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Kinesin-like protein KIN-4A (Protein BRITTLE CULM 2) (Protein GIBBERELLIN-DEFICIENT DWARF 1)

 KN4A_ORYSJ              Reviewed;        1035 AA.
Q6YUL8; A0A0P0XKI2; B9G250; Q6YUL7;
04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 105.
RecName: Full=Kinesin-like protein KIN-4A {ECO:0000305};
AltName: Full=Protein BRITTLE CULM 2 {ECO:0000303|PubMed:20444225};
AltName: Full=Protein GIBBERELLIN-DEFICIENT DWARF 1 {ECO:0000303|PubMed:21325138};
Name=KIN4A {ECO:0000305};
Synonyms=BC2 {ECO:0000303|PubMed:20444225},
GDD1 {ECO:0000303|PubMed:21325138};
OrderedLocusNames=Os09g0114500 {ECO:0000312|EMBL:BAF24494.1},
LOC_Os09g02650 {ECO:0000305};
ORFNames=OJ1134_E08.39-1 {ECO:0000312|EMBL:BAD16507.1},
OJ1134_E08.39-2 {ECO:0000312|EMBL:BAD16508.1},
OsJ_28385 {ECO:0000312|EMBL:EEE69196.1};
Oryza sativa subsp. japonica (Rice).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
NCBI_TaxID=39947 {ECO:0000312|Proteomes:UP000059680};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=16100779; DOI=10.1038/nature03895;
International rice genome sequencing project (IRGSP);
"The map-based sequence of the rice genome.";
Nature 436:793-800(2005).
[2]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=18089549; DOI=10.1093/nar/gkm978;
The rice annotation project (RAP);
"The rice annotation project database (RAP-DB): 2008 update.";
Nucleic Acids Res. 36:D1028-D1033(2008).
[3]
GENOME REANNOTATION.
STRAIN=cv. Nipponbare;
PubMed=24280374; DOI=10.1186/1939-8433-6-4;
Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H.,
McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
Buell C.R., Matsumoto T.;
"Improvement of the Oryza sativa Nipponbare reference genome using
next generation sequence and optical map data.";
Rice 6:4-4(2013).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Nipponbare;
PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H.,
Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
Samudrala R., Wang J., Wong G.K.-S., Yang H.;
"The genomes of Oryza sativa: a history of duplications.";
PLoS Biol. 3:266-281(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Nipponbare;
PubMed=12869764; DOI=10.1126/science.1081288;
The rice full-length cDNA consortium;
"Collection, mapping, and annotation of over 28,000 cDNA clones from
japonica rice.";
Science 301:376-379(2003).
[6]
GENE FAMILY, AND NOMENCLATURE.
PubMed=19106179; DOI=10.1093/aob/mcn248;
Guo L., Ho C.M., Kong Z., Lee Y.R., Qian Q., Liu B.;
"Evaluating the microtubule cytoskeleton and its interacting proteins
in monocots by mining the rice genome.";
Ann. Bot. 103:387-402(2009).
[7]
FUNCTION, ENZYME REGULATION, SUBUNIT, SUBCELLULAR LOCATION, NUCLEAR
LOCALIZATION SIGNAL, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-971;
LYS-972; LYS-986 AND ARG-987, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Nipponbare;
PubMed=20444225; DOI=10.1111/j.1365-313X.2010.04238.x;
Zhang M., Zhang B., Qian Q., Yu Y., Li R., Zhang J., Liu X., Zeng D.,
Li J., Zhou Y.;
"Brittle Culm 12, a dual-targeting kinesin-4 protein, controls cell-
cycle progression and wall properties in rice.";
Plant J. 63:312-328(2010).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Zhonghua 10;
PubMed=21325138; DOI=10.1105/tpc.110.081901;
Li J., Jiang J., Qian Q., Xu Y., Zhang C., Xiao J., Du C., Luo W.,
Zou G., Chen M., Huang Y., Feng Y., Cheng Z., Yuan M., Chong K.;
"Mutation of rice BC12/GDD1, which encodes a kinesin-like protein that
binds to a GA biosynthesis gene promoter, leads to dwarfism with
impaired cell elongation.";
Plant Cell 23:628-640(2011).
-!- FUNCTION: Microtubule-dependent motor protein involved in the
control of the oriented deposition of cellulose microfibrils
(PubMed:20444225, PubMed:21325138). Involved in wall biogenesis
and modification, and contributes to cell-cycle progression and
cell division (PubMed:20444225). Acts as a transcriptional
activator in gibberellic acid (GA) biosynthesis pathway. Binds
specifically to the DNA sequence 5'-ACCAACTTGAA-3' of the ent-
kaurene oxidase 2 (CYP701A6 or OsKO2) promoter. May regulate
CYP701A6 gene expression and mediates cell elongation by
regulating the GA biosynthesis pathway (PubMed:21325138).
{ECO:0000269|PubMed:20444225, ECO:0000269|PubMed:21325138}.
-!- ENZYME REGULATION: May be regulated by cyclin-dependent kinase A.
{ECO:0000305|PubMed:20444225}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20444225}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20444225,
ECO:0000269|PubMed:21325138}. Cytoplasm, cytoskeleton
{ECO:0000305|PubMed:20444225, ECO:0000305|PubMed:21325138}.
Note=Associated with mitotic microtubule arrays during cell
division. {ECO:0000269|PubMed:20444225}.
-!- TISSUE SPECIFICITY: Expressed in young tissues with cell
divisions, including initiating adventitious roots, primary root
tips, flower primordia, intercalary meristems, sub-epidermal
regions of young culms and panicles.
