KN4A_ARATH
ID KN4A_ARATH Reviewed; 1035 AA.
AC Q8GS71; Q9FIJ9;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Kinesin-like protein KIN-4A {ECO:0000305};
DE AltName: Full=AtKINESIN-4A {ECO:0000303|PubMed:25600279};
DE AltName: Full=Protein FRAGILE FIBER 1 {ECO:0000303|PubMed:12468730};
GN Name=KIN4A {ECO:0000305}; Synonyms=FRA1 {ECO:0000312|EMBL:AAN86114.1};
GN OrderedLocusNames=At5g47820 {ECO:0000312|Araport:AT5G47820};
GN ORFNames=MCA23.16 {ECO:0000312|EMBL:BAB11329.1};
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 [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=12468730; DOI=10.1105/tpc.005801;
RA Zhong R., Burk D.H., Morrison W.H., Ye Z.H.;
RT "A kinesin-like protein is essential for oriented deposition of cellulose
RT microfibrils and cell wall strength.";
RL Plant Cell 14:3101-3117(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 TISSUE SPECIFICITY, AND FUNCTION.
RX DOI=10.1111/j.1672-9072.2007.00521.x;
RA Zhou J., Qiu J., Ye Z.H.;
RT "Alteration in secondary wall deposition by overexpression of the Fragile
RT Fiber1 kinesin-like protein in Arabidopsis.";
RL J. Integr. Plant Biol. 8:1235-1243(2007).
RN [7]
RP FUNCTION, SUBUNIT, AND DOMAIN.
RX PubMed=21914648; DOI=10.1093/mp/ssr077;
RA Zhu C., Dixit R.;
RT "Single molecule analysis of the Arabidopsis FRA1 kinesin shows that it is
RT a functional motor protein with unusually high processivity.";
RL Mol. Plant 4:879-885(2011).
RN [8]
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 [9]
RP FUNCTION, 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).
RN [10]
RP DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25646318; DOI=10.1104/pp.114.251462;
RA Zhu C., Ganguly A., Baskin T.I., McClosky D.D., Anderson C.T., Foster C.,
RA Meunier K.A., Okamoto R., Berg H., Dixit R.;
RT "The fragile Fiber1 kinesin contributes to cortical microtubule-mediated
RT trafficking of cell wall components.";
RL Plant Physiol. 167:780-792(2015).
CC -!- FUNCTION: Kinesin-like motor protein involved in the control of the
CC oriented deposition of cellulose microfibrils (PubMed:12468730, Ref.6).
CC Its motor activity is directed toward the microtubule's plus end. It
CC possesses the potential to drive long-distance transport of cargo along
CC cortical microtubules (PubMed:21914648, PubMed:25646318). Regulates
CC cell wall mechanics during cell elongation, by the regulation of
CC primary and secondary walls deposition (Ref.6, PubMed:25600279,
CC PubMed:25646318). Contributes to cortical microtubule-mediated
CC trafficking of cell wall components (PubMed:25646318).
CC {ECO:0000269|PubMed:12468730, ECO:0000269|PubMed:21914648,
CC ECO:0000269|PubMed:25600279, ECO:0000269|PubMed:25646318,
CC ECO:0000269|Ref.6}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21914648}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25646318}.
CC Cytoplasm, cytoskeleton {ECO:0000305|PubMed:12468730}.
CC Note=Concentrated around the periphery of the cytoplasm.
CC {ECO:0000269|PubMed:12468730}.
CC -!- TISSUE SPECIFICITY: Expressed in stems and flowers (PubMed:12468730).
CC Detected in cells undergoing secondary wall deposition including
CC developing interfascicular fibers and xylem cells, but also in dividing
CC cells and expanding/elongating parenchyma cells (Ref.6).
CC {ECO:0000269|PubMed:12468730, ECO:0000269|Ref.6}.
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:0000305|PubMed:21914648}.
CC -!- DISRUPTION PHENOTYPE: Reduced length of roots and inflorescence stems.
CC Altered orientation of cellulose microfibrils in fiber walls leading to
CC dramatic reduction in fiber mechanical strength. No apparent alteration
CC in cell wall composition. Lower expansion rate of the inflorescence
CC stem along with the reduced thickness of both primary and secondary
CC cell walls leading to mechanically weaker stems (PubMed:25646318).
CC {ECO:0000269|PubMed:12468730, ECO:0000269|PubMed:25600279,
CC ECO:0000269|PubMed:25646318}.
CC -!- MISCELLANEOUS: Overexpression of KIN4A/FRA1 caused a severe reduction
CC in the thickness of secondary walls in interfascicular fibers and
CC deformation of vessels, an increase in the number of secondary wall
CC layers, which are accompanied with a marked decrease in stem strength.
CC {ECO:0000269|Ref.6}.
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=BAB11329.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY158083; AAN86114.1; -; mRNA.
DR EMBL; AY158084; AAN86115.1; -; Genomic_DNA.
