PTBP2_ARATH
ID PTBP2_ARATH Reviewed; 429 AA.
AC Q9FGL9;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Polypyrimidine tract-binding protein homolog 2;
GN OrderedLocusNames=At5g53180; ORFNames=MFH8.12;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Plays a role in pre-mRNA splicing. Binds to the
CC polypyrimidine tract of introns. May promote the binding of U2 snRNP to
CC pre-mRNA (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FGL9-1; Sequence=Displayed;
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DR EMBL; AB025622; BAB08421.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96318.1; -; Genomic_DNA.
DR EMBL; BT015760; AAU90050.1; -; mRNA.
DR EMBL; BT020199; AAV59265.1; -; mRNA.
DR RefSeq; NP_200130.1; NM_124697.5. [Q9FGL9-1]
DR AlphaFoldDB; Q9FGL9; -.
DR SMR; Q9FGL9; -.
DR BioGRID; 20644; 1.
DR IntAct; Q9FGL9; 1.
DR STRING; 3702.AT5G53180.1; -.
DR iPTMnet; Q9FGL9; -.
DR PaxDb; Q9FGL9; -.
DR PRIDE; Q9FGL9; -.
DR ProteomicsDB; 248847; -. [Q9FGL9-1]
DR EnsemblPlants; AT5G53180.1; AT5G53180.1; AT5G53180. [Q9FGL9-1]
DR GeneID; 835399; -.
DR Gramene; AT5G53180.1; AT5G53180.1; AT5G53180. [Q9FGL9-1]
DR KEGG; ath:AT5G53180; -.
DR Araport; AT5G53180; -.
DR TAIR; locus:2163746; AT5G53180.
DR eggNOG; KOG1190; Eukaryota.
DR HOGENOM; CLU_033500_0_0_1; -.
DR InParanoid; Q9FGL9; -.
DR OMA; AMPFHGH; -.
DR OrthoDB; 1545178at2759; -.
DR PhylomeDB; Q9FGL9; -.
DR PRO; PR:Q9FGL9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGL9; baseline and differential.
DR Genevisible; Q9FGL9; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000932; C:P-body; IDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IDA:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:TAIR.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:TAIR.
DR GO; GO:0006417; P:regulation of translation; IEP:TAIR.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR CDD; cd12686; RRM1_PTBPH1_PTBPH2; 1.
DR CDD; cd12691; RRM2_PTBPH1_PTBPH2; 1.
DR CDD; cd12690; RRM3_PTBPH1_PTBPH2; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR021790; PTBP1-like_RRM2.
DR InterPro; IPR034792; PTBPH1/PTBPH2_RRM1.
DR InterPro; IPR034793; PTBPH1/PTBPH2_RRM2.
DR InterPro; IPR034794; PTBPH1/PTBPH2_RRM3.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF11835; RRM_8; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Repeat; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..429
FT /note="Polypyrimidine tract-binding protein homolog 2"
FT /id="PRO_0000081742"
FT DOMAIN 18..96
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 110..197
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 243..323
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 331..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 429 AA; 46884 MW; 210C72EC3ADD41B5 CRC64;
MSSVSSQPQF RYTQPPSKVL HLRNLPWECT EEELIELGKP FGTVVNTKCN VGANRNQAFI
EFEDLNQAIQ MISYYASSSE PAQVRGKTVY LQYSNRQEIV NNKTTADVVG NVLLVTIEGD
DARMVSIDVL HLVFSAFGFV HKITTFEKTA GYQALVQFTD AETATAAKLA LDGRSIPRYL
LAETVGQCSL KITYSAHTDL TVKFQSHRSR DYTNPYLPVA PSAIDSTGQV AVGVDGKKME
PESNVLLASI ENMQYAVTLD VLHMVFAAFG EVQKIAMFDK NGGVQALIQY SDVQTAVVAK
EALEGHCIYD GGFCKLHITY SRHTDLSIKV NNDRSRDYTM PNPPVPMPQQ PVQNPYAGNP
QQYHAAGGSH HQQQQQPQGG WVQPGGQGSM GMGGGGHNHY MAPPSSSSMH QGPGGHMPPQ
HYGGPGPMH
