RUK_ARATH
ID RUK_ARATH Reviewed; 1366 AA.
AC F4JY37;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Serine/threonine-protein kinase RUNKEL {ECO:0000305};
DE AltName: Full=Protein EMBRYO DEFECTIVE 3013 {ECO:0000305};
DE AltName: Full=Protein RUNKEL {ECO:0000303|PubMed:11089872};
DE EC=2.7.11.1 {ECO:0000305};
GN Name=RUK {ECO:0000303|PubMed:11089872}; Synonyms=EMB3013 {ECO:0000305};
GN OrderedLocusNames=At5g18700 {ECO:0000312|EMBL:AED92600.1};
GN ORFNames=T1A4.80 {ECO:0000305};
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 [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 [2]
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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11089872; DOI=10.1023/a:1006457723760;
RA Nacry P., Mayer U., Jurgens G.;
RT "Genetic dissection of cytokinesis.";
RL Plant Mol. Biol. 43:719-733(2000).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta, and cv. Wassilewskija;
RX PubMed=12421698; DOI=10.1242/dev.00152;
RA Sorensen M.B., Mayer U., Lukowitz W., Robert H., Chambrier P., Juergens G.,
RA Somerville C., Lepiniec L., Berger F.;
RT "Cellularisation in the endosperm of Arabidopsis thaliana is coupled to
RT mitosis and shares multiple components with cytokinesis.";
RL Development 129:5567-5576(2002).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-33 AND ASP-121,
RP INDUCTION, INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=19268593; DOI=10.1016/j.cub.2009.02.021;
RA Krupnova T., Sasabe M., Ghebreghiorghis L., Gruber C.W., Hamada T.,
RA Dehmel V., Strompen G., Stierhof Y.-D., Lukowitz W., Kemmerling B.,
RA Machida Y., Hashimoto T., Mayer U., Juergens G.;
RT "Microtubule-associated kinase-like protein RUNKEL needed for cell plate
RT expansion in Arabidopsis cytokinesis.";
RL Curr. Biol. 19:518-523(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=23451828; DOI=10.1111/tpj.12160;
RA Krupnova T., Stierhof Y.-D., Hiller U., Strompen G., Mueller S.;
RT "The microtubule-associated kinase-like protein RUNKEL functions in somatic
RT and syncytial cytokinesis.";
RL Plant J. 74:781-791(2013).
CC -!- FUNCTION: Essential protein that regulates phragmoplast microtubule
CC organization during cell plate expansion in cytokinesis during cell
CC division, both somatic and syncytial (PubMed:11089872, PubMed:19268593,
CC PubMed:23451828). Required for endosperm cellularisation
CC (PubMed:12421698, PubMed:23451828). In pollen development, involved in
CC cellularisation during microsporogenesis by regulating radial
CC microtubules (MT) organization in microspore mother cells
CC (PubMed:23451828). Seems to not have kinase activity (PubMed:19268593).
CC {ECO:0000269|PubMed:11089872, ECO:0000269|PubMed:12421698,
CC ECO:0000269|PubMed:19268593, ECO:0000269|PubMed:23451828}.
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 Evidence={ECO:0000305};
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; Evidence={ECO:0000305};
CC -!- SUBUNIT: Binds to microtubules (MT). {ECO:0000269|PubMed:19268593}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:19268593}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:19268593}. Note=Colocalizes also with mitotic
CC preprophase band. {ECO:0000269|PubMed:19268593}.
CC -!- TISSUE SPECIFICITY: Expressed in proliferating tissues of seedlings,
CC lateral roots, young rosette leaves, siliques, flowers, embryos and
CC stems (including apical meristem). {ECO:0000269|PubMed:19268593,
CC ECO:0000269|PubMed:23451828}.
CC -!- INDUCTION: Cell-cycle-regulated. {ECO:0000269|PubMed:19268593}.
CC -!- DISRUPTION PHENOTYPE: Seedling lethal (PubMed:19268593). Abnormal cell
CC division with defective cytokinesis due to abnormal phragmoplast
CC organization and arrested cell plate expansion, leading to enlarged
CC cells and nuclei as well as incomplete cell walls (PubMed:11089872,
CC PubMed:19268593). In metaphase and anaphase, enlarged cells with
CC several mitotic spindles or a single greatly enlarged spindle
CC (PubMed:19268593). Impaired endosperm development with altered
CC cellularisation (PubMed:12421698, PubMed:23451828). Cellularization
CC defects caused by disorganized radial microtubules (MT) arrays in
CC seedlings and adult tissues, as well as during male meiocyte
CC development. Irregular and incomplete or absent intersporal cell walls
CC in male tetrads, resulting in abnormal pollen and reduced fertility.
CC Sterile and aborted ovules (PubMed:23451828).
CC {ECO:0000269|PubMed:11089872, ECO:0000269|PubMed:12421698,
CC ECO:0000269|PubMed:19268593, ECO:0000269|PubMed:23451828}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC051627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92600.1; -; Genomic_DNA.
DR RefSeq; NP_197371.2; NM_121875.4.
DR AlphaFoldDB; F4JY37; -.
DR SMR; F4JY37; -.
DR STRING; 3702.AT5G18700.1; -.
DR iPTMnet; F4JY37; -.
DR PaxDb; F4JY37; -.
DR PRIDE; F4JY37; -.
DR ProteomicsDB; 226676; -.
DR EnsemblPlants; AT5G18700.1; AT5G18700.1; AT5G18700.
