KN12A_ORYSJ
ID KN12A_ORYSJ Reviewed; 1155 AA.
AC Q7XKR9; A0A0P0W917; B9FEL0; Q9LLF1;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Kinesin-like protein KIN-12A {ECO:0000305};
DE Short=OsKinesin-12A {ECO:0000303|PubMed:19106179};
DE AltName: Full=Phragmoplast-associated kinesin-related protein 1 {ECO:0000303|PubMed:10898978};
DE Short=OsPAKRP1 {ECO:0000303|PubMed:10898978};
GN Name=KIN12A {ECO:0000305}; Synonyms=PAKRP1 {ECO:0000303|PubMed:19106179};
GN OrderedLocusNames=Os04g0350300 {ECO:0000312|EMBL:BAS88723.1},
GN LOC_Os04g28260 {ECO:0000305};
GN ORFNames=OsJ_14379 {ECO:0000312|EMBL:EEE60793.1},
GN OSJNBa0038P21.12 {ECO:0000312|EMBL:CAE05519.1};
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=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 [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 [MRNA] OF 339-1155, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=10898978; DOI=10.1016/s0960-9822(00)00564-9;
RA Lee Y.R.J., Liu B.;
RT "Identification of a phragmoplast-associated kinesin-related protein in
RT higher plants.";
RL Curr. Biol. 10:797-800(2000).
RN [7]
RP GENE FAMILY, NOMENCLATURE, AND SUBCELLULAR LOCATION.
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: Plus-end directed kinesin-like motor enzyme that plays a
CC critical role in the organization of phragmoplast microtubules during
CC cytokinesis. {ECO:0000250|UniProtKB:Q9LDN0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, phragmoplast
CC {ECO:0000269|PubMed:10898978, ECO:0000269|PubMed:19106179}.
CC Note=Localized to the midline of the nascent phragmoplast (late
CC anaphase) essentially at the plus end of phragmoplast microtubules.
CC {ECO:0000269|PubMed:19106179}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-12 subfamily.
CC {ECO:0000303|PubMed:19106179}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF14445.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS88723.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAE05519.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EEE60793.1; 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; AL731588; CAE05519.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008210; BAF14445.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014960; BAS88723.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000141; EEE60793.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF210816; AAF78897.1; -; mRNA.
DR AlphaFoldDB; Q7XKR9; -.
DR SMR; Q7XKR9; -.
DR IntAct; Q7XKR9; 1.
DR STRING; 4530.OS04T0350300-00; -.
DR PRIDE; Q7XKR9; -.
DR eggNOG; KOG4280; Eukaryota.
DR HOGENOM; CLU_009194_1_0_1; -.
DR InParanoid; Q7XKR9; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
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:UniProtKB.
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:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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 PANTHER; PTHR24115; PTHR24115; 1.
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..1155
FT /note="Kinesin-like protein KIN-12A"
FT /id="PRO_0000437194"
FT DOMAIN 141..482
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 47..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..353
FT /note="Microtubules-binding"
FT /evidence="ECO:0000305|PubMed:10898978"
FT REGION 382..388
FT /note="Microtubules-binding"
FT /evidence="ECO:0000305|PubMed:10898978"
FT REGION 431..435
FT /note="Microtubules-binding"
FT /evidence="ECO:0000305|PubMed:10898978"
FT COILED 823..861
FT /evidence="ECO:0000255"
FT COILED 934..971
FT /evidence="ECO:0000255"
FT COILED 1006..1089
FT /evidence="ECO:0000255"
FT COMPBIAS 47..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 221..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1155 AA; 127987 MW; 49B3B47F4D3E6F22 CRC64;
MSTTLRRAWS SLNGNDGVLP YFLATLNEVS LLQARPPPGH AAAALALRRR RRDTPPSRRR
VPKENVDPGS SPAGHSPFRS PTSSAKPLGN RNRGLLPPRP PSSNPLKRKL DVSPAAAADS
SGGAAAAAAA AGGGCPAPDS GVQVVVRIRP PCRVEEEEDA RAPDLCVRKT ATNSVAIQGQ
DFTFDAVADE VSTQEDIFKL VGLPLVENCL SGFNSSIFAY GQTGSGKTYT MWGPLSALSE
DSTCSERGLT PRVFEQLFSR IKEEQGKHED KELTYHCVCS FLEIYNEQIT DLLDPSPKSL
QIREDVRTAC VYVESLTKEL VFTTKDVTQL LVKGLSNRRT GATSANADSS RSHCVFTCVI
KSESKNLEDG SNSTRTSRIN LVDLAGSERQ KLTHAFGDRL KEAGNINRSL SQLGNLINIL
AEISQSGKQR HVPYRDSKLT FLLQESLGGN AKLAMICAVS PSQSCKSETL STLRFAQRAK
SIKNNAVVNE QKEEDVNMLR EQIRQLKDEL HRMKSGGSDG SNGSFSTGWN ARRSLHLLKM
SLSRPTTFQT IHEDSGDVEM EIDENDVEKP YNQDNMVISP PGDKECKELQ ASLKINGGTS
LDVFDGENLM PTKRSCSDDR YKLNLAASIQ RGLQVIENHQ NNGAWRRASV GFNARIVDVQ
PCKVDVAIQT EPEESEARDN PLALISSHVL GTSATVSNDP NACRDLQLVQ YDAGITRDEP
KQQQILKAVE KVLAGAIRRE MARDEQCVKQ AAEIQQLNRL VQQYKHEREC NAVIAQTREG
KIARLESLMD GTLPTEEFIN EEYLSLMNEH KILQQKYENH PELLRAEIEL KRLQEELELC
RNYIDEKEVL QEEIQDLKSH LHFMLSSSAS IRRLWPPVQL SHGVGPSPVT NDADGDNNAV
DTPDWAEAES KWVTLTEELR VELEANKSLV GRLRSELESE KKCSEEVKEA LQTAMQGHAR
ILEQYAELEE RHIGLLAMHR KIREGVEDVK ARAAKAGVKG AELRFINSLA AEMAVLRAEN
KGLQDQLGDT AEAVQAAGEL LVRLKEAEEA EALAQRRALL AEQETEKAYQ EIDNLKKNYD
QEIVALNQRL SESSHHQETT LAIEACDMET TKYDTAGSPG DQQWREEFNQ QGGSFEVSKS
TDLNSWFSGY DKCNI