KN7D_ARATH
ID KN7D_ARATH Reviewed; 1055 AA.
AC Q8W5R5; Q8RWW4; Q9SVI8;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Kinesin-like protein KIN-7D, mitochondrial {ECO:0000305};
DE AltName: Full=Mitochondria-targeted kinesin-related protein 2 {ECO:0000303|PubMed:11706156};
DE Flags: Precursor;
GN Name=KIN7D {ECO:0000305}; Synonyms=MKRP2 {ECO:0000312|EMBL:BAB71852.1};
GN OrderedLocusNames=At4g39050 {ECO:0000312|Araport:AT4G39050};
GN ORFNames=F19H22.150 {ECO:0000312|EMBL:CAB38825.1};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 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 [5]
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 [6]
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 [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=CAB38825.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80568.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB062739; BAB71852.1; -; mRNA.
DR EMBL; AL035679; CAB38825.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161594; CAB80568.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE87012.1; -; Genomic_DNA.
DR EMBL; AY091060; AAM13881.1; -; mRNA.
DR EMBL; AY150516; AAN13032.1; -; mRNA.
DR PIR; T06065; T06065.
DR RefSeq; NP_195616.2; NM_120065.3.
DR AlphaFoldDB; Q8W5R5; -.
DR SMR; Q8W5R5; -.
DR IntAct; Q8W5R5; 44.
DR STRING; 3702.AT4G39050.1; -.
DR iPTMnet; Q8W5R5; -.
DR PaxDb; Q8W5R5; -.
DR PRIDE; Q8W5R5; -.
DR ProteomicsDB; 250699; -.
DR EnsemblPlants; AT4G39050.1; AT4G39050.1; AT4G39050.
DR GeneID; 830060; -.
DR Gramene; AT4G39050.1; AT4G39050.1; AT4G39050.
DR KEGG; ath:AT4G39050; -.
DR Araport; AT4G39050; -.
DR TAIR; locus:2120187; AT4G39050.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_004957_0_0_1; -.
DR InParanoid; Q8W5R5; -.
DR OMA; MISDQMD; -.
DR OrthoDB; 101117at2759; -.
DR PhylomeDB; Q8W5R5; -.
DR PRO; PR:Q8W5R5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8W5R5; 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: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 GO; GO:0031347; P:regulation of defense response; IMP:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
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 PANTHER; PTHR24115; PTHR24115; 1.
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; Coiled coil; Metal-binding; Microtubule; Mitochondrion;
KW Motor protein; Nucleotide-binding; Reference proteome; Transit peptide;
KW Zinc; Zinc-finger.
FT TRANSIT 1..96
FT /note="Mitochondrion"
FT /evidence="ECO:0000303|PubMed:11706156"
FT CHAIN 97..1055
FT /note="Kinesin-like protein KIN-7D, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000436462"
FT DOMAIN 98..415
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT ZN_FING 1008..1043
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 419..503
FT /evidence="ECO:0000255"
FT COILED 618..653
FT /evidence="ECO:0000255"
FT COILED 694..823
FT /evidence="ECO:0000255"
FT COILED 880..911
FT /evidence="ECO:0000255"
FT BINDING 178..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 893
FT /note="E -> K (in Ref. 4; AAM13881)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1055 AA; 116464 MW; B69EC383FF14AB7B CRC64;
MASSSSRTRS SRPPSPASST SSSHLSNRLI PRSNSTSASS LITSAAGIAS RSMTPSRTFS
DSGLIGSGSF GIGSPVPYPS EELLGDPMDD TISSERDSIS VTVRFRPLSD REYQRGDEVA
WYPDGDTLVR HEYNPLTAYA FDKVFGPQAT TIDVYDVAAR PVVKAAMEGV NGTVFAYGVT
SSGKTHTMHG DQESPGIIPL AIKDVFSIIQ DTPGREFLLR VSYLEIYNEV INDLLDPTGQ
NLRVREDSQG TYVEGIKEEV VLSPGHALSF IAAGEEHRHV GSNNFNLLSS RSHTIFTLMV
ESSATGDEYD GVIFSQLNLI DLAGSESSKT ETTGLRRKEG SYINKSLLTL GTVIGKLSEG
KATHIPYRDS KLTRLLQSSL SGHGHVSLIC TITPASSSSE ETHNTLKFAS RAKSIEIYAS
RNQIIDEKSL IKKYQREIST LKLELDQLRR GMLVGVSHEE LMSLKQQLEE GQVKMQSRLE
EEEEAKAALM SRIQKLTKLI LVSTKNSIPG YSGDIPTHQR SLSAGKDDKF DSLLLESDNL
GSPSSTLALL SEGSLGFNHR RSSSKLNDEN SPGAEFTQGV MTPDEIDLLV EQVKMLAGEI
AFSTSTLKRL VDQSVNDPEN SQTQIQNLER EIHEKQRQMR GLEQLIIESG EASIANASLV
EMQQKVMSLM TQCNEKSFEL EIKSADNCIL QEQLQEKCTE NKELHEKVNL LEQRLNAVSS
EKSSPSCSNK AVSGEYADEL KKKIQSQEIE NEELKLEHVQ IVEENSGLRV QNQKLAEEAS
YAKELASAAA VELKNLASEV TKLSLQNTKL EKELAAARDL AQTRNPMNGV NRKYNDGARS
GRKGRISSSR SSGDEFDAWN LDPEDLKMEL QVRKQREVAL ESALAEKEFI EDEYRKKAEE
AKRREEALEN DLANMWVLVA KLKKDNGALP EPNGTDPGRE LEKSQSHAVL KERQVSSAPR
QPEVVVVAKT EETPKEEPLV ARLKARMQEM KEKEMKSQAN GDANSHICKV CFESPTAAIL
LPCRHFCLCK SCSLACSECP ICRTKISDRL FAFPS
