KN7L_ARATH
ID KN7L_ARATH Reviewed; 977 AA.
AC F4K3X8; Q9FG03;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 08-JUN-2016, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Kinesin-like protein KIN-7L, chloroplastic {ECO:0000305};
DE Flags: Precursor;
GN Name=KIN7L {ECO:0000305};
GN OrderedLocusNames=At5g06670 {ECO:0000312|Araport:AT5G06670};
GN ORFNames=F15M7.20 {ECO:0000312|EMBL:BAB11416.1};
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
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=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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AED91048.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB11416.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP002543; BAB11416.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP002032; BAB11416.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED91048.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; ANM70790.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70791.1; -; Genomic_DNA.
DR RefSeq; NP_001318493.1; NM_001342891.1.
DR RefSeq; NP_001332372.1; NM_001342893.1.
DR RefSeq; NP_001332373.1; NM_001342892.1.
DR RefSeq; NP_196285.5; NM_120750.5.
DR AlphaFoldDB; F4K3X8; -.
DR SMR; F4K3X8; -.
DR STRING; 3702.AT5G06670.1; -.
DR iPTMnet; F4K3X8; -.
DR PaxDb; F4K3X8; -.
DR PRIDE; F4K3X8; -.
DR EnsemblPlants; AT5G06670.2; AT5G06670.2; AT5G06670.
DR EnsemblPlants; AT5G06670.3; AT5G06670.3; AT5G06670.
DR GeneID; 830555; -.
DR Gramene; AT5G06670.2; AT5G06670.2; AT5G06670.
DR Gramene; AT5G06670.3; AT5G06670.3; AT5G06670.
DR KEGG; ath:AT5G06670; -.
DR Araport; AT5G06670; -.
DR TAIR; locus:2144103; AT5G06670.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_004957_0_0_1; -.
DR InParanoid; F4K3X8; -.
DR OrthoDB; 101117at2759; -.
DR PRO; PR:F4K3X8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K3X8; 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: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; 3.40.850.10; -; 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; Chloroplast; Coiled coil; Microtubule; Motor protein;
KW Nucleotide-binding; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..977
FT /note="Kinesin-like protein KIN-7L, chloroplastic"
FT /id="PRO_0000436470"
FT DOMAIN 66..385
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 386..471
FT /evidence="ECO:0000255"
FT COILED 626..688
FT /evidence="ECO:0000255"
FT COILED 732..942
FT /evidence="ECO:0000255"
FT COMPBIAS 551..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 146..153
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 977 AA; 109134 MW; 43AD87187C0F534F CRC64;
MGSKQVSKTR NGGFSKLKTV ESSASSTTSS SKLYQEASVD SHSSPTSSSV RSKPQLPPKP
LQSKENVTVT VRFRPLSPRE IRKGEEIAWY ADGETIVRNE NNQSIAYAYD RVFGPTTTTR
NVYDVAAQHV VNGAMAGVNG TIFAYGVTSS GKTHTMHGNQ RSPGIIPLAV KDAFSIIQET
PRREFLLRVS YFEIYNEVVN DLLNPAGQNL RIREDEQGTY IEGIKEEVVL SPAHVLSLIA
AGEEHRHIGS TSFNLLSSRS HTMFTLTIES SPLGDNNEGG AVHLSQLNLI DLAGSESSKA
ETSGLRRKEG SYINKSLLTL GTVISKLTDR RASHVPYRDS KLTRLLESSL SGHGRVSLIC
TVTPASSNSE ETHNTLKFAH RAKHIEIQAA QNKIIDEKSL IKKYQYEIRQ LKEELEQLKQ
GIKPVSQLKD ISGDDIDIVL LKQKLEEEED AKAALLSRIQ RLTKLILVSN KTPQTSRFSY
RADPRRRHSF GEEELAYLPH KRRDLTDDEN LELYVSREGT PEIIDDAFIE EKKTRKHGLL
NWLKIKKKDS SLGGSSLSDK SSAVKSNSTP STPQGEGSDF HTESRLSEGS ALADQIIETM
ENREAHEDSF HEIETPETRI KMIDQMEILR EQQKTLSEEM AQQSRSFKLL SEEAAKAPQN
EEIKAEIINL NGDIKAKNDQ IATLGKQILD FVIASHDELD KSDIVQAVSE MRAQLNEKCF
ELEVKAADNR IIQEQLTEKT SFCEDLQEEV ANLKQQLSDA LELGDINSVT CHMQQSSQSP
NKNEEKVIEA QAFEIEELKL KAAELSELNE QLEIRNKKLA EESSYAKELA SAAAIELKAL
SEEIARLMNH NERLAADLAA VQKSSVTTPQ GKTGNLRNGR RESVSKRKEQ ENSLMELKRE
LTVSKEREVS FEAALIEKIQ REAELQRTVE ESKQREAYLE NELANMWGLV AKLRSQGAAN
SGLSDSVSET RIEHFGT
