KN14F_ARATH
ID KN14F_ARATH Reviewed; 1087 AA.
AC Q8W1Y3; F4J373; O22240;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Kinesin-like protein KIN-14F {ECO:0000305};
DE AltName: Full=AtKIN14h;
DE AltName: Full=Kinesin KP1 {ECO:0000303|PubMed:21406623};
DE AltName: Full=Kinesin-like protein 1 {ECO:0000303|PubMed:16212879};
DE Short=AtKP1 {ECO:0000303|PubMed:16212879};
GN Name=KIN14F {ECO:0000305}; Synonyms=KP1 {ECO:0000312|EMBL:AAK92458.3};
GN OrderedLocusNames=At3g44730 {ECO:0000312|Araport:AT3G44730};
GN ORFNames=T32N15.10 {ECO:0000312|EMBL:AAB70034.1};
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Stem;
RX PubMed=16212879; DOI=10.1038/sj.cr.7290342;
RA Ni C.Z., Wang H.Q., Xu T., Qu Z., Liu G.Q.;
RT "AtKP1, a kinesin-like protein, mainly localizes to mitochondria in
RT Arabidopsis thaliana.";
RL Cell Res. 15:725-733(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [4]
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 [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 INDUCTION.
RX PubMed=19669906; DOI=10.1007/s11103-009-9533-7;
RA Xiong J.Y., Lai C.X., Qu Z., Yang X.Y., Qin X.H., Liu G.Q.;
RT "Recruitment of AtWHY1 and AtWHY3 by a distal element upstream of the
RT kinesin gene AtKP1 to mediate transcriptional repression.";
RL Plant Mol. Biol. 71:437-449(2009).
RN [7]
RP FUNCTION, INTERACTION WITH VDAC3, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=21406623; DOI=10.1105/tpc.110.082420;
RA Yang X.Y., Chen Z.W., Xu T., Qu Z., Pan X.D., Qin X.H., Ren D.T., Liu G.Q.;
RT "Arabidopsis kinesin KP1 specifically interacts with VDAC3, a mitochondrial
RT protein, and regulates respiration during seed germination at low
RT temperature.";
RL Plant Cell 23:1093-1106(2011).
RN [8]
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: Required for keeping the ATP levels stable and balancing the
CC aerobic respiration pathways during seed germination at low
CC temperature. {ECO:0000269|PubMed:21406623}.
CC -!- SUBUNIT: Interacts (via C-terminus) with VDAC3.
CC {ECO:0000269|PubMed:21406623}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC Mitochondrion {ECO:0000269|PubMed:21406623}. Note=Associated with VDAC3
CC in mitochondrion. {ECO:0000269|PubMed:21406623}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems and flowers (at
CC protein level). {ECO:0000269|PubMed:16212879}.
CC -!- INDUCTION: Down-regulated by salicylic acid (SA).
CC {ECO:0000269|PubMed:19669906}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:21406623}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-14 subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70034.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF398149; AAK92458.3; -; mRNA.
DR EMBL; AC002534; AAB70034.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77940.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65657.1; -; Genomic_DNA.
DR RefSeq; NP_001319684.1; NM_001339170.1.
DR RefSeq; NP_190059.3; NM_114341.4.
DR AlphaFoldDB; Q8W1Y3; -.
DR SMR; Q8W1Y3; -.
DR BioGRID; 8922; 2.
DR STRING; 3702.AT3G44730.1; -.
DR iPTMnet; Q8W1Y3; -.
DR PaxDb; Q8W1Y3; -.
DR PRIDE; Q8W1Y3; -.
DR ProteomicsDB; 250748; -.
DR EnsemblPlants; AT3G44730.1; AT3G44730.1; AT3G44730.
DR EnsemblPlants; AT3G44730.4; AT3G44730.4; AT3G44730.
DR GeneID; 823602; -.
DR Gramene; AT3G44730.1; AT3G44730.1; AT3G44730.
DR Gramene; AT3G44730.4; AT3G44730.4; AT3G44730.
DR KEGG; ath:AT3G44730; -.
DR Araport; AT3G44730; -.
DR TAIR; locus:2101645; AT3G44730.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_001485_0_0_1; -.
DR PRO; PR:Q8W1Y3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8W1Y3; baseline and differential.
DR Genevisible; Q8W1Y3; AT.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; IMP: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:0009845; P:seed germination; IMP:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00033; CH; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Mitochondrion; Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1087
FT /note="Kinesin-like protein KIN-14F"
FT /id="PRO_0000429024"
FT DOMAIN 1..110
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 377..705
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 136..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 710..749
FT /evidence="ECO:0000255"
FT COMPBIAS 774..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..858
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 461..468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 428
FT /note="V -> A (in Ref. 1; AAK92458)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1087 AA; 121149 MW; 03E4E88B93394ED6 CRC64;
MDQGAMETLP EKPSEDEFSL ALRNGLILCN VLNKVNPGSV LKVVENPITP AIQYADGAAQ
SAIQYFENMR NFLKAVEDMQ LLTFGASDLE KGGSSNKVVD CILCLKGFYE WKQAGGVGVW
RYGGTVRIVS FNRKGSSPPQ YGIGSESTTD ESVSLDESES SQYDQLLDFL HLSNEISAEE
SETAISLAFL FDHFALQLLH GYLKESDGIN DMPLNEMVID TLLNRVVKDF SAILVSQGAQ
LGSFLRKILK CDNGDLSRSE FLAAVFRYLQ HRKDLVSKEF SKFCKCGGKL EFSRLNAREF
SPGHVEAIGL QQKELEEVKS NFVETRSQVK QMQSEWQKEL QRIVHHVKAM EVTSSSYHKV
LEENRLLYNE VQDLKGTIRV YCRVRPFFQE QKDMQSTVDY IGENGNIIIN NPFKQEKDAR
KIFSFNKVFG QTVSQEQIYI DTQPVIRSVL DGFNVCIFAY GQTGSGKTYT MSGPDLMTET
TWGVNYRALR DLFQLSNART HVVTYEIGVQ MIEIYNEQVR DLLVSDGSSR RLDIRNNSQL
NGLNVPDANL IPVSNTRDVL DLMRIGQKNR AVGATALNER SSRSHSVLTV HVQGKELASG
SILRGCLHLV DLAGSERVEK SEAVGERLKE AQHINKSLSA LGDVIYALAQ KSSHVPYRNS
KLTQVLQDSL GGQAKTLMFV HINPEVNAVG ETISTLKFAQ RVASIELGAA RSNKETGEIR
DLKDEISSLK SAMEKKEAEL EQLRSGSIRN TTECQRARAV SPFHLPRTGN GAGTKAEASP
QPNDGTRSYE TRSCSTGKQR KSGFPSALRN REASPRMPNL AEERLNPSPS RRSLSTDRAS
TIKSRNKPDV TQNLPVSRTP FPARVPVVKS FSTVPLNPSA ENNHRLHTDN SSEAFQNHQK
LSARKLFPEI EEEHIRHALH IRQGGVKKTR AESSKAKAKQ PSPARFQKLD VGISLRSDAD
SEAKVGNYQT QKGNNNHNVI HSRFQNFDVG ISLFSDLCAG DKSDSTLKSD SSETDNEPPS
KSKNAQRNSS KNSLNHKLRT IYAHEDTSLV DDKPSNGTAH IKEGNNNISM PEFRRSRSTH
HARFMVP
