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KN12E_ARATH
ID   KN12E_ARATH             Reviewed;        1263 AA.
AC   F4J1U4; Q9LXV6;
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-12E {ECO:0000305};
GN   Name=KIN12E {ECO:0000305};
GN   OrderedLocusNames=At3g44050 {ECO:0000312|Araport:AT3G44050};
GN   ORFNames=F26G5 {ECO:0000312|EMBL:AL353814},
GN   T15B3_190 {ECO:0000312|EMBL:CAB88133.1};
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=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(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=CAB88133.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL163975; CAB88133.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL353814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002686; AEE77856.1; -; Genomic_DNA.
DR   PIR; T48959; T48959.
DR   RefSeq; NP_189991.2; NM_114273.4.
DR   AlphaFoldDB; F4J1U4; -.
DR   SMR; F4J1U4; -.
DR   STRING; 3702.AT3G44050.1; -.
DR   iPTMnet; F4J1U4; -.
DR   PaxDb; F4J1U4; -.
DR   PRIDE; F4J1U4; -.
DR   ProteomicsDB; 238400; -.
DR   EnsemblPlants; AT3G44050.1; AT3G44050.1; AT3G44050.
DR   GeneID; 823523; -.
DR   Gramene; AT3G44050.1; AT3G44050.1; AT3G44050.
DR   KEGG; ath:AT3G44050; -.
DR   Araport; AT3G44050; -.
DR   TAIR; locus:2097184; AT3G44050.
DR   eggNOG; KOG4280; Eukaryota.
DR   HOGENOM; CLU_005600_1_0_1; -.
DR   InParanoid; F4J1U4; -.
DR   OMA; AHETAII; -.
DR   OrthoDB; 38542at2759; -.
DR   PRO; PR:F4J1U4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; F4J1U4; 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:0005641; C:nuclear envelope lumen; IDA:TAIR.
DR   GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR   GO; GO:0005819; C:spindle; 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; IBA:GO_Central.
DR   GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:1901673; P:regulation of mitotic spindle assembly; IEA:InterPro.
DR   GO; GO:0051225; P:spindle assembly; IMP:TAIR.
DR   Gene3D; 3.40.850.10; -; 1.
DR   InterPro; IPR044986; KIF15/KIN-12E.
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   PANTHER; PTHR37739; PTHR37739; 3.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 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..1263
FT                   /note="Kinesin-like protein KIN-12E"
FT                   /id="PRO_0000437192"
FT   DOMAIN          93..430
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          21..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          679..737
FT                   /evidence="ECO:0000255"
FT   COILED          764..805
FT                   /evidence="ECO:0000255"
FT   COILED          831..881
FT                   /evidence="ECO:0000255"
FT   COILED          905..966
FT                   /evidence="ECO:0000255"
FT   COILED          1091..1168
FT                   /evidence="ECO:0000255"
FT   COILED          1193..1251
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        30..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         174..181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1263 AA;  142668 MW;  FC87CC9942D867BE CRC64;
     MPFISETASA IKRRFGFNDR PAPSESLRSV PCTPEANTVS RDNHTHQSLL FSSAVRSMPE
     LDEDGAICAG SAQISRSQSF EFNEDPAFWK DHNVQVIIRT RPLSSSEISV QGNNKCVRQD
     NGQAITWIGN PESRFTFDLV ADENVSQEQM FKVAGVPMVE NVVAGYNSCM FAYGQTGSGK
     THTMLGDIEG GTRRHSVNCG MTPRVFEYLF SRIQKEKEVR KEEKLHFTCR CSFLEIYNEQ
     ILDLLDPSSY NLQLREDHKK GIHVENLKEI EVSSARDVIQ QLMQGAANRK VAATNMNRAS
     SRSHSVFTCI IESKWVSQGV THHRFARLNL VDLAGSERQK SSGAEGERLK EATNINKSLS
     TLGLVIMNLV SVSNGKSVHV PYRDSKLTFL LQDSLGGNSK TIIIANISPS SSCSLETLST
     LKFAQRAKLI KNNAIVNEDA SGDVIAMRLQ IQQLKKEVTR LRGMGGVDNQ DMDTISMGCP
     ASPMSLKWDG FNGSFTPLTT HKRMSKVKDY EVALVGAFRR EREKDVALQA LTAENEASMK
     LEKKREDEIR GLKMMLKLRD SAIKSLQGVT SGKIPVEAHL QKEKGDLMKE IEVLRAQVDR
     NQEVTKFATE NLRLKEEIRR LKSQGEEGER DILNQQIQAL QAKLLEALDW KLMHESDSSM
     VKEDGNISNM FCSNQNQESK KLSSIQDENE FLRMQAIQNR AEMESLQKSL SFSLDEKERL
     QKLVDNLSNE LEGKIRSSGM VGDDDQMEVK TMVQAIACVS QREAEAHETA IKLSKENDDL
     RQKIKVLIED NNKLIELYEQ VAEENSSRAW GKIETDSSSN NADAQNSAEI ALEVEKSAAE
     EQKKMIGNLE NQLTEMHDEN EKLMSLYENA MKEKDELKRL LSSPDQKKPI EANSDTEMEL
     CNISSEKSTE DLNSAKLKLE LAQEKLSISA KTIGVFSSLE ENILDIIKLS KESKETEEKV
     KEHQSELGSI KTVSDQTNAR KEVAEKKLAA LRCSLSNFAS SAVYFQQREE RARAHVNSFS
     GYLNQKNEEL DVIRSHKREI DAAMGKIQQS EAELKSNIVM LKIKVDEENK RHEEEGVLCT
     IDNILRTGKA TDLLKSQEEK TKLQSEMKLS REKLASVRKE VDDMTKKSLK LEKEIKTMET
     EIEKSSKTRT ESEMELENTI QEKQTIQEME EQGMSEIQNM IIEIHQLVFE SDLRKEEAMI
     IREELIAEEL RAKDVHTNMI ERVENALKTL ENQNNSVSGK IEEEVENVLS LVHEASRLLE
     VSH
 
 
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