KN7A_ARATH
ID KN7A_ARATH Reviewed; 974 AA.
AC Q8S905; Q9LPQ5;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Kinesin-like protein KIN-7A {ECO:0000305};
DE AltName: Full=NPK1-activating kinesin-1 {ECO:0000303|PubMed:11955449};
DE Short=AtNACK1 {ECO:0000312|EMBL:BAB88748.1};
DE AltName: Full=Protein HINKEL {ECO:0000303|PubMed:11818068};
GN Name=KIN7A {ECO:0000305};
GN Synonyms=HIK {ECO:0000303|PubMed:11818068},
GN NACK1 {ECO:0000312|EMBL:BAB88748.1};
GN OrderedLocusNames=At1g18370 {ECO:0000312|Araport:AT1G18370};
GN ORFNames=F15H18.12 {ECO:0000312|EMBL:AAF25984.1};
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 DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=11955449; DOI=10.1016/s0092-8674(02)00691-8;
RA Nishihama R., Soyano T., Ishikawa M., Araki S., Tanaka H., Asada T.,
RA Irie K., Ito M., Terada M., Banno H., Yamazaki Y., Machida Y.;
RT "Expansion of the cell plate in plant cytokinesis requires a kinesin-like
RT protein/MAPKKK complex.";
RL Cell 109:87-99(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11818068; DOI=10.1016/s0960-9822(01)00655-8;
RA Strompen G., El Kasmi F., Richter S., Lukowitz W., Assaad F.F.,
RA Juergens G., Mayer U.;
RT "The Arabidopsis HINKEL gene encodes a kinesin-related protein involved in
RT cytokinesis and is expressed in a cell cycle-dependent manner.";
RL Curr. Biol. 12:153-158(2002).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15569152; DOI=10.1111/j.1365-2443.2004.00798.x;
RA Tanaka H., Ishikawa M., Kitamura S., Takahashi Y., Soyano T., Machida C.,
RA Machida Y.;
RT "The AtNACK1/HINKEL and STUD/TETRASPORE/AtNACK2 genes, which encode
RT functionally redundant kinesins, are essential for cytokinesis in
RT Arabidopsis.";
RL Genes Cells 9:1199-1211(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.
RX PubMed=19825582; DOI=10.1093/mp/ssn042;
RA Oh S.A., Bourdon V., Das 'Pal M., Dickinson H., Twell D.;
RT "Arabidopsis kinesins HINKEL and TETRASPORE act redundantly to control cell
RT plate expansion during cytokinesis in the male gametophyte.";
RL Mol. Plant 1:794-799(2008).
RN [9]
RP FUNCTION.
RX PubMed=20802223; DOI=10.1093/pcp/pcq135;
RA Takahashi Y., Soyano T., Kosetsu K., Sasabe M., Machida Y.;
RT "HINKEL kinesin, ANP MAPKKKs and MKK6/ANQ MAPKK, which phosphorylates and
RT activates MPK4 MAPK, constitute a pathway that is required for cytokinesis
RT in Arabidopsis thaliana.";
RL Plant Cell Physiol. 51:1766-1776(2010).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF THR-145; THR-687 AND THR-703.
RX PubMed=22006334; DOI=10.1073/pnas.1110174108;
RA Sasabe M., Boudolf V., De Veylder L., Inze D., Genschik P., Machida Y.;
RT "Phosphorylation of a mitotic kinesin-like protein and a MAPKKK by cyclin-
RT dependent kinases (CDKs) is involved in the transition to cytokinesis in
RT plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:17844-17849(2011).
RN [11]
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 [12]
RP SUBCELLULAR LOCATION.
RX PubMed=23451828; DOI=10.1111/tpj.12160;
RA Krupnova T., Stierhof Y.-D., Hiller U., Strompen G., Mueller S.;
RT "The microtubule-associated kinase-like protein RUNKEL functions in somatic
RT and syncytial cytokinesis.";
RL Plant J. 74:781-791(2013).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=25502072; DOI=10.1007/s10265-014-0687-2;
RA Sasabe M., Ishibashi N., Haruta T., Minami A., Kurihara D., Higashiyama T.,
RA Nishihama R., Ito M., Machida Y.;
RT "The carboxyl-terminal tail of the stalk of Arabidopsis NACK1/HINKEL
RT kinesin is required for its localization to the cell plate formation
RT site.";
RL J. Plant Res. 128:327-336(2015).
