KN1_ARATH
ID KN1_ARATH Reviewed; 465 AA.
AC Q8GW44; F4J114; Q8LEG9; Q9LY67;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Kinesin-like protein KIN-1 {ECO:0000305};
DE AltName: Full=AtKIN-1 {ECO:0000303|PubMed:24667993};
DE AltName: Full=AtPSS1 {ECO:0000303|PubMed:25330379};
DE AltName: Full=Pollen semi-sterility protein 1 {ECO:0000305};
GN Name=KIN1 {ECO:0000303|PubMed:24667993};
GN Synonyms=PSS1 {ECO:0000303|PubMed:25330379};
GN OrderedLocusNames=At3g63480 {ECO:0000312|Araport:AT3G63480};
GN ORFNames=MAA21_110 {ECO:0000312|EMBL:CAB87801.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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] (ISOFORM 2).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [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, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=24667993; DOI=10.1007/s00299-014-1594-7;
RA Wang H., Liu R., Wang J., Wang P., Shen Y., Liu G.;
RT "The Arabidopsis kinesin gene AtKin-1 plays a role in the nuclear division
RT process during megagametogenesis.";
RL Plant Cell Rep. 33:819-828(2014).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, AND INTERACTION WITH WIP1 AND
RP WIP2.
RX PubMed=25330379; DOI=10.1371/journal.pgen.1004674;
RA Duroc Y., Lemhemdi A., Larcheveque C., Hurel A., Cuacos M., Cromer L.,
RA Horlow C., Armstrong S.J., Chelysheva L., Mercier R.;
RT "The kinesin AtPSS1 promotes synapsis and is required for proper crossover
RT distribution in meiosis.";
RL PLoS Genet. 10:E1004674-E1004674(2014).
CC -!- FUNCTION: Kinesin-like motor protein that promotes synapsis and is
CC required for proper crossover distribution in meiosis
CC (PubMed:25330379). Plays a role in the nuclear division cycles during
CC megagametogenesis (PubMed:24667993). {ECO:0000269|PubMed:24667993,
CC ECO:0000269|PubMed:25330379}.
CC -!- SUBUNIT: Homodimer. Interacts with WIP1 and WIP2.
CC {ECO:0000269|PubMed:25330379}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8GW44-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8GW44-2; Sequence=VSP_058305;
CC -!- TISSUE SPECIFICITY: Specifically expressed in ovules and anthers.
CC {ECO:0000269|PubMed:24667993}.
CC -!- DISRUPTION PHENOTYPE: Partial seed abortion due to defects in
CC megagametogenesis (PubMed:24667993, PubMed:25330379). Defects in pollen
CC viability (PubMed:25330379). {ECO:0000269|PubMed:24667993,
CC ECO:0000269|PubMed:25330379}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-1 subfamily.
CC {ECO:0000303|PubMed:16448571}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB87801.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL163818; CAB87801.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE80490.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80491.1; -; Genomic_DNA.
DR EMBL; AK119094; BAC43667.1; -; mRNA.
DR EMBL; BT005391; AAO63455.1; -; mRNA.
DR EMBL; AY085419; AAM62646.1; -; mRNA.
DR PIR; T49189; T49189.
DR RefSeq; NP_567148.1; NM_116213.3. [Q8GW44-2]
DR RefSeq; NP_850742.1; NM_180411.3. [Q8GW44-1]
DR AlphaFoldDB; Q8GW44; -.
DR SMR; Q8GW44; -.
DR IntAct; Q8GW44; 2.
DR STRING; 3702.AT3G63480.1; -.
DR PaxDb; Q8GW44; -.
DR PRIDE; Q8GW44; -.
DR ProteomicsDB; 237060; -. [Q8GW44-1]
DR EnsemblPlants; AT3G63480.1; AT3G63480.1; AT3G63480. [Q8GW44-2]
DR EnsemblPlants; AT3G63480.2; AT3G63480.2; AT3G63480. [Q8GW44-1]
DR GeneID; 825523; -.
DR Gramene; AT3G63480.1; AT3G63480.1; AT3G63480. [Q8GW44-2]
DR Gramene; AT3G63480.2; AT3G63480.2; AT3G63480. [Q8GW44-1]
DR KEGG; ath:AT3G63480; -.
DR Araport; AT3G63480; -.
DR TAIR; locus:2087378; AT3G63480.
DR eggNOG; KOG0240; Eukaryota.
DR OMA; GKPNHVP; -.
DR OrthoDB; 1334528at2759; -.
DR PhylomeDB; Q8GW44; -.
DR PRO; PR:Q8GW44; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8GW44; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:TAIR.
DR GO; GO:0009561; P:megagametogenesis; IMP:TAIR.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0009555; P:pollen development; IMP:UniProtKB.
DR GO; GO:0048316; P:seed development; IMP:UniProtKB.
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 Alternative splicing; ATP-binding; Coiled coil; Microtubule; Motor protein;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..465
FT /note="Kinesin-like protein KIN-1"
FT /id="PRO_0000436184"
FT DOMAIN 3..334
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 338..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 402..444
FT /evidence="ECO:0000255"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT VAR_SEQ 175
FT /note="E -> EASFI (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_058305"
FT CONFLICT 217..219
FT /note="IQQ -> VQE (in Ref. 5; AAM62646)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="S -> P (in Ref. 5; AAM62646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 51407 MW; 8252309294F1249A CRC64;
MSNVTVCARF RPRSSKEMRD PSRDGVCARP IDAETFVFQD DKEDEFTFSL DRVFYEDSTQ
AAVYEFLALP IMRDAVNGIN GTIITYGQTG AGKTYSMEGP GIQDCDEHNK GLLPRVVHGM
FEQISSSNDI ARYTVKLSMV EIYMEKVRDL LDLSKANIQI KENKTQGILL SGVTEVPVSD
SVEALQHLCT GLANRAVGET QMNMSSSRSH CAYLFTIQQD SVKDKRVKTG KLILVDLAGS
EKADKTGAEG RVLEEAKTIN KSLSALGNVI NALTSGPSSK GNHIPYRDSK LTRILQDALG
GNSRMALLCC CSPSTLNASE TLSTLRFGMR AKHIKASPRA SEVKSAKAQE EPSSVTKDEK
CGRILEKMKE RMSNEDIKML EDVFIQEGII FSLDSMAEVE TVYEDIVSKT IQSLQQAVDE
LQQKVKKLEA ENIGIQEQAL RNHEPGSVGK MSRFISSWYA SFFTS