DR GeneID; 831988; -.
DR Gramene; AT5G18700.1; AT5G18700.1; AT5G18700.
DR KEGG; ath:AT5G18700; -.
DR Araport; AT5G18700; -.
DR TAIR; locus:2180044; AT5G18700.
DR eggNOG; KOG0597; Eukaryota.
DR HOGENOM; CLU_003494_0_0_1; -.
DR InParanoid; F4JY37; -.
DR OMA; NWYETNN; -.
DR OrthoDB; 219167at2759; -.
DR PhylomeDB; F4JY37; -.
DR PRO; PR:F4JY37; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JY37; baseline and differential.
DR Genevisible; F4JY37; AT.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0009524; C:phragmoplast; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009574; C:preprophase band; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007349; P:cellularization; IMP:UniProtKB.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
DR GO; GO:0010342; P:endosperm cellularization; IMP:UniProtKB.
DR GO; GO:0009556; P:microsporogenesis; IMP:UniProtKB.
DR GO; GO:0000914; P:phragmoplast assembly; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010245; P:radial microtubular system formation; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR044591; RUK.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46562; PTHR46562; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Kinase;
KW Microtubule; Nucleotide-binding; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1366
FT /note="Serine/threonine-protein kinase RUNKEL"
FT /id="PRO_0000433640"
FT REPEAT 595..633
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 638..675
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 699..737
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 835..872
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 878..907
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 908..945
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 946..986
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 992..1018
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 1019..1057
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 1072..1111
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 1279..1316
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 1329..1366
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REGION 276..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..413
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 121
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 33
FT /note="K->W: Able to rescue the seedling lethality of
FT disrupted plants, but later retarded development, and
FT cytokinesis defects observed in flowers."
FT /evidence="ECO:0000269|PubMed:19268593"
FT MUTAGEN 121
FT /note="D->A: Able to rescue the seedling lethality of
FT disrupted plants, but later retarded development, and
FT cytokinesis defects observed in flowers."
FT /evidence="ECO:0000269|PubMed:19268593"
SQ SEQUENCE 1366 AA; 152283 MW; 3AF38611B432122F CRC64;
MNQYHIYEAI GHGKCSTVYK GRKKKTIEYF ACKSVDKSRK NKVLQEVRIL HSLNHPNVLK
FYAWYETSAH MWLVLEYCVG GDLRTLLQQD CKLPEESIYG LAYDLVIALQ YLHSKGIIYC
DLKPSNILLD ENGHIKLCDF GLSRKLDDIS KSPSTGKRGT PYYMAPELYE DGGIHSFASD
LWALGCVLYE CYTGRPPFVA REFTQLVKSI HSDPTPPLPG NASRSFVNLI ESLLIKDPAQ
RIQWADLCGH AFWKSKINLV QLPTQPAFDD MIGINTKPCL SERNGDRPNK TPPKYREKDR
KGGSKQNENS IQGSKGHETP IKGTPGGSKA QAKLPSRATE EKHGGRPAAN RQVNILRLSR
IAKANLQKEN EKENYRRPLP NSNENCAEVK IDNTDMELDF DENNDDEGPD ESEGTENTSC
AQEERVMSHN ENHRRQRVVS SNVPDENSSA NETPTLGEAR DCHEDQSEPM DMSAAPPSAS
PQLKTHRGRE TSGVAVNHDS SKAPTSLTDV FWHISDLSVR PVMPSRKSDK EAVHSLSFET
PQPSDFSKKG KQELEPLNNR IITVLSGSSS GLSEKQNLIR YLETLSTNAD AANILTNGPI
MLVLVKVLRL SKTPAFRVQI ASLIGLLIRH STSIEDDLAN SGILDSLTNG LRDKHEKVRR
FSMAALGELL FYISTQNEHK DFKPPESPSK ETRSASGWQV SNALISLVSS VLRKGEDDLT
QVYALRTIEN ICSQGAYWAT RFSSQDLISN LCYIYKATGK QESMRQTAGS CLVRLARFNP
PCIQTVVEKL SLKEIASSFV KGSAREQQVC LNLLNMAMIG SHTFTSFGRH LVTLTEEKNL
FPSLLSIIEQ GTEVLRGKAL LFVAFLCKNS RRWLTNFFCN ARFLPVVDRL AKEKDSYLQQ
CLEAFVNVIA SIIPGMLDTI TNDIQQLMTG RRHGPVSPLN SRAPVKTNAH LFPVVLHLLG
SSSFKNKMVT PQVLRQLANL TKLVEASFQG RDDFRVTLLQ VLECITGDAP LVTQNGEIII
REILPSLAAI YNGNKDGDAR FLCLKIWFDS LTILLTECTE IEQQISEDLK SISNSHFLPL
YPALIQDEDP IPAYAQKLLV MLVEFDYIKI SNLLRHNTVS QCFEFLLGDL SSANVNNVKL
CLALASAPEM ESKLLSQLKV VRRIGNLLEF VNAKDMEDFL EPTLSLCRAF LLRSLGNKKG
LSSNYTKEPT LLSEASFTFE VDPQECIRDI ADFGSNIGLF LHFAGLDDDT SIAVADIASE
CVVLLLKAAS REATTGFLTN LPKITPILDS WRRRKSTELH LLVLKRVLHC LGYACKQYLS
QAMILSISGH DVSKINAIVS EMKNSDAAGL NSIASLVAME LQRLPR
