KN7F_ARATH
ID KN7F_ARATH Reviewed; 836 AA.
AC F4JUI9; Q0WLK7; Q9SVJ8;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Kinesin-like protein KIN-7F {ECO:0000305};
GN Name=KIN7F {ECO:0000305};
GN OrderedLocusNames=At4g38950 {ECO:0000312|Araport:AT4G38950};
GN ORFNames=F19H22.50 {ECO:0000312|EMBL:CAB38815.1};
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 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 [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).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-7 subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB38815.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80558.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035679; CAB38815.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161594; CAB80558.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86997.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86998.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67224.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67225.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67226.1; -; Genomic_DNA.
DR EMBL; AK230191; BAF02000.1; -; mRNA.
DR PIR; T06055; T06055.
DR RefSeq; NP_001119143.1; NM_001125671.2.
DR RefSeq; NP_001329067.1; NM_001342517.1.
DR RefSeq; NP_001329068.1; NM_001342515.1.
DR RefSeq; NP_001329069.1; NM_001342516.1.
DR RefSeq; NP_195606.2; NM_120055.5.
DR AlphaFoldDB; F4JUI9; -.
DR SMR; F4JUI9; -.
DR STRING; 3702.AT4G38950.1; -.
DR PaxDb; F4JUI9; -.
DR PRIDE; F4JUI9; -.
DR ProteomicsDB; 237097; -.
DR EnsemblPlants; AT4G38950.1; AT4G38950.1; AT4G38950.
DR EnsemblPlants; AT4G38950.2; AT4G38950.2; AT4G38950.
DR EnsemblPlants; AT4G38950.3; AT4G38950.3; AT4G38950.
DR EnsemblPlants; AT4G38950.4; AT4G38950.4; AT4G38950.
DR EnsemblPlants; AT4G38950.5; AT4G38950.5; AT4G38950.
DR GeneID; 830050; -.
DR Gramene; AT4G38950.1; AT4G38950.1; AT4G38950.
DR Gramene; AT4G38950.2; AT4G38950.2; AT4G38950.
DR Gramene; AT4G38950.3; AT4G38950.3; AT4G38950.
DR Gramene; AT4G38950.4; AT4G38950.4; AT4G38950.
DR Gramene; AT4G38950.5; AT4G38950.5; AT4G38950.
DR KEGG; ath:AT4G38950; -.
DR Araport; AT4G38950; -.
DR TAIR; locus:2120272; AT4G38950.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_013407_1_0_1; -.
DR InParanoid; F4JUI9; -.
DR OMA; THMSEKI; -.
DR OrthoDB; 185841at2759; -.
DR PRO; PR:F4JUI9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JUI9; baseline and differential.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
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; IPR021881; NACK_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF11995; DUF3490; 1.
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; Coiled coil; Isopeptide bond; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome; Ubl conjugation.
FT CHAIN 1..836
FT /note="Kinesin-like protein KIN-7F"
FT /id="PRO_0000436464"
FT DOMAIN 13..335
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 422..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 344..420
FT /evidence="ECO:0000255"
FT COMPBIAS 444..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CROSSLNK 707
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:F4JQ51"
FT CONFLICT 123
FT /note="Y -> C (in Ref. 3; BAF02000)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 836 AA; 94464 MW; 5F68EDA3F4F3A366 CRC64;
MEKTQMPVAR EEKILVLVRL RPLNQKEIAA NEAADWECIN DTTILYRNTL REGSNFPSAY
SFDKVYRGEC PTRQVYEDGT KEIALSVVKG INCSIFAYGQ TSSGKTYTMT GITEFAVADI
FDYIFQHEER AFSVKFSAIE IYNEAIRDLL SSDGTSLRLR DDPEKGTVVE KATEETLRDW
NHLKELLSIC EAQRKIGETS LNERSSRSHQ MIRLTVESSA REFLGKENST TLMASVNFID
LAGSERASQA MSAGTRLKEG CHINRSLLTL GTVIRKLSKG RQGHINFRDS KLTRILQPCL
GGNARTAIIC TLSPARSHVE LTKNTLLFAC CAKEVTTKAR INVVMSDKAL LKQLQRELAR
LETELRNPAS SPASNCDCAM TVRKKDLQIQ KMEKEIAELR KQRDLAQSRL EDFMRMIEHN
VASKPGTPHF GNHTDKWEDG SVSETSGVVD SDRRSFISDG MSTPLSISRA YVHSHSDDDD
LDEDLPRRSE DLSEEYCREV QCIETEESVT VYNNKKDKRA EPENVLGCGE DANGETSVSQ
NVRVRSWNRR ETVSGPSTPP ENIGTGFLGR PESHKIAFPD LEFGSTVSRN DSMSSCGSDS
TGTQSIRTPL GEEGGITSIR TFVEGLKEMA KRQGEVSNAE DSGKMRRDIG LDSMDREFER
QRQEILELWQ TCNISLVHRT YFYLLFKGDE ADSIYIGVEL RRLLFMKDSF SQGNQALEGG
ETLTLASSRK ELHRERKMLS KLVGKRFSGE ERKRIYHKFG IAINSKRRRL QLVNELWSNP
KDMTQVMESA DVVAKLVRFA EQGRAMKEMF GLTFTPPSFL TTRRSHSWRK SMPALF