RN [14]
RP FUNCTION.
RX PubMed=26745275; DOI=10.1371/journal.pone.0146492;
RA Gillmor C.S., Roeder A.H., Sieber P., Somerville C., Lukowitz W.;
RT "A genetic screen for mutations affecting cell division in the Arabidopsis
RT thaliana embryo identifies seven loci required for cytokinesis.";
RL PLoS ONE 11:E0146492-E0146492(2016).
CC -!- FUNCTION: Probable plus end-directed motor protein that functions in
CC the NACK-PQR (ANP1-MKK6-MPK4) MAP kinase signaling pathway, which is
CC essential for somatic cell cytokinesis, especially for the cell-plate
CC formation and its expansion. Regulates the activity and the
CC localization of ANP1, probably by association through the non-catalytic
CC region of the kinase. Functionally redundant with NACK2 and essential
CC to promote the progression of cytokinesis and for cellularization
CC (formation of the cell plate) during microgametogenesis and
CC megagametogenesis. {ECO:0000269|PubMed:11818068,
CC ECO:0000269|PubMed:11955449, ECO:0000269|PubMed:15569152,
CC ECO:0000269|PubMed:19825582, ECO:0000269|PubMed:20802223,
CC ECO:0000269|PubMed:22006334, ECO:0000303|PubMed:26745275}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:23451828, ECO:0000269|PubMed:25502072}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, flowers, pollen mother cells
CC and embryos. {ECO:0000269|PubMed:15569152}.
CC -!- DEVELOPMENTAL STAGE: Expressed in a patchy pattern during
CC embryogenesis. {ECO:0000269|PubMed:11818068}.
CC -!- PTM: Phosphorylated at Thr-145, Thr-687 and Thr-703 by CDKAs and CDKBs.
CC Phosphorylated NACK1 fails to mediate cytokinesis.
CC {ECO:0000250|UniProtKB:Q8S950}.
CC -!- DISRUPTION PHENOTYPE: Growth defects, dwarf plants with small, humped
CC cotyledons and leaves. Development arrested at the vegetative stage
CC without production of reproductive organs.
CC {ECO:0000269|PubMed:11818068, ECO:0000269|PubMed:11955449,
CC ECO:0000269|PubMed:15569152}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-7 subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF25984.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB081599; BAB88748.1; -; mRNA.
DR EMBL; AC013354; AAF25984.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29708.1; -; Genomic_DNA.
DR RefSeq; NP_173273.2; NM_101695.5.
DR AlphaFoldDB; Q8S905; -.
DR SMR; Q8S905; -.
DR BioGRID; 23657; 2.
DR STRING; 3702.AT1G18370.1; -.
DR PaxDb; Q8S905; -.
DR PRIDE; Q8S905; -.
DR ProteomicsDB; 238228; -.
DR EnsemblPlants; AT1G18370.1; AT1G18370.1; AT1G18370.
DR GeneID; 838418; -.
DR Gramene; AT1G18370.1; AT1G18370.1; AT1G18370.
DR KEGG; ath:AT1G18370; -.
DR Araport; AT1G18370; -.
DR TAIR; locus:2014069; AT1G18370.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_013407_0_0_1; -.
DR InParanoid; Q8S905; -.
DR OMA; WIMGWNP; -.
DR OrthoDB; 122200at2759; -.
DR PhylomeDB; Q8S905; -.
DR PRO; PR:Q8S905; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8S905; baseline and differential.
DR Genevisible; Q8S905; AT.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0009524; C:phragmoplast; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IGI:TAIR.
DR GO; GO:0009558; P:embryo sac cellularization; IGI:TAIR.
