KN12A_ARATH
ID KN12A_ARATH Reviewed; 1292 AA.
AC Q9LDN0; O23274;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Kinesin-like protein KIN-12A {ECO:0000305};
DE AltName: Full=Phragmoplast-associated kinesin-related protein 1 {ECO:0000303|PubMed:10898978};
DE Short=AtPAKRP1 {ECO:0000303|PubMed:10898978};
GN Name=KIN12A {ECO:0000305}; Synonyms=PAKRP1 {ECO:0000312|EMBL:AAF78893.1};
GN OrderedLocusNames=At4g14150 {ECO:0000312|Araport:AT4G14150};
GN ORFNames=dl3115c {ECO:0000312|EMBL:CAB10194.1},
GN FCAALL.159 {ECO:0000312|EMBL:CAB78457.1};
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 [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10898978; DOI=10.1016/s0960-9822(00)00564-9;
RA Lee Y.R.J., Liu B.;
RT "Identification of a phragmoplast-associated kinesin-related protein in
RT higher plants.";
RL Curr. Biol. 10:797-800(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
RP GENE FAMILY.
RX PubMed=11472632; DOI=10.1186/1471-2164-2-2;
RA Reddy A.S., Day I.S.;
RT "Kinesins in the Arabidopsis genome: a comparative analysis among
RT eukaryotes.";
RL BMC Genomics 2:2-2(2001).
RN [6]
RP SUBCELLULAR LOCATION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=15258761; DOI=10.1007/s00425-004-1324-4;
RA Pan R., Lee Y.R., Liu B.;
RT "Localization of two homologous Arabidopsis kinesin-related proteins in the
RT phragmoplast.";
RL Planta 220:156-164(2004).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16448571; DOI=10.1186/1471-2164-7-18;
RA Richardson D.N., Simmons M.P., Reddy A.S.;
RT "Comprehensive comparative analysis of kinesins in photosynthetic
RT eukaryotes.";
RL BMC Genomics 7:18-18(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17720869; DOI=10.1105/tpc.107.050716;
RA Lee Y.R., Li Y., Liu B.;
RT "Two Arabidopsis phragmoplast-associated kinesins play a critical role in
RT cytokinesis during male gametogenesis.";
RL Plant Cell 19:2595-2605(2007).
RN [9]
RP INTERACTION WITH TIO.
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 [10]
RP REVIEW.
RX PubMed=22038119; DOI=10.1007/s00709-011-0343-9;
RA Zhu C., Dixit R.;
RT "Functions of the Arabidopsis kinesin superfamily of microtubule-based
RT motor proteins.";
RL Protoplasma 249:887-899(2012).
CC -!- FUNCTION: Plus-end directed kinesin-like motor enzyme that plays a
CC critical role in the organization of phragmoplast microtubules during
CC cytokinesis. Constitutes a signaling module in association with
CC serine/threonine-protein kinase TIO that is required to support
CC phragmoplast expansion and cell-plate growth in plant cells. Binds
CC microtubules in an ATP-sensitive manner. {ECO:0000269|PubMed:10898978,
CC ECO:0000269|PubMed:17720869}.
CC -!- SUBUNIT: Homodimer and heterodimer with KIN12B. Interacts with TIO.
CC {ECO:0000269|PubMed:15258761, ECO:0000269|PubMed:22709276}.
CC -!- INTERACTION:
CC Q9LDN0; Q8L7Y8: KIN12B; NbExp=2; IntAct=EBI-6280428, EBI-6280461;
CC Q9LDN0; Q2QAV0: TIO; NbExp=3; IntAct=EBI-6280428, EBI-6280536;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:10898978, ECO:0000269|PubMed:15258761}.
CC Note=Localized to the midline of the nascent phragmoplast (late
CC anaphase) and remains associated with the expanding phragmoplast ring.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Kin12a and kin12b double
CC mutant display defective pollen grains leading to the production of
CC fewer seeds. {ECO:0000269|PubMed:15258761,
CC ECO:0000269|PubMed:17720869}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-12 subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10194.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 3 genes: At4g14145, At4g14147 and At4g14150.; Evidence={ECO:0000305};
CC Sequence=CAB78457.1; Type=Erroneous gene model prediction; Note=The predicted gene has been split into 3 genes: At4g14145, At4g14147 and At4g14150.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF193767; AAF78893.1; -; mRNA.
DR EMBL; AF193768; AAF78894.1; -; Genomic_DNA.
DR EMBL; Z97335; CAB10194.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161538; CAB78457.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83384.1; -; Genomic_DNA.
DR PIR; H71402; H71402.
DR RefSeq; NP_567423.1; NM_117492.2.
DR AlphaFoldDB; Q9LDN0; -.
DR SMR; Q9LDN0; -.
DR BioGRID; 12351; 1.
DR IntAct; Q9LDN0; 2.
DR STRING; 3702.AT4G14150.1; -.
DR PaxDb; Q9LDN0; -.
DR PRIDE; Q9LDN0; -.
DR ProteomicsDB; 250760; -.
