KINUC_ARATH
ID KINUC_ARATH Reviewed; 1051 AA.
AC Q9SV36; A9CP38; F4JE41;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Kinesin-like protein KIN-UC {ECO:0000305};
DE AltName: Full=AtKINUc {ECO:0000303|PubMed:21387573};
DE AltName: Full=Protein ARMADILLO REPEAT KINESIN1 {ECO:0000303|PubMed:17971038};
DE AltName: Full=Protein ARMADILLO REPEAT-CONTAINING KINESIN 1 {ECO:0000305};
DE AltName: Full=Protein CA-ROP2 ENHANCER 1 {ECO:0000303|PubMed:17957256};
DE AltName: Full=Protein MORPHOGENESIS OF ROOT HAIR 2 {ECO:0000303|PubMed:17957256};
GN Name=KINUC {ECO:0000303|PubMed:21387573};
GN Synonyms=ARK1 {ECO:0000312|EMBL:BAF95585.1},
GN CAE1 {ECO:0000303|PubMed:17957256}, MRH2 {ECO:0000312|EMBL:ABX58060.1};
GN OrderedLocusNames=At3g54870 {ECO:0000312|Araport:AT3G54870};
GN ORFNames=F28P10.150 {ECO:0000312|EMBL:CAB41097.2};
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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH ACTIN AND TUBULIN.
RX PubMed=17957256; DOI=10.1371/journal.pone.0001074;
RA Yang G., Gao P., Zhang H., Huang S., Zheng Z.-L.;
RT "A mutation in MRH2 kinesin enhances the root hair tip growth defect caused
RT by constitutively activated ROP2 small GTPase in Arabidopsis.";
RL PLoS ONE 2:E1074-E1074(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH NEK5.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17971038; DOI=10.1111/j.1365-313x.2007.03327.x;
RA Sakai T., van der Honing H., Nishioka M., Uehara Y., Takahashi M.,
RA Fujisawa N., Saji K., Seki M., Shinozaki K., Jones M.A., Smirnoff N.,
RA Okada K., Wasteneys G.O.;
RT "Armadillo repeat-containing kinesins and a NIMA-related kinase are
RT required for epidermal-cell morphogenesis in Arabidopsis.";
RL Plant J. 53:157-171(2008).
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 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 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 [7]
RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=18539780; DOI=10.1104/pp.108.119529;
RA Yoo C.-M., Wen J., Motes C.M., Sparks J.A., Blancaflor E.B.;
RT "A class one ADP-ribosylation factor GTPase-activating protein is critical
RT for maintaining directional root hair growth in Arabidopsis thaliana.";
RL Plant Physiol. 147:1659-1674(2008).
RN [8]
RP IDENTIFICATION.
RX PubMed=21387573; DOI=10.1002/cm.20508;
RA Malcos J.L., Cyr R.J.;
RT "An ungrouped plant kinesin accumulates at the preprophase band in a cell
RT cycle-dependent manner.";
RL Cytoskeleton 68:247-258(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).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24400013; DOI=10.3389/fpls.2013.00528;
RA Yoo C.M., Blancaflor E.B.;
RT "Overlapping and divergent signaling pathways for ARK1 and AGD1 in the
RT control of root hair polarity in Arabidopsis thaliana.";
RL Front. Plant Sci. 4:528-528(2013).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=25159991; DOI=10.1105/tpc.114.126789;
RA Eng R.C., Wasteneys G.O.;
RT "The microtubule plus-end tracking protein ARMADILLO-REPEAT KINESIN1
RT promotes microtubule catastrophe in Arabidopsis.";
RL Plant Cell 26:3372-3386(2014).
CC -!- FUNCTION: Acts as a plus-end microtubule-dependent motor protein
CC (PubMed:25159991). Involved in the control of root hair tip growth by
CC promoting microtubule depolymerization and limiting the accumulation of
CC endoplasmic microtubules (PubMed:17957256, PubMed:17971038,
CC PubMed:24400013, PubMed:25159991). In vitro, binds to polymerized actin
CC through ARM repeats, and to polymerized tubulin through N-terminal
CC motor domain (PubMed:17957256). {ECO:0000269|PubMed:17957256,
CC ECO:0000269|PubMed:17971038, ECO:0000269|PubMed:24400013,
CC ECO:0000269|PubMed:25159991}.
CC -!- SUBUNIT: Interacts (via C-terminus) with NEK5.
CC {ECO:0000269|PubMed:17957256, ECO:0000269|PubMed:17971038}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:18539780, ECO:0000269|PubMed:25159991}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:25159991}. Cytoplasm,
CC cytoskeleton, phragmoplast {ECO:0000269|PubMed:25159991}.
CC Note=Colocalizes with microtubules. {ECO:0000269|PubMed:18539780,
CC ECO:0000269|PubMed:25159991}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SV36-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SV36-2; Sequence=VSP_059313, VSP_059314;
CC -!- TISSUE SPECIFICITY: Expressed in young root hair-forming cells and in
CC root hair-producing cells at the boundary between the hypocotyl and
CC root. Expressed in cotyledons, young leaves, trichomes and flowers.
CC {ECO:0000269|PubMed:17957256, ECO:0000269|PubMed:17971038,
CC ECO:0000269|PubMed:25159991}.
CC -!- DOMAIN: D-BOX motif functions as a recognition motif for the
CC ubiquitination machinery. {ECO:0000250|UniProtKB:Q9FZ06}.
CC -!- DISRUPTION PHENOTYPE: Wavy growth phenotype with altered root hairs
CC displaying multiple tips and branches (PubMed:18539780,
CC PubMed:24400013). Reduced microtubules catastrophe frequency and growth
CC rates (PubMed:25159991). {ECO:0000269|PubMed:18539780,
CC ECO:0000269|PubMed:24400013, ECO:0000269|PubMed:25159991}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Ungrouped subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB41097.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; EU257694; ABX58060.1; -; mRNA.
