KN13B_ARATH
ID KN13B_ARATH Reviewed; 684 AA.
AC Q940Y8; Q9LW81;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Kinesin-like protein KIN-13B {ECO:0000305};
DE AltName: Full=AtKINESIN-13B {ECO:0000303|PubMed:25232944};
DE Short=AtKIN13B {ECO:0000303|PubMed:25232944};
GN Name=KIN13B {ECO:0000305};
GN Synonyms=KINESIN-13B {ECO:0000303|PubMed:25232944};
GN OrderedLocusNames=At3g16060 {ECO:0000312|Araport:AT3G16060,
GN ECO:0000312|EMBL:AEE75767.1};
GN ORFNames=MSL1.9 {ECO:0000312|EMBL:BAB02671.1};
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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [7]
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25232944; DOI=10.1371/journal.pgen.1004627;
RA Fujikura U., Elsaesser L., Breuninger H., Sanchez-Rodriguez C., Ivakov A.,
RA Laux T., Findlay K., Persson S., Lenhard M.;
RT "Atkinesin-13A modulates cell-wall synthesis and cell expansion in
RT Arabidopsis thaliana via the THESEUS1 pathway.";
RL PLoS Genet. 10:E1004627-E1004627(2014).
CC -!- FUNCTION: Acts redundantly with KIN13A to modulate cell wall synthesis
CC and cell expansion via the THE1 pathway. {ECO:0000269|PubMed:25232944}.
CC -!- DISRUPTION PHENOTYPE: Enlarged petals and leaves.
CC {ECO:0000269|PubMed:25232944}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-13 subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02671.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB012247; BAB02671.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75767.1; -; Genomic_DNA.
DR EMBL; AY052352; AAK96543.1; -; mRNA.
DR EMBL; AY059654; AAL31147.1; -; mRNA.
DR RefSeq; NP_566534.1; NM_112476.3.
DR AlphaFoldDB; Q940Y8; -.
DR SMR; Q940Y8; -.
DR IntAct; Q940Y8; 1.
DR STRING; 3702.AT3G16060.1; -.
DR iPTMnet; Q940Y8; -.
DR PaxDb; Q940Y8; -.
DR PRIDE; Q940Y8; -.
DR ProteomicsDB; 237096; -.
DR EnsemblPlants; AT3G16060.1; AT3G16060.1; AT3G16060.
DR GeneID; 820851; -.
DR Gramene; AT3G16060.1; AT3G16060.1; AT3G16060.
DR KEGG; ath:AT3G16060; -.
DR Araport; AT3G16060; -.
DR TAIR; locus:2093382; AT3G16060.
DR eggNOG; KOG0246; Eukaryota.
DR HOGENOM; CLU_001485_19_2_1; -.
DR InParanoid; Q940Y8; -.
DR OMA; NEYYMEP; -.
DR OrthoDB; 418348at2759; -.
DR PhylomeDB; Q940Y8; -.
DR PRO; PR:Q940Y8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q940Y8; baseline and differential.
DR GO; GO:0005874; C: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:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007019; P:microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:1903338; P:regulation of cell wall organization or biogenesis; 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; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..684
FT /note="Kinesin-like protein KIN-13B"
FT /id="PRO_0000437199"
FT DOMAIN 169..492
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 596..626
FT /evidence="ECO:0000255"
FT COMPBIAS 72..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 258..265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 684 AA; 76772 MW; B7BB09F56686661D CRC64;
MSGRQRSVAA AVHHQRQLSD NPLDMSSSNG RWLQSTGLQH FQSSANDYGY YAGGQGGGGQ
AARGYQNAQR GNEFFGEPTT PQYGARPTNQ RKNNDESEFS PGLLDLHSFD TELLPEIPVS
NQLDGPSLFN PSQGQSFDDF EAYNKQPNRS RVLAENLAAE KERMNAVAKI KVVVRKRPLN
KKESTKNEED IVDTHANCLT VHETKLKVDL TAYVEKHEFV FDAVLDEEVS NDEVYRETVE
PVVPLIFQRI KATCFAYGQT GSGKTYTMKP LPLKASRDIL RLMHHTYRNQ GFQLFVSFFE
IYGGKLYDLL SERKKLCMRE DGKQQVCIVG LQEYRVSDTD AIMELIERGS ATRSTGTTGA
NEESSRSHAI LQLAIKKSVE GNQSKPPRLV GKLSFIDLAG SERGADTTDN DKQTRLEGAE
INKSLLALKE CIRALDNDQG HIPFRGSKLT EVLRDSFMGN SRTVMISCIS PSSGSCEHTL
NTLRYADRVK SLSKGNASKK DVSSSTMNLR ESTKIPLSSA LPTPSNFDDD VNEMWTEEND
EFDASDYEQD KQMWKKNGKL EPSYNGMAQE RIPKPTIQMK SRDMPRPDMK KSNSDDNLNA
LLQEEEDLVN AHRKQVEDTM NIVKEEMNLL VEADQPGNQL DGYISRLNTI LSQKAAGILQ
LQNRLAHFQK RLREHNVLVS TTGY
