KN5C_TOBAC
ID KN5C_TOBAC Reviewed; 1006 AA.
AC O23826;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Kinesin-like protein KIN-5C {ECO:0000305};
DE AltName: Full=125 kDa kinesin-related protein;
GN Name=KIN5C {ECO:0000305}; Synonyms=TKRP125 {ECO:0000303|PubMed:9044048};
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 149-163 AND 194-211,
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Bright Yellow 2;
RX PubMed=9044048; DOI=10.1242/jcs.110.2.179;
RA Asada T., Kuriyama R., Shibaoka H.;
RT "TKRP125, a kinesin-related protein involved in the centrosome-independent
RT organization of the cytokinetic apparatus in tobacco BY-2 cells.";
RL J. Cell Sci. 110:179-189(1997).
RN [2]
RP FUNCTION.
RC STRAIN=cv. Bright Yellow 2;
RX PubMed=7983184; DOI=10.1242/jcs.107.8.2249;
RA Asada T., Shibaoka H.;
RT "Isolation of polypeptides with microtubule-translocating activity from
RT phragmoplasts of tobacco BY-2 cells.";
RL J. Cell Sci. 107:2249-2257(1994).
RN [3]
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).
CC -!- FUNCTION: Responsible for microtubule translocation. May be important
CC for the organization of phragmoplast-specific arrays of microtubules
CC (PubMed:7983184). Plays an essential role in stabilizing the mitotic
CC spindle. Required during mitotic cytokinesis (By similarity).
CC {ECO:0000250|UniProtKB:F4IIS5, ECO:0000269|PubMed:7983184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9044048}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9044048}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:9044048}. Note=Microtubule-
CC associated. {ECO:0000269|PubMed:9044048}.
CC -!- DEVELOPMENTAL STAGE: Expressed during S phase. Expression increases as
CC cell moves from S phase to M phase and then decreases rapidly as cell
CC enters the G1 phase. Expression increases again during the G2 phase.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-5/BimC subfamily. {ECO:0000305}.
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DR EMBL; D83711; BAA23159.1; -; mRNA.
DR PIR; T02017; T02017.
DR RefSeq; NP_001312103.1; NM_001325174.1.
DR AlphaFoldDB; O23826; -.
DR SMR; O23826; -.
DR GeneID; 107774014; -.
DR KEGG; nta:107774014; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1006
FT /note="Kinesin-like protein KIN-5C"
FT /id="PRO_0000125377"
FT DOMAIN 9..355
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT COILED 371..522
FT /evidence="ECO:0000255"
FT BINDING 95..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 150
FT /note="T -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="E -> F (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="D -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1006 AA; 113711 MW; 890C0E0F3504AA7D CRC64;
MSNKEKGVNV QVLLRCRPFS NDELRNNAPQ VVTCNDYQRE VAVSQNIAGK HIDRIFTFDK
VFGPSAQQRD LYDQAIVPIV NEVLEGFNCT IFAYGQTGTG KTYTMEGECK RSKSGPNGEL
PQEAGVIPRA VKQVFDTLES QNAEYSVKVT FLELYNEEIT DLLAPEDLKV ALEDRQKKQL
PLMEDGKGGV LVRGLEEEIV TSANEIFTLL ERGSAKRRTA ETLLNKQSSR SHSLFSITIH
IKEATPEGEE LIKCGKLNLV DLAGSENISR SGAREGRARE AGEINKSLLT LGRVINALVE
HLGHIPYRDS KLTRLLRDSL GGRTKTCIIA TVSPAVHCLE ETLSTLDYAH RAKNIKNKPE
VNQKMMKSTL IKDLYGEIER LKAEVYAARE KNGVYIPKER YYQEENERKA MADQIEQMGV
SIENHQKQFE ELQSRHDSQV QQCSDLTCKL DVTQKQLNQT SKLLAYTEEQ LRQSQYTLKE
RDFIISEQKK AENALAHQAC VLRADLEKSI QENASLFQKI AREDKLSTDN RSLVNNFQAE
LAKQLGSLSS TLATSVCRQT EHLQCVEKFC HNFLDSHDKA VLDLKRKINS SMALYISHFE
AMQNVVRLHK ATSNATLEEV STLASSNSIS TKEFLDAEAV EANSMFDELQ STLSTHQGEM
AHFARELRQR FNDSTEHLTN ISAIIQRFFD KLLDESKRLE KHATTVDEIQ TNSIAEFEKA
YEEQSKSDAE KLIADVTSLV SNHMRRQKEL VGARLVDLRE TVSGNRTFLD GHVSSMEGIT
TDAKRKWQDF YMQAEGETKE NADFSAAKHC RMESLMQKCV STAETALKRW QSTHELVNDM
GNQHVLTMHS VVRNICDNNE QHVTDFDSTR ESAEEDVKRN SEDIIKSIDS LSGEERGSIS
GVLDTTSAHS ETLDVLKKDH CMQSTSIEQI ALETFQQKYM DYEPTGATPI RSEPDVPSKV
TIESLRAMPM EVLLEEFREN NSFESFQVKE VKPSLIPRSP FSQINN
