RBPL_ORYSJ
ID RBPL_ORYSJ Reviewed; 425 AA.
AC Q0J9Y2; A0A0N7KJR0; Q7XM93;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=RNA-binding protein L {ECO:0000303|PubMed:20217123};
GN Name=RBP-L {ECO:0000303|PubMed:20217123};
GN OrderedLocusNames=Os04g0625800 {ECO:0000312|EMBL:BAS91113.1},
GN LOC_Os04g53440 {ECO:0000305};
GN ORFNames=OSJNBb0060E08.6 {ECO:0000312|EMBL:CAE04743.3};
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=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(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 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 [6]
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 [7]
RP INTERACTION WITH RBP-P.
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 [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30659066; DOI=10.1104/pp.18.01434;
RA Tian L., Chou H.L., Zhang L., Okita T.W.;
RT "Targeted endoplasmic reticulum localization of storage protein mRNAs
RT requires the RNA-binding protein RBP-L.";
RL Plant Physiol. 179:1111-1131(2019).
RN [9]
RP FUNCTION, AND INTERACTION WITH RAB5A.
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). Binds
CC strongly to glutelin and prolamin mRNAs, particularly to 3'-UTR and
CC zipcode RNA (PubMed:30659066). Recognizes and binds to glutelin zipcode
CC RNA, which is required for proper mRNA localization to cisternal
CC endoplasmic reticulum (PubMed:30659066). Recognizes and binds to
CC prolamin zipcode RNA, which is required for proper mRNA localization to
CC the protein body endoplasmic reticulum that delimits the prolamine
CC intracisternal inclusion granules (PubMed:30659066). Required for the
CC correct localization of glutelin and prolamine mRNA in endosperm cells
CC during grain development (PubMed:30659066). RBP-L and RBP-P form a
CC quaternary 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:30659066, ECO:0000269|PubMed:32471860}.
CC -!- SUBUNIT: Interacts with RBP-P (PubMed:30190374). Interacts with RAB5A
CC (PubMed:32471860). {ECO:0000269|PubMed:30190374,
CC ECO:0000269|PubMed:32471860}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30659066}. Cytoplasm
CC {ECO:0000269|PubMed:30659066}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding RBP45 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE04743.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL606669; CAE04743.3; ALT_INIT; Genomic_DNA.
DR EMBL; AP008210; BAF15855.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS91113.1; -; Genomic_DNA.
DR EMBL; AK120834; BAH00195.1; -; mRNA.
DR RefSeq; XP_015636969.1; XM_015781483.1.
DR AlphaFoldDB; Q0J9Y2; -.
DR SMR; Q0J9Y2; -.
DR STRING; 4530.OS04T0625800-01; -.
DR PRIDE; Q0J9Y2; -.
DR EnsemblPlants; Os04t0625800-01; Os04t0625800-01; Os04g0625800.
DR GeneID; 4337064; -.
DR Gramene; Os04t0625800-01; Os04t0625800-01; Os04g0625800.
DR KEGG; osa:4337064; -.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_016304_2_1_1; -.
DR InParanoid; Q0J9Y2; -.
DR OMA; QYPANAS; -.
DR OrthoDB; 775799at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; -; 3.
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; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..425
FT /note="RNA-binding protein L"
FT /id="PRO_0000451590"
FT DOMAIN 90..170
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 180..259
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 284..356
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 46196 MW; AA93C45F71EACB9B CRC64;
MQQPPSQPQP GMGGPPPPPQ GAAGQPPQWG AIPPPMPPHQ YGAPPPQQPP AMWGQPPPQA
HYGQVPPPQP YYAAPPPQAM PAPAAADEVK TLWIGDLQPW MDESYIYNCF AATGEVQSVK
LIRDKQSGQL QGYGFVEFTS RAAADRILQT YNGQMMPNVE MVFRLNWASA GEKRDDTPDY
TIFVGDLAAD VTDYLLQETF RVHYPSVKGA KVVTDKMTMR SKGYGFVKFG DPTEQARAMT
EMNGMLCSSR PMRIGPAANK KTTGVQERVP NAQGAQSEND PNNTTIFVGG LDPNVTEDVL
KQVFAPYGEV VHVKIPVGKR CGFVQYVNRP SAEQALAVLQ GTLIGGQNVR LSWGRSLSNK
QPQHDSNQWG AGAGAGGYYG GYGQGYEAYG GYAQPQDPNM YGYGAYAGYP NYQQQQVAQQ
QPPQQ
