PRP31_ARATH
ID PRP31_ARATH Reviewed; 485 AA.
AC Q8RXN6; O80740;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=U4/U6 small nuclear ribonucleoprotein Prp31 homolog {ECO:0000305};
DE AltName: Full=Pre-mRNA-processing factor 31 homolog {ECO:0000305};
DE AltName: Full=Protein EMBRYO DEFECTIVE 1220 {ECO:0000305};
GN Name=PRP31 {ECO:0000303|PubMed:25684655}; Synonyms=EMB1220 {ECO:0000305};
GN OrderedLocusNames=At1g60170 {ECO:0000312|Araport:AT1G60170};
GN ORFNames=T13D8.6 {ECO:0000312|EMBL:AAC24050.1};
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].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH STA1 AND ZOP1, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=25684655; DOI=10.1016/j.molp.2015.02.003;
RA Du J.L., Zhang S.W., Huang H.W., Cai T., Li L., Chen S., He X.J.;
RT "The splicing factor PRP31 is involved in transcriptional gene silencing
RT and stress response in Arabidopsis.";
RL Mol. Plant 8:1053-1068(2015).
CC -!- FUNCTION: Involved in pre-mRNA splicing. Required for the assembly of
CC the U4/U5/U6 tri-snRNP complex, one of the building blocks of the
CC spliceosome (By similarity). Functions in association with STA1 and
CC ZOP1 in spliceosome dynamics and pre-mRNA splicing. Required for
CC transcriptional regulation and pre-mRNA splicing of cold-responsive
CC genes, such as LTI78/RD29A, KIN2/COR6.6 or COR15A, especially under
CC cold stress. May play a role in stress response. Involved in
CC transcriptional gene silencing of endogenous transposable elements,
CC independently of the RNA-directed DNA methylation (RdDM) pathway. Seems
CC not to participate in the small RNA biogenesis of the RdDM pathway
CC (PubMed:25684655). {ECO:0000250|UniProtKB:Q8WWY3,
CC ECO:0000269|PubMed:25684655}.
CC -!- SUBUNIT: Component of the U4/U6-U5 tri-snRNP complex composed of the
CC U4, U6 and U5 snRNAs and pre-mRNA-splicing factors (By similarity).
CC Interacts with STA1 and SOP1 (PubMed:25684655).
CC {ECO:0000250|UniProtKB:Q8WWY3, ECO:0000269|PubMed:25684655}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25684655}. Nucleus,
CC Cajal body {ECO:0000269|PubMed:25684655}.
CC -!- DISRUPTION PHENOTYPE: Developmental defects, semi-dwarf phenotype and
CC reduced growth. {ECO:0000269|PubMed:25684655}.
CC -!- SIMILARITY: Belongs to the PRP31 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24050.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004473; AAC24050.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33664.1; -; Genomic_DNA.
DR EMBL; AY080777; AAL87261.1; -; mRNA.
DR EMBL; AY117155; AAM51230.1; -; mRNA.
DR EMBL; AY084782; AAM61349.1; -; mRNA.
DR PIR; T02269; T02269.
DR RefSeq; NP_564754.1; NM_104707.4.
DR AlphaFoldDB; Q8RXN6; -.
DR SMR; Q8RXN6; -.
DR IntAct; Q8RXN6; 1.
DR MINT; Q8RXN6; -.
DR STRING; 3702.AT1G60170.1; -.
DR iPTMnet; Q8RXN6; -.
DR PaxDb; Q8RXN6; -.
DR PRIDE; Q8RXN6; -.
DR ProteomicsDB; 226508; -.
DR EnsemblPlants; AT1G60170.1; AT1G60170.1; AT1G60170.
DR GeneID; 842312; -.
DR Gramene; AT1G60170.1; AT1G60170.1; AT1G60170.
DR KEGG; ath:AT1G60170; -.
DR Araport; AT1G60170; -.
DR TAIR; locus:2195698; AT1G60170.
DR eggNOG; KOG2574; Eukaryota.
DR HOGENOM; CLU_026337_2_1_1; -.
DR InParanoid; Q8RXN6; -.
DR OMA; IIGNGPM; -.
DR OrthoDB; 791296at2759; -.
DR PhylomeDB; Q8RXN6; -.
DR PRO; PR:Q8RXN6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RXN6; baseline and differential.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0097526; C:spliceosomal tri-snRNP complex; IBA:GO_Central.
DR GO; GO:0005687; C:U4 snRNP; IBA:GO_Central.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0070417; P:cellular response to cold; IMP:TAIR.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin assembly; IMP:TAIR.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0008380; P:RNA splicing; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IEA:InterPro.
DR Gene3D; 1.10.246.90; -; 1.
DR InterPro; IPR042239; Nop_C.
DR InterPro; IPR002687; Nop_dom.
DR InterPro; IPR036070; Nop_dom_sf.
DR InterPro; IPR012976; NOSIC.
DR InterPro; IPR027105; Prp31.
DR InterPro; IPR019175; Prp31_C.
DR PANTHER; PTHR13904; PTHR13904; 1.
DR Pfam; PF01798; Nop; 1.
DR Pfam; PF09785; Prp31_C; 1.
DR SMART; SM00931; NOSIC; 1.
DR SUPFAM; SSF89124; SSF89124; 1.
DR PROSITE; PS51358; NOP; 1.
PE 1: Evidence at protein level;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Spliceosome; Stress response.
FT CHAIN 1..485
FT /note="U4/U6 small nuclear ribonucleoprotein Prp31 homolog"
FT /id="PRO_0000437258"
FT DOMAIN 216..334
FT /note="Nop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00690"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 352..365
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305"
FT COMPBIAS 10..36
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 52645 MW; 2B6924E67CE1443F CRC64;
MATLEDSFLA DLDELSDNEA ELDENDGDVG KEEEDVDMDM ADLETLNYDD LDNVSKLQKS
QRYADIMHKV EEALGKDSDG AEKGTVLEDD PEYKLIVDCN QLSVDIENEI VIVHNFIKDK
YKLKFQELES LVHHPIDYAC VVKKIGNETD LALVDLADLL PSAIIMVVSV TALTTKGSAL
PEDVLQKVLE ACDRALDLDS ARKKVLEFVE SKMGSIAPNL SAIVGSAVAA KLMGTAGGLS
ALAKMPACNV QVLGHKRKNL AGFSSATSQS RVGYLEQTEI YQSTPPGLQA RAGRLVAAKS
TLAARVDATR GDPLGISGKA FREEIRKKIE KWQEPPPARQ PKPLPVPDSE PKKRRGGRRL
RKMKERYQVT DMRKLANRMA FGTPEESSLG DGLGEGYGML GQAGSNRLRV SSVPSKLKIN
AKVAKKLKER QYAGGATTSG LTSSLAFTPV QGIELCNPQQ ALGLGSGTQS TYFSESGTFS
KLKKI