DR EMBL; AB290928; BAF95585.1; -; mRNA.
DR EMBL; AL049655; CAB41097.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79303.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64395.1; -; Genomic_DNA.
DR PIR; T06733; T06733.
DR RefSeq; NP_001326426.1; NM_001339702.1. [Q9SV36-1]
DR RefSeq; NP_191047.3; NM_115344.4. [Q9SV36-2]
DR AlphaFoldDB; Q9SV36; -.
DR SMR; Q9SV36; -.
DR STRING; 3702.AT3G54870.1; -.
DR iPTMnet; Q9SV36; -.
DR PaxDb; Q9SV36; -.
DR PRIDE; Q9SV36; -.
DR ProteomicsDB; 238217; -. [Q9SV36-1]
DR EnsemblPlants; AT3G54870.1; AT3G54870.1; AT3G54870. [Q9SV36-2]
DR EnsemblPlants; AT3G54870.2; AT3G54870.2; AT3G54870. [Q9SV36-1]
DR GeneID; 824652; -.
DR Gramene; AT3G54870.1; AT3G54870.1; AT3G54870. [Q9SV36-2]
DR Gramene; AT3G54870.2; AT3G54870.2; AT3G54870. [Q9SV36-1]
DR KEGG; ath:AT3G54870; -.
DR Araport; AT3G54870; -.
DR eggNOG; KOG0240; Eukaryota.
DR HOGENOM; CLU_014436_0_0_1; -.
DR InParanoid; Q9SV36; -.
DR OMA; FRTGHNE; -.
DR PhylomeDB; Q9SV36; -.
DR PRO; PR:Q9SV36; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SV36; baseline and differential.
DR Genevisible; Q9SV36; 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:0005819; C:spindle; 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:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
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; PF00514; Arm; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00185; ARM; 3.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50176; ARM_REPEAT; 2.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Motor protein; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..1051
FT /note="Kinesin-like protein KIN-UC"
FT /id="PRO_0000342330"
FT DOMAIN 104..441
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REPEAT 792..831
FT /note="ARM 1"
FT REPEAT 833..873
FT /note="ARM 2"
FT REPEAT 875..915
FT /note="ARM 3"
FT REPEAT 917..956
FT /note="ARM 4; degenerate"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 452..534
FT /evidence="ECO:0000255"
FT COILED 568..761
FT /evidence="ECO:0000255"
FT MOTIF 411..419
FT /note="D-BOX"
FT /evidence="ECO:0000250|UniProtKB:Q9FZ06"
FT COMPBIAS 23..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 189..196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT VAR_SEQ 917..941
FT /note="EKFLKLLKEEEGIKGLLTMAQSGNI -> GKHKIKNFASDDFQYSLYNLCVK
FT IY (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_059313"
FT VAR_SEQ 942..1051
FT /note="Missing (in isoform 2)"
FT /id="VSP_059314"
SQ SEQUENCE 1051 AA; 117375 MW; 90ED45F63E82518B CRC64;
MSSSNSSSAV RSSAKHAAER IQQHLPPNSN HAVSLSSSSL NLPARTSIVA PGIAHSSRLK
DRPSASSSSS SSSVSASSPS TRRSGTPVRR SQSKDFDDDN DPGRVRVSVR VRPRNGEELI
SDADFADLVE LQPEIKRLKL RKNNWNSESY KFDEVFTDTA SQKRVYEGVA KPVVEGVLSG
YNGTIMAYGQ TGTGKTYTVG KIGKDDAAER GIMVRALEDI LLNASSASIS VEISYLQLYM
ETIQDLLAPE KNNISINEDA KTGEVSVPGA TVVNIQDLDH FLQVLQVGET NRHAANTKMN
TESSRSHAIL TVYVRRAMNE KTEKAKPESL GDKAIPRVRK SKLLIVDLAG SERINKSGTD
GHMIEEAKFI NLSLTSLGKC INALAEGSSH IPTRDSKLTR LLRDSFGGSA RTSLIITIGP
SARYHAETTS TIMFGQRAMK IVNMVKLKEE FDYESLCRKL ETQVDHLTAE VERQNKLRNS
EKHELEKRLR ECENSFAEAE KNAVTRSKFL EKENTRLELS MKELLKDLQL QKDQCDLMHD
KAIQLEMKLK NTKQQQLENS AYEAKLADTS QVYEKKIAEL VQRVEDEQAR STNAEHQLTE
MKNILSKQQK SIHEQEKGNY QYQRELAETT HTYESKIAEL QKKLEGENAR SNAAEDQLRQ
MKRLISDRQV ISQENEEANE LKIKLEELSQ MYESTVDELQ TVKLDYDDLL QQKEKLGEEV
RDMKERLLLE EKQRKQMESE LSKLKKNLRE SENVVEEKRY MKEDLSKGSA ESGAQTGSQR
SQGLKKSLSG QRATMARLCE EVGIQKILQL IKSEDLEVQI QAVKVVANLA AEEANQVKIV
EEGGVEALLM LVQSSQNSTI LRVASGAIAN LAMNEKSQDL IMNKGGAQLL AKMVTKTDDP
QTLRMVAGAL ANLCGNEKFL KLLKEEEGIK GLLTMAQSGN IDIIAQVARG MANFAKCETR
EIMQGRRKGR SLLLEEGVLE WLTSNSHIDS ASTQRHIELA LCHLAQNEEN ANDFKRTGSV
TEIVRISVES SRDDIRSLAK KILKTNPYFS S
