KN14J_ARATH
ID KN14J_ARATH Reviewed; 1071 AA.
AC B3H6Z8; E1ACC4; Q9CAC9; Q9SH47;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Kinesin-like protein KIN-14J {ECO:0000305};
DE AltName: Full=Kinesin KinG {ECO:0000312|EMBL:ADL28383.1};
GN Name=KIN14J {ECO:0000305};
GN OrderedLocusNames=At1g63640 {ECO:0000312|Araport:AT1G63640};
GN ORFNames=F24D7.17 {ECO:0000312|EMBL:AAG52420.1},
GN F2K11.1 {ECO:0000312|EMBL:AAF19694.1};
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. Landsberg erecta;
RX PubMed=21182528; DOI=10.1111/j.1469-8137.2010.03587.x;
RA Buschmann H., Green P., Sambade A., Doonan J.H., Lloyd C.W.;
RT "Cytoskeletal dynamics in interphase, mitosis and cytokinesis analysed
RT through Agrobacterium-mediated transient transformation of tobacco BY-2
RT cells.";
RL New Phytol. 190:258-267(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment==A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=B3H6Z8-1; Sequence=Displayed;
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=AAF19694.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG52420.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; HM590591; ADL28383.1; -; mRNA.
DR EMBL; AC008047; AAF19694.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011622; AAG52420.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34122.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59867.1; -; Genomic_DNA.
DR PIR; C96661; C96661.
DR RefSeq; NP_001322194.1; NM_001334116.1. [B3H6Z8-1]
DR RefSeq; NP_176551.3; NM_105041.4. [B3H6Z8-1]
DR AlphaFoldDB; B3H6Z8; -.
DR SMR; B3H6Z8; -.
DR STRING; 3702.AT1G63640.1; -.
DR iPTMnet; B3H6Z8; -.
DR PaxDb; B3H6Z8; -.
DR PRIDE; B3H6Z8; -.
DR EnsemblPlants; AT1G63640.1; AT1G63640.1; AT1G63640. [B3H6Z8-1]
DR EnsemblPlants; AT1G63640.4; AT1G63640.4; AT1G63640. [B3H6Z8-1]
DR GeneID; 842668; -.
DR Gramene; AT1G63640.1; AT1G63640.1; AT1G63640. [B3H6Z8-1]
DR Gramene; AT1G63640.4; AT1G63640.4; AT1G63640. [B3H6Z8-1]
DR KEGG; ath:AT1G63640; -.
DR Araport; AT1G63640; -.
DR TAIR; locus:2026639; AT1G63640.
DR eggNOG; KOG0239; Eukaryota.
DR InParanoid; B3H6Z8; -.
DR PhylomeDB; B3H6Z8; -.
DR PRO; PR:B3H6Z8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; B3H6Z8; baseline and differential.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
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; PF00307; CH; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00033; CH; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..1071
FT /note="Kinesin-like protein KIN-14J"
FT /id="PRO_0000438045"
FT DOMAIN 39..142
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 472..800
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 157..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 299..389
FT /evidence="ECO:0000255"
FT COILED 811..844
FT /evidence="ECO:0000255"
FT COMPBIAS 891..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 556..563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 35
FT /note="M -> V (in Ref. 1; ADL28383)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="L -> I (in Ref. 1; ADL28383)"
FT /evidence="ECO:0000305"
FT CONFLICT 808
FT /note="S -> N (in Ref. 1; ADL28383)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1071 AA; 119785 MW; B230C3939692FB43 CRC64;
MSSHLSQDAN MNGVYVRSDV SSMLSFDGSE SRESMDDSKK GHQSLVEWLN ETLPYLKLPW
EASEDELRAC LRDGTVLCSL LNQLSPGSMR MGGSFEPASV KIERFLTAMD EMALPRFEVS
DIEQGDMVPV LQSLKALKAS FSDGSYDKNS LAARRRWSLP EDHSDSRGDD RNFTDGFQSK
EGSEIDMSDA KISDLLKSNS LRNAPTRSLF DMLDKLLDES MTKMNGHVSH AMASLLSALV
QVIEQRISNQ ADNLKNQNIL FRVREEKYRS RIKVLESLAA GTTKENEIVT NCMEHIKLEK
TRIEEKERSE EKDVVRLRKE KERSDAEIRQ LKQELKLVKE THENQCLELE AKAQKTRDEL
EKKLKDAELH VVDSSRKVKE LEKLCQSKSQ RWEKKECIYQ NFIDNHSGAL QELSATSLSI
KHEVVRTQRK YFEDLNYYGL KLKGVADAAK NYHVVLEENR RLYNEVQELK GNIRVYCRIR
PFLPGQNSRQ TTIEYIGETG ELVVANPFKQ GKDTHRLFKF NKVFDQAATQ EEVFLDTRPL
IRSILDGYNV CIFAYGQTGS GKTYTMSGPS ITSKEDWGVN YRALNDLFLL TQSRQNTVMY
EVGVQMVEIY NEQVRDILSD GGSSRRLGIW NTALPNGLAV PDASMHCVRS TEDVLELMNI
GLMNRTVGAT ALNERSSRSH CVLSVHVRGV DVETDSILRG SLHLVDLAGS ERVDRSEATG
ERLKEAQHIN KSLSALGDVI FALAHKNPHV PYRNSKLTQV LQSSLGGQAK TLMFVQVNPD
GDSYAETVST LKFAERVSGV ELGAAKSSKE GRDVRQLMEQ VSNLKDVIAK KDEELQNFQK
VKGNNATSLK RGLSNLRLVG PTSPRRHSIG ASPNARRGKA SGLFGRGTSD VDNCSEYSSK
HSDSGSQQSS DERKHQKDYH QPSKFAGAAK GIDFDDEDVE LVGLADADSE DRLSDISDSC
LSMGTETDGS ISSAVELTLF PETAKPLELI ERPEARMTSE KLEKSVKMGK TEPKDRTNIP
SKIPKQTLKP PGQTRPSRLS IATSSSSKAL TGAKRPTIST SSSAKPLNRR R