DR EMBL; AB016886; BAB11329.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95575.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95576.1; -; Genomic_DNA.
DR RefSeq; NP_199593.2; NM_124156.5.
DR RefSeq; NP_851151.1; NM_180820.2.
DR AlphaFoldDB; Q8GS71; -.
DR SMR; Q8GS71; -.
DR STRING; 3702.AT5G47820.2; -.
DR iPTMnet; Q8GS71; -.
DR PaxDb; Q8GS71; -.
DR PRIDE; Q8GS71; -.
DR ProteomicsDB; 250746; -.
DR EnsemblPlants; AT5G47820.1; AT5G47820.1; AT5G47820.
DR EnsemblPlants; AT5G47820.2; AT5G47820.2; AT5G47820.
DR GeneID; 834833; -.
DR Gramene; AT5G47820.1; AT5G47820.1; AT5G47820.
DR Gramene; AT5G47820.2; AT5G47820.2; AT5G47820.
DR KEGG; ath:AT5G47820; -.
DR Araport; AT5G47820; -.
DR TAIR; locus:2160912; AT5G47820.
DR eggNOG; KOG0244; Eukaryota.
DR HOGENOM; CLU_001485_4_2_1; -.
DR InParanoid; Q8GS71; -.
DR OMA; PAFNKQH; -.
DR OrthoDB; 369179at2759; -.
DR PhylomeDB; Q8GS71; -.
DR PRO; PR:Q8GS71; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GS71; baseline and differential.
DR Genevisible; Q8GS71; AT.
DR GO; GO:0055028; C:cortical microtubule; IDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:UniProtKB.
DR GO; GO:0010215; P:cellulose microfibril organization; IMP:TAIR.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IDA:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR GO; GO:0009832; P:plant-type cell wall biogenesis; IMP:TAIR.
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 1: Evidence at protein level;
KW ATP-binding; Cell wall biogenesis/degradation; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Motor protein; Nucleotide-binding;
KW Reference proteome; Transport.
FT CHAIN 1..1035
FT /note="Kinesin-like protein KIN-4A"
FT /id="PRO_0000431962"
FT DOMAIN 11..370
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 704..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 408..436
FT /evidence="ECO:0000255"
FT COILED 504..707
FT /evidence="ECO:0000255"
FT COILED 881..911
FT /evidence="ECO:0000255"
FT COMPBIAS 710..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 90..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1035 AA; 116734 MW; 6DF0B4C16B88588C CRC64;
MESTPPPDDC SVKVAVHIRP LIGDERIQGC QDCVTVVTGK PQVQIGSHSF TFDHVYGSSG
SPSTEMYEEC AAPLVDGLFQ GYNATVLAYG QTGSGKTYTM GTGCGDSSQT GIIPQVMNAL
FTKIETLKQQ IEFQIHVSFI EIHKEEVQDL LDPCTVNKSD TNNTGHVGKV AHVPGKPPIQ
IRETSNGVIT LAGSTEVSVS TLKEMAACLD QGSVSRATGS TNMNNQSSRS HAIFTITVEQ
MRKINTDSPE NGAYNGSLKE EYLCAKLHLV DLAGSERAKR TGSDGLRFKE GVHINKGLLA
LGNVISALGD EKKRKDGAHV PYRDSKLTRL LQDSLGGNSR TVMIACISPA DINAEETLNT
LKYANRARNI RNKPVVNRDP VSSEMLKMRQ QVEYLQAELS LRTGGSSCAE VQALKERIVW
LETANEELCR ELHEYRSRCP GVEHSEKDFK DIRADDIVGS VRPDGLKRSL HSIESSNYPM
VEATTGDSRE IDEEAKEWEH KLLQNSMDKE LYELNRRLEE KESEMKLFDG YDPAALKQHF
GKKIAEVEDE KRSVQEERNR LLAEIENLAS DGQAQKLQDV HAQNLKALEA QILDLKKKQE
SQVQLLKQKQ KSDDAARRLQ DEIQSIKAQK VQLQHRMKQE AEQFRQWKAS REKELLQLRK
EGRKSEYERH KLQALNQRQK MVLQRKTEEA AMATKRLKEL LEARKSSPRE HSAGTNGFGT
NGQTNEKSLQ RWLDHELEVM VNVHEVRHEY EKQSHVRAAL AEELAVLRQV DEFAVKGLSP
PRGKNGFARA SSLSPNARMA RISSLENMLV ISSNSLVAMA SQLSEAEERE RAFTNRGRWN
QLRSMGEAKN LLQYMFNSLA ETRCQLWEKD VEIKEMKDQF KEIVGLLRQS ELRRKEAEKE
LKLREQAIAT SLGTPPSSVK HVAEDLSTPS PMTVPAQKQL KFTPGIANGK VRGPAAFLDT
NKKMVPMGQV SMRKLSAVGK QGGRLWRWKR SHHQWIVQFK WKWQKPWRLS EWIRTSDETL
LKSKPRLKAL PNKIM
