KN5B_ARATH
ID KN5B_ARATH Reviewed; 1039 AA.
AC Q0WQJ7; Q9ZUS4;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Kinesin-like protein KIN-5B {ECO:0000305};
DE AltName: Full=AtKRP125a {ECO:0000303|PubMed:11472632};
GN Name=KIN5B {ECO:0000305};
GN OrderedLocusNames=At2g37420 {ECO:0000312|Araport:AT2G37420};
GN ORFNames=F3G5.21 {ECO:0000312|EMBL:AAC98061.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENE FAMILY.
RX PubMed=11472632; DOI=10.1186/1471-2164-2-2;
RA Reddy A.S., Day I.S.;
RT "Kinesins in the Arabidopsis genome: a comparative analysis among
RT eukaryotes.";
RL BMC Genomics 2:2-2(2001).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16448571; DOI=10.1186/1471-2164-7-18;
RA Richardson D.N., Simmons M.P., Reddy A.S.;
RT "Comprehensive comparative analysis of kinesins in photosynthetic
RT eukaryotes.";
RL BMC Genomics 7:18-18(2006).
RN [6]
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 [7]
RP REVIEW.
RX PubMed=22038119; DOI=10.1007/s00709-011-0343-9;
RA Zhu C., Dixit R.;
RT "Functions of the Arabidopsis kinesin superfamily of microtubule-based
RT motor proteins.";
RL Protoplasma 249:887-899(2012).
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 -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-5/BimC subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC98061.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005896; AAC98061.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09396.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61462.1; -; Genomic_DNA.
DR EMBL; AK228698; BAF00602.1; -; mRNA.
DR PIR; E84792; E84792.
DR RefSeq; NP_001323679.1; NM_001336659.1.
DR RefSeq; NP_850281.1; NM_179950.3.
DR AlphaFoldDB; Q0WQJ7; -.
DR SMR; Q0WQJ7; -.
DR STRING; 3702.AT2G37420.1; -.
DR PaxDb; Q0WQJ7; -.
DR PRIDE; Q0WQJ7; -.
DR ProteomicsDB; 238227; -.
DR EnsemblPlants; AT2G37420.1; AT2G37420.1; AT2G37420.
DR EnsemblPlants; AT2G37420.2; AT2G37420.2; AT2G37420.
DR GeneID; 818318; -.
DR Gramene; AT2G37420.1; AT2G37420.1; AT2G37420.
DR Gramene; AT2G37420.2; AT2G37420.2; AT2G37420.
DR KEGG; ath:AT2G37420; -.
DR Araport; AT2G37420; -.
DR TAIR; locus:2049791; AT2G37420.
DR eggNOG; KOG0243; Eukaryota.
DR HOGENOM; CLU_001485_33_0_1; -.
DR InParanoid; Q0WQJ7; -.
DR OMA; ENCLQEC; -.
DR OrthoDB; 179272at2759; -.
DR PhylomeDB; Q0WQJ7; -.
DR PRO; PR:Q0WQJ7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q0WQJ7; baseline and differential.
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 ATP-binding; Cytoplasm; Cytoskeleton; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..1039
FT /note="Kinesin-like protein KIN-5B"
FT /id="PRO_0000436269"
FT DOMAIN 48..390
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1008..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 134..141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1039 AA; 117581 MW; 297D4AE76D8426F7 CRC64;
MSFTPEVVSR KSGVGVIPSP APFLTPRLER RRPDSFSNRL DRDNKEVNVQ VILRCKPLSE
EEQKSSVPRV ISCNEMRREV NVLHTIANKQ VDRLFNFDKV FGPKSQQRSI YDQAIAPIVH
EVLEGFSCTV FAYGQTGTGK TYTMEGGMRK KGGDLPAEAG VIPRAVRHIF DTLEAQNADY
SMKVTFLELY NEEVTDLLAQ DDSSRSSEDK QRKPISLMED GKGSVVLRGL EEEVVYSAND
IYALLERGSS KRRTADTLLN KRSSRSHSVF TITVHIKEES MGDEELIKCG KLNLVDLAGS
ENILRSGARD GRAREAGEIN KSLLTLGRVI NALVEHSSHV PYRDSKLTRL LRDSLGGKTK
TCIIATISPS AHSLEETLST LDYAYRAKNI KNKPEANQKL SKAVLLKDLY LELERMKEDV
RAARDKNGVY IAHERYTQEE VEKKARIERI EQLENELNLS ESEVSKFCDL YETEKEKLLD
VESDLKDCKR NLHNSNKDLL DLKENYIQVV SKLKEKEVIV SRMKASETSL IDRAKGLRCD
LQHASNDINS LFTRLDQKDK LESDNQSMLL KFGSQLDQNL KDLHRTVLGS VSQQQQQLRT
MEEHTHSFLA HKYDATRDLE SRIGKTSDTY TSGIAALKEL SEMLQKKASS DLEKKNTSIV
SQIEAVEKFL TTSATEASAV AQDIHNLLND QKKLLALAAR QQEQGLVRSM RSAQEISNST
STIFSNIYNQ AHDVVEAIRA SQAEKSRQLD AFEMKFKEEA EREEKQALND ISLILSKLTS
KKTAMISDAS SNIREHDIQE EKRLYEQMSG MQQVSIGAKE ELCDYLKKEK THFTENTIAS
AESITVMDSY LEDCLGRAND SKTLWETTET GIKNLNTKYQ QELNVTMEDM AKENEKVQDE
FTSTFSSMDA NFVSRTNELH AAVNDSLMQD RENKETTEAI VETCMNQVTL LQENHGQAVS
NIRNKAEQSL IKDYQVDQHK NETPKKQSIN VPSLDSIEEM RTLFSQNTLS EEHTSLEKIS
TKQGLGEANN RTPFLEVNK
