ID   KN14P_ARATH             Reviewed;        1025 AA.
AC   Q0WN69; Q9C9A8; Q9C9S6;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Kinesin-like protein KIN-14P {ECO:0000305};
GN   Name=KIN14P {ECO:0000305};
GN   OrderedLocusNames=At1g73860 {ECO:0000312|Araport:AT1G73860};
GN   ORFNames=F25P22.28 {ECO:0000312|EMBL:AAG52083.1},
GN   F2P9.27 {ECO:0000312|EMBL:AAG52533.1};
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   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   [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   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=AAG52083.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG52533.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC012679; AAG52083.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC016662; AAG52533.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE35517.1; -; Genomic_DNA.
DR   EMBL; AK229581; BAF01431.1; -; mRNA.
DR   PIR; B96766; B96766.
DR   RefSeq; NP_177527.3; NM_106046.5.
DR   AlphaFoldDB; Q0WN69; -.
DR   SMR; Q0WN69; -.
DR   STRING; 3702.AT1G73860.1; -.
DR   PaxDb; Q0WN69; -.
DR   PRIDE; Q0WN69; -.
DR   ProteomicsDB; 237064; -.
DR   EnsemblPlants; AT1G73860.1; AT1G73860.1; AT1G73860.
DR   GeneID; 843722; -.
DR   Gramene; AT1G73860.1; AT1G73860.1; AT1G73860.
DR   KEGG; ath:AT1G73860; -.
DR   Araport; AT1G73860; -.
DR   TAIR; locus:2027854; AT1G73860.
DR   eggNOG; KOG0239; Eukaryota.
DR   HOGENOM; CLU_001485_1_2_1; -.
DR   InParanoid; Q0WN69; -.
DR   OrthoDB; 364605at2759; -.
DR   PhylomeDB; Q0WN69; -.
DR   PRO; PR:Q0WN69; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q0WN69; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
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   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Microtubule; Motor protein; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..1025
FT                   /note="Kinesin-like protein KIN-14P"
FT                   /id="PRO_0000438049"
FT   DOMAIN          509..838
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          1..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          881..926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          939..977
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          994..1025
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          203..425
FT                   /evidence="ECO:0000255"
FT   COILED          847..879
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        65..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..286
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        899..920
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         593..600
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1025 AA;  115129 MW;  B56FBB58FE280A99 CRC64;
     MNPMRDQPGS PYGDSTPRSP FSPFSPLSVD DRHRNHADTK TPRSPFSPFS PLSGDERHKS
     LAESKFQQAL ASSGQLDPLS PGSMHHGGHK FHEVFQMKQG RYDLQASKIS EMMKSSSLDN
     APTQSLLSVL NGILDESIER KNGEIPQRVA CLLRKVVQEI ERRISTQAEH LRTQNNIFKT
     REEKYQSRIN VLEALASGTG VEHEIATQQL RQIETEKSMW EEKKKHEEED MVKLMKQNDQ
     HNLEISALKQ ELETTKRKYE QQYSQIESQT KTEKSKWEEQ KKNEEEDMDK LLKENDQFNL
     QISALRQELE TTRKAYEQQC SQMESQTMVA TTGLESRLKE LEQEGKVVNT AKNALEERVK
     ELEQMGKEAH SAKNALEEKI KQLQQMEKET KTANTSLEGK IQELEQNLVM WKTKVREMEK
     KSESNHQRWS QKELSYKSFI DNQSQALLEL RSYSRSIKQE ILKVQENYTD QFSQLGKKLI
     ELSNAAENYH AVLTENRKLF NELQELKGNI RVFCRVRPFL PAQGAANTVV EYVGEDGELV
     VTNPTRPGKD GLRQFKFNKV YSPTASQADV FSDIRPLVRS VLDGYNVCIF AYGQTGSGKT
     YTMTGPDGSS EEDWGVNYRA LNDLFKISQS RKGNISYEVG VQMVEIYNEQ VLDLLSDDNS
     QKKTLGILST TQQNGLAVPD ASMYPVTSTS DVITLMDIGL QNRAVGSTAL NERSSRSHSI
     VTVHVRGKDL KTGSVLYGNL HLVDLAGSER VDRSEVTGDR LREAQHINKS LSSLGDVIFS
     LASKSSHVPY RNSKLTQLLQ TSLGGRAKTL MFVQLNPDAT SYSESMSTLK FAERVSGVEL
     GAAKTSKEGK DVRDLMEQLA SLKDTIARKD EEIERLQHQP QRLQKSMMRR KSIGHTDDIN
     SDTGEYSSQS RYSVTDGESL ASSAEAEYDE RLSEITSDAA SMGTQGSIDV TKRPPRISDR
     AKSVTAKSST SVTRPLDKLR KVATRTTSTV AKVTGLTSSS KGLASSSIKK TGSTSSLAKS
     SKRWA