KN12C_ARATH
ID KN12C_ARATH Reviewed; 2066 AA.
AC Q27IK7; Q9LUT5;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Kinesin-like protein KIN-12C {ECO:0000305};
DE AltName: Full=Phragmoplast orienting kinesin 1 {ECO:0000303|PubMed:16682350};
GN Name=KIN12C {ECO:0000305}; Synonyms=POK1 {ECO:0000312|EMBL:ABD62996.1};
GN OrderedLocusNames=At3g17360 {ECO:0000312|Araport:AT3G17360};
GN ORFNames=MGD8.20 {ECO:0000312|EMBL:BAB02740.1};
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], TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP FUNCTION, AND INTERACTION WITH TAN.
RX PubMed=16682350; DOI=10.1016/j.cub.2006.03.034;
RA Muller S., Han S., Smith L.G.;
RT "Two kinesins are involved in the spatial control of cytokinesis in
RT Arabidopsis thaliana.";
RL Curr. Biol. 16:888-894(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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 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 INTERACTION WITH RANGAP1 AND TAN.
RX PubMed=19011093; DOI=10.1073/pnas.0806157105;
RA Xu X.M., Zhao Q., Rodrigo-Peiris T., Brkljacic J., He C.S., Mueller S.,
RA Meier I.;
RT "RanGAP1 is a continuous marker of the Arabidopsis cell division plane.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18637-18642(2008).
RN [8]
RP INTERACTION WITH TAN, AND FUNCTION.
RX PubMed=21172800; DOI=10.1242/jcs.073676;
RA Rasmussen C.G., Sun B., Smith L.G.;
RT "Tangled localization at the cortical division site of plant cells occurs
RT by several mechanisms.";
RL J. Cell Sci. 124:270-279(2011).
RN [9]
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: Involved in the spatial control of cytokinesis by a proper
CC phragmoplast guidance. Localizes TAN to the cortical division sites
CC (CDS) during cytokinesis via direct binding.
CC {ECO:0000269|PubMed:16682350, ECO:0000269|PubMed:21172800}.
CC -!- SUBUNIT: Interacts with TAN. Interacts with RANGAP1.
CC {ECO:0000269|PubMed:16682350, ECO:0000269|PubMed:19011093,
CC ECO:0000269|PubMed:21172800}.
CC -!- INTERACTION:
CC Q27IK7; Q9LE82: RANGAP1; NbExp=2; IntAct=EBI-6881384, EBI-1779351;
CC Q27IK7; Q84M91: TAN; NbExp=2; IntAct=EBI-6881384, EBI-6881406;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in tissues enriched in dividing cells,
CC such as root meristems, root primordia, and leaf primordia/young
CC leaves. {ECO:0000269|PubMed:16682350}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Pok1 and pok2 double mutant
CC dissplays smaller cotyledons as well as shorter, wider roots and
CC hypocotyls with adult plants exhibiting a dwarfed stature and producing
CC reduced numbers of seeds. {ECO:0000269|PubMed:16682350}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-12 subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02740.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ399529; ABD62996.1; -; mRNA.
DR EMBL; AB022216; BAB02740.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75943.1; -; Genomic_DNA.
DR RefSeq; NP_188362.2; NM_112614.4.
DR AlphaFoldDB; Q27IK7; -.
DR SMR; Q27IK7; -.
DR DIP; DIP-46422N; -.
DR IntAct; Q27IK7; 2.
DR STRING; 3702.AT3G17360.1; -.
DR PaxDb; Q27IK7; -.
DR PRIDE; Q27IK7; -.
DR EnsemblPlants; AT3G17360.1; AT3G17360.1; AT3G17360.
DR GeneID; 820999; -.
DR Gramene; AT3G17360.1; AT3G17360.1; AT3G17360.
DR KEGG; ath:AT3G17360; -.
DR Araport; AT3G17360; -.
DR TAIR; locus:2089000; AT3G17360.
DR eggNOG; ENOG502QR1R; Eukaryota.
DR HOGENOM; CLU_000399_1_1_1; -.
DR InParanoid; Q27IK7; -.
DR PhylomeDB; Q27IK7; -.
DR PRO; PR:Q27IK7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q27IK7; baseline and differential.
