KN4C_ORYSJ
ID KN4C_ORYSJ Reviewed; 1284 AA.
AC B9F2Y7; Q0DXN2; Q6Z2W0;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Kinesin-like protein KIN-4C {ECO:0000305};
GN Name=KIN4C {ECO:0000305};
GN OrderedLocusNames=Os02g0742800/Os02g0742900 {ECO:0000312|EMBL:BAF10005.1,
GN ECO:0000312|EMBL:BAF10006.1}, LOC_Os02g50910 {ECO:0000305};
GN ORFNames=OJ1734_E02.4/OJ1734_E02.5 {ECO:0000312|EMBL:BAD16101.1},
GN OsJ_08347 {ECO:0000312|EMBL:EEE57794.1},
GN P0585G03.27/P0585G03.28 {ECO:0000312|EMBL:BAD15740.1};
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=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] OF 1-304, AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 734-1284.
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).
CC -!- FUNCTION: Microtubule-dependent motor protein involved in the control
CC of the oriented deposition of cellulose microfibrils.
CC {ECO:0000250|UniProtKB:Q6YUL8}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6YUL8}.
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:0000250|UniProtKB:Q6YUL8}.
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=BAD15740.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD16101.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF10005.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes Os02g0742800 and Os02g0742900.; Evidence={ECO:0000305};
CC Sequence=BAF10006.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes Os02g0742800 and Os02g0742900.; Evidence={ECO:0000305};
CC Sequence=BAS80868.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes Os02g0742800 and Os02g0742900.; Evidence={ECO:0000305};
CC Sequence=BAS80869.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes Os02g0742800 and Os02g0742900.; Evidence={ECO:0000305};
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DR EMBL; AP004800; BAD15740.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP005297; BAD16101.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008208; BAF10005.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008208; BAF10006.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014958; BAS80868.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014958; BAS80869.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000139; EEE57794.1; -; Genomic_DNA.
DR EMBL; AK064545; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK106279; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; B9F2Y7; -.
DR SMR; B9F2Y7; -.
DR STRING; 4530.OS02T0742800-01; -.
DR PaxDb; B9F2Y7; -.
DR PRIDE; B9F2Y7; -.
DR eggNOG; KOG0244; Eukaryota.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; Cell wall biogenesis/degradation; Coiled coil; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1284
FT /note="Kinesin-like protein KIN-4C"
FT /id="PRO_0000436188"
FT DOMAIN 12..364
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1040..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 407..445
FT /evidence="ECO:0000255"
FT COILED 561..711
FT /evidence="ECO:0000255"
FT COILED 911..950
FT /evidence="ECO:0000255"
FT COMPBIAS 1044..1070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 906
FT /note="L -> F (in Ref. 5; AK106279)"
FT /evidence="ECO:0000305"
FT CONFLICT 1177
FT /note="N -> K (in Ref. 5; AK106279)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1284 AA; 143049 MW; B38C336460983B1C CRC64;
MEGSEAAQQK DSVKVVVNIR PLITPELLLG CTDCVTVTPG EPQVQIGPHV FTYDHVFGST
GSPSSLIFEQ CVHPLIDSLF RGYNATVLAY GQTGSGKTYT MGTNYTGEAN CGGIIPQVME
TIFKKADALK DGTEFLIRVS FIEIFKEEVF DLLDASHAAL RLDSGSVAKA TAPARVPIQI
RETGNGGITL AGVTEAEVKT KEEMASFLAR GSSSRATGST NMNSQSSRSH AIFTISMDQK
KTSSASDKLS NDDYDILSSK FHLVDLAGSE RAKRTGADGL RLKEGIHINR GLLALGNVIS
ALGDEKKRKE GAFVPYRDSK LTRLLQDSLG GNSKTAMIAC ISPADSNAEE TINTLKYANR
ARNIQNKAVV WSFSLKINRD PVTAEMQKLR SQLEQLQTEL LFSRSGSAAL EELQLLQQKV
SLLELKNSEL NHELKERELS YEQLAQSALA AQLEKDQLML KIESARNGKS WDDIENTDTD
QDVEVMKRYI LKIQQLESEL TRQKFSSTCK NDLHDRFAMD KDLLLDDLGS GCEVGTPDAS
SAVNFRITPV PAGEADEEKE RDHSSMQDKL DKELQELDKR LQQKEAEMKE FAKSDTSVLK
QHYEKKLNEM EQEKKALQKE IEELRHALTN ITSSTDESAQ KLKENYLQKL NTLESQVSEL
KKKQEAQQQL IRQKQRSDEA AKRLQEDIHR IKSQKVQLQQ KIKQESEQFR SWKAAREKEV
LQLKKEGRRN EYEMHKLLAL NQRQKMVLQR KTEEAAMATK RLKESLEAKK STRDTYGSAS
GSGIQALMRA IDDELEVTVR AYELRSHYER QMQERAAISK EIAKLKECPQ AMSPSARSSR
ISALENMLSS SSSAMVSMAS QLSEAEERER AFNGKGRWNH VRSLPDAKNT MNYLFQLASS
SRCQQLDKEV MCKEKEHLIC DLKEKVVALN GRIRQLETQV KDLNNQNMLL FTAISEAKNP
VGTSRKGTVG SEDGQHYAMR KSIRASHSLH YSKNSFLWSD DMDISDSEKS EGSDADWEAS
DADYGASDAD WECSKKVRRR RQTVSSHLNP NPGSGTTQKS AKSEMASQEK STSLDLAPQC
CSCSKYSSCK TQKCECRASG SHCGGDCGCI TSRCSNRVDM KEEKEGGGVV EVSSSDDVDD
AKVQEIVKEG VMLLENSMSE KEAQETKSRK PLADIGNGVV KQTGAKPKQR KNWRKSTVQL
VPSAPPLPPT APQNTEPVPR NRDIPLRLPR AMSSPAVDSI PLTDRNAAKP DESMSSNKEN
VTAVRARSPA RPRKNANEKE NHLR
