KN14E_ARATH
ID KN14E_ARATH Reviewed; 1260 AA.
AC Q9FHN8; O22326; O23102; Q0WM77; Q39130; Q8VZV4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Kinesin-like protein KIN-14E {ECO:0000305};
DE AltName: Full=Kinesin-like calmodulin-binding protein {ECO:0000303|PubMed:8636137, ECO:0000303|PubMed:9434184};
DE AltName: Full=Protein ZWICHEL {ECO:0000303|PubMed:9177205};
GN Name=KIN14E {ECO:0000305};
GN Synonyms=KCBP {ECO:0000312|EMBL:AAC37475.1},
GN ZWI {ECO:0000312|EMBL:AAB61712.1};
GN OrderedLocusNames=At5g65930 {ECO:0000312|Araport:AT5G65930};
GN ORFNames=K14B20.10 {ECO:0000312|EMBL:BAB11140.1};
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=8636137; DOI=10.1074/jbc.271.12.7052;
RA Reddy A.S., Safadi F., Narasimhulu S.B., Golovkin M., Hu X.;
RT "A novel plant calmodulin-binding protein with a kinesin heavy chain motor
RT domain.";
RL J. Biol. Chem. 271:7052-7060(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9434184; DOI=10.1016/s0378-1119(97)00546-5;
RA Reddy A.S., Narasimhulu S.B., Day I.S.;
RT "Structural organization of a gene encoding a novel calmodulin-binding
RT kinesin-like protein from Arabidopsis.";
RL Gene 204:195-200(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9177205; DOI=10.1073/pnas.94.12.6261;
RA Oppenheimer D.G., Pollock M.A., Vacik J., Szymanski D.B., Ericson B.,
RA Feldmann K., Marks M.D.;
RT "Essential role of a kinesin-like protein in Arabidopsis trichome
RT morphogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6261-6266(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 885-1254.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, SUBUNIT, AND CALMODULIN-BINDING.
RX PubMed=9418053; DOI=10.1046/j.1365-313x.1997.12051139.x;
RA Narasimhulu S.B., Kao Y.L., Reddy A.S.;
RT "Interaction of Arabidopsis kinesin-like calmodulin-binding protein with
RT tubulin subunits: modulation by Ca(2+)-calmodulin.";
RL Plant J. 12:1139-1149(1997).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=9450347; DOI=10.1046/j.1365-313x.1997.12061429.x;
RA Bowser J., Reddy A.S.;
RT "Localization of a kinesin-like calmodulin-binding protein in dividing
RT cells of Arabidopsis and tobacco.";
RL Plant J. 12:1429-1437(1997).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=8990207; DOI=10.1073/pnas.94.1.322;
RA Song H., Golovkin M., Reddy A.S., Endow S.A.;
RT "In vitro motility of AtKCBP, a calmodulin-binding kinesin protein of
RT Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:322-327(1997).
RN [11]
RP FUNCTION, SUBUNIT, AND CALMODULIN-BINDING.
RX PubMed=9712269;
RX DOI=10.1002/(sici)1097-0169(1998)40:4<408::aid-cm8>3.0.co;2-6;
RA Deavours B.E., Reddy A.S., Walker R.A.;
RT "Ca2+/calmodulin regulation of the Arabidopsis kinesin-like calmodulin-
RT binding protein.";
RL Cell Motil. Cytoskeleton 40:408-416(1998).
RN [12]
RP REVIEW.
RX PubMed=10066632; DOI=10.1016/s1369-5266(98)80045-9;
RA Oppenheimer D.G.;
RT "Genetics of plant cell shape.";
RL Curr. Opin. Plant Biol. 1:520-524(1998).
RN [13]
RP FUNCTION, SUBUNIT, AND CALMODULIN-BINDING.
RX PubMed=9634584; DOI=10.2307/3870682;
RA Narasimhulu S.B., Reddy A.S.;
RT "Characterization of microtubule binding domains in the Arabidopsis
RT kinesin-like calmodulin binding protein.";
RL Plant Cell 10:957-965(1998).
