KN4A_ORYSJ
ID KN4A_ORYSJ Reviewed; 1035 AA.
AC Q6YUL8; A0A0P0XKI2; B9G250; Q6YUL7;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Kinesin-like protein KIN-4A {ECO:0000305};
DE AltName: Full=Protein BRITTLE CULM 2 {ECO:0000303|PubMed:20444225};
DE AltName: Full=Protein GIBBERELLIN-DEFICIENT DWARF 1 {ECO:0000303|PubMed:21325138};
GN Name=KIN4A {ECO:0000305};
GN Synonyms=BC2 {ECO:0000303|PubMed:20444225},
GN GDD1 {ECO:0000303|PubMed:21325138};
GN OrderedLocusNames=Os09g0114500 {ECO:0000312|EMBL:BAF24494.1},
GN LOC_Os09g02650 {ECO:0000305};
GN ORFNames=OJ1134_E08.39-1 {ECO:0000312|EMBL:BAD16507.1},
GN OJ1134_E08.39-2 {ECO:0000312|EMBL:BAD16508.1},
GN OsJ_28385 {ECO:0000312|EMBL:EEE69196.1};
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 {ECO:0000312|Proteomes:UP000059680};
RN [1]
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 [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, NUCLEAR
RP LOCALIZATION SIGNAL, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-971; LYS-972;
RP LYS-986 AND ARG-987, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Nipponbare;
RX PubMed=20444225; DOI=10.1111/j.1365-313x.2010.04238.x;
RA Zhang M., Zhang B., Qian Q., Yu Y., Li R., Zhang J., Liu X., Zeng D.,
RA Li J., Zhou Y.;
RT "Brittle Culm 12, a dual-targeting kinesin-4 protein, controls cell-cycle
RT progression and wall properties in rice.";
RL Plant J. 63:312-328(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Zhonghua 10;
RX PubMed=21325138; DOI=10.1105/tpc.110.081901;
RA Li J., Jiang J., Qian Q., Xu Y., Zhang C., Xiao J., Du C., Luo W., Zou G.,
RA Chen M., Huang Y., Feng Y., Cheng Z., Yuan M., Chong K.;
RT "Mutation of rice BC12/GDD1, which encodes a kinesin-like protein that
RT binds to a GA biosynthesis gene promoter, leads to dwarfism with impaired
RT cell elongation.";
RL Plant Cell 23:628-640(2011).
CC -!- FUNCTION: Microtubule-dependent motor protein involved in the control
CC of the oriented deposition of cellulose microfibrils (PubMed:20444225,
CC PubMed:21325138). Involved in wall biogenesis and modification, and
CC contributes to cell-cycle progression and cell division
CC (PubMed:20444225). Acts as a transcriptional activator in gibberellic
CC acid (GA) biosynthesis pathway. Binds specifically to the DNA sequence
CC 5'-ACCAACTTGAA-3' of the ent-kaurene oxidase 2 (CYP701A6 or OsKO2)
CC promoter. May regulate CYP701A6 gene expression and mediates cell
CC elongation by regulating the GA biosynthesis pathway (PubMed:21325138).
CC {ECO:0000269|PubMed:20444225, ECO:0000269|PubMed:21325138}.
CC -!- ACTIVITY REGULATION: May be regulated by cyclin-dependent kinase A.
CC {ECO:0000305|PubMed:20444225}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20444225}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20444225,
CC ECO:0000269|PubMed:21325138}. Cytoplasm, cytoskeleton
CC {ECO:0000305|PubMed:20444225, ECO:0000305|PubMed:21325138}.
CC Note=Associated with mitotic microtubule arrays during cell division.
CC {ECO:0000269|PubMed:20444225}.
CC -!- TISSUE SPECIFICITY: Expressed in young tissues with cell divisions,
CC including initiating adventitious roots, primary root tips, flower
CC primordia, intercalary meristems, sub-epidermal regions of young culms
CC and panicles. {ECO:0000269|PubMed:20444225}.
CC -!- DOMAIN: Composed of an N-terminal domain which is responsible for the
CC motor activity of kinesin (it hydrolyzes ATP and binds microtubule) and
CC a central to C-terminal alpha-helical coiled coil domain that mediates
CC the heavy chain dimerization. {ECO:0000305|PubMed:20444225}.
CC -!- DISRUPTION PHENOTYPE: Dwarf plants due to significant reduction in cell
CC number (PubMed:20444225). Dwarf plants due to significant reduction in
CC cell elongation (PubMed:21325138). This phenotype can be rescued by
CC exogenous gibberellic acid (GA3) treatment (PubMed:21325138). Reduced
CC mechanical strength (brittleness) due to an alteration in cellulose
CC microfibril orientation and wall composition (PubMed:20444225).
CC {ECO:0000269|PubMed:20444225, ECO:0000269|PubMed:21325138}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-4 subfamily.
CC {ECO:0000303|PubMed:19106179}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK100974; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD16508.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP005860; BAD16507.1; -; Genomic_DNA.
DR EMBL; AP005860; BAD16508.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008215; BAF24494.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT06843.1; -; Genomic_DNA.
DR EMBL; CM000146; EEE69196.1; -; Genomic_DNA.
DR EMBL; AK100974; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015612252.1; XM_015756766.1.
