KN14N_ARATH
ID KN14N_ARATH Reviewed; 754 AA.
AC P46875; Q0WS04; Q9FH38;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Kinesin-like protein KIN-14N {ECO:0000305};
DE AltName: Full=AtKIN14d {ECO:0000303|PubMed:18088313};
DE AltName: Full=Kinesin-like protein KatC {ECO:0000303|PubMed:8075402, ECO:0000303|PubMed:8492804};
GN Name=KIN14N {ECO:0000305};
GN Synonyms=ATK3 {ECO:0000305}, KATC {ECO:0000312|EMBL:BAA04674.1};
GN OrderedLocusNames=At5g54670 {ECO:0000312|Araport:AT5G54670};
GN ORFNames=K5F14.1 {ECO:0000312|EMBL:BAB09933.1}, MRB17.18;
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], MICROTUBULE-BINDING, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=8075402; DOI=10.1007/bf00028881;
RA Mitsui H., Nakatani K., Yamaguchi-Shinozaki K., Shinozaki K., Nishikawa K.,
RA Takahashi H.;
RT "Sequencing and characterization of the kinesin-related genes katB and katC
RT of Arabidopsis thaliana.";
RL Plant Mol. Biol. 25:865-876(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION.
RX PubMed=8492804; DOI=10.1007/bf00291995;
RA Mitsui H., Yamaguchi-Shinozaki K., Shinozaki K., Nishikawa K.,
RA Takahashi H.;
RT "Identification of a gene family (kat) encoding kinesin-like proteins in
RT Arabidopsis thaliana and the characterization of secondary structure of
RT KatA.";
RL Mol. Gen. Genet. 238:362-368(1993).
RN [7]
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 [8]
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 [9]
RP MICROTUBULE-BINDING, AND SUBUNIT.
RX PubMed=17244481; DOI=10.5483/bmbrep.2007.40.1.044;
RA Jiang S., Li M., Xu T., Ren D., Liu G.;
RT "Two kinesins from Arabidopsis, KatB and KatC, have a second microtubule-
RT binding site in the tail domain.";
RL J. Biochem. Mol. Biol. 40:44-52(2007).
RN [10]
RP IDENTIFICATION.
RX PubMed=18088313; DOI=10.1111/j.1365-313x.2007.03391.x;
RA Quan L., Xiao R., Li W., Oh S.A., Kong H., Ambrose J.C., Malcos J.L.,
RA Cyr R., Twell D., Ma H.;
RT "Functional divergence of the duplicated AtKIN14a and AtKIN14b genes:
RT critical roles in Arabidopsis meiosis and gametophyte development.";
RL Plant J. 53:1013-1026(2008).
RN [11]
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 -!- SUBUNIT: Bind to microtubules in an ATP-insensitive manner (in vitro)
CC (PubMed:8075402, PubMed:17244481). Homodimer and heterodimer with
CC KIN14M/KATB (in vitro) (PubMed:17244481). {ECO:0000269|PubMed:17244481,
CC ECO:0000269|PubMed:8075402}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- DOMAIN: Composed of three structural domains; a small globular N-
CC terminal, a central alpha-helical coiled coil and a large globular C-
CC terminal which is responsible for the motor activity (it hydrolyzes ATP
CC and binds microtubules).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-14 subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09933.1; 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; D21138; BAA04674.1; -; mRNA.
DR EMBL; AB022214; BAB09933.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96525.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68862.1; -; Genomic_DNA.
DR EMBL; BT003156; AAO24588.1; -; mRNA.
DR EMBL; AK228138; BAF00095.1; -; mRNA.
DR PIR; S48020; S48020.
DR RefSeq; NP_001330580.1; NM_001345094.1.
DR RefSeq; NP_568811.1; NM_124848.3.
DR AlphaFoldDB; P46875; -.
DR SMR; P46875; -.
DR BioGRID; 20800; 2.
DR STRING; 3702.AT5G54670.1; -.
DR iPTMnet; P46875; -.
DR PaxDb; P46875; -.
DR PRIDE; P46875; -.
DR ProteomicsDB; 238210; -.
DR EnsemblPlants; AT5G54670.1; AT5G54670.1; AT5G54670.
DR EnsemblPlants; AT5G54670.2; AT5G54670.2; AT5G54670.
DR GeneID; 835556; -.
DR Gramene; AT5G54670.1; AT5G54670.1; AT5G54670.
DR Gramene; AT5G54670.2; AT5G54670.2; AT5G54670.
DR KEGG; ath:AT5G54670; -.
DR Araport; AT5G54670; -.
DR TAIR; locus:2157533; AT5G54670.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_001485_12_2_1; -.
DR InParanoid; P46875; -.
DR OMA; MNQGQRF; -.
DR OrthoDB; 364605at2759; -.
DR PhylomeDB; P46875; -.
DR PRO; PR:P46875; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P46875; baseline and differential.
DR Genevisible; P46875; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; IDA:TAIR.
DR GO; GO:0008017; F:microtubule binding; IDA:TAIR.
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:0051225; P:spindle assembly; 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; Cytoplasm; Cytoskeleton; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..754
FT /note="Kinesin-like protein KIN-14N"
FT /id="PRO_0000125382"
FT DOMAIN 396..733
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..45
FT /note="Globular"
FT REGION 13..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..86
FT /note="Microtubule-binding"
FT /evidence="ECO:0000269|PubMed:17244481"
FT REGION 207..754
FT /note="Microtubule-binding"
FT /evidence="ECO:0000269|PubMed:8075402"
FT COILED 85..209
FT /evidence="ECO:0000255"
FT COILED 262..394
FT /evidence="ECO:0000255"
FT BINDING 481..488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 754 AA; 85030 MW; 76091CD5B5D9C531 CRC64;
MVGAMANNGR IRSAFPVTNG SKDLTPNSAP ASTTGSEYGP VEFTREDVET LLNERIKYKS
KFNYKERCEN MMDYIKRLRL CIRWFQELEL DYAFEQEKLK NALELNEKHC VDMEVSLKNK
EEELNMIIEE LRKNFESVQV QLAREQTEKL AANDSLGKEK EARLSVEKAQ AGLTEELGKA
QGDLQTANQR IQSVNDMYKL LQEYNSSLQL YNSKLQGDLD EAHETIKRGE KERTAIIENI
GNLKGQFSAL QEQLAASKAS QEDIMKQKGE LVNEIASLKV ELQQVKDDRD RHLVEVKTLQ
TEATKYNDFK DAITELETTC SSQSTQIRQL QDRLVNSERR LQVSDLSTFE KMNEYEDQKQ
SIIDLKSRVE EAELKLVEGE KLRKKLHNTI LELKGNIRVF CRVRPLLPGE NNGDEGKTIS
YPTSLEALGR GIDLMQNAQK HAFTFDKVFA PTASQEDVFT EISQLVQSAL DGYKVCIFAY
GQTGSGKTYT MMGRPGNVEE KGLIPRCLEQ IFETRQSLRS QGWKYELQVS MLEIYNETIR
DLLSTNKEAV RTDSGVSPQK HAIKHDASGN THVAELTILD VKSSREVSFL LDHAARNRSV
GKTQMNEQSS RSHFVFTLRI SGVNESTEQQ VQGVLNLIDL AGSERLSKSG STGDRLKETQ
AINKSLSSLG DVIFALAKKE DHVPFRNSKL TYLLQPCLGG DAKTLMFVNI APESSSTGES
LCSLRFAARV NACEIGTPRR QTNIKPLENR LSLG
