KN7M_ARATH
ID KN7M_ARATH Reviewed; 1058 AA.
AC Q9SJU0; Q94BQ1;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Kinesin-like protein KIN-7M, chloroplastic {ECO:0000305};
DE Flags: Precursor;
GN Name=KIN7M {ECO:0000305};
GN OrderedLocusNames=At2g21380 {ECO:0000312|Araport:AT2G21380};
GN ORFNames=F3K23.14 {ECO:0000312|EMBL:AAD23684.2};
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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=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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-7 subfamily.
CC {ECO:0000303|PubMed:16448571}.
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DR EMBL; AC006841; AAD23684.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07168.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62121.1; -; Genomic_DNA.
DR EMBL; AY039966; AAK64143.1; -; mRNA.
DR EMBL; AY150452; AAN12893.1; -; mRNA.
DR PIR; E84600; E84600.
DR RefSeq; NP_001324300.1; NM_001335746.1.
DR RefSeq; NP_565510.1; NM_127709.3.
DR AlphaFoldDB; Q9SJU0; -.
DR SMR; Q9SJU0; -.
DR IntAct; Q9SJU0; 4.
DR STRING; 3702.AT2G21380.1; -.
DR iPTMnet; Q9SJU0; -.
DR PaxDb; Q9SJU0; -.
DR PRIDE; Q9SJU0; -.
DR ProteomicsDB; 237140; -.
DR EnsemblPlants; AT2G21380.1; AT2G21380.1; AT2G21380.
DR EnsemblPlants; AT2G21380.2; AT2G21380.2; AT2G21380.
DR GeneID; 816676; -.
DR Gramene; AT2G21380.1; AT2G21380.1; AT2G21380.
DR Gramene; AT2G21380.2; AT2G21380.2; AT2G21380.
DR KEGG; ath:AT2G21380; -.
DR Araport; AT2G21380; -.
DR TAIR; locus:2050044; AT2G21380.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_004957_0_0_1; -.
DR InParanoid; Q9SJU0; -.
DR OMA; NRNGTRP; -.
DR OrthoDB; 101117at2759; -.
DR PhylomeDB; Q9SJU0; -.
DR PRO; PR:Q9SJU0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJU0; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
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 InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Coiled coil; Metal-binding; Microtubule;
KW Motor protein; Nucleotide-binding; Plastid; Reference proteome;
KW Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 61..1058
FT /note="Kinesin-like protein KIN-7M, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000436471"
FT DOMAIN 104..421
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT ZN_FING 1011..1046
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 422..509
FT /evidence="ECO:0000255"
FT COILED 621..658
FT /evidence="ECO:0000255"
FT COILED 704..826
FT /evidence="ECO:0000255"
FT COILED 873..904
FT /evidence="ECO:0000255"
FT COILED 935..999
FT /evidence="ECO:0000255"
FT COMPBIAS 824..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 184..191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1058 AA; 117090 MW; F97660F723A9A506 CRC64;
MASSSSRTRS RSPFSHRRPP SPYSSASSTS SSLINNRLLP RSSSTPTSTV YNSGGVTGSR
SMSITRTISD SGPIGGSGTY GAQSYPSEGL IGESGQTITS ERDSISVTVR FRPMSEREYQ
RGDEIVWYPD ADKMVRNEYN PLTAYAFDKV FGPQSTTPEV YDVAAKPVVK AAMEGVNGTV
FAYGVTSSGK THTMHGDQDF PGIIPLAIKD VFSIIQETTG REFLLRVSYL EIYNEVINDL
LDPTGQNLRI REDSQGTYVE GIKEEVVLSP GHALSFIAAG EEHRHVGSNN FNLMSSRSHT
IFTLMIESSA HGDQYDGVIF SQLNLIDLAG SESSKTETTG LRRKEGAYIN KSLLTLGTVI
GKLTEGKTTH VPFRDSKLTR LLQSSLSGHG HVSLICTVTP ASSSTEETHN TLKFASRAKR
IEINASRNKI IDEKSLIKKY QKEISTLKVE LDQLRRGVLV GVSHEELLSL KQQLQEGQVK
MQSRLEEEEE AKAALMSRIQ KLTKLILVST KNSIPGYLGD TPAHSRSISA GKDDKLDSLL
LDSDNLASPS STLSLASDAR RSSSKFKDEN SPVGSRAELT QGVMTPDEMD LLVEQVKMLA
GEIAFGTSTL KRLVDQSMND PENSKTQIQN LENDIQEKQR QMKSLEQRIT ESGEASIANA
SSIEMQEKVM RLMTQCNEKS FELEIISADN RILQEQLQTK CTENNELHEK VHLLEQRLSS
QKATLSCCDV VTEEYVDELK KKVQSQEIEN EKLKLEHVQS VEEKSGLRVQ NQKLAEEASY
AKELASAAAI ELKNLADEVT KLSLQNAKLE KELVAARDLA AAAQKRNNNS MNSAANRNGT
RPGRKARISD SWNLNQENLT MELQARKQRE AVLEAALAEK EYIEEEFRKK AEEAKRREEA
LENDLANMWV LVAKLKKANS GALSIQKSDE AEPAKEDEVT ELDNKNEQNA ILKERQLVNG
HEEVIVAKAE ETPKEEPLVA RLKARMQEMK EKEMKSQAAA AANADANSHI CKVCFESPTA
TILLPCRHFC LCKSCSLACS ECPICRTKIS DRLFAFPS