DR EnsemblPlants; AT4G14150.1; AT4G14150.1; AT4G14150.
DR GeneID; 827054; -.
DR Gramene; AT4G14150.1; AT4G14150.1; AT4G14150.
DR KEGG; ath:AT4G14150; -.
DR Araport; AT4G14150; -.
DR TAIR; locus:2129455; AT4G14150.
DR eggNOG; KOG4280; Eukaryota.
DR HOGENOM; CLU_009194_0_0_1; -.
DR InParanoid; Q9LDN0; -.
DR OMA; MEDACCH; -.
DR OrthoDB; 130600at2759; -.
DR PhylomeDB; Q9LDN0; -.
DR PRO; PR:Q9LDN0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9LDN0; baseline and differential.
DR Genevisible; Q9LDN0; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0009524; C:phragmoplast; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007112; P:male meiosis cytokinesis; IGI:TAIR.
DR GO; GO:0055046; P:microgametogenesis; IMP:TAIR.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0080175; P:phragmoplast microtubule organization; IMP:UniProtKB.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1292
FT /note="Kinesin-like protein KIN-12A"
FT /id="PRO_0000419695"
FT DOMAIN 91..426
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..297
FT /note="Microtubules-binding"
FT /evidence="ECO:0000305|PubMed:10898978"
FT REGION 326..332
FT /note="Microtubules-binding"
FT /evidence="ECO:0000305|PubMed:10898978"
FT REGION 375..379
FT /note="Microtubules-binding"
FT /evidence="ECO:0000305|PubMed:10898978"
FT REGION 424..461
FT /note="Neck"
FT /evidence="ECO:0000305|PubMed:10898978"
FT REGION 677..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 945..992
FT /evidence="ECO:0000255"
FT COILED 1047..1232
FT /evidence="ECO:0000255"
FT COMPBIAS 677..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 165..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1292 AA; 144632 MW; 7C07BD03495E5934 CRC64;
MKKHFTLPRN AILRDGGEPH SPNPSISKSK PPRKLRSAKE NAPPLDRNTS TPDHRSMRMK
NPLPPRPPPS NPLKRKLSAE TATESGFSDS GVKVIVRMKP LNKGEEGDMI VEKMSKDSLT
VSGQTFTFDS IANPESTQEQ MFQLVGAPLV ENCLSGFNSS VFAYGQTGSG KTYTMWGPAN
GLLEEHLCGD QRGLTPRVFE RLFARIKEEQ VKHAERQLNY QCRCSLLEIY NEQITDLLDP
SQKNLMIRED VKSGVYVENL TEEYVKNLTD VSQLLIKGLG NRRTGATSVN TESSRSHCVF
TCVVESRCKN VADGLSSFKT SRINLVDLAG SERQKSTGAA GERLKEAGNI NRSLSQLGNL
INILAEISQT GKPRHIPYRD SRLTFLLQES LGGNAKLAMV CAVSPSQSCR SETFSTLRFA
QRAKAIQNKA VVNEVMQDDV NFLRGVIHQL RDELQRMKND GNNPTNPNVA YSTAWNARRS
LNLLRSFGLG HPRSLPHEDN DGDIEMEIDE AAVERLCVQV GLQSSLASEG INHDMNRVKS
IHSSDGQSIE KRLPEDSDVA MEDACCHTEN HEPETVDNMR TETETGIREN QIKTHSQTLD
HESSFQPLSV KDALCSSLNK SEDVSSCPDL VPQDVTSANV LIADGVDDPE HLVNSASPSL
CIDPVGATPV LKSPTLSVSP TIRNSRKSLK TSELSTASQK DSEGENLVTE AADPSPATSK
KMNNCSSALS TQKSKVFPVR TERLASSLHK GIKLLESYCQ STAQRRSTYR FSFKAPDSEP
STSISKADAG VQTIPGADAI SEENTKEFLC CKCKCREQFD AQQMGDMPNL QLVPVDNSEV
AEKSKNQVPK AVEKVLAGSI RREMALEEFC TKQASEITQL NRLVQQYKHE RECNAIIGQT
REDKIIRLES LMDGVLSKED FLDEEFASLL HEHKLLKDMY QNHPEVLKTK IELERTQEEV
ENFKNFYGDM GEREVLLEEI QDLKLQLQCY IDPSLKSALK TCTLLKLSYQ APPVNAIPES
QDESLEKTLE QERLCWTEAE TKWISLSEEL RTELEASKAL INKQKHELEI EKRCGEELKE
AMQMAMEGHA RMLEQYADLE EKHMQLLARH RRIQDGIDDV KKAAARAGVR GAESRFINAL
AAEISALKVE KEKERQYLRD ENKSLQTQLR DTAEAIQAAG ELLVRLKEAE EGLTVAQKRA
MDAEYEAAEA YRQIDKLKKK HENEINTLNQ LVPQSHIHNE CSTKCDQAVE PSVNASSEQQ
WRDEFEPLYK KETEFSNLAE PSWFSGYDRC NI