RN [14]
RP INTERACTION WITH CAM2; CAM4 AND CAM6.
RX PubMed=10531384; DOI=10.1074/jbc.274.44.31727;
RA Reddy V.S., Safadi F., Zielinski R.E., Reddy A.S.;
RT "Interaction of a kinesin-like protein with calmodulin isoforms from
RT Arabidopsis.";
RL J. Biol. Chem. 274:31727-31733(1999).
RN [15]
RP FUNCTION, SUBUNIT, AND CALMODULIN-BINDING.
RX PubMed=10623599; DOI=10.1006/bbrc.1999.1896;
RA Kao Y.L., Deavours B.E., Phelps K.K., Walker R.A., Reddy A.S.;
RT "Bundling of microtubules by motor and tail domains of a kinesin-like
RT calmodulin-binding protein from Arabidopsis: regulation by
RT Ca(2+)/Calmodulin.";
RL Biochem. Biophys. Res. Commun. 267:201-207(2000).
RN [16]
RP INTERACTION WITH KIPK1.
RX PubMed=10788494; DOI=10.1074/jbc.275.18.13737;
RA Day I.S., Miller C., Golovkin M., Reddy A.S.;
RT "Interaction of a kinesin-like calmodulin-binding protein with a protein
RT kinase.";
RL J. Biol. Chem. 275:13737-13745(2000).
RN [17]
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 [18]
RP INTERACTION WITH AN.
RX PubMed=11889034; DOI=10.1093/emboj/21.6.1280;
RA Folkers U., Kirik V., Schoebinger U., Falk S., Krishnakumar S.,
RA Pollock M.A., Oppenheimer D.G., Day I., Reddy A.S., Juergens G.,
RA Huelskamp M., Reddy A.R.;
RT "The cell morphogenesis gene ANGUSTIFOLIA encodes a CtBP/BARS-like protein
RT and is involved in the control of the microtubule cytoskeleton.";
RL EMBO J. 21:1280-1288(2002).
RN [19]
RP FUNCTION, AND INTERACTION WITH KIC.
RX PubMed=14688294; DOI=10.1105/tpc.016600;
RA Reddy V.S., Day I.S., Thomas T., Reddy A.S.N.;
RT "KIC, a novel Ca2+ binding protein with one EF-hand motif, interacts with a
RT microtubule motor protein and regulates trichome morphogenesis.";
RL Plant Cell 16:185-200(2004).
RN [20]
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 [21]
RP FUNCTION, SUBUNIT, AND CALMODULIN-BINDING.
RX PubMed=17951708; DOI=10.1007/978-1-59745-490-2_2;
RA Reddy A.S.;
RT "Analysis of calcium/calmodulin regulation of a plant kinesin using co-
RT sedimentation and ATPase assays.";
RL Methods Mol. Biol. 392:23-36(2007).
RN [22]
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).
RN [23]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP MUTAGENESIS OF THR-976, AND SUBUNIT.
RX PubMed=26287478; DOI=10.7554/elife.09351;
RA Tian J., Han L., Feng Z., Wang G., Liu W., Ma Y., Yu Y., Kong Z.;
RT "Orchestration of microtubules and the actin cytoskeleton in trichome cell
RT shape determination by a plant-unique kinesin.";
RL Elife 4:E09351-E09351(2015).
RN [24]
RP INTERACTION WITH AIR9, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=25908862; DOI=10.1242/jcs.156570;
RA Buschmann H., Dols J., Kopischke S., Pena E.J., Andrade-Navarro M.A.,
RA Heinlein M., Szymanski D.B., Zachgo S., Doonan J.H., Lloyd C.W.;
RT "Arabidopsis KCBP interacts with AIR9 but stays in the cortical division
RT zone throughout mitosis via its MyTH4-FERM domain.";
RL J. Cell Sci. 128:2033-2046(2015).
