KN7B_ARATH
ID KN7B_ARATH Reviewed; 938 AA.
AC Q8LNZ2; A0A1I9LTQ9; Q8L5J2; Q8LGU3; Q9LXL3;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Kinesin-like protein KIN-7B {ECO:0000305};
DE AltName: Full=NPK1-activating kinesin-2 {ECO:0000303|PubMed:11955449};
DE Short=AtNACK2 {ECO:0000312|EMBL:BAC03248.1};
DE AltName: Full=Protein STUD {ECO:0000303|PubMed:11472632};
DE AltName: Full=Protein TETRASPORE {ECO:0000303|PubMed:12694597};
GN Name=KIN7B {ECO:0000305};
GN Synonyms=NACK2 {ECO:0000312|EMBL:BAC03248.1},
GN STD {ECO:0000303|PubMed:11472632}, TES {ECO:0000312|EMBL:CAD42234.1,
GN ECO:0000312|EMBL:CAD42658.1, ECO:0000312|EMBL:CAD45645.1,
GN ECO:0000312|EMBL:CAD48111.1};
GN OrderedLocusNames=At3g43210 {ECO:0000312|Araport:AT3G43210};
GN ORFNames=F7K15.60 {ECO:0000312|EMBL:CAB89042.1};
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].
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 [GENOMIC DNA / MRNA], FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Col-3, cv. Landsberg erecta, and cv. Wassilewskija-2;
RC TISSUE=Flower;
RX PubMed=12694597; DOI=10.1046/j.1365-313x.2003.01713.x;
RA Yang C.Y., Spielman M., Coles J.P., Li Y., Ghelani S., Bourdon V.,
RA Brown R.C., Lemmon B.E., Scott R.J., Dickinson H.G.;
RT "TETRASPORE encodes a kinesin required for male meiotic cytokinesis in
RT Arabidopsis.";
RL Plant J. 34:229-240(2003).
RN [3]
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 [4]
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9217006; DOI=10.1242/dev.124.13.2645;
RA Spielman M., Preuss D., Li F.L., Browne W.E., Scott R.J., Dickinson H.G.;
RT "TETRASPORE is required for male meiotic cytokinesis in Arabidopsis
RT thaliana.";
RL Development 124:2645-2657(1997).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9224679; DOI=10.1006/dbio.1997.8554;
RA Hulskamp M., Parekh N.S., Grini P., Schneitz K., Zimmermann I., Lolle S.J.,
RA Pruitt R.E.;
RT "The STUD gene is required for male-specific cytokinesis after telophase II
RT of meiosis in Arabidopsis thaliana.";
RL Dev. Biol. 187:114-124(1997).
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
RP FUNCTION, INTERACTION WITH ANP3, AND DISRUPTION PHENOTYPE.
RX PubMed=21575092; DOI=10.1111/j.1365-313x.2011.04642.x;
RA Zeng Q., Chen J.G., Ellis B.E.;
RT "AtMPK4 is required for male-specific meiotic cytokinesis in Arabidopsis.";
RL Plant J. 67:895-906(2011).
RN [13]
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 [14]
RP INTERACTION WITH TIO/FU.
RX PubMed=24146312; DOI=10.1007/s00497-013-0235-6;
RA Oh S.A., Bourdon V., Dickinson H.G., Twell D., Park S.K.;
RT "Arabidopsis Fused kinase TWO-IN-ONE dominantly inhibits male meiotic
RT cytokinesis.";
RL Plant Reprod. 27:7-17(2014).
CC -!- FUNCTION: Probable plus end-directed motor protein that functions in
CC the NACK-PQR (ANP3-MKK6-MPK4) MAP kinase signaling pathway, which is
CC essential for somatic cell cytokinesis, especially for the cell-plate
CC formation and its expansion. May regulate the activity and the
CC localization of ANP3, probably by association through the non-catalytic
CC region of the kinase. Functionally redundant with NACK1 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:12694597,
CC ECO:0000269|PubMed:15569152, ECO:0000269|PubMed:19825582,
CC ECO:0000269|PubMed:20802223, ECO:0000269|PubMed:21575092,
CC ECO:0000269|PubMed:9217006, ECO:0000269|PubMed:9224679}.
CC -!- SUBUNIT: Interacts with ANP3 (PubMed:21575092). Interacts with TIO/FU
CC (PubMed:24146312). {ECO:0000269|PubMed:21575092,
CC ECO:0000269|PubMed:24146312}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000250|UniProtKB:Q8S905}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, flowers, pollen mother
CC cells and embryos. {ECO:0000269|PubMed:15569152}.
CC -!- DISRUPTION PHENOTYPE: Enlarged pollen grains containing four vegetative
CC nuclei and up to eight sperm cells. Short siliques with low fertility.
CC {ECO:0000269|PubMed:12694597, ECO:0000269|PubMed:15569152,
CC ECO:0000269|PubMed:21575092, ECO:0000269|PubMed:9217006,
CC ECO:0000269|PubMed:9224679}.
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=CAB89042.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAD42234.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD42658.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD45645.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD48111.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB088121; BAC03248.1; -; mRNA.
DR EMBL; AJ495781; CAD42234.1; ALT_INIT; mRNA.
DR EMBL; AJ496182; CAD42658.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ508243; CAD48111.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ507734; CAD45645.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL353871; CAB89042.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE77774.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65967.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65968.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65969.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65970.1; -; Genomic_DNA.
