KN4C_ARATH
ID KN4C_ARATH Reviewed; 1300 AA.
AC F4K0J3; Q8GX87; Q9FME7;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Kinesin-like protein KIN-4C {ECO:0000305};
DE AltName: Full=AtKINESIN-4C {ECO:0000303|PubMed:25600279};
GN Name=KIN4C {ECO:0000305};
GN OrderedLocusNames=At5g60930 {ECO:0000312|Araport:AT5G60930};
GN ORFNames=MSL3.5 {ECO:0000312|EMBL:BAB10642.1};
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=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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] OF 627-1300.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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).
RN [7]
RP IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25600279; DOI=10.1016/j.molp.2015.01.004;
RA Kong Z., Ioki M., Braybrook S., Li S., Ye Z.H., Julie Lee Y.R., Hotta T.,
RA Chang A., Tian J., Wang G., Liu B.;
RT "Kinesin-4 functions in vesicular transport on cortical microtubules and
RT regulates cell wall mechanics during cell elongation in plants.";
RL Mol. Plant 8:1011-1023(2015).
CC -!- FUNCTION: Kinesin-like motor protein involved in the control of the
CC oriented deposition of cellulose microfibrils.
CC {ECO:0000250|UniProtKB:Q8GS71}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8GS71}.
CC -!- DOMAIN: Composed of an N-terminal domain which is responsible for the
CC motor activity of kinesin (it hydrolyzes ATP and binds microtubule) and
CC a central to C-terminal alpha-helical coiled coil domain that mediates
CC the heavy chain dimerization. {ECO:0000250|UniProtKB:Q8GS71}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:25600279}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-4 subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AED97398.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB10642.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAC42985.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB008269; BAB10642.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97398.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; ANM70805.1; -; Genomic_DNA.
DR EMBL; AK118373; BAC42985.1; ALT_TERM; mRNA.
DR RefSeq; NP_001332385.1; NM_001345436.1.
DR RefSeq; NP_001332386.1; NM_001345437.1.
DR RefSeq; NP_200901.2; NM_125486.3.
DR AlphaFoldDB; F4K0J3; -.
DR SMR; F4K0J3; -.
DR STRING; 3702.AT5G60930.1; -.
DR iPTMnet; F4K0J3; -.
DR PaxDb; F4K0J3; -.
DR PRIDE; F4K0J3; -.
DR ProteomicsDB; 237121; -.
DR EnsemblPlants; AT5G60930.3; AT5G60930.3; AT5G60930.
DR GeneID; 836214; -.
DR Gramene; AT5G60930.3; AT5G60930.3; AT5G60930.
DR KEGG; ath:AT5G60930; -.
DR Araport; AT5G60930; -.
DR TAIR; locus:2173537; AT5G60930.
DR eggNOG; KOG0244; Eukaryota.
DR HOGENOM; CLU_001485_4_2_1; -.
DR InParanoid; F4K0J3; -.
DR OMA; KEMCDME; -.
DR OrthoDB; 369179at2759; -.
DR PRO; PR:F4K0J3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K0J3; baseline and differential.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007052; P:mitotic spindle organization; 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 2: Evidence at transcript level;
KW ATP-binding; Cell wall biogenesis/degradation; Coiled coil; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1300
FT /note="Kinesin-like protein KIN-4C"
FT /id="PRO_0000436186"
FT DOMAIN 6..360
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 956..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 580..615
FT /evidence="ECO:0000255"
FT COILED 653..697
FT /evidence="ECO:0000255"
FT COILED 781..823
FT /evidence="ECO:0000255"
FT COMPBIAS 956..975
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1018
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85..92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 627
FT /note="K -> M (in Ref. 3; BAC42985)"
FT /evidence="ECO:0000305"
FT CONFLICT 822
FT /note="I -> IS (in Ref. 3; BAC42985)"
FT /evidence="ECO:0000305"
FT CONFLICT 1134
FT /note="A -> V (in Ref. 3; BAC42985)"
FT /evidence="ECO:0000305"
FT CONFLICT 1190
FT /note="T -> A (in Ref. 3; BAC42985)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1300 AA; 145364 MW; 4FC4C11E62669518 CRC64;
MESTECVRVA VNIRPLITPE LLNGCTDCIT VAPKEPQVHI GSHTFTYDFV YGNGGYPCSE
IYNHCVAPLV DALFKGYNAT VLAYGQTGSG KTYTMGTNYS GDCTNGGVIP NVMEDIFRRV
ETTKDSSELL IRVSFIEIFK EEVFDLLDSN SSALLKNDSG VQAKHTALSR APIQIRETAS
GGITLAGVTE AEVKTKEEMG SFLARGSLSR ATGSTNMNSQ SSRSHAIFTI TLEQKKIAGG
SCTTTEDGGE DILCAKLHLV DLAGSERAKR TGADGMRLKE GIHINKGLLA LGNVISALGD
EKKRKEGGHV PYRDSKLTRL LQDSLGGNSK TVMIACVSPA DTNAEETLNT LKYANRARNI
QNKAVINRDP ATAQMQRMRS QIEQLQTELL FYRGDSGAFD ELQILKHKIS LLEASNRELH
NELQERRVAS EHFSKRAYDA QVEKDKLIMI IESVRNGKSL DEIESCQNED VGLVNKYVSK
IQELEGELLH IKNLKKTSNH QYSDDSYDVG PRSNNVLFPS SNESSDCEDK VMDVTDELEF
QEKEIEHCSL QEKLDMELKE LDKRLEEKEA EMKRFSSGGT SVLKQHYEKK VYDLEQEKRA
LQREIEGLRH NLASIPSGPG DGAQKLKEEY VQKLNTLETQ VSVLKKKQDA QAQLMRQKQK
SDDAAIKLQD EIHRIKSQKV QLQQKIKQES EQFRAWKASR EKEVMQLKKE GRRNEYEMHK
LMALNQKQKL VLQRKTEEAS QVTKRLKELL DNRKASSRET LSGANGPGTQ ALMQAIEHEI
EVTVRVHEVR SEYERQTEER ARMAKEVARL REENELLKNA KISVHGDTMS PGARNSRIFA
LENMLATSSS TLVSMASQLS EAEERERVFG GRGRWNQVRT LGDAKSIMNY LFNLASTARC
LARDKEADCR EKDVLIRDLK EKIVKFSSYV RYMEIQKADL VHQVKAQTSA MKKLSADENL
KNEHSMKKQE TRNSTIVLED MDTSDSEASD HEREDPDLDD EWKPEHESER ESEQESVIKL
NRKRNFKVGR RRSSVVMRRS YEENSETPSD DAVKSDVCCC TCSKSSSCKT MKCQCRATKG
SCGPSCGCSS VKCSNRNADG KENNSISESE ALENGENSQE SDEKDKGQQQ QVLASRGAML
LQNALADKPE EETNDDGGTR RRRKPLSDIG NTTGKSNVPR PSQRKKWKKT VLQLVPVGPP
ALPPTHTNTH LIPEANSVTV DSDTARMPEN SDSGESNSIK LKLPRAMRSA SSNGSNLLRE
RNADQNGSES GGNSGFVQSN SGRASGSRTS DEKENHTRRV
