KN14I_ORYSJ
ID KN14I_ORYSJ Reviewed; 1248 AA.
AC Q7XPJ0; A0A0P0WGB9; A3AYE3; Q84VE4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Kinesin-like protein KIN-14I {ECO:0000305};
DE AltName: Full=Kinesin-like calmodulin-binding protein {ECO:0000305};
DE Short=OsKCBP {ECO:0000303|PubMed:19106179};
GN Name=KIN14I {ECO:0000305}; Synonyms=KCBP {ECO:0000303|PubMed:19106179};
GN OrderedLocusNames=Os04g0666900 {ECO:0000312|EMBL:BAS91515.1},
GN LOC_Os04g57140 {ECO:0000305};
GN ORFNames=OsJ_16543 {ECO:0000312|EMBL:EAZ32332.1},
GN OSJNBa0087O24.20 {ECO:0000312|EMBL:CAE03597.1};
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 [MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=14750518; DOI=10.1023/b:plan.0000007001.30865.0f;
RA Cooper B., Hutchison D., Park S., Guimil S., Luginbuehl P., Ellero C.,
RA Goff S.A., Glazebrook J.;
RT "Identification of rice (Oryza sativa) proteins linked to the cyclin-
RT mediated regulation of the cell cycle.";
RL Plant Mol. Biol. 53:273-279(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-1248.
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 [8]
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).
CC -!- FUNCTION: Minus-end microtubule-dependent motor protein involved in the
CC regulation of cell division. {ECO:0000250|UniProtKB:Q9FHN8}.
CC -!- SUBUNIT: Binds microtubules via its N-terminus containing the MyTH4
CC domain and binds F-actin via its FERM domain. Binding to calmodulin
CC inhibits microtubule binding activity. {ECO:0000250|UniProtKB:Q9FHN8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9FHN8}.
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=AK073209; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAF16096.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS91515.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAZ32332.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY224540; AAO72660.1; -; mRNA.
DR EMBL; AL606646; CAE03597.1; -; Genomic_DNA.
DR EMBL; AP008210; BAF16096.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014960; BAS91515.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000141; EAZ32332.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK073209; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015636574.1; XM_015781088.1.
DR AlphaFoldDB; Q7XPJ0; -.
DR SMR; Q7XPJ0; -.
DR STRING; 4530.OS04T0666900-01; -.
DR PaxDb; Q7XPJ0; -.
DR PRIDE; Q7XPJ0; -.
DR GeneID; 4337322; -.
DR KEGG; osa:4337322; -.
DR eggNOG; KOG0239; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR HOGENOM; CLU_001485_14_0_1; -.
DR InParanoid; Q7XPJ0; -.
DR OrthoDB; 364605at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q7XPJ0; OS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.25.40.530; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR000857; MyTH4_dom.
DR InterPro; IPR038185; MyTH4_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR011254; Prismane-like_sf.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00784; MyTH4; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00295; B41; 1.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00139; MyTH4; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56821; SSF56821; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS51016; MYTH4; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1248
FT /note="Kinesin-like protein KIN-14I"
FT /id="PRO_0000403274"
FT DOMAIN 88..244
FT /note="MyTH4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00359"
FT DOMAIN 249..563
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 872..1193
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 675..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1223
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9FHN8"
FT REGION 1220..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 586..659
FT /evidence="ECO:0000255"
FT COILED 708..799
FT /evidence="ECO:0000255"
FT COMPBIAS 679..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 953..960
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 605
FT /note="E -> G (in Ref. 7; AK073209)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1248 AA; 141786 MW; 30D6867F456E2D72 CRC64;
MNGGGASGGD GYDSDGYSFA PPTPTTLSMS IPPELAGAIP LIDRFQVEGF LKAMQKQIHS
AGKRGFFSKK SVGPHVREKF TLEDMLCFQK DPIPTSLLKI SSDLVSRSIK LFHVILKYMG
IDSPAIISLD ERIELVAKLY KHTLKRSELR DELFAQISKQ TRNNPDRAWL IRAWELMYLC
ASSMPPSKDI GAYLSEYVHY IAHGATTDSD VRVLALNTLN ALKRSVKAGP RVTIPAREEI
EALLSSRKLT TIVFFLDETF EEITYDMATT VADAVEELAG IIKLSVYSSF SLFECRKVVN
GSKSSDVGNE EYIGLDDNKY IGDLLSEFKA AKDRNKGEIL HCKLVFKKRL FRESDEAITD
PMFVQLSYVQ LQHDYILGNY PVGRDDAAQL SALQILVEIG FVDNPESCVE WISLLERFLP
RQVAITRAKR DWELDIVSRY QLMEHLSKDD ARQQFLRILR TLPYGNSVFF SVRKIDDPIG
LLPGRIILGI NKRGVHFFRP VPKEYLHSAE LRDIMQFGSS NTAVFFKMRV AGVLHIFQFE
TKQGEEICVA LQTHINDVML RRYSKARSAT SAVSQNDVSQ TYKPPNIEIY EKRVQELSKA
VEESERKADL LNEELQKKTK QERDMQKELE GLRDTLQSER QSIKEVTNDL DKLKSLCDEK
DSSLQASLME KTRLETRLKS GQGQESSNRT GVSGNHFERD TLPTVGTVNN SIEMLAKLEE
ELKSCKKELD ASKELSKKLT MENNLLDQKV QRLERAKSEE KSNMERVYED ECCKLKSRIA
ELEQKLESRT RSLNVTESTL ALRNAEVDTL QNSLKELDEL REFKADVDRK NQQTAEILKR
QGAQLIELEN LYKQEQVLRK RYYNTIEDMK GKIRVFCRLR PLNDKELIEK DKNIVCSPDE
FTVAHPWKDD KSKQHIYDRV FDANTTQEEV FEDTKYLVQS AVDGYNVCIF AYGQTGSGKT
FTIYGSENNP GLTPRATSEL FRVIKRDGHK YSFSLKAYMV ELYQDNLVDL LLAKNATHQK
LEIKKDSKGV VTVENVTVVN ISSFEELRAI ILRGSERRHT AGTNMNVESS RSHLILSIII
ESTNLQTQSY ARGKLSFVDL AGSERVKKSG SAGKQLKEAQ SINKSLSALA DVIGALSSDG
QHIPYRNHKL TMLMSDSLGG NAKTLMFVNV SPAESNLEET YNSLMYASRV RCIVNDTSKH
VAPKEIMRLK KLIAYWKEQA GKRSEDDDLE EIQEERTPKE KADNRLTS
