; Q2QAV0; -.
DR OMA; FYEPIDK; -.
DR OrthoDB; 979202at2759; -.
DR PhylomeDB; Q2QAV0; -.
DR PRO; PR:Q2QAV0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q2QAV0; baseline and differential.
DR Genevisible; Q2QAV0; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0009524; C:phragmoplast; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019894; F:kinesin binding; IPI:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:UniProtKB.
DR GO; GO:0009558; P:embryo sac cellularization; IMP:TAIR.
DR GO; GO:0007112; P:male meiosis cytokinesis; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR045193; Fused-like.
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 PANTHER; PTHR22983; PTHR22983; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00185; ARM; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
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; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1322
FT /note="Serine/threonine-protein kinase TIO"
FT /id="PRO_0000419694"
FT DOMAIN 6..256
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 1056..1098
FT /note="ARM 1"
FT REPEAT 1101..1140
FT /note="ARM 2"
FT REPEAT 1143..1182
FT /note="ARM 3"
FT REPEAT 1183..1223
FT /note="ARM 4"
FT REPEAT 1226..1273
FT /note="ARM 5"
FT REPEAT 1281..1320
FT /note="ARM 6"
FT REGION 1000..1322
FT /note="Required for the binding to Kinesin-12 members"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 12..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 35
FT /note="K->A: Alters binding to Kinesin-12 members."
FT /evidence="ECO:0000269|PubMed:22709276"
FT MUTAGEN 127
FT /note="D->A: Alters binding to Kinesin-12 members; when
FT associated with A-132."
FT /evidence="ECO:0000269|PubMed:22709276"
FT MUTAGEN 132
FT /note="N->A: Alters binding to Kinesin-12 members; when
FT associated with A-127."
FT /evidence="ECO:0000269|PubMed:22709276"
FT CONFLICT 230
FT /note="E -> K (in Ref. 1; AAZ66047)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1322 AA; 145414 MW; EBAB948B8406BCCC CRC64;
MGVEDYHVIE LVGEGSFGRV YKGRRKYTGQ TVAMKFIMKQ GKTDKDIHSL RQEIEILRKL
KHENIIEMLD SFENAREFCV VTEFAQGELF EILEDDKCLP EEQVQAIAKQ LVKALDYLHS
NRIIHRDMKP QNILIGAGSV VKLCDFGFAR AMSTNTVVLR SIKGTPLYMA PELVKEQPYD
RTVDLWSLGV ILYELYVGQP PFYTNSVYAL IRHIVKDPVK YPDEMSTYFE SFLKGLLNKE
PHSRLTWPAL REHPFVKETQ EEVEAREIHT AVVDNKAAWM LKGNGGQQRN EKCDSVTLVE
DMSATKGLAD VQSDMKSAVK VNSPPTEDFV GFPTQEEIKS SGNPTLDKLE NTSRTVKGAQ
VIGENDKALD LVLLSLERFS KSPDSKRDKD VACSVQSLRI ISNLVATRAI VSVGLIEKIT
CALLDFTDAL VGMKSPEFNN IIPKSLSVTK NLVGHVEGNN IHSSYIRHWT KVVEIFIQVV
RWEEEGTGRI IYEACSCITT MLSRVAQDLK SSTPDSVSKQ ILEHANMSRI VDHLCLCLAS
SGSSLTSGSS QMLAAACEAC RAIWILIDTS ETFFKNDDVN ILPLDALQNR LSQHDIGNSE
WGPLSEKLVD TVTRAYLRSK HVQVAVGHCL HQRVEAPLVS AIQLLSRCCL HNGILPSMLC
GLPSSLPITT VVSGGEDGTV ISEIFSILSY ATLSSKDQQT GEKDNFEGRL NNLVFHSCLM
LATVAQCLKL TGRNSVLLML TTSPKKHQHR LSAIANHIAS DDKIEASLQN HSASAMLALA
SILALEKGSS AGSSVSELVV SLIPRATKLC YHLRPMPSNE GEVISHSANY AKWHGLLDGC
IGLLESRLKW GGPLAVQQLI ASGTPLLLIN LLAGKLSNAS PEDIKKTSNR IGLSPIGVVW
TISSICHCLS GGTTFRQVLV KIETMKLITC LLSDAHIKLV KSWGGPGGGK DGVRETINVI
IDLLAFPFVA LQSQPGSLSA TASVNSGFIL NIGSPGVRVC MEDRDLLKAI EEDMDKYIIV
LLEVGVPSLI LRCLDHLELK DLVRPVAFLA KMVGRPRLAV DLVSKGLLDP NRMKKLLNQS
SPREVILDIL MIISDLSRMD KAFYKYIGEA SVLQPLKEYL THVDPNIRAK ACSALGNMCR
HNGYFYSALA EHQIIGLLID RCADPDKRTQ KFACFAIGNA AYHNDTLYEE LRRSITQLAN
VLTTAEEDKT KANAAGALSN LVRNSNKLCE DIVSKGALQT LLRLVADCST LALNPSKKET
ASESPLKIAL FSLAKMCSNH QICRQFVKSS ELFPVIARLK QSPEANIAHY ASVIVAKVSG
ES
