KN14B_ARATH
ID KN14B_ARATH Reviewed; 1264 AA.
AC Q9FKP4;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Kinesin-like protein KIN-14B {ECO:0000305};
DE AltName: Full=Kinesin CDKA-1-associated protein 2 {ECO:0000303|PubMed:15247388};
DE AltName: Full=Kinesin-like protein KCA2 {ECO:0000303|PubMed:15247388};
DE AltName: Full=Kinesin-like protein for actin-based chloroplast movement 2 {ECO:0000303|PubMed:20418504};
GN Name=KIN14B {ECO:0000305};
GN Synonyms=KAC2 {ECO:0000303|PubMed:20418504},
GN KCA2 {ECO:0000303|PubMed:15247388};
GN OrderedLocusNames=At5g65460 {ECO:0000312|Araport:AT5G65460};
GN ORFNames=MNA5.20 {ECO:0000312|EMBL:BAB11568.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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 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 [4]
RP SUBUNIT, INTERACTION WITH CDKA-1, AND TISSUE SPECIFICITY.
RX PubMed=15247388; DOI=10.1104/pp.104.044818;
RA Vanstraelen M., Torres Acosta J.A., De Veylder L., Inze D., Geelen D.;
RT "A plant-specific subclass of C-terminal kinesins contains a conserved a-
RT type cyclin-dependent kinase site implicated in folding and dimerization.";
RL Plant Physiol. 135:1417-1429(2004).
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP INTERACTION WITH AT4G14310.
RX PubMed=20706207; DOI=10.1038/msb.2010.53;
RA Van Leene J., Hollunder J., Eeckhout D., Persiau G., Van De Slijke E.,
RA Stals H., Van Isterdael G., Verkest A., Neirynck S., Buffel Y., De Bodt S.,
RA Maere S., Laukens K., Pharazyn A., Ferreira P.C.G., Eloy N., Renne C.,
RA Meyer C., Faure J.-D., Steinbrenner J., Beynon J., Larkin J.C.,
RA Van de Peer Y., Hilson P., Kuiper M., De Veylder L., Van Onckelen H.,
RA Inze D., Witters E., De Jaeger G.;
RT "Targeted interactomics reveals a complex core cell cycle machinery in
RT Arabidopsis thaliana.";
RL Mol. Syst. Biol. 6:397-397(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=20418504; DOI=10.1073/pnas.0912773107;
RA Suetsugu N., Yamada N., Kagawa T., Yonekura H., Uyeda T.Q., Kadota A.,
RA Wada M.;
RT "Two kinesin-like proteins mediate actin-based chloroplast movement in
RT Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8860-8865(2010).
RN [9]
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 [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27310016; DOI=10.1371/journal.pone.0157429;
RA Suetsugu N., Higa T., Gotoh E., Wada M.;
RT "Light-induced movements of chloroplasts and nuclei are regulated in both
RT cp-actin-filament-dependent and -independent manners in Arabidopsis
RT thaliana.";
RL PLoS ONE 11:E0157429-E0157429(2016).
CC -!- FUNCTION: Kinesin-like protein required for chloroplast movements and
CC anchor to the plasma membrane. Mediates chloroplast movement via
CC chloroplast actin (cp-actin) filaments. Required for the chloroplast
CC avoidance response under high intensity blue light. Mediates
CC redundantly with CHUP1 the nuclear avoidance response under high
CC intensity blue light (PubMed:27310016). May be involved in division
CC plane determination (Probable). {ECO:0000250|UniProtKB:Q9LX99,
CC ECO:0000269|PubMed:20418504, ECO:0000269|PubMed:27310016}.
CC -!- SUBUNIT: Homodimer and heterodimer with KCA1 (PubMed:15247388).
CC Interacts with CDKA-1 (PubMed:15247388). Interacts with At4g14310
CC (PubMed:20706207). {ECO:0000269|PubMed:15247388,
CC ECO:0000269|PubMed:20706207}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20418504}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
CC {ECO:0000269|PubMed:15247388}.
CC -!- DISRUPTION PHENOTYPE: Impaired chloroplast accumulation and slow
CC avoidance movement under strong blue light (PubMed:20418504). Double
CC mutant kac1kac2 exhibits an increase in leaf transmittance and a
CC partial defect in nuclear avoidance response under strong blue light
CC exposure (PubMed:27310016). {ECO:0000269|PubMed:20418504,
CC ECO:0000269|PubMed:27310016}.
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; AB011479; BAB11568.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98059.1; -; Genomic_DNA.
DR RefSeq; NP_201349.3; NM_125944.3.
DR AlphaFoldDB; Q9FKP4; -.
DR SMR; Q9FKP4; -.
DR BioGRID; 21913; 1.
DR IntAct; Q9FKP4; 1.
