KINUA_ARATH
ID KINUA_ARATH Reviewed; 919 AA.
AC Q9FZ06; Q9LNA4;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Kinesin-like protein KIN-UA {ECO:0000305};
DE AltName: Full=AtKINUa {ECO:0000303|PubMed:21387573};
DE AltName: Full=Protein ARMADILLO REPEAT KINESIN3 {ECO:0000305};
DE AltName: Full=Protein ARMADILLO REPEAT-CONTAINING KINESIN 3 {ECO:0000305};
DE AltName: Full=kinesin-like protein PAK {ECO:0000303|Ref.2};
GN Name=KINUA {ECO:0000303|PubMed:21387573};
GN Synonyms=ARK3 {ECO:0000312|EMBL:BAF95587.1},
GN PAK {ECO:0000312|EMBL:AAG08965.1};
GN OrderedLocusNames=At1g12430 {ECO:0000312|Araport:AT1G12430};
GN ORFNames=F5O11.15 {ECO:0000312|EMBL:AAF79654.1};
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, AND 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Lai L.P., Cyr R.J., Doyle J.J., Nasrallah J.B.;
RT "The kinesin-like protein PAK has an Armadillo motif tail and is involved
RT in guard cell development in Arabidopsis.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 IDENTIFICATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF
RP 382-ARG--LEU-385, AND DISRUPTION PHENOTYPE.
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 [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).
CC -!- SUBUNIT: Interacts (via C-terminus) with NEK5.
CC {ECO:0000269|PubMed:17971038}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21387573}. Note=Colocalizes with microtubules
CC during interphase. Accumulated at the preprophase band in a cell cycle-
CC dependent manner with a high expression during prophase that decreases
CC after nuclear envelope breakdown. {ECO:0000269|PubMed:21387573}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FZ06-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, guard cells, trichomes,
CC vascular tissues, stele of the root tip region and columella cells
CC (PubMed:17971038). Highest expression detected in guard cells
CC (PubMed:21387573). {ECO:0000269|PubMed:17971038,
CC ECO:0000269|PubMed:21387573}.
CC -!- DOMAIN: D-BOX motif functions as a recognition motif for the
CC ubiquitination machinery. {ECO:0000303|PubMed:21387573}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:21387573}.
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=AAF79654.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB290930; BAF95587.1; -; mRNA.
DR EMBL; AF159052; AAG08965.1; -; mRNA.
DR EMBL; AC025416; AAF79654.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28880.1; -; Genomic_DNA.
DR RefSeq; NP_563908.1; NM_101115.3. [Q9FZ06-1]
DR AlphaFoldDB; Q9FZ06; -.
DR SMR; Q9FZ06; -.
DR STRING; 3702.AT1G12430.2; -.
DR iPTMnet; Q9FZ06; -.
DR PaxDb; Q9FZ06; -.
DR EnsemblPlants; AT1G12430.1; AT1G12430.1; AT1G12430. [Q9FZ06-1]
DR GeneID; 837799; -.
DR Gramene; AT1G12430.1; AT1G12430.1; AT1G12430. [Q9FZ06-1]
DR KEGG; ath:AT1G12430; -.
DR Araport; AT1G12430; -.
DR eggNOG; KOG0240; Eukaryota.
DR InParanoid; Q9FZ06; -.
DR OMA; HRFATNT; -.
DR PhylomeDB; Q9FZ06; -.
DR PRO; PR:Q9FZ06; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZ06; baseline and differential.
DR Genevisible; Q9FZ06; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
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 GO; GO:0032886; P:regulation of microtubule-based process; IEA:InterPro.
DR GO; GO:0048364; P:root development; IEA:InterPro.
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; IPR027640; Kinesin-like_fam.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR033291; KINU_plant.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR PANTHER; PTHR24115:SF840; PTHR24115:SF840; 1.
DR Pfam; PF00514; Arm; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00185; ARM; 4.
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..919
FT /note="Kinesin-like protein KIN-UA"
FT /id="PRO_0000342332"
FT DOMAIN 70..412
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REPEAT 650..689
FT /note="ARM 1"
FT REPEAT 691..731
FT /note="ARM 2"
FT REPEAT 733..773
FT /note="ARM 3"
FT REPEAT 775..814
FT /note="ARM 4"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 428..492
FT /evidence="ECO:0000255"
FT COILED 530..621
FT /evidence="ECO:0000255"
FT MOTIF 382..390
FT /note="D-BOX"
FT /evidence="ECO:0000303|PubMed:21387573"
FT COMPBIAS 1..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 155..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MUTAGEN 382..385
FT /note="RTSL->ATSA: No decreased expression after nuclear
FT envelope breakdown."
FT /evidence="ECO:0000269|PubMed:21387573"
SQ SEQUENCE 919 AA; 100887 MW; F530FD1B55E54F58 CRC64;
MSTTSGTGGV SYRNGTQRSS LRTQSSASTS SGGQKASVKS KSVLRKSSPA ALGGGSSKSG
GGGDAGVPGR VRVAVRLRPR NGEELIADAD FADCVELQPE LKRLKLRKNN WDTDTFEFDE
VLTEYASQKR VYEVVAKPVV EGVLDGYNGT IMAYGQTGTG KTYTLGQLGE EDVADRGIMV
RAMEDILAEV SLETDSISVS YLQLYMETVQ DLLDPSNDNI AIVEDPKNGD VSLPGATLVE
IRDQQSFLEL LQLGEAHRFA ANTKLNTESS RSHAILMVNV RRSMKTRDGL SSESNGNSHM
TKSLKPPVVR KGKLVVVDLA GSERINKSGS EGHTLEEAKS INLSLSALGK CINALAENSS
HVPFRDSKLT RLLRDSFGGT ARTSLVITIG PSPRHRGETT STIMFGQRAM KVENMVKIKE
EFDYKSLSRR LEVQLDNLIE ENERQQKAFV DEIERITVEA HNQISEAEKR YANALEDEKL
RYQNDYMESI KKLEENWSKN QKKLAAERLA LGEKNGLDIT SNGNRSIAPA LEEVSELKKL
LQKEAQSKMA AEEEVNRLKH QLNEFKKVEA SGNSEIMRLH KMLENETQQK EKLEGEIATL
HSQLLQLSLT ADETRRNLEQ HGSEKTSGAR DSLMSQLRLP QIQDPGNAEK PPVARLFEQV
GLQKILSLLE AEDADVRIHA VKVVANLAAE EANQQQIVEA GGLTSLLMLL KNTEDETIHR
VAAGAIANLA MNETNQELIM DQGGIGLLSS TAANAEDPQT LRMVAGAIAN LCGNDKLQTK
LRSEGGIAAL LGMVRCGHPD VLAQVARGIA NFAKCESRAS TQGTKRGKSL LIEDGALSWI
VQNAKTETAA IRRHIELALC HLAQHEGNAK EMVKEGAMWE LVRISRDCSR EDIRSLAHRT
LTSSPTFLTE LRRLRVDIR
