KINUB_ARATH
ID KINUB_ARATH Reviewed; 894 AA.
AC Q9LPC6; A9CP40; Q0WMY6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Kinesin-like protein KIN-UB {ECO:0000305};
DE AltName: Full=AtKINUb {ECO:0000303|PubMed:21387573};
DE AltName: Full=Protein ARMADILLO REPEAT KINESIN2 {ECO:0000303|PubMed:17971038};
DE AltName: Full=Protein ARMADILLO REPEAT-CONTAINING KINESIN 2 {ECO:0000305};
GN Name=KINUB {ECO:0000303|PubMed:21387573};
GN Synonyms=ARK2 {ECO:0000312|EMBL:BAF95586.1};
GN OrderedLocusNames=At1g01950 {ECO:0000312|Araport:AT1G01950};
GN ORFNames=F22M8.8 {ECO:0000312|EMBL:AAF76473.1};
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], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP 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 [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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 684-894.
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 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.
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 -!- FUNCTION: Involved in the control of epidermal-cell morphogenesis in
CC roots and helical growth of roots by promoting microtubule
CC depolymerization and limiting the accumulation of endoplasmic
CC microtubules. Seems to be involved in the control of cell-file rotation
CC (or twisting). {ECO:0000269|PubMed:17971038}.
CC -!- SUBUNIT: Interacts (via C-terminus) with NEK5.
CC {ECO:0000269|PubMed:17971038}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
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=Q9LPC6-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in the basal regions and petioles of
CC immature leaves and in the root elongation zone.
CC {ECO:0000269|PubMed:17971038}.
CC -!- DOMAIN: D-BOX motif functions as a recognition motif for the
CC ubiquitination machinery. {ECO:0000250|UniProtKB:Q9FZ06}.
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=AAF76473.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB290929; BAF95586.1; -; mRNA.
DR EMBL; AC020622; AAF76473.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27357.1; -; Genomic_DNA.
DR EMBL; AK229671; BAF01514.1; -; mRNA.
DR PIR; D86151; D86151.
DR RefSeq; NP_171697.3; NM_100075.8. [Q9LPC6-1]
DR AlphaFoldDB; Q9LPC6; -.
DR SMR; Q9LPC6; -.
DR STRING; 3702.AT1G01950.3; -.
DR iPTMnet; Q9LPC6; -.
DR PaxDb; Q9LPC6; -.
DR PRIDE; Q9LPC6; -.
DR EnsemblPlants; AT1G01950.1; AT1G01950.1; AT1G01950. [Q9LPC6-1]
DR GeneID; 839306; -.
DR Gramene; AT1G01950.1; AT1G01950.1; AT1G01950. [Q9LPC6-1]
DR KEGG; ath:AT1G01950; -.
DR Araport; AT1G01950; -.
DR eggNOG; KOG0240; Eukaryota.
DR InParanoid; Q9LPC6; -.
DR PhylomeDB; Q9LPC6; -.
DR PRO; PR:Q9LPC6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPC6; baseline and differential.
DR Genevisible; Q9LPC6; 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 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; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24115; PTHR24115; 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..894
FT /note="Kinesin-like protein KIN-UB"
FT /id="PRO_0000342331"
FT DOMAIN 60..402
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REPEAT 626..665
FT /note="ARM 1"
FT REPEAT 667..707
FT /note="ARM 2"
FT REPEAT 709..749
FT /note="ARM 3"
FT REPEAT 751..790
FT /note="ARM 4"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 423..588
FT /evidence="ECO:0000255"
FT MOTIF 372..380
FT /note="D-BOX"
FT /evidence="ECO:0000250|UniProtKB:Q9FZ06"
FT COMPBIAS 17..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 145..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 894 AA; 98423 MW; 7902A8AA2A1F3829 CRC64;
MAMASSRNGA VRGSMRPVSG ANSSNLRSSS FKSRIPSSAP APRRSSSASI GAADNGVPGR
VRVAVRLRPR NADESVADAD FADCVELQPE LKRLKLRKNN WDTETYEFDE VLTEAASQKR
VYEVVAKPVV ESVLEGYNGT VMAYGQTGTG KTFTLGRLGD EDTAARGIMV RSMEDIIGGT
SLDTDSISVS YLQLYMETIQ DLLDPTNDNI AIVEDPRTGD VSLPGATHVE IRNQQNFLEL
LQLGETHRVA ANTKLNTESS RSHAILMVHV KRSVVENEFP VSNEMESSSH FVRPSKPLVR
RSKLVLVDLA GSERVHKSGS EGHMLEEAKS INLSLSALGK CINAIAENSP HVPLRDSKLT
RLLRDSFGGT ARTSLIVTIG PSPRHRGETT STILFGQRAM KVENMLKIKE EFDYKSLSKK
LEVQLDKVIA ENERQLKAFD DDVERINRQA QNRISEVEKN FAEALEKEKL KCQMEYMESV
KKLEEKLISN QRNHENGKRN GEVNGVVTAS EFTRLKESLE NEMKLRKSAE EEVSKVKSQS
TLKTRSGEGE DAGITRLQKL LEDEALQKKK LEEEVTILRS QLVQLTFEAD QMRRCLDRGA
PGNSYSGTDS LPSRHSQARE SVNGQKAPFA TLCEQVGLQK ILQLLESDDA NIRIHAVKVV
ANLAAEEANQ EKIVEAGGLT SLLMLLRSYE DETVRRVAAG AIANLAMNEV SQQLIVDQGG
ISLLSLTAAD AEDPQTLRMV AGAIANLCGN DKLQARLWSD GGIKALLGMV RCGHPDVLAQ
VARGIANFAK CESRATTQGV KSGRSLLIED GALPWIVQHA NDEAAPIRRH IELALCHLAQ
HEVNAKEMIS GGALWELVRI SKECSREDIR SLAHRTLSSS PVFRSEIRRL GIQF
