KN5D_ARATH
ID KN5D_ARATH Reviewed; 1058 AA.
AC Q9LZU5;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Kinesin-like protein KIN-5D {ECO:0000305};
GN Name=KIN5D {ECO:0000305};
GN OrderedLocusNames=At3g45850 {ECO:0000312|Araport:AT3G45850};
GN ORFNames=F16L2_60 {ECO:0000312|EMBL:CAB82809.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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 [4]
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 [5]
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 [6]
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}.
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DR EMBL; AL162459; CAB82809.1; -; Genomic_DNA.
DR EMBL; CP002686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T47525; T47525.
DR AlphaFoldDB; Q9LZU5; -.
DR SMR; Q9LZU5; -.
DR STRING; 3702.AT3G45850.1; -.
DR iPTMnet; Q9LZU5; -.
DR PaxDb; Q9LZU5; -.
DR PeptideAtlas; Q9LZU5; -.
DR PRIDE; Q9LZU5; -.
DR EnsemblPlants; AT3G45850.2; AT3G45850.2; AT3G45850.
DR Gramene; AT3G45850.2; AT3G45850.2; AT3G45850.
DR Araport; AT3G45850; -.
DR TAIR; locus:2077132; AT3G45850.
DR eggNOG; KOG0243; Eukaryota.
DR HOGENOM; CLU_001485_33_0_1; -.
DR InParanoid; Q9LZU5; -.
DR PhylomeDB; Q9LZU5; -.
DR PRO; PR:Q9LZU5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LZU5; 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 3: Inferred from homology;
KW ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1058
FT /note="Kinesin-like protein KIN-5D"
FT /evidence="ECO:0000255"
FT /id="PRO_0000436270"
FT DOMAIN 48..390
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 438..517
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..41
FT /note="Basic and acidic residues"
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 1058 AA; 119009 MW; 4A7CE824B4E1B792 CRC64;
MDSIQQRRGG IVSLSPAQTP RSSDKSARES RSSESNSTNR NDKEKGVNVQ VILRCRPLSE
DEARIHTPVV ISCNENRREV AATQSIAGKH IDRHFAFDKV FGPASQQKDL YDQAICPIVF
EVLEGYNCTI FAYGQTGTGK TYTMEGGARK KNGEFPSDAG VIPRAVKQIF DILEAQGAEY
SMKVTFLELY NEEISDLLAP EETIKFVDEK SKKSIALMED GKGSVFVRGL EEEIVSTANE
IYKILEKGSA KRRTAETLLN KQSSRSHSIF SITIHIKENT PEGEEMIKCG KLNLVDLAGS
ENISRSGARE GRAREAGEIN KSLLTLGRVI NALVEHSGHI PYRDSKLTRL LRESLGGKTK
TCVIATISPS IHCLEETLST LDYAHRAKNI KNKPEINQKM MKSAVMKDLY SEIDRLKQEV
YAAREKNGIY IPKDRYIQEE AEKKAMAEKI ERLELQSESK DKRVVDLQEL YNSQQILTAE
LSEKLEKTEK KLEETEHSLF DLEEKYRQAN ATIKEKEFVI SNLLKSEKSL VERAFQLRTE
LESASSDVSN LFSKIERKDK IEDGNRFLIQ KFQSQLTQQL ELLHKTVASS VTQQEVQLKH
MEEDMESFVS TKSEATEELR DRLSKLKRVY GSGIEALDNI AVKLDGNSQS TFSSLNSEVS
KHSHELENVF KGFASEADML LQDLQSSLNK QEEKLITFAQ QQRKAHSRAV DTARSVSKVT
VEFFKTLDTH ATKLTGIVEE AQTVNHKKLS EFENKFEECA ANEERQLLEK VAELLANSNA
RKKNLVQMAV HDLRESASTR TTTLQHEMST MQDSTSSIKA EWSIHMEKTE SSHHEDTSAV
ESGKKAMQEV LLNCLEKTEM SAHQWRKAQE SLVSLERNNV ASVDSIVRGG MDANENLRSQ
FSTAVSSSLD VFDAANSSLL TSIDHSLQLD NDACTKVNSM IIPCCEDLIE LKSDHNHKII
EITENAGKCL LDEYVVDEPS CSTPKKRPID IPSIESIEEL RTPASEELLR AFRDEKLSKQ
ANGDAKQQQQ QQQQHLIRAS SLYEAAVSDS RYPLSAVN
