KN13A_ARATH
ID KN13A_ARATH Reviewed; 794 AA.
AC Q940B8; Q56WU1; Q9LUS1;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Kinesin-like protein KIN-13A {ECO:0000305};
DE AltName: Full=AtKINESIN-13A {ECO:0000303|PubMed:15574882, ECO:0000303|PubMed:25232944};
DE Short=AtKIN13A {ECO:0000303|PubMed:25232944};
GN Name=KIN13A {ECO:0000303|PubMed:25232944, ECO:0000305};
GN Synonyms=KINESIN-13A {ECO:0000303|PubMed:15574882};
GN OrderedLocusNames=At3g16630 {ECO:0000312|Araport:AT3G16630};
GN ORFNames=MGL6.9 {ECO:0000312|EMBL:BAB02754.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=15574882; DOI=10.1091/mbc.e04-05-0400;
RA Lu L., Lee Y.R., Pan R., Maloof J.N., Liu B.;
RT "An internal motor kinesin is associated with the Golgi apparatus and plays
RT a role in trichome morphogenesis in Arabidopsis.";
RL Mol. Biol. Cell 16:811-823(2005).
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19939242; DOI=10.1186/1471-2229-9-138;
RA Wei L., Zhang W., Liu Z., Li Y.;
RT "AtKinesin-13A is located on Golgi-associated vesicle and involved in
RT vesicle formation/budding in Arabidopsis root-cap peripheral cells.";
RL BMC Plant Biol. 9:138-138(2009).
RN [9]
RP INTERACTION WITH ICR2 AND ICR5, AND SUBCELLULAR LOCATION.
RX PubMed=20832900; DOI=10.1016/j.ejcb.2010.08.003;
RA Mucha E., Hoefle C., Huckelhoven R., Berken A.;
RT "RIP3 and AtKinesin-13A - a novel interaction linking Rho proteins of
RT plants to microtubules.";
RL Eur. J. Cell Biol. 89:906-916(2010).
RN [10]
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 [11]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH ICR5,
RP SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=24280391; DOI=10.1105/tpc.113.117853;
RA Oda Y., Fukuda H.;
RT "Rho of plant GTPase signaling regulates the behavior of Arabidopsis
RT kinesin-13A to establish secondary cell wall patterns.";
RL Plant Cell 25:4439-4450(2013).
RN [12]
RP MUTAGENESIS OF LEU-334, DISRUPTION PHENOTYPE, AND FUNCTION.
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: Internal motor kinesin involved in trichome morphogenesis
CC (PubMed:15574882). Participates in regulating the formation of Golgi-
CC associated vesicles (PubMed:19939242). Plays a central role in
CC microtubule disassembly via the active ARAC10-ICR5 cascade, which
CC establishes the secondary cell wall pattern in metaxylem vessel cells
CC (PubMed:24280391). Acts redundantly with KIN13B to modulate cell wall
CC synthesis and cell expansion via the THE1 pathway (PubMed:25232944).
CC {ECO:0000269|PubMed:15574882, ECO:0000269|PubMed:19939242,
CC ECO:0000269|PubMed:24280391, ECO:0000269|PubMed:25232944}.
CC -!- SUBUNIT: Component of the active ARAC10-IRC5-KIN13A complex
CC (PubMed:24280391). Interacts (via-C-terminus) with ICR2 and ICR5 (via
CC N-terminus). No interactions with ICR1 (PubMed:20832900,
CC PubMed:24280391). {ECO:0000269|PubMed:20832900,
CC ECO:0000269|PubMed:24280391}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack
CC {ECO:0000269|PubMed:15574882, ECO:0000269|PubMed:19939242}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:20832900,
CC ECO:0000269|PubMed:24280391}. Note=Localized to cortical microtubules
CC in secondary wall pits when associated with ICR5. The N-terminal region
CC of the protein is required for its localization at microtubules, but
CC the truncated protein can be recruited to microtubules upon interaction
CC with ICR5. {ECO:0000269|PubMed:20832900, ECO:0000269|PubMed:24280391}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, young and mature
CC seedlings (PubMed:15574882, PubMed:19939242). Preferentially expressed
CC in the secondary cell wall pits of differentiating metaxylem vessel
CC cells (at the protein level) (PubMed:24280391).
CC {ECO:0000269|PubMed:15574882, ECO:0000269|PubMed:19939242,
CC ECO:0000269|PubMed:24280391}.
CC -!- DISRUPTION PHENOTYPE: No obvious growth phenotype, but leaf trichomes
CC with 4 branches instead of 3 and decreased size and number of Golgi-
CC associated vesicles in root-cap peripheral cells (PubMed:15574882,
CC PubMed:19939242). Smaller pits in the secondary cell walls of root
CC metaxylem vessels (PubMed:24280391). Enlarged petals and overbranched
CC trichomes (PubMed:25232944). {ECO:0000269|PubMed:15574882,
CC ECO:0000269|PubMed:19939242, ECO:0000269|PubMed:24280391,
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=BAB02754.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB022217; BAB02754.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75845.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75846.1; -; Genomic_DNA.
