RBPP_ORYSJ
ID RBPP_ORYSJ Reviewed; 490 AA.
AC Q9LJ04; A2ZRK1; Q0JNU2;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=RNA-binding protein P {ECO:0000303|PubMed:20217123};
GN Name=RBP-P {ECO:0000303|PubMed:20217123};
GN OrderedLocusNames=Os01g0265800 {ECO:0000312|EMBL:BAS71462.1},
GN LOC_Os01g16090 {ECO:0000305};
GN ORFNames=OsJ_01215 {ECO:0000312|EMBL:EAZ11348.1},
GN P0499C11.21 {ECO:0000312|EMBL:BAA90354.1};
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=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 [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=20217123; DOI=10.1007/s00425-010-1125-x;
RA Crofts A.J., Crofts N., Whitelegge J.P., Okita T.W.;
RT "Isolation and identification of cytoskeleton-associated prolamine mRNA
RT binding proteins from developing rice seeds.";
RL Planta 231:1261-1276(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=24682961; DOI=10.1007/s11103-014-0191-z;
RA Doroshenk K.A., Tian L., Crofts A.J., Kumamaru T., Okita T.W.;
RT "Characterization of RNA binding protein RBP-P reveals a possible role in
RT rice glutelin gene expression and RNA localization.";
RL Plant Mol. Biol. 85:381-394(2014).
RN [9]
RP FUNCTION, INTERACTION WITH RBP-L AND RBP-208, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ALA-252; GLY-373 AND GLY-401.
RX PubMed=30190374; DOI=10.1105/tpc.18.00321;
RA Tian L., Chou H.L., Zhang L., Hwang S.K., Starkenburg S.R., Doroshenk K.A.,
RA Kumamaru T., Okita T.W.;
RT "RNA-binding protein RBP-P is required for glutelin and prolamine mRNA
RT localization in rice endosperm cells.";
RL Plant Cell 30:2529-2552(2018).
RN [10]
RP FUNCTION, AND INTERACTION WITH NSF.
RX PubMed=32471860; DOI=10.1105/tpc.20.00111;
RA Tian L., Doroshenk K.A., Zhang L., Fukuda M., Washida H., Kumamaru T.,
RA Okita T.;
RT "Zipcode RNA-binding proteins and membrane trafficking proteins cooperate
RT to transport glutelin mRNAs in rice endosperm.";
RL Plant Cell 32:2566-2581(2020).
CC -!- FUNCTION: RNA-binding protein that binds to a cis-localization element
CC or zipcode, within the 5'-CDS of prolamine RNA (PubMed:20217123,
CC PubMed:24682961). Binds strongly to glutelin mRNA, particularly to 3'-
CC UTR and zipcode RNA (PubMed:24682961). Recognizes and binds to glutelin
CC zipcode RNA, which is required for proper mRNA localization to
CC cisternal endoplasmic reticulum (PubMed:24682961). Exhibits strong
CC binding activity to a glutelin intron sequence and may participate in
CC mRNA splicing (PubMed:24682961). Required for the correct localization
CC of glutelin and prolamine mRNA in endosperm cells during grain
CC development (PubMed:30190374). RBP-P and RBP-L form a quaternary
CC complex with the membrane trafficking factors NSF and RAB5A
CC (PubMed:32471860). This quaternay complex carries glutelin mRNAs for
CC active transport on endosomes to the cortical endoplasmic reticulum
CC membrane, and enables endosome-mediated glutelin mRNA transport in
CC endosperm cells (PubMed:32471860). {ECO:0000269|PubMed:20217123,
CC ECO:0000269|PubMed:24682961, ECO:0000269|PubMed:30190374,
CC ECO:0000269|PubMed:32471860}.
CC -!- SUBUNIT: Forms homodimers (PubMed:30190374). Interacts with RBP-L and
CC RBP-208 (PubMed:30190374). Interacts with NSF (PubMed:32471860).
