FLP1_ORYSJ
ID FLP1_ORYSJ Reviewed; 109 AA.
AC Q9LGE3; A0A0P0V0S4;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Flowering-promoting factor 1-like protein 1;
DE AltName: Full=FPF1-like protein 1;
DE AltName: Full=Protein ROOT ARCHITECTURE ASSOCIATED 1;
DE Short=OsRAA1;
GN Name=RAA1; OrderedLocusNames=Os01g0257300, LOC_Os01g15340;
GN ORFNames=OsJ_01159, P0462H08.5;
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 [MRNA], TISSUE SPECIFICITY, INDUCTION, AND FUNCTION.
RC STRAIN=cv. Nipponbare;
RX PubMed=15247372; DOI=10.1104/pp.104.041996;
RA Ge L., Chen H., Jiang J.F., Zhao Y., Xu M.L., Xu Y.Y., Tan K.H., Xu Z.H.,
RA Chong K.;
RT "Overexpression of OsRAA1 causes pleiotropic phenotypes in transgenic rice
RT plants, including altered leaf, flower, and root development and root
RT response to gravity.";
RL Plant Physiol. 135:1502-1513(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP FUNCTION, GTP-BINDING, AND TISSUE SPECIFICITY.
RX PubMed=16173467; DOI=10.1016/j.jplph.2004.12.001;
RA Han Y., Wang X., Jiang J., Xu Y., Xu Z., Chong K.;
RT "Biochemical character of the purified OsRAA1, a novel rice protein with
RT GTP-binding activity, and its expression pattern in Oryza sativa.";
RL J. Plant Physiol. 162:1057-1063(2005).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
RP RPT4, PROTEIN DEGRADATION, AND MUTAGENESIS OF ARG-73 AND LEU-76.
RX PubMed=18701670; DOI=10.1104/pp.108.125294;
RA Han Y., Cao H., Jiang J., Xu Y., Du J., Wang X., Yuan M., Wang Z., Xu Z.,
RA Chong K.;
RT "Rice ROOT ARCHITECTURE ASSOCIATED1 binds the proteasome subunit RPT4 and
RT is degraded in a D-box and proteasome-dependent manner.";
RL Plant Physiol. 148:843-855(2008).
RN [10]
RP FUNCTION, AND PROTEIN DEGRADATION.
RX PubMed=20037474; DOI=10.4161/psb.5.3.10661;
RA Xu Y., Cao H., Chong K.;
RT "APC-targeted RAA1 degradation mediates the cell cycle and root development
RT in plants.";
RL Plant Signal. Behav. 5:218-223(2010).
CC -!- FUNCTION: GTP-binding protein that functions in the development of root
CC systems, which are mediated by auxin. Acts as a cell cycle regulator
CC during root development. Proteasome-mediated degradation of the protein
CC is necessary for the transition of metaphase to anaphase in mitosis.
CC {ECO:0000269|PubMed:15247372, ECO:0000269|PubMed:16173467,
CC ECO:0000269|PubMed:18701670, ECO:0000269|PubMed:20037474}.
CC -!- SUBUNIT: Interacts with RPT4. {ECO:0000269|PubMed:18701670}.
CC -!- INTERACTION:
CC Q9LGE3; Q9FXT8: OsRPT4; NbExp=6; IntAct=EBI-6050331, EBI-6050314;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18701670}. Nucleus
CC {ECO:0000269|PubMed:18701670}. Note=During mitosis, associates with
CC mitotic spindles.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the apical meristem, the
CC elongation zone of root tip, steles of the branch zone, and the young
CC lateral root. Also expressed in spikes. Expressed in roots and spikes
CC (at protein level). {ECO:0000269|PubMed:15247372,
CC ECO:0000269|PubMed:16173467}.
CC -!- INDUCTION: By auxin. {ECO:0000269|PubMed:15247372}.
CC -!- DOMAIN: D-box [RxxLxx(L/I)xN] is the common motif recognized by the E3
CC ubiquitin ligase APC specifically acting during transition from
CC metaphase to anaphase.
CC -!- PTM: Ubiquitinated. RPT4 mediates its proteasome-dependent degradation.
CC -!- DISRUPTION PHENOTYPE: RNAi mutants display reduced seedling height
CC phenotype, because of abnormal cell division.
CC {ECO:0000269|PubMed:18701670}.
CC -!- MISCELLANEOUS: Overexpression results in reduced growth of the primary
CC root, an increased number of adventitious roots, a helix primary root
CC and a delayed gravitropic response of roots in seedlings.
CC -!- SIMILARITY: Belongs to the FPF1 family. {ECO:0000305}.
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DR EMBL; AY659938; AAT94064.1; -; mRNA.
DR EMBL; AP002525; BAB07982.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF04545.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS71400.1; -; Genomic_DNA.
DR EMBL; CM000138; EAZ11300.1; -; Genomic_DNA.
DR EMBL; AK070626; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015631985.1; XM_015776499.1.
DR AlphaFoldDB; Q9LGE3; -.
DR SMR; Q9LGE3; -.
DR IntAct; Q9LGE3; 1.
DR STRING; 4530.OS01T0257300-01; -.
DR PaxDb; Q9LGE3; -.
DR PRIDE; Q9LGE3; -.
DR EnsemblPlants; Os01t0257300-01; Os01t0257300-01; Os01g0257300.
DR GeneID; 4326229; -.
DR Gramene; Os01t0257300-01; Os01t0257300-01; Os01g0257300.
DR KEGG; osa:4326229; -.
DR eggNOG; ENOG502S12G; Eukaryota.
DR HOGENOM; CLU_121629_0_1_1; -.
DR InParanoid; Q9LGE3; -.
DR OMA; KNLGWER; -.
DR OrthoDB; 1536466at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR Genevisible; Q9LGE3; OS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0045841; P:negative regulation of mitotic metaphase/anaphase transition; IDA:UniProtKB.
DR GO; GO:0009909; P:regulation of flower development; IEA:InterPro.
DR GO; GO:2000280; P:regulation of root development; IMP:UniProtKB.
DR GO; GO:0009733; P:response to auxin; IDA:UniProtKB.
DR InterPro; IPR039274; FPF1.
DR PANTHER; PTHR33433; PTHR33433; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..109
FT /note="Flowering-promoting factor 1-like protein 1"
FT /id="PRO_0000417316"
FT MOTIF 73..81
FT /note="D-box"
FT MUTAGEN 73
FT /note="R->G: Abolishes its proteasome-dependent
FT degradation."
FT /evidence="ECO:0000269|PubMed:18701670"
FT MUTAGEN 76
FT /note="L->V: Abolishes its proteasome-dependent
FT degradation."
FT /evidence="ECO:0000269|PubMed:18701670"
FT CONFLICT 39
FT /note="S -> C (in Ref. 7; AK070626)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 109 AA; 12034 MW; C0F5ED79788DBAFF CRC64;
MSGVWVFKNG VVRLVEKQQA TAGTAVAGGR RKALVHTPSG QVVSSYAALE ARLTALGWER
YYEDPSLFQF HKRGSLDLIS LPADFSAFSS VHMYDIVVKN RDSFRVVDA