{ECO:0000269|PubMed:20444225}.
-!- DOMAIN: Composed of an N-terminal domain which is responsible for
the motor activity of kinesin (it hydrolyzes ATP and binds
microtubule) and a central to C-terminal alpha-helical coiled coil
domain that mediates the heavy chain dimerization.
{ECO:0000305|PubMed:20444225}.
-!- DISRUPTION PHENOTYPE: Dwarf plants due to significant reduction in
cell number (PubMed:20444225). Dwarf plants due to significant
reduction in cell elongation (PubMed:21325138). This phenotype can
be rescued by exogenous gibberellic acid (GA3) treatment
(PubMed:21325138). Reduced mechanical strength (brittleness) due
to an alteration in cellulose microfibril orientation and wall
composition (PubMed:20444225). {ECO:0000269|PubMed:20444225,
ECO:0000269|PubMed:21325138}.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Kinesin family. KIN-4 subfamily.
{ECO:0000303|PubMed:19106179}.
-!- SEQUENCE CAUTION:
Sequence=AK100974; Type=Frameshift; Positions=870; Evidence={ECO:0000305};
Sequence=BAD16508.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AP005860; BAD16507.1; -; Genomic_DNA.
EMBL; AP005860; BAD16508.1; ALT_SEQ; Genomic_DNA.
EMBL; AP008215; BAF24494.1; -; Genomic_DNA.
EMBL; AP014965; BAT06843.1; -; Genomic_DNA.
EMBL; CM000146; EEE69196.1; -; Genomic_DNA.
EMBL; AK100974; -; NOT_ANNOTATED_CDS; mRNA.
RefSeq; XP_015612252.1; XM_015756766.1.
RefSeq; XP_015612253.1; XM_015756767.1.
RefSeq; XP_015612254.1; XM_015756768.1.
UniGene; Os.22630; -.
ProteinModelPortal; Q6YUL8; -.
SMR; Q6YUL8; -.
STRING; 39947.LOC_Os09g02650.1; -.
PaxDb; Q6YUL8; -.
PRIDE; Q6YUL8; -.
EnsemblPlants; OS09T0114500-01; OS09T0114500-01; OS09G0114500.
GeneID; 4346402; -.
Gramene; OS09T0114500-01; OS09T0114500-01; OS09G0114500.
KEGG; osa:4346402; -.
eggNOG; KOG0244; Eukaryota.
eggNOG; COG5059; LUCA.
HOGENOM; HOG000030222; -.
KO; K10395; -.
OMA; KEINEGC; -.
OrthoDB; EOG093601IQ; -.
Reactome; R-OSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
Reactome; R-OSA-983189; Kinesins.
Proteomes; UP000059680; Chromosome 9.
ExpressionAtlas; Q6YUL8; baseline and differential.
Genevisible; Q6YUL8; OS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008574; F:ATP-dependent microtubule motor activity, plus-end-directed; IBA:GO_Central.
GO; GO:0008017; F:microtubule binding; IEA:InterPro.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0010215; P:cellulose microfibril organization; IMP:UniProtKB.
GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
GO; GO:0009832; P:plant-type cell wall biogenesis; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0009937; P:regulation of gibberellic acid mediated signaling pathway; IMP:UniProtKB.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.40.850.10; -; 1.
InterPro; IPR027640; Kinesin-like_fam.
InterPro; IPR019821; Kinesin_motor_CS.
InterPro; IPR001752; Kinesin_motor_dom.
InterPro; IPR036961; Kinesin_motor_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR24115; PTHR24115; 1.
Pfam; PF00225; Kinesin; 1.
PRINTS; PR00380; KINESINHEAVY.
SMART; SM00129; KISc; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00411; KINESIN_MOTOR_1; 1.
PROSITE; PS50067; KINESIN_MOTOR_2; 1.
1: Evidence at protein level;
Activator; ATP-binding; Cell cycle; Cell wall biogenesis/degradation;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; DNA-binding;
Growth regulation; Microtubule; Motor protein; Nucleotide-binding;
Nucleus; Reference proteome; Transcription; Transcription regulation.
CHAIN 1 1035 Kinesin-like protein KIN-4A.
/FTId=PRO_0000431963.
DOMAIN 10 369 Kinesin motor. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
NP_BIND 89 96 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00283}.
COILED 380 437 {ECO:0000255}.
COILED 498 702 {ECO:0000255}.
COILED 850 904 {ECO:0000255}.
MOTIF 971 987 Nuclear localization signal.
{ECO:0000269|PubMed:20444225}.
MUTAGEN 971 971 K->A: Loss of nuclear targeting.
{ECO:0000269|PubMed:20444225}.
MUTAGEN 972 972 K->A: Loss of nuclear targeting.
{ECO:0000269|PubMed:20444225}.
MUTAGEN 986 986 K->A: Reduces nuclear targeting.
{ECO:0000269|PubMed:20444225}.
MUTAGEN 987 987 R->A: Reduces nuclear targeting.
{ECO:0000269|PubMed:20444225}.
CONFLICT 174 174 G -> D (in Ref. 5; AK100974).
{ECO:0000305}.
CONFLICT 224 224 N -> S (in Ref. 5; AK100974).
{ECO:0000305}.
CONFLICT 364 364 N -> D (in Ref. 5; AK100974).
{ECO:0000305}.
CONFLICT 480 480 Missing (in Ref. 4; EEE69196).
{ECO:0000305}.
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


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