KN14C_ARATH
ID KN14C_ARATH Reviewed; 793 AA.
AC Q07970; Q7FKK6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Kinesin-like protein KIN-14C {ECO:0000305};
DE AltName: Full=AtKIN14a {ECO:0000303|PubMed:18088313};
DE AltName: Full=Kinesin-like protein KatA {ECO:0000303|PubMed:8492804, ECO:0000303|PubMed:8597656};
GN Name=KIN14C {ECO:0000305};
GN Synonyms=ATK1 {ECO:0000303|PubMed:11973272},
GN KATA {ECO:0000303|PubMed:8597656, ECO:0000312|EMBL:BAA01972.1};
GN OrderedLocusNames=At4g21270 {ECO:0000312|Araport:AT4G21270};
GN ORFNames=F7J7.210 {ECO:0000312|EMBL:CAA17546.1},
GN T6K22.10 {ECO:0000312|EMBL:CAA20193.1};
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].
RC STRAIN=cv. Columbia;
RX PubMed=8492804; DOI=10.1007/bf00291995;
RA Mitsui H., Yamaguchi-Shinozaki K., Shinozaki K., Nishikawa K.,
RA Takahashi H.;
RT "Identification of a gene family (kat) encoding kinesin-like proteins in
RT Arabidopsis thaliana and the characterization of secondary structure of
RT KatA.";
RL Mol. Gen. Genet. 238:362-368(1993).
RN [2]
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 [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 SUBCELLULAR LOCATION.
RX PubMed=8597656; DOI=10.2307/3870073;
RA Liu B., Cyr R.J., Palevitz B.A.;
RT "A kinesin-like protein, KatAp, in the cells of arabidopsis and other
RT plants.";
RL Plant Cell 8:119-132(1996).
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.
RX PubMed=12112142; DOI=10.1002/cm.10045;
RA Marcus A.I., Ambrose J.C., Blickley L., Hancock W.O., Cyr R.J.;
RT "Arabidopsis thaliana protein, ATK1, is a minus-end directed kinesin that
RT exhibits non-processive movement.";
RL Cell Motil. Cytoskeleton 52:144-150(2002).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11973272; DOI=10.1242/dev.129.10.2401;
RA Chen C., Marcus A., Li W., Hu Y., Calzada J.-P., Grossniklaus U., Cyr R.J.,
RA Ma H.;
RT "The Arabidopsis ATK1 gene is required for spindle morphogenesis in male
RT meiosis.";
RL Development 129:2401-2409(2002).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12686621; DOI=10.1091/mbc.e02-09-0586;
RA Marcus A.I., Li W., Ma H., Cyr R.J.;
RT "A kinesin mutant with an atypical bipolar spindle undergoes normal
RT mitosis.";
RL Mol. Biol. Cell 14:1717-1726(2003).
RN [9]
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 [10]
RP FUNCTION, 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 [11]
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 has a minus-end directed polarity. Plays a crucial
CC role in spindle morphogenesis in male meiosis. In mitosis, is required
CC for normal microtubule accumulation at the spindle poles during
CC prophase and may play a role in spindle assembly during prometaphase.
CC {ECO:0000269|PubMed:11973272, ECO:0000269|PubMed:12112142,
CC ECO:0000269|PubMed:12686621, ECO:0000269|PubMed:18088313}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:8597656}. Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:8597656}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:8597656}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:8597656}. Note=Colocalizes with microtubules during
CC preprophase and cytokinesis. In M-phase, locates to the preprophase
CC band. Present mainly in the midzone at metaphase and later during
CC anaphase. Associated with the ends of the kinetochore fibers near the
CC kinetochores. Detected on the phragmoplast by late cytokinesis.
CC {ECO:0000269|PubMed:8597656}.
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).
CC -!- DISRUPTION PHENOTYPE: Plants show defects in male meiosis, producing an
CC abnormal number of microspores of variable sizes. Dividing cells of
CC mutant plants lack spindle bipolarity in metaphase of mitosis. Kin14c
CC and kin14d double mutant is gametophytically lethal (PubMed:18088313).