RN [25]
RP INTERACTION WITH KIPK1 AND KIPK2, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=25262228; DOI=10.1093/jxb/eru390;
RA Humphrey T.V., Haasen K.E., Aldea-Brydges M.G., Sun H., Zayed Y.,
RA Indriolo E., Goring D.R.;
RT "PERK-KIPK-KCBP signalling negatively regulates root growth in Arabidopsis
RT thaliana.";
RL J. Exp. Bot. 66:71-83(2015).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 875-1260 IN COMPLEX WITH ADP AND
RP KIC, AND MUTAGENESIS OF CYS-1130.
RX PubMed=19416847; DOI=10.1073/pnas.0811131106;
RA Vinogradova M.V., Malanina G.G., Reddy A.S., Fletterick R.J.;
RT "Structure of the complex of a mitotic kinesin with its calcium binding
RT regulator.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8175-8179(2009).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 875-1260 IN COMPLEX WITH ADP,
RP SUBUNIT, AND MUTAGENESIS OF CYS-1130.
RX PubMed=23805258; DOI=10.1371/journal.pone.0066669;
RA Vinogradova M.V., Malanina G.G., Waitzman J.S., Rice S.E., Fletterick R.J.;
RT "Plant kinesin-like calmodulin binding protein employs its regulatory
RT domain for dimerization.";
RL PLoS ONE 8:E66669-E66669(2013).
CC -!- FUNCTION: Minus-end microtubule-dependent motor protein involved in the
CC regulation of cell division and trichome morphogenesis through
CC microtubules bundling. Possesses basal and microtubule-stimulated
CC ATPase activities. Acts as a hub that brings together microtubules and
CC actin filaments to modulate the cytoskeleton during trichome formation
CC and morphogenesis (PubMed:26287478). Could be involved in the negative
CC regulation of root growth (PubMed:25262228).
CC {ECO:0000269|PubMed:10623599, ECO:0000269|PubMed:14688294,
CC ECO:0000269|PubMed:17951708, ECO:0000269|PubMed:25262228,
CC ECO:0000269|PubMed:26287478, ECO:0000269|PubMed:8636137,
CC ECO:0000269|PubMed:8990207, ECO:0000269|PubMed:9177205,
CC ECO:0000269|PubMed:9418053, ECO:0000269|PubMed:9634584,
CC ECO:0000269|PubMed:9712269}.
CC -!- SUBUNIT: Homodimer (via C-terminus) (PubMed:23805258). Binds
CC microtubules via its N-terminus containing the MyTH4 domain and binds
CC F-actin via its FERM domain (PubMed:26287478). Interacts with KIPK1
CC (PubMed:10788494, PubMed:25262228). Interacts with KIPK2
CC (PubMed:25262228). Interacts with AN (PubMed:11889034). Interacts with
CC AIR9 (PubMed:25908862). Interacts (via C-terminus) with KIC, CAM2, CAM4
CC and CAM6. KIC and calmodulin show competitive binding to KCBP. Binding
CC to calmodulin inhibits microtubule binding activity. Binding to KIC
CC inhibits microtubule binding activity and microtubule-stimulated ATPase
CC activity. {ECO:0000269|PubMed:10531384, ECO:0000269|PubMed:10623599,
CC ECO:0000269|PubMed:10788494, ECO:0000269|PubMed:11889034,
CC ECO:0000269|PubMed:14688294, ECO:0000269|PubMed:17951708,
CC ECO:0000269|PubMed:19416847, ECO:0000269|PubMed:23805258,
CC ECO:0000269|PubMed:25262228, ECO:0000269|PubMed:25908862,
CC ECO:0000269|PubMed:26287478, ECO:0000269|PubMed:8990207,
CC ECO:0000269|PubMed:9418053, ECO:0000269|PubMed:9634584,
CC ECO:0000269|PubMed:9712269}.
