KN14D_ARATH
ID KN14D_ARATH Reviewed; 790 AA.
AC F4JGP4; Q0WP75; Q6NQ77; Q9M0X6;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Kinesin-like protein KIN-14D {ECO:0000305};
DE AltName: Full=AtKIN14b {ECO:0000303|PubMed:18088313};
GN Name=KIN14D {ECO:0000305}; Synonyms=ATK5 {ECO:0000303|PubMed:15659646};
GN OrderedLocusNames=At4g05190 {ECO:0000312|Araport:AT4G05190};
GN ORFNames=C17L7.110 {ECO:0000312|EMBL:AC012392},
GN C6L9.1 {ECO:0000312|EMBL:CAB81061.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
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 (SEP-2004) 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, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15659646; DOI=10.1091/mbc.e04-10-0935;
RA Ambrose J.C., Li W., Marcus A., Ma H., Cyr R.;
RT "A minus-end-directed kinesin with plus-end tracking protein activity is
RT involved in spindle morphogenesis.";
RL Mol. Biol. Cell 16:1584-1592(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, AND DISRUPTION PHENOTYPE.
RX PubMed=17220198; DOI=10.1105/tpc.106.047613;
RA Ambrose J.C., Cyr R.;
RT "The kinesin ATK5 functions in early spindle assembly in Arabidopsis.";
RL Plant Cell 19:226-236(2007).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18088313; DOI=10.1111/j.1365-313x.2007.03391.x;
RA Quan L., Xiao R., Li W., Oh S.A., Kong H., Ambrose J.C., Malcos J.L.,
RA Cyr R., Twell D., Ma H.;
RT "Functional divergence of the duplicated AtKIN14a and AtKIN14b genes:
RT critical roles in Arabidopsis meiosis and gametophyte development.";
RL Plant J. 53:1013-1026(2008).
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).
CC -!- FUNCTION: Kinesin that supports microtubule movement in an ATP-
CC dependent manner and that functions as a minus-end directed motor as
CC well as a plus-end tracking protein. During mitosis, is involved in
CC early spindle assembly. Participates in the capture of antiparallel
CC interpolar microtubules and helps in generating force to coalign
CC microtubules. {ECO:0000269|PubMed:15659646,
CC ECO:0000269|PubMed:17220198, ECO:0000269|PubMed:18088313}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC phragmoplast. Note=In interphase, is enriched specifically at growing
CC microtubule plus-ends. In dividing cells, accumulates in spindle
CC midzones and phragmoplast leading edges.
CC -!- TISSUE SPECIFICITY: Slightly expressed in anther lobes with pollen
CC mother cells at anther stage 5. Strongly expressed at anther stage 6 in
CC the tapetum and meiotic cells. Also detected in the gynoecium and the
CC ovule. {ECO:0000269|PubMed:18088313}.
CC -!- DOMAIN: Composed of three structural domains; a small globular N-
CC terminal, a central alpha-helical coiled coil and a large globular C-
CC terminal which is responsible for the motor activity (it hydrolyzes ATP
CC and binds microtubules). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but dividing cells of mutant plants exhibit abnormally
CC broadened mitotic spindles in metaphase and anaphase. However, this
CC does not affect chromosome alignment and segregation. Kin14c and kin14d
CC double mutant is gametophytically lethal (PubMed:18088313).
CC {ECO:0000269|PubMed:15659646, ECO:0000269|PubMed:17220198,
CC ECO:0000269|PubMed:18088313}.
CC -!- MISCELLANEOUS: By measuring the velocity of microtubule translocation,
CC the speed of ATK5 was determined to be 6.30 um/min at 20 degrees
CC Celsius. {ECO:0000305|PubMed:15659646}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-14 subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB81061.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC012392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161503; CAB81061.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82489.1; -; Genomic_DNA.
DR EMBL; BT010582; AAQ82843.1; -; mRNA.