CC {ECO:0000269|PubMed:11973272, ECO:0000269|PubMed:12686621,
CC ECO:0000269|PubMed:18088313}.
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=CAA20193.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D11371; BAA01972.1; -; mRNA.
DR EMBL; AL021960; CAA17546.1; -; Genomic_DNA.
DR EMBL; AL031187; CAA20193.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161554; CAB79127.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84434.1; -; Genomic_DNA.
DR PIR; S34830; S34830.
DR RefSeq; NP_193859.1; NM_118246.2.
DR AlphaFoldDB; Q07970; -.
DR SMR; Q07970; -.
DR BioGRID; 13167; 2.
DR STRING; 3702.AT4G21270.1; -.
DR iPTMnet; Q07970; -.
DR PaxDb; Q07970; -.
DR PRIDE; Q07970; -.
DR ProteomicsDB; 238202; -.
DR EnsemblPlants; AT4G21270.1; AT4G21270.1; AT4G21270.
DR GeneID; 827876; -.
DR Gramene; AT4G21270.1; AT4G21270.1; AT4G21270.
DR KEGG; ath:AT4G21270; -.
DR Araport; AT4G21270; -.
DR TAIR; locus:2127378; AT4G21270.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_001485_12_2_1; -.
DR InParanoid; Q07970; -.
DR OMA; QADETHV; -.
DR OrthoDB; 364605at2759; -.
DR PhylomeDB; Q07970; -.
DR PRO; PR:Q07970; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q07970; baseline and differential.
DR Genevisible; Q07970; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005872; C:minus-end kinesin complex; TAS:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
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:0008569; F:minus-end-directed microtubule motor activity; IDA:TAIR.
DR GO; GO:0009971; P:anastral spindle assembly involved in male meiosis; IMP:TAIR.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; 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 cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore; Meiosis; Microtubule;
KW Mitosis; Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..793
FT /note="Kinesin-like protein KIN-14C"
FT /id="PRO_0000125380"
FT DOMAIN 431..772
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..69
FT /note="Globular"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 120..375
FT /evidence="ECO:0000255"
FT COMPBIAS 21..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 516..523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 793 AA; 89047 MW; 85A195206D825C4E CRC64;
MASRNQNRPP RSPNAKKEGL GGISFDKRRK VETQGGTGRR QAFSAVNKQD VTMNSDVGSI
EECGKVDFTK DEILALLSER AKAGKFDTKA KIEQMTDIIK RLKVCVKWFQ QADETHVQEK
ENLKVSLESS EQKYNHKELE ARTKEEELQA TISKLEENVV SLHEKLAKEE SSTQDAIECH
RREKEARVAA EKVQASLGEE LDKVKEEKMA AKQKVTSLED MYKRLQEYNT SLQQYNSKLQ
TDLETVRAAL TRAEKEKSSI LENLSTLRGH SKSLQDQLSS SRVLQDDAIK QKDSLLSEVT
NLRNELQQVR DDRDRQVVQS QKLSEEIRKY QENVGKSSQE LDILTAKSGS LEETCSLQKE
RLNMLEQQLA IANERQKMAD ASVSLTRTEF EEQKHLLCEL QDRLADMEHQ LCEGELLRKK
LHNTILELKG NIRVFCRVRP LLPDDGGRHE ATVIAYPTST EAQGRGVDLV QSGNKHPFTF
DKVFNHEASQ EEVFFEISQL VQSALDGYKV CIFAYGQTGS GKTYTMMGRP EAPDQKGLIP
RSLEQIFQAS QSLGAQGWKY KMQVSMLEIY NETIRDLLST NRTTSMDLVR ADSGTSGKQY
TITHDVNGHT HVSDLTIFDV CSVGKISSLL QQAAQSRSVG KTQMNEQSSR SHFVFTMRIS
GVNESTEQQV QGVLNLIDLA GSERLSKSGA TGDRLKETQA INKSLSALSD VIFALAKKED
HVPFRNSKLT YLLQPCLGGD SKTLMFVNIS PDPTSAGESL CSLRFAARVN ACEIGIPRRQ
TSTKLLDSRL SYG
