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Kinesin-like protein KIN-14B (Kinesin CDKA-1-associated protein 2) (Kinesin-like protein KCA2) (Kinesin-like protein for actin-based chloroplast movement 2)

 KN14B_ARATH             Reviewed;        1264 AA.
Q9FKP4;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
23-MAY-2018, entry version 108.
RecName: Full=Kinesin-like protein KIN-14B {ECO:0000305};
AltName: Full=Kinesin CDKA-1-associated protein 2 {ECO:0000303|PubMed:15247388};
AltName: Full=Kinesin-like protein KCA2 {ECO:0000303|PubMed:15247388};
AltName: Full=Kinesin-like protein for actin-based chloroplast movement 2 {ECO:0000303|PubMed:20418504};
Name=KIN14B {ECO:0000305};
Synonyms=KAC2 {ECO:0000303|PubMed:20418504},
KCA2 {ECO:0000303|PubMed:15247388};
OrderedLocusNames=At5g65460 {ECO:0000312|Araport:AT5G65460};
ORFNames=MNA5.20 {ECO:0000312|EMBL:BAB11568.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9679202; DOI=10.1093/dnares/5.2.131;
Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
features of the regions of 1,381,565 bp covered by twenty one
physically assigned P1 and TAC clones.";
DNA Res. 5:131-145(1998).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
GENE FAMILY.
PubMed=11472632; DOI=10.1186/1471-2164-2-2;
Reddy A.S., Day I.S.;
"Kinesins in the Arabidopsis genome: a comparative analysis among
eukaryotes.";
BMC Genomics 2:2-2(2001).
[4]
SUBUNIT, INTERACTION WITH CDKA-1, AND TISSUE SPECIFICITY.
PubMed=15247388; DOI=10.1104/pp.104.044818;
Vanstraelen M., Torres Acosta J.A., De Veylder L., Inze D., Geelen D.;
"A plant-specific subclass of C-terminal kinesins contains a conserved
a-type cyclin-dependent kinase site implicated in folding and
dimerization.";
Plant Physiol. 135:1417-1429(2004).
[5]
GENE FAMILY, AND NOMENCLATURE.
PubMed=16448571; DOI=10.1186/1471-2164-7-18;
Richardson D.N., Simmons M.P., Reddy A.S.;
"Comprehensive comparative analysis of kinesins in photosynthetic
eukaryotes.";
BMC Genomics 7:18-18(2006).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[7]
INTERACTION WITH AT4G14310.
PubMed=20706207; DOI=10.1038/msb.2010.53;
Van Leene J., Hollunder J., Eeckhout D., Persiau G., Van De Slijke E.,
Stals H., Van Isterdael G., Verkest A., Neirynck S., Buffel Y.,
De Bodt S., Maere S., Laukens K., Pharazyn A., Ferreira P.C.G.,
Eloy N., Renne C., Meyer C., Faure J.-D., Steinbrenner J., Beynon J.,
Larkin J.C., Van de Peer Y., Hilson P., Kuiper M., De Veylder L.,
Van Onckelen H., Inze D., Witters E., De Jaeger G.;
"Targeted interactomics reveals a complex core cell cycle machinery in
Arabidopsis thaliana.";
Mol. Syst. Biol. 6:397-397(2010).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=20418504; DOI=10.1073/pnas.0912773107;
Suetsugu N., Yamada N., Kagawa T., Yonekura H., Uyeda T.Q., Kadota A.,
Wada M.;
"Two kinesin-like proteins mediate actin-based chloroplast movement in
Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 107:8860-8865(2010).
[9]
REVIEW.
PubMed=22038119; DOI=10.1007/s00709-011-0343-9;
Zhu C., Dixit R.;
"Functions of the Arabidopsis kinesin superfamily of microtubule-based
motor proteins.";
Protoplasma 249:887-899(2012).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=27310016; DOI=10.1371/journal.pone.0157429;
Suetsugu N., Higa T., Gotoh E., Wada M.;
"Light-induced movements of chloroplasts and nuclei are regulated in
both cp-actin-filament-dependent and -independent manners in
Arabidopsis thaliana.";
PLoS ONE 11:E0157429-E0157429(2016).
-!- FUNCTION: Kinesin-like protein required for chloroplast movements
and anchor to the plasma membrane. Mediates chloroplast movement
via chloroplast actin (cp-actin) filaments. Required for the
chloroplast avoidance response under high intensity blue light.
