KN12F_ARATH
ID KN12F_ARATH Reviewed; 1114 AA.
AC F4JDI6; Q9LJY3;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Kinesin-like protein KIN-12F {ECO:0000305};
GN Name=KIN12F {ECO:0000305};
GN OrderedLocusNames=At3g20150 {ECO:0000312|Araport:AT3G20150};
GN ORFNames=MAL21.18 {ECO:0000312|EMBL:BAB01875.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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-12 subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01875.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000383; BAB01875.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76340.1; -; Genomic_DNA.
DR RefSeq; NP_188650.2; NM_112906.5.
DR AlphaFoldDB; F4JDI6; -.
DR SMR; F4JDI6; -.
DR STRING; 3702.AT3G20150.1; -.
DR iPTMnet; F4JDI6; -.
DR PaxDb; F4JDI6; -.
DR PRIDE; F4JDI6; -.
DR ProteomicsDB; 237095; -.
DR EnsemblPlants; AT3G20150.1; AT3G20150.1; AT3G20150.
DR GeneID; 821558; -.
DR Gramene; AT3G20150.1; AT3G20150.1; AT3G20150.
DR KEGG; ath:AT3G20150; -.
DR Araport; AT3G20150; -.
DR TAIR; locus:2087650; AT3G20150.
DR eggNOG; KOG4280; Eukaryota.
DR HOGENOM; CLU_009194_0_0_1; -.
DR InParanoid; F4JDI6; -.
DR OMA; KCTEMES; -.
DR OrthoDB; 130600at2759; -.
DR PRO; PR:F4JDI6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; F4JDI6; baseline and differential.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
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 3: Inferred from homology;
KW ATP-binding; Coiled coil; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1114
FT /note="Kinesin-like protein KIN-12F"
FT /id="PRO_0000437193"
FT DOMAIN 104..436
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 761..791
FT /evidence="ECO:0000255"
FT COILED 872..942
FT /evidence="ECO:0000255"
FT COILED 1038..1081
FT /evidence="ECO:0000255"
FT COMPBIAS 7..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 175..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1114 AA; 125113 MW; B4B1731A488F91E0 CRC64;
MADNRIAGSL PTSSKWSFLP KSVSSHFKPS SNPRSSNPDI ENAPPQNPNI HNPRNQSVSS
KSTAYKNQMD SPNCRSQVSA SRPRAISALK TRNEVEEEGA SNPHVKVVVR IKPTKEYCWK
VKKVSKVSYS VRDRHFTFDS VLDSNLNQDD VFQQIGVPLV RDALSGYNTS VLSYGQNGSG
KTYTMWGPAG SMLEDPSPKG EQGLAPRIFQ MLFSEIQREK IKSGGKEVNY QCRCSFLEIY
NGQISDLIDQ TQRNLKIKDD AKNGIYVENL TEEYVDSYED VAQILMKGLS SRKVGATSTS
FQSSRSHVIL SFIVESWNKG ASSRCFNTTR TSRINLVDLA GAGTNERDAT KHCVEEEKFL
KKSLSELGHV VNSLAENVHP GISDRSLHKT SCLTHLLQES LGGNSKLTIL CNIFPSDKDT
KRTMSTLRFG ERAKAMGNKP MINEISEEDV NDLSDQIRLL KEELSKVKAD ACHSVGSKND
YFGAKNARES LNQLRVSLNR SLMLPKIDND EEEITVDEDD FKELHLQIKS LRGSFNQKLK
KFPVNRDSVN SSFVTAFGES ELMDDDEICS EEVEVEENDF GESLEEHDSA ATVCKSSEKS
RIEEFVSENS ISISPCRQSL ILQEPIQSES PKFRDSLRKS IALSSSCLRN QNSLAKSIKS
TCFAESQHIR SSLRGSKIFT GSTESLAASL RRGLDIIDNP MNPASNRCSV SLSSDNLTMQ
PPTDDRLPLS PLCPTCRICS SKLPSVVEGD GYHMEGVLEK QQELEKLCSE QAAKIEQLTR
LVGQHKLQTE DETEKLMGAS NGERLPSANE NQLLSCITET YDVKQISDDD SKKTDFDIGE
KEALLKEIED LKKKLQTPVT MSTNELRSSL LARSFQLRSK NAEKDIEEER LRCTEMESEW
ISLTDEFRVE IETQRTRAEK AEAQLKQEKL SSEELEDALR RAVLGHARFV EHYTELQEKY
NDLCSKHKAT VEWITELKKA VAKAGKKGCG SRFAKSLASE LSALRVERER ERDLLKKENI
SLKIQLRNTA EAVHTAGEVL VRLREAEQSA SAAEEKFNEV EEENEKLKKK MEKLKRRHKL
EVVTIKKSLK QNTLPESALQ PLHQRNSAIE EEGM
