KN14M_ARATH
ID KN14M_ARATH Reviewed; 745 AA.
AC P46864; Q9T047;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Kinesin-like protein KIN-14M {ECO:0000305};
DE AltName: Full=AtKIN14c {ECO:0000303|PubMed:18088313};
DE AltName: Full=Kinesin-like protein KatB {ECO:0000303|PubMed:8075402, ECO:0000303|PubMed:8492804};
GN Name=KIN14M {ECO:0000305};
GN Synonyms=ATK2 {ECO:0000305}, KATB {ECO:0000303|PubMed:8492804,
GN ECO:0000312|EMBL:BAA04673.1};
GN OrderedLocusNames=At4g27180 {ECO:0000312|Araport:AT4G27180};
GN ORFNames=T24A18.130 {ECO:0000312|EMBL:CAB38848.1};
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=8075402; DOI=10.1007/bf00028881;
RA Mitsui H., Nakatani K., Yamaguchi-Shinozaki K., Shinozaki K., Nishikawa K.,
RA Takahashi H.;
RT "Sequencing and characterization of the kinesin-related genes katB and katC
RT of Arabidopsis thaliana.";
RL Plant Mol. Biol. 25:865-876(1994).
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 IDENTIFICATION.
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 [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 MICROTUBULE-BINDING, AND SUBUNIT.
RX PubMed=17244481; DOI=10.5483/bmbrep.2007.40.1.044;
RA Jiang S., Li M., Xu T., Ren D., Liu G.;
RT "Two kinesins from Arabidopsis, KatB and KatC, have a second microtubule-
RT binding site in the tail domain.";
RL J. Biochem. Mol. Biol. 40:44-52(2007).
RN [8]
RP IDENTIFICATION.
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 [9]
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: Bind to microtubules in an ATP-insensitive manner (in vitro).
CC Homodimer and heterodimer with KIN14N/KATC (in vitro).
CC {ECO:0000269|PubMed:17244481}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
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 -!- 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=CAB38848.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79573.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D21137; BAA04673.1; -; mRNA.
DR EMBL; AL035680; CAB38848.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161566; CAB79573.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85310.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66187.1; -; Genomic_DNA.
DR PIR; T06048; T06048.
DR RefSeq; NP_001328096.1; NM_001341838.1.
DR RefSeq; NP_567768.1; NM_118852.3.
DR AlphaFoldDB; P46864; -.
DR SMR; P46864; -.
DR BioGRID; 14113; 2.
DR STRING; 3702.AT4G27180.1; -.
DR iPTMnet; P46864; -.
DR PaxDb; P46864; -.
DR PRIDE; P46864; -.
DR ProteomicsDB; 237063; -.
DR EnsemblPlants; AT4G27180.1; AT4G27180.1; AT4G27180.
DR EnsemblPlants; AT4G27180.2; AT4G27180.2; AT4G27180.
DR GeneID; 828826; -.
DR Gramene; AT4G27180.1; AT4G27180.1; AT4G27180.
DR Gramene; AT4G27180.2; AT4G27180.2; AT4G27180.
DR KEGG; ath:AT4G27180; -.
DR Araport; AT4G27180; -.
DR TAIR; locus:2136437; AT4G27180.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_001485_12_2_1; -.
DR InParanoid; P46864; -.
DR OMA; IDMTQNG; -.
DR OrthoDB; 364605at2759; -.
DR PhylomeDB; P46864; -.
DR PRO; PR:P46864; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P46864; baseline and differential.
DR Genevisible; P46864; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; ISS:TAIR.
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; IDA:TAIR.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..745
FT /note="Kinesin-like protein KIN-14M"
FT /id="PRO_0000125381"
FT DOMAIN 387..724
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..35
FT /note="Globular"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..77
FT /note="Microtubule-binding"
FT /evidence="ECO:0000269|PubMed:17244481"
FT REGION 198..745
FT /note="Microtubule-binding"
FT /evidence="ECO:0000250|UniProtKB:P46875"
FT COILED 76..223
FT /evidence="ECO:0000255"
FT COILED 259..389
FT /evidence="ECO:0000255"
FT BINDING 472..479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 745 AA; 84359 MW; 6DB352FDF4FD7BC1 CRC64;
MVGEMTNNGR IRPSFPVKDL TSNEGSEYGG PVEFTREDVE TLLHERIKYK SKYNYKERCE
NTMDYVKRLR LCIRWFQELE LDYAFEQEKL KNAMEMNEKH CADLEVNLKV KEEELNMVID
ELRKNFASVQ VQLAKEQTEK LAANESLGKE REARIAVESL QAAITEELAK TQGELQTANQ
RIQAVNDMYK LLQEYNSSLQ LYNSKLQGDL DEAHENIKRG EKERTGIVES IGNLKGQFKA
LQDQLAASKV SQDDVMKQKD ELVNEIVSLK VEIQQVKDDR DRHITEIETL QAEATKQNDF
KDTINELESK CSVQNKEIEE LQDQLVASER KLQVADLSTF EKMNEFEEQK ESIMELKGRL
EEAELKLIEG EKLRKKLHNT IQELKGNIRV FCRVRPLLSG ENSSEEAKTI SYPTSLEALG
RGIDLLQNGQ SHCFTFDKVF VPSASQEDVF VEISQLVQSA LDGYKVCIFA YGQTGSGKTY
TMMGRPGNPD EKGLIPRCLE QIFQTRQSLR SQGWKYELQV SMLEIYNETI RDLLSTNKEA
VRADNGVSPQ KYAIKHDASG NTHVVELTVV DVRSSKQVSF LLDHAARNRS VGKTAMNEQS
SRSHFVFTLK ISGFNESTEQ QVQGVLNLID LAGSERLSKS GSTGDRLKET QAINKSLSSL
GDVIFALAKK EDHVPFRNSK LTYLLQPCLG GDSKTLMFVN ITPEPSSTGE SLCSLRFAAR
VNACEIGTAH RHVNARPLDY RLSLG
