KN14Q_ORYSJ
ID KN14Q_ORYSJ Reviewed; 954 AA.
AC Q0IMS9; B9GDL4; Q2QP07;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Kinesin-like protein KIN-14Q {ECO:0000305};
DE AltName: Full=Kinesin O12;
DE AltName: Full=OsKCH1 {ECO:0000303|PubMed:19561334};
GN Name=KIN14Q {ECO:0000305};
GN Synonyms=KCH1 {ECO:0000303|PubMed:19561334}, O12;
GN OrderedLocusNames=Os12g0547500 {ECO:0000312|EMBL:BAT17539.1},
GN LOC_Os12g36100 {ECO:0000312|EMBL:ABA98869.1};
GN ORFNames=OsJ_36410 {ECO:0000312|EMBL:EEE53371.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19106179; DOI=10.1093/aob/mcn248;
RA Guo L., Ho C.M., Kong Z., Lee Y.R., Qian Q., Liu B.;
RT "Evaluating the microtubule cytoskeleton and its interacting proteins in
RT monocots by mining the rice genome.";
RL Ann. Bot. 103:387-402(2009).
RN [8]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19561334; DOI=10.1093/pcp/pcp094;
RA Frey N., Klotz J., Nick P.;
RT "Dynamic bridges--a calponin-domain kinesin from rice links actin filaments
RT and microtubules in both cycling and non-cycling cells.";
RL Plant Cell Physiol. 50:1493-1506(2009).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20566563; DOI=10.1093/jxb/erq164;
RA Frey N., Klotz J., Nick P.;
RT "A kinesin with calponin-homology domain is involved in premitotic nuclear
RT migration.";
RL J. Exp. Bot. 61:3423-3437(2010).
RN [10]
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, INTERACTION WITH ACTIN,
RP AND SUBCELLULAR LOCATION.
RX PubMed=21047815; DOI=10.1093/jb/mvq122;
RA Umezu N., Umeki N., Mitsui T., Kondo K., Maruta S.;
RT "Characterization of a novel rice kinesin O12 with a calponin homology
RT domain.";
RL J. Biochem. 149:91-101(2011).
RN [11]
RP IDENTIFICATION.
RX PubMed=22843988; DOI=10.1093/jb/mvs076;
RA Umezu N., Umeki N., Mitsui T., Kondo K., Maruta S.;
RT "Rice kinesin O12 is identical to kinesin OsKCH1.";
RL J. Biochem. 152:207-208(2012).
RN [12]
RP FUNCTION, INTERACTION WITH ACTIN, AND ACTIVITY REGULATION.
RX PubMed=27250543; DOI=10.1038/nplants.2015.111;
RA Walter W.J., Machens I., Rafieian F., Diez S.;
RT "The non-processive rice kinesin-14 OsKCH1 transports actin filaments along
RT microtubules with two distinct velocities.";
RL Nat. Plants 1:15111-15111(2015).
CC -!- FUNCTION: Minus end-directed motor protein that transports actin
CC filaments along microtubules. Plays a central role in the polar
CC orientation of actin filaments along microtubules, and thus a
CC contribution to the organization of the cytoskeletal architecture
CC (PubMed:27250543). Links the actin microfilaments with the cortical
CC microtubules in both cycling and non-cycling cells (PubMed:19561334).
CC Required for efficient cell elongation by its participation in the
CC premitotic nuclear positioning (PubMed:20566563).
CC {ECO:0000269|PubMed:19561334, ECO:0000269|PubMed:20566563,
CC ECO:0000269|PubMed:27250543}.
CC -!- ACTIVITY REGULATION: The microtubule-dependent ATPase activity is
CC regulated by actin binding. {ECO:0000269|PubMed:21047815,
CC ECO:0000269|PubMed:27250543}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5 for ATPase activity (in presence of microtubules).
CC {ECO:0000269|PubMed:21047815};
CC -!- SUBUNIT: Forms oligomers in vitro. Interacts with actin microfilaments
CC (PubMed:19561334, PubMed:27250543). Binds to actin in vitro through its
CC calponin-homology (CH) domain (PubMed:21047815).
CC {ECO:0000269|PubMed:19561334, ECO:0000269|PubMed:21047815,
CC ECO:0000269|PubMed:27250543}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19561334, ECO:0000269|PubMed:21047815}.
CC Note=Colocalizes with cortical microtubules and longitudinally oriented
CC actin microfilaments. {ECO:0000269|PubMed:19561334}.
