KN14O_ARATH
ID KN14O_ARATH Reviewed; 1140 AA.
AC F4IAR2; Q9LPQ7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Kinesin-like protein KIN-14O {ECO:0000305};
GN Name=KIN14O {ECO:0000305};
GN OrderedLocusNames=At1g18410 {ECO:0000312|Araport:AT1G18410};
GN ORFNames=F15H18.10 {ECO:0000312|EMBL:AAF25983.1};
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=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 [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 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-14 subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF25983.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC013354; AAF25983.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F4IAR2; -.
DR SMR; F4IAR2; -.
DR STRING; 3702.AT1G18410.1; -.
DR PaxDb; F4IAR2; -.
DR PeptideAtlas; F4IAR2; -.
DR PRIDE; F4IAR2; -.
DR Araport; AT1G18410; -.
DR TAIR; locus:2014129; AT1G18410.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_001485_1_2_1; -.
DR InParanoid; F4IAR2; -.
DR PRO; PR:F4IAR2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4IAR2; 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; 3.40.850.10; -; 1.
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; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1140
FT /note="Kinesin-like protein KIN-14O"
FT /id="PRO_0000438048"
FT DOMAIN 632..952
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1028..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 327..546
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 716..723
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1140 AA; 128008 MW; C56DF919F5D1AC08 CRC64;
MLESEFQREH AFESATEQEL TCPISDNLHE SVEADDDSVQ MLDNLTLNTN PAESCESEEI
QTKALPSSSS GQDLVASDED SEDVELGDTF YSCSELLQRN CCVLPYKAQK KTKENPFDFD
VRTWSSPCDF PRFGEMILLS PVLNPMPFFS CCTKRAIFCS SPGSSHGGST PRSPFSPSSP
RERHNKGLAD SRFQRPLPNS SALDPSSPGS MLHGGHKSHE AFQMKQGRFD LQAAKISELM
KSNNLDNAPT QSLLSIVNGI LDETIERKNG ELPQRVACLL RKVVQEIERR ISTQSEHLRT
QNSVFKAREE KYQSRIKVLE TLASGTSEEN ETEKSKLEEK KKDKEEDMVG IEKENGHYNL
EISTLRRELE TTKKAYEQQC LQMESKTKGA TAGIEDRVKE LEQMRKDASV ARKALEERVR
ELEKMGKEAD AVKMNLEEKV KELQKYKDET ITVTTSIEGK NRELEQFKQE TMTVTTSLEA
QNRELEQAIK ETMTVNTSLE AKNRELEQSK KETMTVNTSL KAKNRELEQN LVHWKSKAKE
MEEKSELKNR SWSQKELSYR SFISFQCQAL QELRFYSKSI KQEILKVQDK YTVEFSQLGK
KLLELGDAAA NYHEVLTENQ KLFNELQELK GNIRVYCRVR PFLRGQGASK TVVEHIGDHG
ELVVLNPTKP GKDAHRKFRF NKVYSPASTQ AEVFSDIKPL IRSVLDGYNV CIFAYGQTGS
GKTYTMTGPD GASEEEWGVN YRALNDLFRI SQSRKSNIAY EVGVQMVEIY NEQVRDLLSG
ILSTTQQNGL AVPDASMYPV TSTSDVLELM SIGLQNRVVS STALNERSSR SHSIVTVHVR
GKDLKTGSAL YGNLHLVDLA GSERVDRSEV TGDRLKEAQH INKSLSALGD VIFSLASKSS
HVPYRNSKLT QLLQSSLGGR AKTLMFVQLN PDITSYSESM STLKFAERVS GVELGAAKSS
KDGRDVRELM EQDTIARKDD EIERLHLLKD INYPQRLQKK SLGQSDDFNS EAGDSQLSIE
DDSRFQHDYT RQSRHSVTDG EALASSTDAE YDDETEGSTD APCAAEGRKP LKISDKPKPV
TPRSNTTTSR PLDKLKQVTM RTTNIAKATS ALLSPSSQGM KKTGSASNFL KSPKDSKRWS
