KN7C_ARATH
ID KN7C_ARATH Reviewed; 890 AA.
AC Q8W5R6; Q9XI03;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Kinesin-like protein KIN-7C, mitochondrial {ECO:0000305};
DE AltName: Full=Mitochondria-targeted kinesin-related protein 1 {ECO:0000303|PubMed:11706156};
DE Flags: Precursor;
GN Name=KIN7C {ECO:0000305}; Synonyms=MKRP1 {ECO:0000312|EMBL:BAB71851.1};
GN OrderedLocusNames=At1g21730 {ECO:0000312|Araport:AT1G21730};
GN ORFNames=F8K7.17 {ECO:0000312|EMBL:AAD41428.1};
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 [MRNA].
RX PubMed=11706156; DOI=10.1104/pp.010631;
RA Itoh R., Fujiwara M., Yoshida S.;
RT "Kinesin-related proteins with a mitochondrial targeting signal.";
RL Plant Physiol. 127:724-726(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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 -!- SUBCELLULAR LOCATION: Mitochondrion {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=AAD41428.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB062738; BAB71851.1; -; mRNA.
DR EMBL; AC007727; AAD41428.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30148.1; -; Genomic_DNA.
DR PIR; H86350; H86350.
DR RefSeq; NP_173592.3; NM_102022.4.
DR AlphaFoldDB; Q8W5R6; -.
DR SMR; Q8W5R6; -.
DR STRING; 3702.AT1G21730.1; -.
DR iPTMnet; Q8W5R6; -.
DR PaxDb; Q8W5R6; -.
DR PRIDE; Q8W5R6; -.
DR ProteomicsDB; 250698; -.
DR EnsemblPlants; AT1G21730.1; AT1G21730.1; AT1G21730.
DR GeneID; 838777; -.
DR Gramene; AT1G21730.1; AT1G21730.1; AT1G21730.
DR KEGG; ath:AT1G21730; -.
DR Araport; AT1G21730; -.
DR TAIR; locus:2036987; AT1G21730.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_004957_1_0_1; -.
DR InParanoid; Q8W5R6; -.
DR OMA; MWMLVAE; -.
DR OrthoDB; 101117at2759; -.
DR PhylomeDB; Q8W5R6; -.
DR PRO; PR:Q8W5R6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8W5R6; baseline and differential.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Microtubule; Mitochondrion; Motor protein;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..73
FT /note="Mitochondrion"
FT /evidence="ECO:0000303|PubMed:11706156"
FT CHAIN 74..890
FT /note="Kinesin-like protein KIN-7C, mitochondrial"
FT /id="PRO_0000436461"
FT DOMAIN 75..394
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 511..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 395..468
FT /evidence="ECO:0000255"
FT COILED 664..693
FT /evidence="ECO:0000255"
FT COILED 729..765
FT /evidence="ECO:0000255"
FT COILED 818..884
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 155..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 890 AA; 98456 MW; 642778E9DCE0A23A CRC64;
MSATRSQRSS TISPARPRRS PATIPMKRPE TPSSSHFSAS PVTSSSPLLR SSPSPSTSSA
AASSTAVAST KLKENITVTI RFRPLSPREV NNGDEIAWYA DGDYTIRNEY NPSLCYGFDR
VFGPPTTTRR VYDIAAQQVV SGAMSGINGT VFAYGVTSSG KTHTMHGEQR SPGIIPLAVK
DVFSIIQETP EREFLLRVSY LEIYNEVIND LLDPTGQNLR IREDSQGTYV EGIKDEVVLS
PAHALSLIAS GEEHRHVGSN NVNLFSSRSH TMFTLTIESS PHGKGDDGED VSLSQLHLID
LAGSESSKTE ITGQRRKEGS SINKSLLTLG TVISKLTDTK AAHIPYRDSK LTRLLQSTLS
GHGRVSLICT ITPASSTSEE THNTLKFAQR CKHVEIKASR NKIMDEKSLI KKYQKEISCL
QEELTQLRHG NQDDLADRKL QVKLQSRLED DEEAKAALMG RIQRLTKLIL VSTKSSLQAA
SVKPDHIWRQ AFGEDELAYL PDRRRENMAD DGAVSTVSEH LKEPRDGNSS LDEMTKDRRK
NKTRGMLGWL KLKKSDGVAG TLPTDGNQSQ ASGSPSSSSK YTQTKTTRRE NAAAIKSIPE
KTVAGDLFSA TVGPEDSSPT GTTIADQMDL LHEQTKILVG EVALRTSSLN RLSEQAARNP
EDFHIRDQIQ KLEDEISEKK DQIRVLEQQI IEIFGMTPYA SDSLGMPQVL SKLTMQLNEK
IFEHEIKSAD NRILQEQLQM TKSENAEMQE TIILLRQQLD SLAERQSTQQ IAGDESSGKN
IHNRNGEESE IYSGAGTPTS VMSLNRVFAQ EETKEIYNET ALNSQALEIE NLKKEKMRLI
EEKDELGKLN KKLTEEASYA KELASAAAVE LQNLAEEVTR LCNENAKLSR