CC {ECO:0000269|PubMed:30190374, ECO:0000269|PubMed:32471860}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24682961,
CC ECO:0000269|PubMed:30190374}. Cytoplasm {ECO:0000269|PubMed:24682961,
CC ECO:0000269|PubMed:30190374}.
CC -!- DEVELOPMENTAL STAGE: During flowering and seed development, expressed
CC very weakly at 3 days after flowering (DAF) (at protein level)
CC (PubMed:24682961). Expression increases until 9 DAF and remains
CC relatively steady until a sharp decline 23 DAF (at protein level)
CC (PubMed:24682961). {ECO:0000269|PubMed:24682961}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF04586.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP001080; BAA90354.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF04586.2; ALT_INIT; Genomic_DNA.
DR EMBL; AP014957; BAS71462.1; -; Genomic_DNA.
DR EMBL; CM000138; EAZ11348.1; -; Genomic_DNA.
DR EMBL; AK099896; BAG94341.1; -; mRNA.
DR EMBL; AK109487; BAG98769.1; -; mRNA.
DR RefSeq; XP_015621304.1; XM_015765818.1.
DR AlphaFoldDB; Q9LJ04; -.
DR SMR; Q9LJ04; -.
DR STRING; 4530.OS01T0265800-01; -.
DR PaxDb; Q9LJ04; -.
DR PRIDE; Q9LJ04; -.
DR EnsemblPlants; Os01t0265800-01; Os01t0265800-01; Os01g0265800.
DR EnsemblPlants; Os01t0265800-02; Os01t0265800-02; Os01g0265800.
DR GeneID; 4326212; -.
DR Gramene; Os01t0265800-01; Os01t0265800-01; Os01g0265800.
DR Gramene; Os01t0265800-02; Os01t0265800-02; Os01g0265800.
DR KEGG; osa:4326212; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_012062_1_6_1; -.
DR InParanoid; Q9LJ04; -.
DR OMA; EDPNTMA; -.
DR OrthoDB; 1202220at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IDA:UniProtKB.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..490
FT /note="RNA-binding protein P"
FT /id="PRO_0000451591"
FT DOMAIN 156..233
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 267..343
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..110
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 252
FT /note="A->T: In P3MH; reduces RNA binding activity."
FT /evidence="ECO:0000269|PubMed:30190374"
FT MUTAGEN 373
FT /note="G->E: In P2MH; growth defects, aberrant flower
FT development leading to infertile panicles."
FT /evidence="ECO:0000269|PubMed:30190374"
FT MUTAGEN 401
FT /note="G->S: In P1MH; reduces RNA binding activity."
FT /evidence="ECO:0000269|PubMed:30190374"
SQ SEQUENCE 490 AA; 49280 MW; E3498FB1C189B9A9 CRC64;
MGKKRKLDSK SPAAARSAAA RAAAAAAAAA AAAAVAEPSS QPEALAEDPA PSSQPLGLSS
EGAGERMMSR EAGGGEEEEV EEVEVEEEVE VDEDEDGEGE GEEEEEAAER DADSIQALLN
SFPKDQLVEL LSAAALSHED VLTAVHRAAD ADPALRKIFV HGLGWDATAE TLTEAFSAYG
EIEDLRVVTD RATGKCKGYG FILFSRRSGA RAALREPQKK IGNRTTACQL ASVGPVPPGG
MATNPAPAVA PAPAQLALPP VSEYTQRKIF VSNVGADIDP QKLLQFFSKY GEIEEGPLGL
DKVTGKPKGF ALFVYKTLDS AKKALQEPHK QFEGVVLHCQ KAIDGPKPNK GGGLGGLYGA
GTSGGRKGAG GYGAHSHSLP GAAVGGHVMP SPVSSLTSLP GVAGGPGVNP ALGQALTAIL
ASQGGGLGLN NILGVGANGS GLPNPGASAG LGSSGLPGMP GAGGYLGGYG GGGGYGSTPP
GGPGRNYMGH
