RBM25_ARATH
ID RBM25_ARATH Reviewed; 899 AA.
AC Q8VY15; B9DFB3; O80743; O80744;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=RNA-binding motif protein 25 {ECO:0000303|PubMed:28971960};
GN Name=RBM25 {ECO:0000303|PubMed:28971960};
GN OrderedLocusNames=At1g60200 {ECO:0000312|Araport:AT1G60200};
GN ORFNames=T13D8.10 {ECO:0000312|EMBL:AAC24053.1},
GN T13D8.9 {ECO:0000312|EMBL:AAC24054.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-507.
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION BY ABSCISIC
RP ACID, AND PHOSPHORYLATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=26404089; DOI=10.1038/ncomms9139;
RA Zhan X., Qian B., Cao F., Wu W., Yang L., Guan Q., Gu X., Wang P.,
RA Okusolubo T.A., Dunn S.L., Zhu J.-K., Zhu J.;
RT "An Arabidopsis PWI and RRM motif-containing protein is critical for pre-
RT mRNA splicing and ABA responses.";
RL Nat. Commun. 6:8139-8139(2015).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=28971960; DOI=10.1534/genetics.117.300149;
RA Kanno T., Lin W.-D., Fu J.L., Chang C.-L., Matzke A.J.M., Matzke M.;
RT "A genetic screen for pre-mRNA splicing mutants of Arabidopsis thaliana
RT identifies putative U1 snRNP components RBM25 and PRP39a.";
RL Genetics 207:1347-1359(2017).
CC -!- FUNCTION: RNA-binding protein that acts as a regulator of alternative
CC pre-mRNA splicing (PubMed:26404089, PubMed:28971960). Negative
CC regulator of responses to abscisic acid (ABA), including in early
CC development (PubMed:26404089). {ECO:0000269|PubMed:26404089,
CC ECO:0000269|PubMed:28971960}.
CC -!- SUBUNIT: Specifically associates with functional splicing complexes (By
CC similarity). Associates with exon junction complex (EJC) proteins (By
CC similarity). {ECO:0000250|UniProtKB:P49756}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00627,
CC ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:26404089}.
CC -!- INDUCTION: Induced by abscisic acid both at transcriptional and at
CC post-translational (pre-mRNA splicing) levels.
CC {ECO:0000269|PubMed:26404089}.
CC -!- DOMAIN: The PWI domain binds nucleic acids with significant help from
CC its N-terminal flanking basic region. It has an equal preference for
CC binding to single- or double-stranded species, and it contributes to
CC RBM25 role in modulation of alternative splicing.
CC {ECO:0000250|UniProtKB:P49756}.
CC -!- PTM: Phosphorylated; the phosphorylation level is repressed by abscisic
CC acid (ABA). {ECO:0000269|PubMed:26404089}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to growth inhibition by
CC abscisic acid (ABA) (PubMed:26404089). Altered transcript accumulation
CC profiles due to impaired pre-messenger RNA (pre-mRNA) splicing (e.g.
CC HAB1 transcripts alternative splicing) (PubMed:26404089,
CC PubMed:28971960). These phenotypes are partially suppressed by an
CC ectopic expression of HAB1 (PubMed:26404089).
CC {ECO:0000269|PubMed:26404089, ECO:0000269|PubMed:28971960}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24053.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC24054.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004473; AAC24053.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC004473; AAC24054.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33666.1; -; Genomic_DNA.
DR EMBL; AY074284; AAL66981.1; -; mRNA.
DR EMBL; BT001972; AAN71971.1; -; mRNA.
DR EMBL; AK316703; BAH19430.1; -; mRNA.
DR PIR; T02272; T02272.
DR PIR; T02273; T02273.
DR RefSeq; NP_176226.3; NM_104710.5.
DR AlphaFoldDB; Q8VY15; -.
DR SMR; Q8VY15; -.
DR STRING; 3702.AT1G60200.1; -.
DR PaxDb; Q8VY15; -.
DR PRIDE; Q8VY15; -.
DR ProteomicsDB; 174718; -.
DR EnsemblPlants; AT1G60200.1; AT1G60200.1; AT1G60200.
DR GeneID; 842315; -.
DR Gramene; AT1G60200.1; AT1G60200.1; AT1G60200.
DR Araport; AT1G60200; -.
DR TAIR; locus:2195568; AT1G60200.
DR eggNOG; KOG2253; Eukaryota.
DR HOGENOM; CLU_007747_0_0_1; -.
DR InParanoid; Q8VY15; -.
DR OrthoDB; 677630at2759; -.
DR PhylomeDB; Q8VY15; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8VY15; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IDA:UniProtKB.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12446; RRM_RBM25; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR002483; PWI_dom.
DR InterPro; IPR036483; PWI_dom_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034268; RBM25_RRM.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF01480; PWI; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00311; PWI; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF101233; SSF101233; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51025; PWI; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Abscisic acid signaling pathway; Coiled coil; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT CHAIN 1..899
FT /note="RNA-binding motif protein 25"
FT /id="PRO_0000454943"
FT DOMAIN 204..281
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 802..899
FT /note="PWI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00627"
FT REGION 1..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 434..578
FT /evidence="ECO:0000255"
FT MOTIF 526..533
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 735..742
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..83
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 899 AA; 101497 MW; 2C9035D065C0E89B CRC64;
MADESSSPAT GDPNSQKPES TTPISIPNPN PNPSLTPPPP QQHSQPPVAP LVPPGPPYAP
PAQIPSSLLP TNLPPPPPFR PGMQFTPVAN FQNPSSGVPP PGSMPQYQPQ PGMRPFQPMA
NGYPGIHGVA PPGAMPPHGL LRYPSPYPTM VRPGFIMRPP GTIGAVQLAP RPLIPGMPGL
RPVMPPMVRP ASLPFVTPAE KPQTTIYIGK IATVENDFMM SILEFCGHVK SCLRAEDPTT
KKPKGFGFYE FESAEGILRA IRLLTQRTID GQELLVNVNQ ATKEYLLKYV EKKIETAKKA
KESQGTKENQ AEGPESEQDK LESADNETGK DGESKIKENI DIANSAVLTD EEREADREAM
EKIETAIEER LKSNPLPPPP PPPADGSGME FAFKSKDGDS NTDVARSDAA ANDVETSGEH
NRPDTSSPDW SKRNDRRSRE RGEKEQEMDR YEREAERERS RKEREQRRKL EDAERAYQTR
LRQWERRERE KEKERQYEKE KEKEKERKRK KEIRYEEEEE EDDDDSRRRW HRAALDERRR
RQLREKEDDL ADRLKEEEEV AEAKRSAEEQ NLQQQQLDAL RILSGQAAIG SETVQTSPIE
NDHKATLQTV GESANEHHAA DFEENGSGNE SMAIDNNSGS EAHAPSKKLG FGLVGSGKRT
SVPSVFYEED EDEARKAKKM KPLVPIDYST EEQEAVAHGG SGNTPPHLAL AAEFAKRISS
TNPKEETIET EKQRSRRSHD KASHRDRERE RERDRDRDRV RDRGDGHSGP TKDAKESGKA
KIIDTKFLDA KQLIDTIPKT KEDLFSYEIN WAMYDKHQVH ERMRPWISKK IMEFLGEEEA
TLVDFIVSNT QQHVQASQML ELLQSILDEE AEMFVLKMWR MLIFEIKRVE AGVPVKSKA
