KN10A_ARATH
ID KN10A_ARATH Reviewed; 869 AA.
AC Q8VWI7; O23291; Q0WT18;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Kinesin-like protein KIN-10A {ECO:0000305};
DE AltName: Full=Phragmoplast-associated kinesin-related protein 2 {ECO:0000303|PubMed:11701879};
DE Short=AtPAKRP2 {ECO:0000303|PubMed:11701879};
GN Name=KIN10A {ECO:0000305}; Synonyms=PAKRP2 {ECO:0000312|EMBL:AAL32294.1};
GN OrderedLocusNames=At4g14330 {ECO:0000312|Araport:AT4G14330};
GN ORFNames=dl3205w {ECO:0000312|EMBL:CAB10212.1},
GN FCAALL.179 {ECO:0000312|EMBL:CAB78475.1};
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 / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=11701879; DOI=10.2307/3871585;
RA Lee Y.R., Giang H.M., Liu B.;
RT "A novel plant kinesin-related protein specifically associates with the
RT phragmoplast organelles.";
RL Plant Cell 13:2427-2439(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
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 [4]
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 [5]
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 [6]
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 [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 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: Probable plus end-directed motor protein that may contribute
CC to the transport of Golgi-derived vesicles in the phragmoplast.
CC {ECO:0000269|PubMed:11701879}.
CC -!- SUBUNIT: Binds microtubules. {ECO:0000269|PubMed:11701879}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11701879}.
CC Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:11701879}.
CC Note=During interphase, present throughout the cytoplasm. Microtubule-
CC associated during late anaphase. {ECO:0000269|PubMed:11701879}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-10 subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10212.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78475.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF320248; AAL32293.1; -; mRNA.
DR EMBL; AF320249; AAL32294.1; -; Genomic_DNA.
DR EMBL; Z97336; CAB10212.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161538; CAB78475.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83420.1; -; Genomic_DNA.
DR EMBL; AK227746; BAE99730.1; -; mRNA.
DR PIR; B71405; B71405.
DR RefSeq; NP_567426.1; NM_117510.5.
DR AlphaFoldDB; Q8VWI7; -.
DR SMR; Q8VWI7; -.
DR STRING; 3702.AT4G14330.1; -.
DR iPTMnet; Q8VWI7; -.
DR PaxDb; Q8VWI7; -.
DR PRIDE; Q8VWI7; -.
DR ProteomicsDB; 230294; -.
DR EnsemblPlants; AT4G14330.1; AT4G14330.1; AT4G14330.
DR GeneID; 827075; -.
DR Gramene; AT4G14330.1; AT4G14330.1; AT4G14330.
DR KEGG; ath:AT4G14330; -.
DR Araport; AT4G14330; -.
DR TAIR; locus:2129630; AT4G14330.
DR eggNOG; KOG0243; Eukaryota.
DR HOGENOM; CLU_007191_0_0_1; -.
DR InParanoid; Q8VWI7; -.
DR OMA; VQQDIIG; -.
DR OrthoDB; 573890at2759; -.
DR PhylomeDB; Q8VWI7; -.
DR PRO; PR:Q8VWI7; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VWI7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0009524; C:phragmoplast; 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; IDA:UniProtKB.
DR GO; GO:0003777; F:microtubule motor activity; IDA:TAIR.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0031535; P:plus-end directed microtubule sliding; IDA:TAIR.
DR GO; GO:0047496; P:vesicle transport along microtubule; TAS:UniProtKB.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 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..869
FT /note="Kinesin-like protein KIN-10A"
FT /id="PRO_0000437032"
FT DOMAIN 48..367
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 393..515
FT /evidence="ECO:0000255"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 129..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 308
FT /note="S -> Y (in Ref. 5; BAE99730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 869 AA; 97419 MW; 7A43F05E705A8898 CRC64;
MAPTPSSSRS NQTQYTLIRT PQTKQRLNFH SKTPNPDGSK DPSPPEHPVE VIGRIRDYPD
RKEKSPSILQ VNTDNQTVRV RADVGYRDFT LDGVSFSEQE GLEEFYKKFI EERIKGVKVG
NKCTIMMYGP TGAGKSHTMF GCGKEPGIVY RSLRDILGDS DQDGVTFVQV TVLEVYNEEI
YDLLSTNSSN NLGIGWPKGA STKVRLEVMG KKAKNASFIS GTEAGKISKE IVKVEKRRIV
KSTLCNERSS RSHCIIILDV PTVGGRLMLV DMAGSENIDQ AGQTGFEAKM QTAKINQGNI
ALKRVVESIA NGDSHVPFRD SKLTMLLQDS FEDDKSKILM ILCASPDPKE MHKTLCTLEY
GAKAKCIVRG SHTPNKDKYG GDESASAVIL GSRIAAMDEF IIKLQSEKKQ KEKERNEAQK
QLKKKEEEVA ALRSLLTQRE ACATNEEEIK EKVNERTQLL KSELDKKLEE CRRMAEEFVE
MERRRMEERI VQQQEELEMM RRRLEEIEVE FRRSNGGSVD ETSGFAKRLR SLYSDDDPGM
VKSMDLDMGD PEPVKQVWGA VSHQSSNTIS SNFTNLLQPK PSENMLTQMY PDRVCLSTVF
EEEEVEEEEE KVIVEDKSIC LITTPMPSLN SEGLGKENCF NGADDKESAS SRRLRIQNIF
TLCGNQRELS QHSGQEEDQA NIASPDKKDN QFFSITNKAE ALAVEEAKEN NISVDQRENG
QLDIYVKWET AADNPRKLIT TLRVTKDATL ADLRKLIEIY LGSDNQAFTF LKLGEPCGAQ
VAKEKESTVQ ATSLPLCNGH AYLATLRPGK SSQHKSLQPA SPLPLNPIEN MMEVTPISKV
TPNHQVDEFS SPNLVAHLSS TPFITLRRH
