ID   KN12D_ARATH             Reviewed;        2771 AA.
AC   Q27IK6; Q9LJ60;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Kinesin-like protein KIN-12D {ECO:0000305};
DE   AltName: Full=Phragmoplast orienting kinesin 2 {ECO:0000303|PubMed:16682350};
GN   Name=KIN12D {ECO:0000305}; Synonyms=POK2 {ECO:0000312|EMBL:ABD62997.1};
GN   OrderedLocusNames=At3g19050 {ECO:0000312|Araport:AT3G19050};
GN   ORFNames=K13E13.17 {ECO:0000312|EMBL:BAB01702.1};
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], TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND
RP   FUNCTION.
RX   PubMed=16682350; DOI=10.1016/j.cub.2006.03.034;
RA   Muller S., Han S., Smith L.G.;
RT   "Two kinesins are involved in the spatial control of cytokinesis in
RT   Arabidopsis thaliana.";
RL   Curr. Biol. 16:888-894(2006).
RN   [2]
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   [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   REVIEW.
RX   PubMed=16530461; DOI=10.1016/j.tplants.2006.02.004;
RA   Vanstraelen M., Inze D., Geelen D.;
RT   "Mitosis-specific kinesins in Arabidopsis.";
RL   Trends Plant Sci. 11:167-175(2006).
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   -!- FUNCTION: Involved in the spatial control of cytokinesis by a proper
CC       phragmoplast guidance. {ECO:0000269|PubMed:16682350}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, phragmoplast
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in tissues enriched in dividing cells,
CC       such as root meristems, root primordia, and leaf primordia/young
CC       leaves. {ECO:0000269|PubMed:16682350}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Pok1 and pok2 double mutant
CC       displays smaller cotyledons as well as shorter, wider roots and
CC       hypocotyls with adult plants exhibiting a dwarfed stature and producing
CC       reduced numbers of seeds. {ECO:0000269|PubMed:16682350}.
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=BAB01702.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ399530; ABD62997.1; -; mRNA.
DR   EMBL; AP000735; BAB01702.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE76188.1; -; Genomic_DNA.
DR   RefSeq; NP_188535.4; NM_112791.6.
DR   SMR; Q27IK6; -.
DR   BioGRID; 6772; 1.
DR   STRING; 3702.AT3G19050.1; -.
DR   iPTMnet; Q27IK6; -.
DR   PaxDb; Q27IK6; -.
DR   PRIDE; Q27IK6; -.
DR   ProteomicsDB; 238225; -.
DR   EnsemblPlants; AT3G19050.1; AT3G19050.1; AT3G19050.
DR   GeneID; 821439; -.
DR   Gramene; AT3G19050.1; AT3G19050.1; AT3G19050.
DR   KEGG; ath:AT3G19050; -.
DR   Araport; AT3G19050; -.
DR   TAIR; locus:2085844; AT3G19050.
DR   eggNOG; KOG4280; Eukaryota.
DR   HOGENOM; CLU_000399_0_0_1; -.
DR   InParanoid; Q27IK6; -.
DR   OMA; RRCAASW; -.
DR   OrthoDB; 38542at2759; -.
DR   PhylomeDB; Q27IK6; -.
DR   PRO; PR:Q27IK6; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q27IK6; baseline and differential.
DR   Genevisible; Q27IK6; AT.
DR   GO; GO:0032153; C:cell division site; IDA:TAIR.
DR   GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0009524; C:phragmoplast; 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:0000911; P:cytokinesis by cell plate formation; IMP:TAIR.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
DR   GO; GO:0080175; P:phragmoplast microtubule organization; IMP:TAIR.
DR   Gene3D; 3.40.850.10; -; 1.
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; 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   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Motor protein; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..2771
FT                   /note="Kinesin-like protein KIN-12D"
FT                   /id="PRO_0000000004"
FT   DOMAIN          193..530
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..404
FT                   /note="Microtubules-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LDN0"
FT   REGION          431..437
FT                   /note="Microtubules-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LDN0"
FT   REGION          479..483
