PTBP1_ARATH
ID PTBP1_ARATH Reviewed; 399 AA.
AC Q9MAC5; O82472;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Polypyrimidine tract-binding protein homolog 1;
GN Name=PTB; OrderedLocusNames=At3g01150; ORFNames=T4P13.16;
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Marin C., Boronat A.;
RT "Nucleotide sequence of an Arabidopsis cDNA encoding a protein with
RT similarity to mammalian polypyrimidine tract-binding protein (PTB).";
RL (er) Plant Gene Register PGR98-157(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [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=Q9MAC5-1; Sequence=Displayed;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC62015.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF076924; AAC62015.1; ALT_FRAME; mRNA.
DR EMBL; AC008261; AAF26159.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73616.1; -; Genomic_DNA.
DR PIR; T51814; T51814.
DR RefSeq; NP_186764.1; NM_110980.4. [Q9MAC5-1]
DR AlphaFoldDB; Q9MAC5; -.
DR SMR; Q9MAC5; -.
DR STRING; 3702.AT3G01150.1; -.
DR iPTMnet; Q9MAC5; -.
DR PaxDb; Q9MAC5; -.
DR PRIDE; Q9MAC5; -.
DR EnsemblPlants; AT3G01150.1; AT3G01150.1; AT3G01150. [Q9MAC5-1]
DR GeneID; 821129; -.
DR Gramene; AT3G01150.1; AT3G01150.1; AT3G01150. [Q9MAC5-1]
DR KEGG; ath:AT3G01150; -.
DR Araport; AT3G01150; -.
DR TAIR; locus:2102142; AT3G01150.
DR eggNOG; KOG1190; Eukaryota.
DR HOGENOM; CLU_033500_0_0_1; -.
DR InParanoid; Q9MAC5; -.
DR OMA; SWDPAMQ; -.
DR PhylomeDB; Q9MAC5; -.
DR PRO; PR:Q9MAC5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9MAC5; baseline and differential.
DR Genevisible; Q9MAC5; 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: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; 2.
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..399
FT /note="Polypyrimidine tract-binding protein homolog 1"
FT /id="PRO_0000081741"
FT DOMAIN 17..95
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 109..196
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 242..322
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 352..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..391
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 399 AA; 43593 MW; A7C556D9B308A8FC CRC64;
MSSSGQTQFR YTQTPSKVVH LRNLPWECVE EELIDLCKRF GKIVNTKSNV GANRNQAFVE
FADLNQAISM VSYYASSSEP AQIRGKTVYI QYSNRHEIVN NQSPGDVPGN VLLVTFEGVE
SHEVSIDVIH LVFSAFGFVH KIATFEKAAG FQALVQFTDV ETASAARSAL DGRSIPRYLL
SAHVGSCSLR MSYSAHTDLN IKFQSHRSRD YTNPYLPVNQ TAMDGSMQPA LGADGKKVES
QSNVLLGLIE NMQYAVTVDV LHTVFSAYGT VQKIAIFEKN GSTQALIQYS DIPTAAMAKE
ALEGHCIYDG GYCKLRLSYS RHTDLNVKAF SDKSRDYTLP DLSLLVAQKG PAVSGSAPPA
GWQNPQAQSQ YSGYGGSPYM YPSSDPNGAS PSGQPPYYG