DR PIR; T49235; T49235.
DR RefSeq; NP_001319676.1; NM_001339092.1.
DR RefSeq; NP_001327899.1; NM_001339094.1.
DR RefSeq; NP_001327900.1; NM_001339093.1.
DR RefSeq; NP_001327901.1; NM_001339095.1.
DR RefSeq; NP_189907.2; NM_114189.3.
DR AlphaFoldDB; Q8LNZ2; -.
DR SMR; Q8LNZ2; -.
DR BioGRID; 8718; 2.
DR STRING; 3702.AT3G43210.1; -.
DR iPTMnet; Q8LNZ2; -.
DR PaxDb; Q8LNZ2; -.
DR PRIDE; Q8LNZ2; -.
DR ProteomicsDB; 250697; -.
DR EnsemblPlants; AT3G43210.1; AT3G43210.1; AT3G43210.
DR EnsemblPlants; AT3G43210.2; AT3G43210.2; AT3G43210.
DR EnsemblPlants; AT3G43210.3; AT3G43210.3; AT3G43210.
DR EnsemblPlants; AT3G43210.4; AT3G43210.4; AT3G43210.
DR EnsemblPlants; AT3G43210.5; AT3G43210.5; AT3G43210.
DR GeneID; 823396; -.
DR Gramene; AT3G43210.1; AT3G43210.1; AT3G43210.
DR Gramene; AT3G43210.2; AT3G43210.2; AT3G43210.
DR Gramene; AT3G43210.3; AT3G43210.3; AT3G43210.
DR Gramene; AT3G43210.4; AT3G43210.4; AT3G43210.
DR Gramene; AT3G43210.5; AT3G43210.5; AT3G43210.
DR KEGG; ath:AT3G43210; -.
DR Araport; AT3G43210; -.
DR TAIR; locus:2084701; AT3G43210.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_013407_0_0_1; -.
DR InParanoid; Q8LNZ2; -.
DR OMA; EREMLYM; -.
DR OrthoDB; 122200at2759; -.
DR PhylomeDB; Q8LNZ2; -.
DR PRO; PR:Q8LNZ2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8LNZ2; baseline and differential.
DR Genevisible; Q8LNZ2; AT.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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; ISS:TAIR.
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:0007112; P:male meiosis cytokinesis; IMP:TAIR.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0010245; P:radial microtubular system formation; IMP: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 Reference proteome.
FT CHAIN 1..938
FT /note="Kinesin-like protein KIN-7B"
FT /id="PRO_0000422317"
FT DOMAIN 29..348
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 450..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 357..431
FT /evidence="ECO:0000255"
FT COILED 555..590
FT /evidence="ECO:0000255"
FT COMPBIAS 463..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 649
FT /note="A -> I (in Ref. 2; CAD42658/CAD45645)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="Q -> P (in Ref. 2; CAD42658/CAD45645)"
FT /evidence="ECO:0000305"
FT CONFLICT 748
FT /note="Q -> R (in Ref. 2; CAD42658/CAD45645)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 938 AA; 106521 MW; 8C570771E1040C78 CRC64;
MMGPPRTPLS KIDKSNPYTP CGSKVTEEKI LVTVRMRPLN WREHAKYDLI AWECPDDETI
VFKNPNPDKA PTKYSFDKVF EPTCATQEVY EGGSRDVALS ALAGTNATIF AYGQTSSGKT
FTMRGVTESV VKDIYEHIRK TQERSFVLKV SALEIYNETV VDLLNRDTGP LRLLDDPEKG
TIVENLVEEV VESRQHLQHL ISICEDQRQV GETALNDKSS RSHQIIRLTI HSSLREIAGC
VQSFMATLNL VDLAGSERAF QTNADGLRLK EGSHINRSLL TLTTVIRKLS SGRKRDHVPY
RDSKLTRILQ NSLGGNARTA IICTISPALS HVEQTKKTLS FAMSAKEVTN CAKVNMVVSE
KKLLKHLQQK VAKLESELRS PEPSSSTCLK SLLIEKEMKI QQMESEMKEL KRQRDIAQSE
LDLERKAKER KGSSECEPFS QVARCLSYHT KEESIPSKSV PSSRRTARDR RKDNVRQSLT
SADPTALVQE IRLLEKHQKK LGEEANQALD LIHKEVTSHK LGDQQAAEKV AKMLSEIRDM
QKSNLLTEEI VVGDKANLKE EINRLNSQEI AALEKKLECV QNTIDMLVSS FQTDEQTPDF
RTQVKKKRLL PFGLSNSPNL QHMIRGPCSP LSGTENKDPE SNVVSANSAP VSFGATPPKR
DDNRCRTQSR EGTPVSRQAN SVDIKRMNRM YKNAAEENIR NIKSYVTGLK ERVAKLQYQK
QLLVCQVLEL EANETGAASE YDATDESQMD WPLCFEEQRK QIIMLWHLCH ISIIHRTQFY
MLFKGDPADQ IYMEVELRRL TWLEQHLAEL GNASPALLGD EPASYVASSI RALKQEREYL
AKRVNTKLGA EEREMLYLKW DVPPVGKQRR QQFINKLWTD PHNMQHVRES AEIVAKLVGF
CDSGETIRKE MFELNFASPS DKKTWMMGWN FISNLLHL
