KN7I_ARATH
ID KN7I_ARATH Reviewed; 1004 AA.
AC F4JQ51; O22974; Q9SU42;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Kinesin-like protein KIN-7I {ECO:0000305};
GN Name=KIN7I {ECO:0000305};
GN OrderedLocusNames=At4g24170 {ECO:0000312|Araport:AT4G24170};
GN ORFNames=T19F6.1 {ECO:0000312|EMBL:CAB51660.1},
GN T19F6.3 {ECO:0000312|EMBL:AAB63609.1};
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 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 [4]
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 [5]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-881, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
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=AAB63609.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB51660.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79327.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC002343; AAB63609.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL109619; CAB51660.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161561; CAB79327.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84858.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67734.1; -; Genomic_DNA.
DR PIR; T13465; T13465.
DR RefSeq; NP_001320052.1; NM_001341646.1.
DR RefSeq; NP_567695.1; NM_118549.2.
DR AlphaFoldDB; F4JQ51; -.
DR SMR; F4JQ51; -.
DR STRING; 3702.AT4G24170.1; -.
DR iPTMnet; F4JQ51; -.
DR PaxDb; F4JQ51; -.
DR PRIDE; F4JQ51; -.
DR ProteomicsDB; 237107; -.
DR EnsemblPlants; AT4G24170.1; AT4G24170.1; AT4G24170.
DR EnsemblPlants; AT4G24170.2; AT4G24170.2; AT4G24170.
DR GeneID; 828517; -.
DR Gramene; AT4G24170.1; AT4G24170.1; AT4G24170.
DR Gramene; AT4G24170.2; AT4G24170.2; AT4G24170.
DR KEGG; ath:AT4G24170; -.
DR Araport; AT4G24170; -.
DR TAIR; locus:2135006; AT4G24170.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_013407_0_0_1; -.
DR InParanoid; F4JQ51; -.
DR OMA; YKSIIAN; -.
DR OrthoDB; 224479at2759; -.
DR PRO; PR:F4JQ51; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JQ51; baseline and differential.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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: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 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Isopeptide bond; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome; Ubl conjugation.
FT CHAIN 1..1004
FT /note="Kinesin-like protein KIN-7I"
FT /id="PRO_0000436467"
FT DOMAIN 6..326
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 567..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 335..402
FT /evidence="ECO:0000255"
FT COILED 517..576
FT /evidence="ECO:0000255"
FT COILED 634..661
FT /evidence="ECO:0000255"
FT COMPBIAS 567..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CROSSLNK 881
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:17272265"
SQ SEQUENCE 1004 AA; 114520 MW; 662100432DC9406A CRC64;
MGGEEKILVS VRVRPLNEKE KTRNDRCDWE CINDTTIICK FHNLPDKSSY TFDKVFGFEC
PTKQVYDDGA KEVALCVLSG INSSIFAYGQ TSSGKTYTMS GITEFAMDDI FAYIDKHKQE
RKFTLKFSAM EIYNEAVRDL LCEDSSTPLR LLDDPERGTV VEKLREETLR DRSHLEELLS
ICETQRKIGE TSLNEISSRS HQILRLTIES SSQQFSPESS ATLAASVCFV DLAGSERASQ
TLSAGSRLKE GCHINRSLLT LGTVIRKLSK GKNGHIPYRD SKLTRILQNS LGGNARTAII
CTMSPARSHL EQSRNTLLFA TCAKEVTTNA QVNLVVSEKA LVKQLQRELA RMENELKNLG
PASASSTSDF YALMLKQKEE LIAKMEEQIH ELKWQRDVAQ SRVENLLKST AEERSSSSSM
DSRRRRISYD STDFDEPRML NNLGKSNLYS PDEDGFLLDD TTPQFPGHNL HDKWEEMAQS
TTQEPEDACK EVRCIEVNSG EAERVQIQDS LDDIVEKKEY EQNYESQKDD ADSSIKNIDM
ELSLYTKPEA EDGVSVKKLI EDVQETEQSV EKQKQSPKKE EMEQYLSRDM SEQVTKSLPE
EEQCVQEYGA YDKLEAQDVL TINKLEESQQ TEQSVEKEDT KKNLSSKKED LKQNLSMDQS
EQLYKSPPED EKCVEVYEGS DKDDNTYEAL KKKVKEMQKT IEYFMSIQSA EEKQSPSFNI
IDDTLSPGEY FKMRRSRSCR ENLLFTKAAA AAASRGFIFE TTNTSFDSDI TVSMDAQSIK
DSDTETSSSS FHEFMAGLRE RTMQHHSTHS DDTDTKTMKP ENTDDGGEKT EFERQQSQII
ELWQVCNVPL VHRTYFFLLF KGDPSDFVYM EVELRRLSFL KDSTETSRKQ TAKAVTRERE
WLAKQIPNKF GKKEKEEVYK KWGVELSSKR RSLQVTHKLW NNNTKDIEHC KESASLIATL
VGFVDSTLTP KEMFGLSLTP TTFNIKPSSG WKFSNSFSRI SFTG
