KN1_ORYSJ
ID KN1_ORYSJ Reviewed; 477 AA.
AC F9W301; A0A0P0XBE1; B9FYS2; Q0J8E3; Q69UI4;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Kinesin-like protein KIN-1 {ECO:0000305};
DE AltName: Full=Kinesin-1-like protein PSS1 {ECO:0000303|PubMed:21282525, ECO:0000312|EMBL:DAA34941.1};
DE AltName: Full=Pollen semi-sterility protein 1 {ECO:0000303|PubMed:21282525};
GN Name=KIN1 {ECO:0000305}; Synonyms=PSS1 {ECO:0000312|EMBL:DAA34941.1};
GN OrderedLocusNames=Os08g0117000, LOC_Os08g02380;
GN ORFNames=OsJ_25827, P0470F10.15;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare {ECO:0000312|EMBL:EEE67939.1};
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RG The rice full-length cDNA consortium;
RT "Oryza sativa full length cDNA.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19106179; DOI=10.1093/aob/mcn248;
RA Guo L., Ho C.M., Kong Z., Lee Y.R., Qian Q., Liu B.;
RT "Evaluating the microtubule cytoskeleton and its interacting proteins in
RT monocots by mining the rice genome.";
RL Ann. Bot. 103:387-402(2009).
RN [7]
RP IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND MUTAGENESIS OF ARG-289.
RC TISSUE=Panicle {ECO:0000312|EMBL:DAA34941.1};
RX PubMed=21282525; DOI=10.1105/tpc.109.073692;
RA Zhou S., Wang Y., Li W., Zhao Z., Ren Y., Wang Y., Gu S., Lin Q., Wang D.,
RA Jiang L., Su N., Zhang X., Liu L., Cheng Z., Lei C., Wang J., Guo X.,
RA Wu F., Ikehashi H., Wang H., Wan J.;
RT "Pollen semi-sterility1 encodes a kinesin-1-like protein important for male
RT meiosis, anther dehiscence, and fertility in rice.";
RL Plant Cell 23:111-129(2011).
CC -!- FUNCTION: Kinesin-like motor protein that exhibits microtubule-
CC stimulated ATPase activity. Plays an essential role in male meiotic
CC chromosomal dynamics, male gametogenesis and anther dehiscence. May
CC play a minor and nonessential role in regulating meiotic spindle
CC formation. {ECO:0000269|PubMed:21282525}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21282525}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:21282525};
CC IsoId=F9W301-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15685292};
CC IsoId=F9W301-2; Sequence=VSP_043950, VSP_043951;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in young roots and
CC leaves, in mature roots, culm, sheath and leaves, and in panicles at
CC various developmental stages. Strongest expression is detected in
CC panicles. In the panicle, expression is detected in anthers, glumme,
CC lemma and palea. In the spikelet, expression is detected in both
CC microsporocyte and the anther walls. {ECO:0000269|PubMed:21282525}.
CC -!- DEVELOPMENTAL STAGE: Expressed during plant development. During young
CC panicle development, highest expression is observed at P4-P5 stages
CC followed by a gradual decline until becomes nearly undetectable at 8
CC days after heading. Expression is significantly up-regulated during
CC anther development and peaks during male meiosis. Expression disappears
CC in postmeiosis anther. {ECO:0000269|PubMed:21282525}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-1 subfamily.
CC {ECO:0000303|PubMed:19106179}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD33096.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF22772.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP004562; BAD33096.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008214; BAF22772.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014964; BAT03561.1; -; Genomic_DNA.
DR EMBL; CM000145; EEE67939.1; -; Genomic_DNA.
DR EMBL; AK287457; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BK007977; DAA34941.1; -; Genomic_DNA.
DR RefSeq; XP_015649862.1; XM_015794376.1. [F9W301-1]
DR RefSeq; XP_015649863.1; XM_015794377.1. [F9W301-1]
DR RefSeq; XP_015649864.1; XM_015794378.1. [F9W301-1]
DR AlphaFoldDB; F9W301; -.
DR SMR; F9W301; -.
DR STRING; 4530.OS08T0117000-01; -.
DR PaxDb; F9W301; -.
DR PRIDE; F9W301; -.
DR EnsemblPlants; Os08t0117000-01; Os08t0117000-01; Os08g0117000. [F9W301-1]
DR GeneID; 4344521; -.
DR Gramene; Os08t0117000-01; Os08t0117000-01; Os08g0117000. [F9W301-1]
DR KEGG; osa:4344521; -.
DR eggNOG; KOG0240; Eukaryota.
DR HOGENOM; CLU_001485_2_13_1; -.
DR InParanoid; F9W301; -.
DR OMA; GKPNHVP; -.
DR OrthoDB; 1334528at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000007752; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR Genevisible; F9W301; OS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; 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 Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Microtubule;
KW Motor protein; Nucleotide-binding; Reference proteome.
FT CHAIN 1..477
FT /note="Kinesin-like protein KIN-1"
FT /id="PRO_0000417974"
FT DOMAIN 3..330
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT COILED 402..451
FT /evidence="ECO:0000255"
FT BINDING 86..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P33176,
FT ECO:0000255|PROSITE-ProRule:PRU00283"
FT VAR_SEQ 200..216
FT /note="QMNLASSRSHCLYIFSV -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15685292"
FT /id="VSP_043950"
FT VAR_SEQ 296..325
FT /note="GGNSRAALLCCCSPSASNAPESLSTVRFGT -> HLS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15685292"
FT /id="VSP_043951"
FT MUTAGEN 289
FT /note="R->H: Diminished microtubule-stimulated ATPase
FT activity, abnormal chromosome congression and segregation
FT and reduced spikelet fertility caused jointly by reduced
FT pollen viability and defective anther dehiscence."
FT /evidence="ECO:0000269|PubMed:21282525"
SQ SEQUENCE 477 AA; 52130 MW; 3B8BC519C2D54449 CRC64;
MSNVTVCVRF RPLSHKERKT NGDKVCFKRL DSESFVFKDE REEDVIFSFD RVFYEDAEQS
DVYNFLAVPI VADAISGING TIITYGQTGA GKTYSMEGPS ILHCNKQKTG LVQRVVDELF
QSLQSSESMA MWSVKLSMVE IYLEKVRDLL DLSKDNLQIK ESKTQGIYIS GATEVSIQNS
SDALECLSEG IANRAVGETQ MNLASSRSHC LYIFSVQQGS TSDERVRGGK IILVDLAGSE
KVEKTGAEGR VLDEAKTINK SLSVLGNVVN ALTTGKPNHV PYRDSKLTRI LQDALGGNSR
AALLCCCSPS ASNAPESLST VRFGTRTKLI KTTPKSISPE VDSIKKPIPD SHGQNDLRDR
ILNKLRLSLK EEDVDLLEEL FVQEGIIFDP NYSVADIDSA CQDAASQEVS LLTQAVEELK
ETVEELTDEN ERLRGELELA QEAAAAAAAA RADGALLGFV PAVAISSLLR PFGFVPD