FT                   /note="Microtubules-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LDN0"
FT   REGION          2727..2771
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1033..1110
FT                   /evidence="ECO:0000255"
FT   COILED          1267..1331
FT                   /evidence="ECO:0000255"
FT   COILED          1410..1505
FT                   /evidence="ECO:0000255"
FT   COILED          2108..2390
FT                   /evidence="ECO:0000255"
FT   COILED          2512..2677
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..133
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2748..2771
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         274..281
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   2771 AA;  315062 MW;  967CBE35008AA4DA CRC64;
     MSKETKLSRR DSDNHDDEIE NVPENLRASL LSLTSNDSLK NPKHECGSKI DRTPSKPRAK
     NPDPALPLRT PDKYRSAAAF SKNRFGWGDK CDSITNTTNA ALLNTTPKTG RVVGRAYSET
     NSTQNTPTKS VSKPPGSCYR GKLDGTGTVR AGGYASLYKG LSSSSGQVST VVNSVEVPHF
     SLKEDPSFWM DHNVQILIRV RPLNSMERSI NGYNRCLKQE SSQCVAWIGP PETRFQFDHV
     ACETIDQETL FRVAGLPMVE NCLSGYNSCI FAYGQTGSGK TYTMLGEVGD LEFKPSPNRG
     MMPRIFEFLF ARIQAEEESR RDERLKYNCK CSFLEIYNEQ ITDLLEPSST NLQLREDIKS
     GVYVENLTEC EVQSVQDILG LITQGSLNRR VGATNMNRES SRSHSVFTCV IESRWEKDST
     ANMRFARLNL VDLAGSERQK TSGAEGDRLK EAASINKSLS TLGHVIMVLV DVANGKPRHI
     PYRDSRLTFL LQDSLGGNSK TMIIANASPS VSCAAETLNT LKFAQRAKLI QNNAVVNEDS
     NEDVLELRRQ IRLLKEELSL LKRQNISRAL SFGSATANFA ESQVDSPSSV MHETGQQQAG
     NLLVYESGGC VRMSRKQLKS LEITLAGSLR REHVADASIK KLEAEIEHLN RLVRQREEDT
     RSTKMMLRFR EDKIQRLESL LGNHISADSF LLEENNVLSE EIQLLQAKID KNPELTRFAL
     ENIRLLDQLR RFQEFYEEGE REILLGEVSN LRNQLFQFLD ENSDWQKHVD DGIEPQGASR
     MSKENCSLQE ELKKTCYELE KCRSNLGSCL EENAKLSREI NDLQAMVSDI RACTPDEHSS
     VNKQKALLGT QNFEPHETLA CEQANYVEEI IKLQLDLDVQ KIILDEERTL RGDTEAQAVR
     LKFDIEVLKD QLLLISKQQK NVYSELGETK SAVAALESQN IILIQEAVEL RRIKENYFEL
     LKKQELDIPA MKSKQCDEFK DNPAEDSEID TKFKKMQASL EKAKRLNMLY KSDIASKACG
     DEEMDEVCKQ AEAATAEVIV CLQNELEVLQ KEVNDFQSKE NVTEKQVEIL ETQMEELQDK
     LRDTTMDNEQ LQEQLRGKDM ELLIISNEME LLTSELEEIL LNGNEGLTDA CYQADLISGS
     LPDKRIWISE QVGGLIRTLS ERELMIEDLE SCLEDANKKR CDIESMLKSL KGAAIVMNEA
     HQREFEEKET DVLLLKSQLC TKTETILRLQ EKLKMAERLI YEASDCATAS LIIVNRYSEV
     TESHTFELKQ KDFQVAESTG TILSLKQQVQ DLEATCKEFR SKLLEEEKNA SAMEQKLEEI
     EETSISAMKE KLSELKGGVS DLRSCITMCQ EHDKYTEAEN SLSSPAHCSE GQEPGRNVVV
     SSCIEKTPNN NHTESMRLSS KVSSERGKVI ILLKQEMESA LASLKEVQVE MANLKGEKEE
     LKASEKRSLS NLNDLAAQIC NLNTVMSNME EQYEHKMEVT DHKLKTLEHE IAKMKIEADQ
     EYVENLCILK KFEEAQGTIR EADITVNELV IANEKMRFDL EKQKKRGISL VGEKKALVEK
     LQELESINVK ENEKLAYLEK LFESSLMGIG NLVEELATVV RKLQDESSVA LTGMAKDLSE
     LKSWVSETNS ARLFLEDIWS EIIMKDCAIS VLHLCHMGIL LETVTGINTE NGLLQRGLCV
     SNSSIAGLRD NNLRLRRELE MFANLKGKLL TDIKNGFERI SRNEEATNLL TTKLSSFDQK
     ISGLQYQEDL MLQRSNSMGS QLDILLKEID LSNGDLAETL LEQERHLNQK NDFFDTEVQL
     YLMDLCSKDV ELLVLAQTAK EYSSCLAVVD RELLDHHVIV EDLKEKLIVS QVEGELKDQC
     LVDNKLETVS VKEELTEAQS KIKVLSSDLD RSVQKIAEID EVNKDFGERV IFLESSITGL
     QQELAMKASE LYSLEHSRSV TAEELDIKER DVQVYADIVS SLKKENVSLK NKFIHFGEDQ
     FKALDVTRLS IAKCSHLTED SKKLEKLTRD GMAISDKMLQ LICENVDKAS VFADTVQSLQ
     IDVQELLSEN LNLHDELLRK DDVLKGLSFD LSLLQESASN SRDKKDETKE IMVHVEALEK
     TLALKTFELE DAVSHAQMLE VRLQESKEIT RNLEVDTEKA RKCQEKLSAE NKDIRAEAED
     LLAEKCSLEE EMIQTKKVSE SMEMELFNLR NALGQLNDTV AFTQRKLNDA IDERDNLQDE
     VLNLKEEFGK MKSEAKEMEA RYIEAQQIAE SRKTYADERE EEVKLLEGSV EELEYTINVL
     ENKVNVVKDE AERQRLQREE LEMELHTIRQ QMESARNADE EMKRILDEKH MDLAQAKKHI
     EALERNTADQ KTEITQLSEH ISELNLHAEA QASEYMHKFK ELEAMAEQVK PEIHVSQAID
     SSLSKGSGKP RGSGSPFRCI GLGITQQMRS EKDEELAAAR LRIEELETVV STRQKEIFLL
     NSKLAKVDSM THDINRVLLG VKQNVTNCAS FLDSQQVLKI AEMLQHNSSD SRERDLEVSH
     LKQQLNEYNE KRQGWIEEIE GKQTELVTAQ IKLEEHRQYQ QLLKKENELL KKENFSHKIK
     VMELEGEVKK LSSHQNPEWR TRDQARIKEE NNVLKLQLDE LNLKLRRADV SVSRAKEELA
     FYRASSVKNP HSNFDKTHQL STKLKETEED RMQLAQELLS LCTSILKAAG VTGEDFTDIN
     PEVAEEALEQ LKTKLGLLES EVHHFRLKGK AKSRRSRNPE RKMPSMPSPR RSWSQSPRSM
     SQVPFFSSLD R