CC -!- INTERACTION:
CC Q9FHN8; F4IIU4: AIR9; NbExp=6; IntAct=EBI-1749651, EBI-12513601;
CC Q9FHN8; P25854: CAM4; NbExp=2; IntAct=EBI-1749651, EBI-1235664;
CC Q9FHN8; P25069: CAM5; NbExp=2; IntAct=EBI-1749651, EBI-1397259;
CC Q9FHN8; Q682T9: CAM5; NbExp=2; IntAct=EBI-1749651, EBI-1749673;
CC Q9FHN8; Q03509: CAM6; NbExp=2; IntAct=EBI-1749651, EBI-1236097;
CC Q9FHN8; Q9ZPX9: KIC; NbExp=5; IntAct=EBI-1749651, EBI-2353491;
CC Q9FHN8; Q9LFA2: KIPK1; NbExp=4; IntAct=EBI-1749651, EBI-1103859;
CC Q9FHN8-1; Q9ZPX9: KIC; NbExp=2; IntAct=EBI-15777922, EBI-2353491;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:25908862}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:25908862, ECO:0000269|PubMed:9450347}. Cytoplasm,
CC cytoskeleton, phragmoplast {ECO:0000269|PubMed:25908862,
CC ECO:0000269|PubMed:9450347}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:26287478}. Note=Colocalizes with microtubules
CC during preprophase and cytokinesis. In M-phase, locates to the
CC preprophase band then remained in the cotical division site throughout
CC mitotis and cytokinesis. Also detected towards the poles of the
CC anaphase spindle and on the phragmoplast but absent from the metaphase
CC spindle (PubMed:9450347, PubMed:25908862). Colocalizes with
CC microtubules along the trichome branch and colocalizes with F-actin at
CC the branch apex (PubMed:26287478). {ECO:0000269|PubMed:25908862,
CC ECO:0000269|PubMed:26287478, ECO:0000269|PubMed:9450347}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FHN8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FHN8-2; Sequence=VSP_040367;
CC -!- TISSUE SPECIFICITY: Widely expressed with the highest levels in flowers
CC (PubMed:8636137). Strongly expressed in the root tip (PubMed:25908862).
CC Highly detected in the branch apex of the trichome (PubMed:26287478).
CC {ECO:0000269|PubMed:25908862, ECO:0000269|PubMed:26287478,
CC ECO:0000269|PubMed:8636137}.
CC -!- DISRUPTION PHENOTYPE: Trichomes with reduced branch number
CC (PubMed:9177205, PubMed:25262228, PubMed:26287478). Impairment of
CC trichomes branch tip sharpening due to disrupted transverse cortical F-
CC actin cap (PubMed:26287478). {ECO:0000269|PubMed:25262228,
CC ECO:0000269|PubMed:26287478, ECO:0000269|PubMed:9177205}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-14 subfamily.
CC {ECO:0000303|PubMed:16448571}.
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DR EMBL; L40358; AAC37475.1; -; mRNA.
DR EMBL; AF002220; AAC49901.1; -; Genomic_DNA.
DR EMBL; AF002678; AAB61712.1; -; Genomic_DNA.
DR EMBL; AB018108; BAB11140.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98125.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98126.1; -; Genomic_DNA.
DR EMBL; AY063811; AAL36167.1; -; mRNA.
DR EMBL; AK229953; BAF01779.1; -; mRNA.
DR RefSeq; NP_569022.2; NM_125990.4. [Q9FHN8-1]
DR RefSeq; NP_851276.1; NM_180945.2. [Q9FHN8-2]
DR PDB; 3H4S; X-ray; 2.40 A; A=875-1260.
DR PDB; 4FRZ; X-ray; 2.40 A; A/B=875-1260.
DR PDBsum; 3H4S; -.
DR PDBsum; 4FRZ; -.
DR AlphaFoldDB; Q9FHN8; -.
DR SMR; Q9FHN8; -.
DR BioGRID; 21965; 3.
DR DIP; DIP-54846N; -.
DR IntAct; Q9FHN8; 8.
DR STRING; 3702.AT5G65930.3; -.
DR iPTMnet; Q9FHN8; -.
DR PaxDb; Q9FHN8; -.
DR PRIDE; Q9FHN8; -.
DR EnsemblPlants; AT5G65930.1; AT5G65930.1; AT5G65930. [Q9FHN8-2]
DR EnsemblPlants; AT5G65930.2; AT5G65930.2; AT5G65930. [Q9FHN8-1]
DR GeneID; 836723; -.