DR GO; GO:0048229; P:gametophyte development; IGI:TAIR.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
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; IPR021881; NACK_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF11995; DUF3490; 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 cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Motor protein; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..974
FT /note="Kinesin-like protein KIN-7A"
FT /id="PRO_0000422316"
FT DOMAIN 31..353
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 362..435
FT /evidence="ECO:0000255"
FT COILED 565..603
FT /evidence="ECO:0000255"
FT COMPBIAS 628..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MUTAGEN 145
FT /note="T->A: Inhibition of the function in cytokinesis;
FT when associated with A-687 and A-703."
FT /evidence="ECO:0000269|PubMed:22006334"
FT MUTAGEN 145
FT /note="T->D: Inhibition of the function in cytokinesis;
FT when associated with D-687 and D-703."
FT /evidence="ECO:0000269|PubMed:22006334"
FT MUTAGEN 687
FT /note="T->A: Inhibition of the function in cytokinesis;
FT when associated with A-145 and A-703."
FT /evidence="ECO:0000269|PubMed:22006334"
FT MUTAGEN 687
FT /note="T->D: Inhibition of the function in cytokinesis;
FT when associated with D-145 and D-703."
FT /evidence="ECO:0000269|PubMed:22006334"
FT MUTAGEN 703
FT /note="T->A: Inhibition of the function in cytokinesis;
FT when associated with A-145 and A-687."
FT /evidence="ECO:0000269|PubMed:22006334"
FT MUTAGEN 703
FT /note="T->D: Inhibition of the function in cytokinesis;
FT when associated with D-145 and D-687."
FT /evidence="ECO:0000269|PubMed:22006334"
SQ SEQUENCE 974 AA; 110174 MW; F363210B5DE1D378 CRC64;
MTIKTPGTPV SKMDRTPAVT PGGSSRSREE KIVVTVRLRP MNKRELLAKD QVAWECVNDH
TIVSKPQVQE RLHHQSSFTF DKVFGPESLT ENVYEDGVKN VALSALMGIN ATIFAYGQTS
SGKTYTMRGV TEKAVNDIYN HIIKTPERDF TIKISGLEIY NENVRDLLNS DSGRALKLLD
DPEKGTVVEK LVEETANNDN HLRHLISICE AQRQVGETAL NDTSSRSHQI IRLTIQSTHR
ENSDCVRSYM ASLNFVDLAG SERASQSQAD GTRLREGCHI NLSLMTLTTV IRKLSVGKRS
GHIPYRDSKL TRILQHSLGG NARTAIICTL SPALAHVEQS RNTLYFANRA KEVTNNAHVN
MVVSDKQLVK HLQKEVARLE AERRTPGPST EKDFKIQQME MEIGELRRQR DDAQIQLEEL
RQKLQGDQQQ NKGLNPFESP DPPVRKCLSY SVAVTPSSEN KTLNRNERAR KTTMRQSMIR
QSSTAPFTLM HEIRKLEHLQ EQLGEEATKA LEVLQKEVAC HRLGNQDAAQ TIAKLQAEIR
EMRTVKPSAM LKEVGDVIAP NKSVSANLKE EITRLHSQGS TIANLEEQLE SVQKSIDKLV
MSLPSNISAG DETPKTKNHH HQSKKKKLLP LTPSSASNRQ NFLKSPCSPL SASRQVLDCD
AENKAPQENN SSAARGATTP QGSEKETPQK GEESGDVSSR EGTPGYRRSS SVNMKKMQQM
FQNAAEENVR SIRAYVTELK ERVAKLQYQK QLLVCQVLEL EANDGAGYSV ENEENTIMED
EEQNQVAWHI TFIEERQQII ELWHVCHVSI IHRTQFYLLF KGDQADQIYM EVELRRLTWL
EQHLAEVGNA TPARNCDESV VSLSSSIKAL RREREFLAKR VNSRLTPEER EELYMKWDVP
LEGKQRKLQF VNKLWTDPYD SRHVQESAEI VAKLVGFCES GNISKEMFEL NFAVPSDKRQ
WNIGWDNISN LLHL
