KN5A_ARATH
ID KN5A_ARATH Reviewed; 1042 AA.
AC F4IIS5; Q9SIB3;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Kinesin-like protein KIN-5A {ECO:0000305};
DE AltName: Full=AtKRP125c {ECO:0000303|PubMed:11472632};
DE AltName: Full=Protein LOOPHOLE {ECO:0000303|PubMed:22038119};
DE AltName: Full=Protein RADIALLY SWOLLEN 7 {ECO:0000303|PubMed:12361973};
GN Name=KIN5A {ECO:0000305};
GN Synonyms=LPH {ECO:0000303|PubMed:22038119},
GN RSW7 {ECO:0000303|PubMed:12361973};
GN OrderedLocusNames=At2g28620 {ECO:0000312|Araport:AT2G28620};
GN ORFNames=T8O18.9 {ECO:0000312|EMBL:AAD24373.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 DISRUPTION PHENOTYPE.
RX PubMed=12361973; DOI=10.1242/dev.129.20.4821;
RA Wiedemeier A.M., Judy-March J.E., Hocart C.H., Wasteneys G.O.,
RA Williamson R.E., Baskin T.I.;
RT "Mutant alleles of Arabidopsis RADIALLY SWOLLEN 4 and 7 reduce growth
RT anisotropy without altering the transverse orientation of cortical
RT microtubules or cellulose microfibrils.";
RL Development 129:4821-4830(2002).
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 REVIEW.
RX PubMed=16530461; DOI=10.1016/j.tplants.2006.02.004;
RA Vanstraelen M., Inze D., Geelen D.;
RT "Mitosis-specific kinesins in Arabidopsis.";
RL Trends Plant Sci. 11:167-175(2006).
RN [7]
RP FUNCTION, MUTAGENESIS OF GLU-280, AND SUBCELLULAR LOCATION.
RX PubMed=17652157; DOI=10.1242/jcs.009506;
RA Bannigan A., Scheible W.R., Lukowitz W., Fagerstrom C., Wadsworth P.,
RA Somerville C., Baskin T.I.;
RT "A conserved role for kinesin-5 in plant mitosis.";
RL J. Cell Sci. 120:2819-2827(2007).
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).
RN [9]
RP MUTAGENESIS OF GLY-359, AND 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: Responsible for microtubule translocation. May be important
CC for the organization of phragmoplast-specific arrays of microtubules
CC (By similarity). Plays an essential role in stabilizing the mitotic
CC spindle (PubMed:17652157). Required during mitotic cytokinesis
CC (PubMed:26745275). {ECO:0000250|UniProtKB:O23826,
CC ECO:0000269|PubMed:17652157, ECO:0000269|PubMed:26745275}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17652157}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:17652157}. Note=Microtubule-associated.
CC {ECO:0000269|PubMed:17652157}.
CC -!- DISRUPTION PHENOTYPE: Radially swollen roots without any depletion or
CC disorientation of cortical microtubules or cellulose microfibrils.
CC {ECO:0000269|PubMed:12361973}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-5/BimC subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD24373.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007171; AAD24373.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08150.1; -; Genomic_DNA.
DR PIR; B84687; B84687.
DR RefSeq; NP_180430.2; NM_128423.2.
DR AlphaFoldDB; F4IIS5; -.
DR SMR; F4IIS5; -.
DR STRING; 3702.AT2G28620.1; -.
DR PaxDb; F4IIS5; -.
DR PRIDE; F4IIS5; -.
DR EnsemblPlants; AT2G28620.1; AT2G28620.1; AT2G28620.
DR GeneID; 817411; -.
DR Gramene; AT2G28620.1; AT2G28620.1; AT2G28620.
DR KEGG; ath:AT2G28620; -.
DR Araport; AT2G28620; -.
DR TAIR; locus:2065505; AT2G28620.
DR eggNOG; KOG0243; Eukaryota.
DR HOGENOM; CLU_001485_33_0_1; -.
DR InParanoid; F4IIS5; -.
DR PRO; PR:F4IIS5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IIS5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:UniProtKB.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
DR GO; GO:0009826; P:unidimensional cell growth; 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; IPR027417; P-loop_NTPase.
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; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1042
FT /note="Kinesin-like protein KIN-5A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000436268"
FT DOMAIN 50..392
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 480..517
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MUTAGEN 280
FT /note="E->K: In rsw7-1: Disorganized cortical microtubules
FT during interphase and massive disrupted mitotic spindles."
FT /evidence="ECO:0000269|PubMed:17652157"
FT MUTAGEN 359
FT /note="G->R: In rsw7-lph: Short and swollen seedlings. No
FT functional apical meristems and only rudimentary
FT cotyledons. Cellular abnormalities like cell wall stubs or
FT incomplete, gapped cell walls. Affected mitosis in the male
FT gametophyte."
FT /evidence="ECO:0000269|PubMed:26745275"
SQ SEQUENCE 1042 AA; 116223 MW; C9063E8407AB6585 CRC64;
MDSNNSKKGS SVKSPCQTPR STEKSNRDFR VDSNSNSNPV SKNEKEKGVN IQVIVRCRPF
NSEETRLQTP AVLTCNDRKK EVAVAQNIAG KQIDKTFLFD KVFGPTSQQK DLYHQAVSPI
VFEVLDGYNC TIFAYGQTGT GKTYTMEGGA RKKNGEIPSD AGVIPRAVKQ IFDILEAQSA
AEYSLKVSFL ELYNEELTDL LAPEETKFAD DKSKKPLALM EDGKGGVFVR GLEEEIVSTA
DEIYKVLEKG SAKRRTAETL LNKQSSRSHS IFSVTIHIKE CTPEGEEIVK SGKLNLVDLA
GSENISRSGA REGRAREAGE INKSLLTLGR VINALVEHSG HIPYRESKLT RLLRDSLGGK
TKTCVIATVS PSVHCLEETL STLDYAHRAK HIKNKPEVNQ KMMKSAIMKD LYSEIERLKQ
EVYAAREKNG IYIPKERYTQ EEAEKKAMAD KIEQMEVEGE AKDKQIIDLQ ELYNSEQLVT
AGLREKLDKT EKKLYETEQA LLDLEEKHRQ AVATIKEKEY LISNLLKSEK TLVDRAVELQ
AELANAASDV SNLFAKIGRK DKIEDSNRSL IQDFQSQLLR QLELLNNSVA GSVSQQEKQL
QDMENVMVSF VSAKTKATET LRGSLAQLKE KYNTGIKSLD DIAGNLDKDS QSTLNDLNSE
VTKHSCALED MFKGFTSEAY TLLEGLQGSL HNQEEKLSAF TQQQRDLHSR SMDSAKSVST
VMLDFFKTLD THANKLTKLA EDAQNVNEQK LSAFTKKFEE SIANEEKQML EKVAELLASS
NARKKELVQI AVQDIRQGSS SQTGALQQEM SAMQDSASSI KVQWNSHIVQ AESHHLDNIS
AVEVAKEDMQ KMHLKCLENS KTGTQQWKTA QESLVDLEKR NVATADSIIR GAIENNEKLR
TQFSSAVSTT LSDVDSSNRE IISSIDNSLQ LDKDASTDVN STIVPCSENL KELRTHHDDN
VVEIKQNTGK CLGHEYKVDE ATSSTPRKRE YNIPTVGSIE ELKTPSFEEL LKAFHDCKSP
KQMQNGEAKH VSNGRPPLTA IN