DR RefSeq; XP_015612253.1; XM_015756767.1.
DR RefSeq; XP_015612254.1; XM_015756768.1.
DR AlphaFoldDB; Q6YUL8; -.
DR SMR; Q6YUL8; -.
DR STRING; 4530.OS09T0114500-01; -.
DR PaxDb; Q6YUL8; -.
DR PRIDE; Q6YUL8; -.
DR EnsemblPlants; Os09t0114500-01; Os09t0114500-01; Os09g0114500.
DR GeneID; 4346402; -.
DR Gramene; Os09t0114500-01; Os09t0114500-01; Os09g0114500.
DR KEGG; osa:4346402; -.
DR eggNOG; KOG0244; Eukaryota.
DR HOGENOM; CLU_001485_4_2_1; -.
DR InParanoid; Q6YUL8; -.
DR OMA; PAFNKQH; -.
DR OrthoDB; 369179at2759; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000007752; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR ExpressionAtlas; Q6YUL8; baseline and differential.
DR Genevisible; Q6YUL8; OS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0010215; P:cellulose microfibril organization; IMP:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0009832; P:plant-type cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0009937; P:regulation of gibberellic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0051231; P:spindle elongation; IBA:GO_Central.
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 1: Evidence at protein level;
KW Activator; ATP-binding; Cell cycle; Cell wall biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; DNA-binding; Growth regulation;
KW Microtubule; Motor protein; Nucleotide-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..1035
FT /note="Kinesin-like protein KIN-4A"
FT /id="PRO_0000431963"
FT DOMAIN 10..369
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 697..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 380..437
FT /evidence="ECO:0000255"
FT COILED 498..702
FT /evidence="ECO:0000255"
FT COILED 850..904
FT /evidence="ECO:0000255"
FT MOTIF 971..987
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:20444225"
FT COMPBIAS 703..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..896
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 89..96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MUTAGEN 971
FT /note="K->A: Loss of nuclear targeting."
FT /evidence="ECO:0000269|PubMed:20444225"
FT MUTAGEN 972
FT /note="K->A: Loss of nuclear targeting."
FT /evidence="ECO:0000269|PubMed:20444225"
FT MUTAGEN 986
FT /note="K->A: Reduces nuclear targeting."
FT /evidence="ECO:0000269|PubMed:20444225"
FT MUTAGEN 987
FT /note="R->A: Reduces nuclear targeting."
FT /evidence="ECO:0000269|PubMed:20444225"
FT CONFLICT 174
FT /note="G -> D (in Ref. 5; AK100974)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="N -> S (in Ref. 5; AK100974)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="N -> D (in Ref. 5; AK100974)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="Missing (in Ref. 4; EEE69196)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1035 AA; 116386 MW; 65A210A1AC30B8C4 CRC64;
MTMEHGEDCC VKVAVHVRPL IGDEKLQGCK DCVSVVSGKP QVQIGSHSFT FDHVYGSSGT
PSAAMFEECV APLVDGLFQG YNATVLAYGQ TGSGKTYTMG TACKEGSHIG IIPRAMATLF
DKIDKLKNQV EFQLRVSFIE ILKEEVRDLL DPATAAVGKL ENGNGHATKL SVPGKPPVQI
REASNGVITL AGSTEVHVTT QKEMTACLEQ GSLSRATGST NMNNQSSRSH AIFTITLEQM
RKADPIMTLD GMPIEEMNED YLCAKLHLVD LAGSERAKRT GSDGLRFKEG VHINRGLLAL
GNVISALGDE KKRKEGAHVP YRDSKLTRLL QDSLGGNSKT VMIACISPAD INAEETLNTL
KYANRARNIQ NKPIVNRNPV ADEMKRMRQQ IEYLQAELVS ARGGVVLDDV QGLRERISML
EQKNEDLCRE LYDLRNHGYT DPCEPELQKI GTGYTKGEGL KRSLQSTEPF DVPMTDSVRA
GSPKDIDDEV AKEWEHTMLQ DSMGKELNEL NRQLEQKESE MKMYGSDTVA LKQHFGKKLL
ELEEEKRAVQ QERDRLLAEV ESLNADGQTH KLRDAQLQKL KTLEAQILDL KKKQENQVQL
LKEKQKSDEA AKKLQEEIHS IKAQKVQLQH KIKQEAEQFR QWKATREKEL LQLRKEGRRN
EYERHKLQAL NQRQKLVLQR KTEEAAMATK RLKELLEARK SSGRDNSGMN GTSPGSHMTE
KSLQKWLEQD LEVMVHVHEV RNEYEKQSQL RAALGEELAI LKQEDVMSGA ASPPRGKNGN
SRANTLSPNA RQARIASLES MVTISSNTLV AMASQLSEAE ERERAFSGRG RWNQLRSMAE
AKSLLQYIFN VAADARCQVR EKEMEIKEMK EQMTELVTIL RHSESRRRET EKQLKQREQA
AVTATTSPGN GNGSVKHSAD DSNTPLSPVA VPAQKQLKYS AGIVNSPSKG VPAFNKQHLK
MVPMAQLPVG KKVSIAGQSG KLWRWKRSHH QWLLQFKWKW QKPWKLSEMI RHSDETMTRT
RPRPQLLPHR PQRVM