DR Genevisible; Q27IK7; AT.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IGI:TAIR.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
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..2066
FT /note="Kinesin-like protein KIN-12C"
FT /id="PRO_0000423588"
FT DOMAIN 168..505
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..379
FT /note="Microtubules-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9LDN0"
FT REGION 406..412
FT /note="Microtubules-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9LDN0"
FT REGION 454..458
FT /note="Microtubules-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9LDN0"
FT REGION 1803..1823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2043..2066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1521..1618
FT /evidence="ECO:0000255"
FT COILED 1650..1772
FT /evidence="ECO:0000255"
FT COILED 1905..2051
FT /evidence="ECO:0000255"
FT COMPBIAS 18..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 249..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 2066 AA; 233879 MW; 99A2D185052C8379 CRC64;
MSRNVPRIEM PESEENEFAS LSLFSPSRPP LNSIPDPSQI QKANHLPHFD LVQKLEGTRA
QHQRTLGPEK KFEVLEGRAG NSSDSNPKIV NRNGKSRSEP NSAQSTPTRN GARVSLGGGC
ATGARFLQSF GGRGRIPRGV SIAESVSFAE TTPHFELNED HSFWKDHNVQ VLIRLRPLGT
MERANQGYGK CLKQESPQTL VWLGHPEARF TFDHVASETI SQEKLFRVAG LPMVENCLSG
YNSCVFAYGQ TGSGKTYTMM GEISEAEGSL GEDCGVTARI FEYLFSRIKM EEEERRDENL
KFSCKCSFLE IYNEQITDLL EPSSTNLQLR EDLGKGVYVE NLVEHNVRTV SDVLKLLLQG
ATNRKIAATR MNSESSRSHS VFTCTIESLW EKDSLTRSRF ARLNLVDLAG SERQKSSGAE
GDRLKEAANI NKSLSTLGLV IMSLVDLAHG KHRHVPYRDS RLTFLLQDSL GGNSKTMIIA
NVSPSLCSTN ETLSTLKFAQ RAKLIQNNAK VNEDASGDVT ALQQEIRKLK VQLTSLLKNH
DSCGALSDCI SSLEESRYSG TCKVAGETRQ DKCHCQVKNM NDNMIGALRR EKIAESALQK
SEAEIERIDC LVRDMEEDAK RIKIMLNLRE EKVGEMEFCT SGSLMTKECL IEENKTLKGE
IKLLRDSIDK NPELTRSALE NTKLREQLQR YQKFYEHGER EALLAEVTGL RDQLLDVLEA
KDESFSKHVM KENEMEKEFE DCRNMNSSLI RELDEIQAGL GRYLNFDQIQ SNVVASSTRG
AEQAETMPTI SEIQEEVAIS HSKNYDRGAL VKTDEGIDRS ILQFKLGKLM KDLEEARTLN
CKYEKDHKSQ LSQQEDIEVV REQVETETAR TILELQEEVI ALQSEFQRRI CNLTEENQSI
KDTITARESE IRALNQDWEK ATLELTNFIV AGSKSIKNAS TQIESIICSF PQVNAWIGDY
VEKAAKNCIK KEETILLLQK SLEDARILVA EMNLKLNSLK GATIALNEFQ LGGNAATTEE
AFNLNNDVDR MSDEVDTLES NFKANQYSIL KTERHAEAAL AVTKWLSDSR DQHQMMEKVQ
DQSVKEFGTL SSISASLSAE GNADISLSRD GHLSDATYPK GDELSTSSSD FSNCRWQHDC
ALNVKCQGVS SSESDAQESN NKITSAALIA KNGSAHSVYC GEGRQSVEKP LTIMMGREET
EYKCSKPLSS GVYMGLMQRM DPVRTFFDRF EEVNATMKEA DLTICELVKA NEKSNSVTEM
WLQTHEELIS KEKNLMDDLE QVKSILSACE EEKQVLLNQT HTTLADMENS VSLLEEYFQE
MKRGVEETVE ALFSHARLAG KELLQLISNS RPSLEQIASE FMEREFTMYA TYQCHIGKLI
DQILDQRKQV ITPNLSGQET NQSVKINAIG YNAEDEVTKK QSREEIVTGL ENDEVVQSHE
SLLYENLYLK KELERKEALF EGLLFDFRLL QESASNKRDI KNEMDELFDA LCKVQLELEL
KASQVHELFV HNENLENCSI DLKTALFTSQ SDLEQAKQRI QILAEQNDEL RALVSDLCKE
KAAAEEGLDE QRDLVNRLEK EILHLTTTAE KQLLSAVKSI KENLKKTSDE KDQIVDEICS
LNNKLELAYA IADEKEAIAV EAHQESEASK IYAEQKEEEV KILEISVEEL ERTINILERR
VYDMDEEVKR HRTTQDSLET ELQALRQRLF RFENFTGTMV TTNESTEEYK SHISRSTGLQ
GAHSQIQVLQ KEVAEQTKEI KQLKEYISEI LLHSEAQSSA YQEKYKTLEV MIRDFKLEDS
SSSAAETISH KTEKSSTRSR GSSSPFRCIV GLVQQMKLEK DQELTMARVR VEELESLLAV
KQKEICTLNT RIAAADSMTH DVIRDLLGVK MDITSYAELI DQHQVQRVVE KAQQHAEEIL
SKEQEVMNLK RHIDYLFKDR ESCMSELNKK DTDVLATQIS LDQLQERVQL LSMQNEMLKN
DKSNLLRKLA ELDRTVHNAQ ASNHRVPQTT KDTASFKLAD TDYTKRLENA QKLLSHANNE
LAKYRKTSNN HPSTRTQGQS SGTRYR