DR STRING; 3702.AT5G65460.1; -.
DR iPTMnet; Q9FKP4; -.
DR PaxDb; Q9FKP4; -.
DR PRIDE; Q9FKP4; -.
DR ProMEX; Q9FKP4; -.
DR ProteomicsDB; 237061; -.
DR EnsemblPlants; AT5G65460.1; AT5G65460.1; AT5G65460.
DR GeneID; 836671; -.
DR Gramene; AT5G65460.1; AT5G65460.1; AT5G65460.
DR KEGG; ath:AT5G65460; -.
DR Araport; AT5G65460; -.
DR TAIR; locus:2168292; AT5G65460.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_008815_0_0_1; -.
DR InParanoid; Q9FKP4; -.
DR PhylomeDB; Q9FKP4; -.
DR PRO; PR:Q9FKP4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKP4; baseline and differential.
DR Genevisible; Q9FKP4; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0009904; P:chloroplast accumulation movement; IGI:UniProtKB.
DR GO; GO:0009903; P:chloroplast avoidance movement; IGI:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR GO; GO:0031022; P:nuclear migration along microfilament; IGI:UniProtKB.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR030109; KIN-14.
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 PANTHER; PTHR47972:SF22; PTHR47972:SF22; 1.
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; Cell membrane; Coiled coil; Membrane; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1264
FT /note="Kinesin-like protein KIN-14B"
FT /id="PRO_0000428640"
FT DOMAIN 138..452
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 53..84
FT /evidence="ECO:0000255"
FT COILED 462..511
FT /evidence="ECO:0000255"
FT COILED 545..592
FT /evidence="ECO:0000255"
FT COILED 617..640
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 219..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1264 AA; 140396 MW; E2858F57634C0428 CRC64;
MAEQKSTNMW NWEVTGFESK KSPSSEEGVH RTPSSMLRRY SIPKNSLPPH SSELASKVQS
LKDKVQLAKD DYVGLRQEAT DLQEYSNAKL ERVTRYLGVL ADKSRKLDQY ALETEARISP
LINEKKRLFN DLLTTKGNVK VFCRARPLFE DEGPSIIEFP DNCTIRVNTS DDTLSNPKKE
FEFDRVYGPQ VGQASLFSDV QPFVQSALDG SNVSIFAYGQ THAGKTYTME GSNQDRGLYA
RCFEELMDLA NSDSTSASQF SFSVSVFELY NEQVRDLLSG CQSNLPKINM GLRESVIELS
QEKVDNPSEF MRVLNSAFQN RGNDKSKSTV THLIVSIHIC YSNTITRENV ISKLSLVDLA
GSEGLTVEDD NGDHVTDLLH VTNSISALGD VLSSLTSKRD TIPYENSFLT RILADSLGGS
SKTLMIVNIC PSARNLSEIM SCLNYAARAR NTVPSLGNRD TIKKWRDVAN DARKEVLEKE
RENQRLKQEV TGLKQALKEA NDQCVLLYNE VQRAWRVSFT LQSDLKSENA MVVDKHKIEK
EQNFQLRNQI AQLLQLEQEQ KLQAQQQDST IQNLQSKVKD LESQLSKALK SDMTRSRDPL
EPQPRAAENT LDSSAVTKKL EEELKKRDAL IERLHEENEK LFDRLTEKSV ASSTQVSSPS
SKASPTVQPA DVDSAGTLPS SVDKNEGTIT LVKSSSELVK TTPAGEYLTA ALNDFDPEQY
EGLAAIADGA NKLLMLVLAA VIKAGASREH EILAEIRDSV FSFIRKMEPR RVMDTMLVSR
VRILYIRSLL ARSPELQSIK VSPVERFLEK PYTGRTRSSS GSSSPGRSPV RYYDEQIYGF
KVNLKPEKKS KLVSVVSRIR GHDQDTGRQQ VTGGKLREIQ DEAKSFAIGN KPLAALFVHT
PAGELQRQIR SWLAESFEFL SVTADDVSGV TTGQLELLST AIMDGWMAGV GAAVPPHTDA
LGQLLSEYAK RVYTSQMQHL KDIAGTLASE EAEDAGQVAK LRSALESVDH KRRKILQQMR
SDAALFTLEE GSSPVQNPST AAEDSRLASL ISLDAILKQV KEITRQASVH VLSKSKKKAL
LESLDELNER MPSLLDVDHP CAQREIDTAH QLVETIPEQE DNLQDEKRPS IDSISSTETD
VSQWNVLQFN TGGSSAPFII KCGANSNSEL VIKADARIQE PKGGEIVRVV PRPSVLENMS
LEEMKQVFGQ LPEALSSLAL ARTADGTRAR YSRLYRTLAM KVPSLRDLVG ELEKGGVLKD
TKST