DR Gramene; AT5G65930.1; AT5G65930.1; AT5G65930. [Q9FHN8-2]
DR Gramene; AT5G65930.2; AT5G65930.2; AT5G65930. [Q9FHN8-1]
DR KEGG; ath:AT5G65930; -.
DR Araport; AT5G65930; -.
DR eggNOG; KOG0239; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR HOGENOM; CLU_001485_14_0_1; -.
DR InParanoid; Q9FHN8; -.
DR PhylomeDB; Q9FHN8; -.
DR EvolutionaryTrace; Q9FHN8; -.
DR PRO; PR:Q9FHN8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHN8; baseline and differential.
DR Genevisible; Q9FHN8; AT.
DR GO; GO:0055028; C:cortical microtubule; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0009524; C:phragmoplast; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0043622; P:cortical microtubule organization; IDA:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; IDA:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IDA:UniProtKB.
DR GO; GO:0010091; P:trichome branching; IMP:UniProtKB.
DR GO; GO:0048629; P:trichome patterning; IMP:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.25.40.530; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR011254; Prismane-like_sf.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00784; MyTH4; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00295; B41; 1.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00139; MyTH4; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56821; SSF56821; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS51016; MYTH4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Coiled coil; Cytoplasm; Cytoskeleton; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1260
FT /note="Kinesin-like protein KIN-14E"
FT /id="PRO_0000403273"
FT DOMAIN 115..274
FT /note="MyTH4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 279..593
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 888..1209
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1217..1239
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000303|PubMed:9418053"
FT REGION 1221..1260
FT /note="Homodimerization domain"
FT /evidence="ECO:0000303|PubMed:23805258"
FT REGION 1236..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 615..676
FT /evidence="ECO:0000255"
FT COILED 753..853
FT /evidence="ECO:0000255"
FT BINDING 972..977
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:3H4S, ECO:0007744|PDB:4FRZ"
FT VAR_SEQ 306
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040367"
FT MUTAGEN 976
FT /note="T->N: Defective in ATP hydrolysis. Severe trichome
FT phenotypes."
FT /evidence="ECO:0000269|PubMed:26287478"
FT MUTAGEN 1130
FT /note="C->N: No effect on binding to microtubule or
FT regulation by KIC."
FT /evidence="ECO:0000269|PubMed:19416847,
FT ECO:0000269|PubMed:23805258"
FT CONFLICT 118
FT /note="D -> IPI (in Ref. 1; AAC37475)"
FT /evidence="ECO:0000305"
FT CONFLICT 307..308
FT /note="EL -> V (in Ref. 1; AAC37475)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="D -> G (in Ref. 1; AAC37475)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="V -> D (in Ref. 6; AAL36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="S -> C (in Ref. 2; AAC49901)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="S -> C (in Ref. 2; AAC49901)"
FT /evidence="ECO:0000305"
FT CONFLICT 693
FT /note="T -> P (in Ref. 2; AAC49901)"
FT /evidence="ECO:0000305"
FT CONFLICT 922
FT /note="P -> A (in Ref. 2; AAC49901)"
FT /evidence="ECO:0000305"
FT CONFLICT 977
FT /note="F -> S (in Ref. 1; AAC37475)"
FT /evidence="ECO:0000305"
FT CONFLICT 1044
FT /note="K -> T (in Ref. 1; AAC37475)"
FT /evidence="ECO:0000305"
FT CONFLICT 1085
FT /note="S -> N (in Ref. 6; AAL36167)"
FT /evidence="ECO:0000305"
FT CONFLICT 1192