DR EMBL; AY056129; AAL07208.1; -; mRNA.
DR EMBL; AK226569; BAE98696.1; -; mRNA.
DR EMBL; AK221940; BAD94391.1; -; mRNA.
DR RefSeq; NP_188285.1; NM_112536.3.
DR RefSeq; NP_850598.1; NM_180267.2.
DR AlphaFoldDB; Q940B8; -.
DR SMR; Q940B8; -.
DR BioGRID; 6249; 3.
DR IntAct; Q940B8; 1.
DR STRING; 3702.AT3G16630.1; -.
DR iPTMnet; Q940B8; -.
DR PaxDb; Q940B8; -.
DR PRIDE; Q940B8; -.
DR ProteomicsDB; 237106; -.
DR EnsemblPlants; AT3G16630.1; AT3G16630.1; AT3G16630.
DR EnsemblPlants; AT3G16630.2; AT3G16630.2; AT3G16630.
DR GeneID; 820915; -.
DR Gramene; AT3G16630.1; AT3G16630.1; AT3G16630.
DR Gramene; AT3G16630.2; AT3G16630.2; AT3G16630.
DR KEGG; ath:AT3G16630; -.
DR Araport; AT3G16630; -.
DR TAIR; locus:2089358; AT3G16630.
DR eggNOG; KOG0246; Eukaryota.
DR HOGENOM; CLU_001485_19_0_1; -.
DR InParanoid; Q940B8; -.
DR OMA; PFIPKEM; -.
DR OrthoDB; 418348at2759; -.
DR PhylomeDB; Q940B8; -.
DR PRO; PR:Q940B8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q940B8; baseline and differential.
DR Genevisible; Q940B8; AT.
DR GO; GO:0005795; C:Golgi stack; IDA:TAIR.
DR GO; GO:0005874; C:microtubule; IDA:TAIR.
DR GO; GO:0009531; C:secondary cell wall; 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; IBA:GO_Central.
DR GO; GO:0090058; P:metaxylem development; IMP:UniProtKB.
DR GO; GO:0007019; P:microtubule depolymerization; IDA:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:1903338; P:regulation of cell wall organization or biogenesis; IMP:UniProtKB.
DR GO; GO:0010090; P:trichome morphogenesis; 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; Golgi apparatus;
KW Microtubule; Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..794
FT /note="Kinesin-like protein KIN-13A"
FT /id="PRO_0000425453"
FT DOMAIN 193..526
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 525..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 705..742
FT /evidence="ECO:0000255"
FT COMPBIAS 525..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 282..289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MUTAGEN 334
FT /note="L->F: In kin13a-3: Enhanced petals and leaves size
FT and overbranched trichomes."
FT /evidence="ECO:0000269|PubMed:25232944"
FT CONFLICT 684
FT /note="E -> G (in Ref. 4; BAD94391)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 794 AA; 89082 MW; 13CBD4DDBEE2454B CRC64;
MGGQMQQNNA AAATALYDGA LPTNDAGDAV MARWLQSAGL QHLASPVAST GNDQRHLPNL
LMQGYGAQTA EEKQRLFQLM RNLNFNGEST SESYTPTAHT SAAMPSSEGF FSPEFRGDFG
AGLLDLHAMD DTELLSEHVI TEPFEPSPFM PSVNKEFEED YNLAANRQQR QQTEAEPLGL
LPKSDKENNS VAKIKVVVRK RPLNKKETAK KEEDVVTVSD NSLTVHEPRV KVDLTAYVEK
HEFCFDAVLD EDVSNDEVYR ATIEPIIPII FQRTKATCFA YGQTGSGKTF TMKPLPIRAV
EDLMRLLRQP VYSNQRFKLW LSYFEIYGGK LFDLLSERKK LCMREDGRQQ VCIVGLQEYE
VSDVQIVKDF IEKGNAERST GSTGANEESS RSHAILQLVV KKHVEVKDTR RRNNDSNELP
GKVVGKISFI DLAGSERGAD TTDNDRQTRI EGAEINKSLL ALKECIRALD NDQLHIPFRG
SKLTEVLRDS FVGNSRTVMI SCISPNAGSC EHTLNTLRYA DRVKSLSKSG NSKKDQTANS
MPPVNKDPLL GPNDVEDVFE PPQEVNVPET RRRVVEKDSN SSTSGIDFRQ PTNYREESGI
PSFSMDKGRS EPNSSFAGST SQRNNISSYP QETSDREEKV KKVSPPRGKG LREEKPDRPQ
NWSKRDVSSS DIPTLTNFRQ NASETASRQY ETASRQYETD PSLDENLDAL LEEEEALIAA
HRKEIEDTME IVREEMKLLA EVDQPGSMIE NYVTQLSFVL SRKAAGLVSL QARLARFQHR
LKEQEILSRK RVPR