Mediates redundantly with CHUP1 the nuclear avoidance response
under high intensity blue light (PubMed:27310016). May be involved
in division plane determination (Probable).
{ECO:0000250|UniProtKB:Q9LX99, ECO:0000269|PubMed:20418504,
ECO:0000269|PubMed:27310016}.
-!- SUBUNIT: Homodimer and heterodimer with KCA1 (PubMed:15247388).
Interacts with CDKA-1 (PubMed:15247388). Interacts with At4g14310
(PubMed:20706207). {ECO:0000269|PubMed:15247388,
ECO:0000269|PubMed:20706207}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20418504}.
-!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers.
{ECO:0000269|PubMed:15247388}.
-!- DISRUPTION PHENOTYPE: Impaired chloroplast accumulation and slow
avoidance movement under strong blue light (PubMed:20418504).
Double mutant kac1kac2 exhibits an increase in leaf transmittance
and a partial defect in nuclear avoidance response under strong
blue light exposure (PubMed:27310016).
{ECO:0000269|PubMed:20418504, ECO:0000269|PubMed:27310016}.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Kinesin family. KIN-14 subfamily.
{ECO:0000303|PubMed:16448571}.
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EMBL; AB011479; BAB11568.1; -; Genomic_DNA.
EMBL; CP002688; AED98059.1; -; Genomic_DNA.
RefSeq; NP_201349.3; NM_125944.3.
UniGene; At.28909; -.
ProteinModelPortal; Q9FKP4; -.
SMR; Q9FKP4; -.
BioGrid; 21913; 1.
IntAct; Q9FKP4; 1.
STRING; 3702.AT5G65460.1; -.
iPTMnet; Q9FKP4; -.
PaxDb; Q9FKP4; -.
PRIDE; Q9FKP4; -.
ProMEX; Q9FKP4; -.
EnsemblPlants; AT5G65460.1; AT5G65460.1; AT5G65460.
GeneID; 836671; -.
Gramene; AT5G65460.1; AT5G65460.1; AT5G65460.
KEGG; ath:AT5G65460; -.
Araport; AT5G65460; -.
TAIR; locus:2168292; AT5G65460.
eggNOG; KOG0239; Eukaryota.
eggNOG; COG5059; LUCA.
HOGENOM; HOG000030191; -.
InParanoid; Q9FKP4; -.
OMA; DEHVHGF; -.
OrthoDB; EOG093600IZ; -.
PhylomeDB; Q9FKP4; -.
PRO; PR:Q9FKP4; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9FKP4; baseline and differential.
Genevisible; Q9FKP4; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IBA:GO_Central.
GO; GO:0008017; F:microtubule binding; IDA:TAIR.
GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
GO; GO:0009904; P:chloroplast accumulation movement; IGI:UniProtKB.
GO; GO:0009903; P:chloroplast avoidance movement; IGI:UniProtKB.
GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
GO; GO:0031022; P:nuclear migration along microfilament; IGI:UniProtKB.
Gene3D; 3.40.850.10; -; 1.
InterPro; IPR030109; KIN-14.
InterPro; IPR027640; Kinesin-like_fam.
InterPro; IPR019821; Kinesin_motor_CS.
InterPro; IPR001752; Kinesin_motor_dom.
InterPro; IPR036961; Kinesin_motor_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR24115; PTHR24115; 1.
PANTHER; PTHR24115:SF469; PTHR24115:SF469; 1.
Pfam; PF00225; Kinesin; 1.
PRINTS; PR00380; KINESINHEAVY.
SMART; SM00129; KISc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00411; KINESIN_MOTOR_1; 1.
PROSITE; PS50067; KINESIN_MOTOR_2; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Coiled coil; Complete proteome; Membrane;
Microtubule; Motor protein; Nucleotide-binding; Reference proteome.
CHAIN 1 1264 Kinesin-like protein KIN-14B.
/FTId=PRO_0000428640.
DOMAIN 138 452 Kinesin motor. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
NP_BIND 219 226 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
COILED 53 84 {ECO:0000255}.
COILED 462 511 {ECO:0000255}.
COILED 545 592 {ECO:0000255}.
COILED 617 640 {ECO:0000255}.
COMPBIAS 542 575 Gln-rich.
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


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