KN5C_ORYSJ
ID KN5C_ORYSJ Reviewed; 1008 AA.
AC B7EJ91; A0A0P0XIK4;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 2.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Kinesin-like protein KIN-5C {ECO:0000305};
GN Name=KIN5C {ECO:0000305};
GN OrderedLocusNames=Os08g0558400 {ECO:0000312|EMBL:BAT06676.1,
GN ECO:0000312|EMBL:BAT06677.1}, LOC_Os08g44420 {ECO:0000305};
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=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP REVIEW.
RX PubMed=16530461; DOI=10.1016/j.tplants.2006.02.004;
RA Vanstraelen M., Inze D., Geelen D.;
RT "Mitosis-specific kinesins in Arabidopsis.";
RL Trends Plant Sci. 11:167-175(2006).
RN [5]
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: Responsible for microtubule translocation. May be important
CC for the organization of phragmoplast-specific arrays of microtubules
CC (By similarity). Plays an essential role in stabilizing the mitotic
CC spindle. Required during mitotic cytokinesis (By similarity).
CC {ECO:0000250|UniProtKB:F4IIS5, ECO:0000250|UniProtKB:O23826}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:F4IIS5}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:F4IIS5}. Note=Microtubule-associated.
CC {ECO:0000250|UniProtKB:F4IIS5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=B7EJ91-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B7EJ91-2; Sequence=VSP_058329;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to introns retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-5/BimC subfamily.
CC {ECO:0000303|PubMed:19106179}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAT06676.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAT06677.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP014964; BAT06676.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014964; BAT06677.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK071334; BAG92438.1; -; mRNA.
DR RefSeq; XP_015649381.1; XM_015793895.1. [B7EJ91-1]
DR AlphaFoldDB; B7EJ91; -.
DR SMR; B7EJ91; -.
DR STRING; 4530.OS08T0558400-02; -.
DR PaxDb; B7EJ91; -.
DR PRIDE; B7EJ91; -.
DR EnsemblPlants; Os08t0558400-02; Os08t0558400-02; Os08g0558400. [B7EJ91-2]
DR GeneID; 9271005; -.
DR Gramene; Os08t0558400-02; Os08t0558400-02; Os08g0558400. [B7EJ91-2]
DR KEGG; osa:9271005; -.
DR eggNOG; KOG0243; Eukaryota.
DR HOGENOM; CLU_673343_0_0_1; -.
DR OrthoDB; 179272at2759; -.
DR Proteomes; UP000059680; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; 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:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0090307; P:mitotic spindle assembly; 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 Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1008
FT /note="Kinesin-like protein KIN-5C"
FT /id="PRO_0000436273"
FT DOMAIN 12..359
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 910..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 402..459
FT /evidence="ECO:0000255"
FT COMPBIAS 976..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT VAR_SEQ 1..599
FT /note="Missing (in isoform 2)"
FT /id="VSP_058329"
SQ SEQUENCE 1008 AA; 112666 MW; 9B741625C7AD7019 CRC64;
MSSRQDKEKS VNVQVLLRCR PFSDDEVRSN APQVITCNDY QREVAVTQTI AGKQIDRVFT
FDKVFGPTAK QRDLYDQAII PIVNEVLEGF NCTIFAYGQT GTGKTYTMEG ECRRAKSGPK
GQLPADAGVI PRAVKQIFDT LESQNTEYSV KVTFLELYNE EITDLLAPEE ISKAALEERQ
KKPLPLMEDG KGGVLVRGLE EEIVTNASEI FSLLERGSAK RRTAETLLNK QSSRSHSLFS
ITIHIKEATP EGEELIKCGK LNLVDLAGSE NISRSGAREG RAREAGEINK SLLTLGRVIT
ALVEHLGHVP YRDSKLTRLL RDSLGGRTKT CIIATVSPSV HCLEETLSTL DYAHRAKSIK
NRPEVNQKMM KSTLIKDLYG EIDRLKAEVY AAREKVGVYI PKDRYQQEEN ERKAMADQIE
QMTTSLEANQ KQINDLQEKY DSELQHSADL SKKLEATEKC LDHTSNLLST TKEDLKQAQY
NLKEKDYIIS EQRKAENALI QQACLLRSDL EKSNRENAAL YSKIARGDKL NAANRSVVNS
FQADLASKLD ILSTTLATSI DQQNKHLKSV ENLCKSCVDS HDTATSEIKK KILASKALYM
SHMEAFQNVV LLHKANSNST LEDISSLSAA SCCSLDQLLA CVEGEAQKIF GDIQNLLADH
RSEVAHFTQE LRESFRISLD RTKDMSSFIL GLFDKYVEET SKLQSHSNHT HEAQVKSLED
FQKAYEEQSK SEEQKLLADI TSLVSKHVTR QRELVGGRLN SLGDAARGNK AFLDEHTSAM
EVVTKDAKRK WEMFAEQAEN DCKVGSNFSA AKHCRMETIL QECACTVDTA AQQWKASHAT
VNDLCRKQIA EVEALVRSAI ETNEQHEAEI ASSRATAEEH ASNSSKDLLQ DVDNMLQEAR
NSSSRVVSTV EAHLGESQHL QESHSSHTAG INTHADNAFQ SSYKDYEPTG ETPVRSEPEV
PSKDAIESLR AMPMESLMDE FRENHPYEPS KDRRPSLIPR SPLATINN
