ID   KN4B_ARATH              Reviewed;        1051 AA.
AC   Q94LW7; Q9SNE3;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Kinesin-like protein KIN-4B {ECO:0000305};
DE   AltName: Full=AtKINESIN-4B {ECO:0000303|PubMed:25600279};
GN   Name=KIN4B {ECO:0000305}; Synonyms=KICP-02 {ECO:0000312|EMBL:BAB55445.1};
GN   OrderedLocusNames=At3g50240 {ECO:0000312|Araport:AT3G50240};
GN   ORFNames=F11C1_80 {ECO:0000312|EMBL:CAB62303.1};
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].
RA   Itoh R.;
RT   "An Arabidopsis thaliana gene encoding a kinesin-related protein that
RT   belongs to Chromokinesin/KIF4 subfamily.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [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   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   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   [7]
RP   IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25600279; DOI=10.1016/j.molp.2015.01.004;
RA   Kong Z., Ioki M., Braybrook S., Li S., Ye Z.H., Julie Lee Y.R., Hotta T.,
RA   Chang A., Tian J., Wang G., Liu B.;
RT   "Kinesin-4 functions in vesicular transport on cortical microtubules and
RT   regulates cell wall mechanics during cell elongation in plants.";
RL   Mol. Plant 8:1011-1023(2015).
CC   -!- FUNCTION: Kinesin-like motor protein involved in the control of the
CC       oriented deposition of cellulose microfibrils.
CC       {ECO:0000250|UniProtKB:Q8GS71}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8GS71}.
CC   -!- DOMAIN: Composed of an N-terminal domain which is responsible for the
CC       motor activity of kinesin (it hydrolyzes ATP and binds microtubule) and
CC       a central to C-terminal alpha-helical coiled coil domain that mediates
CC       the heavy chain dimerization. {ECO:0000250|UniProtKB:Q8GS71}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:25600279}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIN-4 subfamily.
CC       {ECO:0000303|PubMed:16448571}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB62303.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB061676; BAB55445.1; -; mRNA.
DR   EMBL; AL132976; CAB62303.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE78644.1; -; Genomic_DNA.
DR   PIR; T45570; T45570.
DR   RefSeq; NP_566931.1; NM_114884.5.
DR   AlphaFoldDB; Q94LW7; -.
DR   SMR; Q94LW7; -.
DR   STRING; 3702.AT3G50240.1; -.
DR   iPTMnet; Q94LW7; -.
DR   PaxDb; Q94LW7; -.
DR   PRIDE; Q94LW7; -.
DR   EnsemblPlants; AT3G50240.1; AT3G50240.1; AT3G50240.
DR   GeneID; 824186; -.
DR   Gramene; AT3G50240.1; AT3G50240.1; AT3G50240.
DR   KEGG; ath:AT3G50240; -.
DR   Araport; AT3G50240; -.
DR   TAIR; locus:2074855; AT3G50240.
DR   eggNOG; KOG0244; Eukaryota.
DR   HOGENOM; CLU_001485_4_2_1; -.
DR   InParanoid; Q94LW7; -.
DR   OrthoDB; 369179at2759; -.
DR   PhylomeDB; Q94LW7; -.
DR   PRO; PR:Q94LW7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q94LW7; baseline and differential.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005875; C:microtubule associated complex; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR   GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   ATP-binding; Cell wall biogenesis/degradation; Coiled coil; Microtubule;
KW   Motor protein; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1051
FT                   /note="Kinesin-like protein KIN-4B"
FT                   /id="PRO_0000436185"
FT   DOMAIN          25..380
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          916..946
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1029..1051
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          414..448
FT                   /evidence="ECO:0000255"
FT   COILED          540..644
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1029..1044
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         104..111
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1051 AA;  118762 MW;  6D12CF65AC097949 CRC64;
     MESHSSLSSS SSSSPPSSLS SESCCVKVAV NVRPLIGDEV TQGCRECVSV SPVTPQVQMG
     THPFTFDHVY GSNGSPSSLM FEECVAPLVD GLFHGYNATV LAYGQTGSGK TYTMGTGIKD
     GTKNGLIPQV MSALFNKIDS VKHQMGFQLH VSFIEILKEE VLDLLDSSVP FNRLANGTPG
     KVVLSKSPVQ IRESPNGVIT LSGATEVPIA TKEEMASCLE QGSLTRATGS TNMNNESSRS
     HAIFTITLEQ MRKISSISVV KDTVDEDMGE EYCCAKLHLV DLAGSERAKR TGSGGVRLKE
     GIHINRGLLA LGNVISALGD EKRRKEGAHV PYRDSKLTRL LQDSLGGNSK TVMIACISPA
     DINAEETLNT LKYANRARNI QNKPVANKDL ICSEMQKMRQ ELQYLQATLC ARGATSSEEV
     QVMREKIMKL ESANEELSRE LHIYRSKRVT LDYCNIDAQE DGVIFSKDDG LKRGFESMDS
     DYEMSEATSG GISEDIGAAE EWEHALRQNS MGKELNELSK RLEEKESEMR VCGIGTETIR
     QHFEKKMMEL EKEKRTVQDE RDMLLAEVEE LAASSDRQAQ VARDNHAHKL KALETQILNL
     KKKQENQVEV LKQKQKSEDA AKRLKTEIQC IKAQKVQLQQ KMKQEAEQFR QWKASQEKEL
     LQLKKEGRKT EHERLKLEAL NRRQKMVLQR KTEEAAMATK RLKELLEARK SSPHDISVIA
     NGQPPSRQTN EKSLRKWLDN ELEVMAKVHQ VRFQYEKQIQ VRAALAVELT SLRQEMEFPS
     NSHQEKNGQF RFLSPNTRLE RIASLESMLD VSSNALTAMG SQLSEAEERE HSLHAKPRWN
     HIQSMTDAKY LLQYVFDSTA EARSKIWEKD RDIKEKKEQL NDLLCLLQLT EVQNREILKE
     KKTREQTVSI ALASTSSSYS GSSRSSSKHY GDNNASDDPS SPSSTYHRAT KHLKYTGPGI
     VNISVRESEA LLEETRKMKA MKKMGQSGKL WKWKRSHHQW LLQFKWKWQK PWKLSEWIKQ
     NDETTMHVMS KSHHDDEDDH SWNRHSMFQG A