DR EMBL; AK175713; BAD43476.1; -; mRNA.
DR EMBL; AK229204; BAF01074.1; -; mRNA.
DR PIR; C85065; C85065.
DR RefSeq; NP_001329202.1; NM_001340542.1.
DR RefSeq; NP_192428.2; NM_116758.4.
DR AlphaFoldDB; F4JGP4; -.
DR SMR; F4JGP4; -.
DR STRING; 3702.AT4G05190.1; -.
DR iPTMnet; F4JGP4; -.
DR PaxDb; F4JGP4; -.
DR PRIDE; F4JGP4; -.
DR EnsemblPlants; AT4G05190.1; AT4G05190.1; AT4G05190.
DR GeneID; 825867; -.
DR Gramene; AT4G05190.1; AT4G05190.1; AT4G05190.
DR KEGG; ath:AT4G05190; -.
DR Araport; AT4G05190; -.
DR TAIR; locus:2115713; AT4G05190.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_001485_12_2_1; -.
DR InParanoid; F4JGP4; -.
DR OMA; RNEHLED; -.
DR OrthoDB; 364605at2759; -.
DR PRO; PR:F4JGP4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JGP4; baseline and differential.
DR Genevisible; F4JGP4; AT.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005876; C:spindle microtubule; IDA:TAIR.
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; IMP:TAIR.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:TAIR.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; IMP:TAIR.
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 cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..790
FT /note="Kinesin-like protein KIN-14D"
FT /id="PRO_0000420251"
FT DOMAIN 428..769
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..66
FT /note="Globular"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 117..316
FT /evidence="ECO:0000255"
FT COILED 347..426
FT /evidence="ECO:0000255"
FT COMPBIAS 22..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 513..520
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 31
FT /note="K -> E (in Ref. 3; AAQ82843 and 4; BAD43476)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="K -> E (in Ref. 3; AAQ82843 and 4; BAD43476)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 790 AA; 89194 MW; 9F347A6FD125906D CRC64;
MPLRNQNRAP LPSPNVKKEA LSSIPFDKRR KETQGTGRRQ VLSTVNRQDA NSDVGSTEEC
GKVEFTKDEV LALLNERAKA GKFDTKGKIE QMTDIIKKLK VCVRWYQQVD ETHVQDKENL
SSSLQSAEKR YSDKELDAKT KEEELRATIT EMKENIESLQ EKLSKEKLSK LDAIENHRRE
KDCRVVAEKL QVSLREELDK VKEEKMAAKQ KVTSLEDMYK RLQEYNTSLQ QYNTKLQTDL
EVAREAHTRA EKEKSSILEN LTTLRGHSKS LQDQLASSRV SQDEAVKQKD SLLMEVNNLQ
SELQQVRDDR DRHVVQSQKL AGEILMYKES VGKSSHELDI LIAKSGSLEE TCSLQKERIK
MLEQELAFAK EKLKMVDLSM SHTMTEFEEQ KQCMHELQDR LADTERQLFE GELLRKKLHN
TILELKGNIR VFCRVRPLLP DDGGRQEASV IAYPTSTESL GRGIDVVQSG NKHPFTFDKV
FDHGASQEEV FFEISQLVQS ALDGYKVCIF AYGQTGSGKT YTMMGRPETP EQKGLIPRSL
EQIFKTSQSL STQGWKYKMQ VSMLEIYNES IRDLLSTSRT IAIESVRADS STSGRQYTIT
HDVNGNTHVS DLTIVDVCSI GQISSLLQQA AQSRSVGKTH MNEQSSRSHF VFTLRISGVN
ESTEQQVQGV LNLIDLAGSE RLSRSGATGD RLKETQAINK SLSALSDVIF ALAKKEDHVP
FRNSKLTYLL QPCLGGDSKT LMFVNISPDP SSTGESLCSL RFAARVNACE IGIPRRQTSA
KLLDSRLSYG
