KN14G_ARATH
ID KN14G_ARATH Reviewed; 987 AA.
AC O81635; O04641;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Kinesin-like protein KIN-14G {ECO:0000305};
DE AltName: Full=Kinesin-like protein KatD {ECO:0000303|PubMed:10196470, ECO:0000303|PubMed:8492804};
GN Name=KIN14G {ECO:0000305};
GN Synonyms=ATK4 {ECO:0000305}, KATD {ECO:0000303|PubMed:8492804,
GN ECO:0000312|EMBL:AAC32191.1};
GN OrderedLocusNames=At5g27000 {ECO:0000312|Araport:AT5G27000};
GN ORFNames=F2P16.12 {ECO:0000312|EMBL:AAB61066.1};
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], CHARACTERIZATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Flower;
RX PubMed=10196470; DOI=10.1016/s0378-1119(99)00070-0;
RA Tamura K., Nakatani K., Mitsui H., Ohashi Y., Takahashi H.;
RT "Characterization of katD, a kinesin-like protein gene specifically
RT expressed in floral tissues of Arabidopsis thaliana.";
RL Gene 230:23-32(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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 [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 -!- FUNCTION: Microtubule-binding motor protein.
CC -!- SUBUNIT: Monomer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Flower specific. {ECO:0000269|PubMed:10196470}.
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=AAB61066.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC32191.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF080249; AAC32191.1; ALT_FRAME; mRNA.
DR EMBL; AF007270; AAB61066.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED93639.1; -; Genomic_DNA.
DR PIR; T01775; T01775.
DR PIR; T51360; T51360.
DR RefSeq; NP_568491.1; NM_122582.2.
DR AlphaFoldDB; O81635; -.
DR SMR; O81635; -.
DR BioGRID; 18033; 1.
DR IntAct; O81635; 1.
DR STRING; 3702.AT5G27000.1; -.
DR iPTMnet; O81635; -.
DR PaxDb; O81635; -.
DR PRIDE; O81635; -.
DR ProteomicsDB; 237138; -.
DR EnsemblPlants; AT5G27000.1; AT5G27000.1; AT5G27000.
DR GeneID; 832758; -.
DR Gramene; AT5G27000.1; AT5G27000.1; AT5G27000.
DR KEGG; ath:AT5G27000; -.
DR Araport; AT5G27000; -.
DR TAIR; locus:2148543; AT5G27000.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_001485_8_0_1; -.
DR InParanoid; O81635; -.
DR OMA; NQRKDTT; -.
DR OrthoDB; 364605at2759; -.
DR PhylomeDB; O81635; -.
DR PRO; PR:O81635; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; O81635; baseline and differential.
DR Genevisible; O81635; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; 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; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
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; PF00307; CH; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00033; CH; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50021; CH; 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..987
FT /note="Kinesin-like protein KIN-14G"
FT /id="PRO_0000125383"
FT DOMAIN 44..163
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 394..721
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 201..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 725..754
FT /evidence="ECO:0000255"
FT COMPBIAS 784..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 478..485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 987 AA; 110009 MW; 8DF360197C78B145 CRC64;
MATTSEINND LSFSVVSIVE DVLQQHSSRS SDVGLVSRKV EESSLRRYEA AGWLRDMIGV
SNGKDFPGEP SEEEFRLGLR SGIVLCNVLN KVNPGSVSKV VEAPDDVADG AALSAFQYFE
NIRNFLVAIE EMGLPSFEAS DMEKGGKSIR IVNCILALKS YSEWKLKGEN GPWRYGSNMK
HNFGSRKLFL RKSSEPFVSS ISRTQSTDML STDQPLSSDG DSRSINGLVR SFIADRKHED
IPNVVESVLN KVMEEVQQRL SIHNEMMKSS SKPIPEDDSS CETVVRSQLC DARQHEEAEE
NSPPQVVEKK FQRTNFEHHE EQKILLNQQK HIQELKQTLY TTKAGMKLLQ MKYQEDFFHL
GKHLNGLAYA ATGYKRVLEE NRKLYNLVQD LKGNIRVYCR VRPFLPGQES GGLSAVEDID
EGTITIRVPS KYGKAGQKPF MFNKVFGPSA TQEEVFSDMQ PLVRSVLDGY NVCIFAYGQT
GSGKTFTMTG PKELTEESLG VNYRALADLF LLSNQRKDTT SYEISVQMLE IYNEQVRDLL
AQDGQTKRLE IRNNSHNGIN VPEASLVPVS STDDVIQLMD LGHMNRAVSS TAMNDRSSRS
HSCVTVHVQG RDLTSGSILH GSMHLVDLAG SERVDKSEVT GDRLKEAQHI NKSLSALGDV
ISSLSQKTSH VPYRNSKLTQ LLQDSLGGSA KTLMFVHISP EPDTLGETIS TLKFAERVGS
VELGAARVNK DNSEVKELKE QIANLKMALV RKGNGNDVQP TAIPINRERI SRRRSLETPT
IRPKLPTMGN TSNNSRPQIM DLSGPEAFND STASSRRHSL DIHELMKSSS PAWPRQPLNG
KDEDRESKSG EWIDKHEELI QNQNPNSPEQ FYQSMVPQQQ SLYGGKQDFE VQSITDNESD
EAATSDCSDS DLLWRLSVQV NVPKVSNIQN SANPKPKKIQ PRTAKLSETR SLIPSLIPAP
SKRPPNTVNS QPQRPTRDGK RRLSLGT