CC -!- TISSUE SPECIFICITY: Expressed in primary leaf, primary root, developing
CC flower and coleoptile. {ECO:0000269|PubMed:20566563}.
CC -!- DISRUPTION PHENOTYPE: Shorter coleoptiles due to impaired cell
CC expansion and increased division. {ECO:0000269|PubMed:20566563}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-14 subfamily.
CC {ECO:0000303|PubMed:19106179}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABA98869.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AK065586; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EEE53371.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DP000011; ABA98869.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008218; BAF29986.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT17539.1; -; Genomic_DNA.
DR EMBL; CM000149; EEE53371.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK065586; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015620619.1; XM_015765133.1.
DR AlphaFoldDB; Q0IMS9; -.
DR SMR; Q0IMS9; -.
DR STRING; 4530.OS12T0547500-01; -.
DR PaxDb; Q0IMS9; -.
DR PRIDE; Q0IMS9; -.
DR EnsemblPlants; Os12t0547500-01; Os12t0547500-01; Os12g0547500.
DR GeneID; 4352456; -.
DR Gramene; Os12t0547500-01; Os12t0547500-01; Os12g0547500.
DR KEGG; osa:4352456; -.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_001485_8_0_1; -.
DR InParanoid; Q0IMS9; -.
DR OMA; ENCNGIQ; -.
DR OrthoDB; 364605at2759; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000007752; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0003777; F:microtubule motor activity; IDA:UniProtKB.
DR GO; GO:0008569; F:minus-end-directed microtubule motor activity; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IDA:UniProtKB.
DR GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR GO; GO:0031534; P:minus-end directed microtubule sliding; IDA:UniProtKB.
DR GO; GO:0007097; P:nuclear migration; IMP:UniProtKB.
DR GO; GO:0051647; P:nucleus localization; IMP:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00033; CH; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..954
FT /note="Kinesin-like protein KIN-14Q"
FT /id="PRO_0000438642"
FT DOMAIN 33..155
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 374..699
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 844..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 704..733
FT /evidence="ECO:0000255"
FT COMPBIAS 844..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 457..464
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 954 AA; 105770 MW; 6F25D3CD240B6539 CRC64;
MMAAAVEEEE MVERMHGWAR DMDVASRRAE EEAMRRYDAA SWLRSTVGVV CARDLPDEPS
EEEFRLGLRN GIVLCNALNK IQPGAIPKVV QAQSDAAGPT DGSALCAYQY FENLRNFLVV
VEDLRLPTFE VSDLEKGGKG VRVVDCVLAL KSFSESNKTG RQASCKYGGL SKPLTARKYF
ILKNTDAFMN KIMKGHSAEA IQSEFSEGQS IVTDFSIESN EMTTSDSLSI LLRKVLLDKK
PEEVPLIVES ILSKVIQEYE HRIAIQNKMD EEEQNLLNIT EQVNHVVVNG DGEVKQFQLE
AQTNFDVQQK QIQELKGALS FVKSGMEQLR LQYSEEFAKL GKHFYTLSNA ASSYHKVLEE
NRKLYNQIQD LKGNIRVYCR VRPFLPGHRS LSSSVADTEE RTITIITPTK YGKDGCKSFS
FNRVFGPAST QEEVFSDMQP LIRSVLDGFN VCIFAYGQTG SGKTFTMSGP KVLTEESLGV
NYRALNDLFN IKAQRKGTID YEISVQMIEI YNEQVRDLLQ DGGNRRLEIR NTPQKGLAVP
DASIVPVTST ADVVELMNQG QKNRAVGSTA INDRSSRSHS CLSVHVQGKY LTSGAMLRGC
MHLVDLAGSE RVDKSEVVGD RLKEAQYINK SLSALGDVIA SLAQKNSHVP YRNSKLTQLL
QDSLGGQAKT LMFVHVSPEL DAVGETISTL KFAERVASVE LGAAKANKEG SEVRELKEQI
ATLKAALAKK EGEPENIQST QSSPDMYRIK RGNAIPAFPK NRQPMEEVGN LEVRNNATPM
QKKASFQFSG VLSENNSSDL AENCNGIQKT DRMAVGNNQF ENGNSILELE PGATQLPTFF
YQRYDPDKQR RRAEPVETDD SDSFDAATSS PSDQEMLLST SGLKADGIAS RGAFIIKKPQ
TKNTKITATK IPNLAMKSPM SEKRLQTPIR NSKQLPFSTT GGRRTRNGKI NTPK