FT /note="N -> D (in Ref. 6; AAL36167)"
FT /evidence="ECO:0000305"
FT STRAND 888..895
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 900..904
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 912..915
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 918..921
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 924..926
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 929..932
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 934..937
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 943..950
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 952..958
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 962..970
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 975..979
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 983..986
FT /evidence="ECO:0007829|PDB:4FRZ"
FT HELIX 988..1002
FT /evidence="ECO:0007829|PDB:3H4S"
FT TURN 1003..1006
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 1007..1019
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 1022..1027
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 1030..1032
FT /evidence="ECO:0007829|PDB:4FRZ"
FT STRAND 1038..1041
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 1047..1050
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 1055..1057
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 1060..1071
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 1084..1087
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 1088..1100
FT /evidence="ECO:0007829|PDB:3H4S"
FT TURN 1101..1103
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 1106..1115
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 1129..1154
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 1161..1163
FT /evidence="ECO:0007829|PDB:4FRZ"
FT HELIX 1165..1169
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 1171..1173
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 1174..1177
FT /evidence="ECO:0007829|PDB:3H4S"
FT STRAND 1179..1186
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 1190..1192
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 1193..1206
FT /evidence="ECO:0007829|PDB:3H4S"
FT HELIX 1219..1240
FT /evidence="ECO:0007829|PDB:3H4S"
SQ SEQUENCE 1260 AA; 143449 MW; EE6B562CAA6201EF CRC64;
MEGQRGSNSS LSSGNGTEVA TDVSSCFYVP NPSGTDFDAE SSSLPPLSPA PQVALSIPAE
LAAAIPLIDR FQVEAFLRLM QKQIQSAGKR GFFYSKKSSG SNVRERFTFE DMLCFQKDPI
PTSLLKINSD LVSRATKLFH LILKYMGVDS SDRSTPPSLD ERIDLVGKLF KKTLKRVELR
DELFAQISKQ TRHNPDRQYL IKAWELMYLC ASSMPPSKDI GGYLSEYIHN VAHDATIEPD
AQVLAVNTLK ALKRSIKAGP RHTTPGREEI EALLTGRKLT TIVFFLDETF EEISYDMATT
VSDAVEELAG TIKLSAFSSF SLFECRKVVS SSKSSDPGNE EYIGLDDNKY IGDLLAEFKA
IKDRNKGEIL HCKLVFKKKL FRESDEAVTD LMFVQLSYVQ LQHDYLLGNY PVGRDDAAQL
CALQILVGIG FVNSPESCID WTSLLERFLP RQIAITRAKR EWELDILARY RSMENVTKDD
ARQQFLRILK ALPYGNSVFF SVRKIDDPIG LLPGRIILGI NKRGVHFFRP VPKEYLHSAE
LRDIMQFGSS NTAVFFKMRV AGVLHIFQFE TKQGEEICVA LQTHINDVML RRYSKARSAA
NSLVNGDISC SSKPQNFEVY EKRLQDLSKA YEESQKKIEK LMDEQQEKNQ QEVTLREELE
AIHNGLELER RKLLEVTLDR DKLRSLCDEK GTTIQSLMSE LRGMEARLAK SGNTKSSKET
KSELAEMNNQ ILYKIQKELE VRNKELHVAV DNSKRLLSEN KILEQNLNIE KKKKEEVEIH
QKRYEQEKKV LKLRVSELEN KLEVLAQDLD SAESTIESKN SDMLLLQNNL KELEELREMK
EDIDRKNEQT AAILKMQGAQ LAELEILYKE EQVLRKRYYN TIEDMKGKIR VYCRIRPLNE
KESSEREKQM LTTVDEFTVE HPWKDDKRKQ HIYDRVFDMR ASQDDIFEDT KYLVQSAVDG
YNVCIFAYGQ TGSGKTFTIY GHESNPGLTP RATKELFNIL KRDSKRFSFS LKAYMVELYQ
DTLVDLLLPK SARRLKLEIK KDSKGMVFVE NVTTIPISTL EELRMILERG SERRHVSGTN
MNEESSRSHL ILSVVIESID LQTQSAARGK LSFVDLAGSE RVKKSGSAGC QLKEAQSINK
SLSALGDVIG ALSSGNQHIP YRNHKLTMLM SDSLGGNAKT LMFVNVSPAE SNLDETYNSL
LYASRVRTIV NDPSKHISSK EMVRLKKLVA YWKEQAGKKG EEEDLVDIEE DRTRKDEADS
