PTBP1_RAT
ID PTBP1_RAT Reviewed; 555 AA.
AC Q00438; Q63568;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Polypyrimidine tract-binding protein 1;
DE Short=PTB;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein I;
DE Short=hnRNP I;
DE AltName: Full=Pyrimidine-binding protein;
DE Short=PYBP;
GN Name=Ptbp1; Synonyms=Ptb, Pybp, Tbfii;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 185-205; 348-365 AND
RP 517-549.
RC TISSUE=Hepatoma;
RX PubMed=1681508; DOI=10.1093/nar/19.19.5237;
RA Brunel F., Alzari P.M., Ferrara P., Zakin M.M.;
RT "Cloning and sequencing of PYBP, a pyrimidine-rich specific single strand
RT DNA-binding protein.";
RL Nucleic Acids Res. 19:5237-5245(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sengupta P.;
RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-13; 84-91; 122-133; 435-452 AND 496-506, ACETYLATION
RP AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Pheochromocytoma;
RA Bienvenut W.V., von Kriegsheim A.F., Kolch W.;
RL Submitted (AUG-2006) to UniProtKB.
CC -!- FUNCTION: Plays a role in pre-mRNA splicing and in the regulation of
CC alternative splicing events. Activates exon skipping of its own pre-
CC mRNA during muscle cell differentiation. Binds to the polypyrimidine
CC tract of introns. May promote RNA looping when bound to two separate
CC polypyrimidine tracts in the same pre-mRNA. May promote the binding of
CC U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching
CC between mutually exclusive exons during maturation of the TPM1 pre-
CC mRNA. Represses the splicing of MAPT/Tau exon 10. Binds to
CC polypyrimidine-rich controlling element (PCE) of CFTR and promotes exon
CC skipping of CFTR exon 9, thereby antagonizing TIA1 and its role in exon
CC inclusion of CFTR exon 9. Plays a role in the splicing of pyruvate
CC kinase PKM by binding repressively to a polypyrimidine tract flanking
CC PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10
CC inclusion and production of the PKM M2 isoform.
CC {ECO:0000250|UniProtKB:P26599}.
CC -!- SUBUNIT: Monomer. Part of a ternary complex containing KHSRP, PTBP1,
CC PTBP2 and HNRPH1. Interacts with RAVER1 and SFPQ (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=PYBP2;
CC IsoId=Q00438-1; Sequence=Displayed;
CC Name=PYBP1;
CC IsoId=Q00438-2; Sequence=VSP_005803;
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DR EMBL; X60789; CAA43202.1; -; mRNA.
DR EMBL; X60790; CAA43203.1; -; mRNA.
DR EMBL; X74565; CAA52653.1; -; mRNA.
DR PIR; S15552; S15552.
DR PIR; S36629; S36629.
DR AlphaFoldDB; Q00438; -.
DR BMRB; Q00438; -.
DR SMR; Q00438; -.
DR IntAct; Q00438; 1.
DR STRING; 10116.ENSRNOP00000043256; -.
DR iPTMnet; Q00438; -.
DR PhosphoSitePlus; Q00438; -.
DR jPOST; Q00438; -.
DR PaxDb; Q00438; -.
DR PeptideAtlas; Q00438; -.
DR PRIDE; Q00438; -.
DR UCSC; RGD:62047; rat. [Q00438-1]
DR RGD; 62047; Ptbp1.
DR eggNOG; KOG1190; Eukaryota.
DR InParanoid; Q00438; -.
DR Reactome; R-RNO-6803529; FGFR2 alternative splicing.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR PRO; PR:Q00438; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0044306; C:neuron projection terminus; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003729; F:mRNA binding; IDA:RGD.
DR GO; GO:0036002; F:pre-mRNA binding; ISO:RGD.
DR GO; GO:0001069; F:regulatory region RNA binding; IDA:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:RGD.
DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IDA:RGD.
DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; IDA:RGD.
DR GO; GO:0003231; P:cardiac ventricle development; IEP:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; ISO:RGD.
DR GO; GO:0006397; P:mRNA processing; IMP:RGD.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0051148; P:negative regulation of muscle cell differentiation; ISS:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:RGD.
DR GO; GO:0033119; P:negative regulation of RNA splicing; ISO:RGD.
DR GO; GO:0022008; P:neurogenesis; ISO:RGD.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IMP:RGD.
DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISO:RGD.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:RGD.
DR GO; GO:1904411; P:positive regulation of secretory granule organization; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045727; P:positive regulation of translation; IMP:RGD.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12777; RRM1_PTBP1; 1.
DR CDD; cd12693; RRM2_PTBP1_like; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR006536; HnRNP-L/PTB.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR021790; PTBP1-like_RRM2.
DR InterPro; IPR034798; PTBP1/2/3_RRM2.
DR InterPro; IPR035000; PTBP1_RRM1.
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; 4.
DR SUPFAM; SSF54928; SSF54928; 4.
DR TIGRFAMs; TIGR01649; hnRNP-L_PTB; 1.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Direct protein sequencing;
KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; RNA-binding; Ubl conjugation.
FT CHAIN 1..555
FT /note="Polypyrimidine tract-binding protein 1"
FT /id="PRO_0000081740"
FT DOMAIN 58..142
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 183..259
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 361..435
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 478..553
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 35..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 126
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT CROSSLNK 64
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT CROSSLNK 217
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT VAR_SEQ 297..321
FT /note="Missing (in isoform PYBP1)"
FT /evidence="ECO:0000305"
FT /id="VSP_005803"
FT CONFLICT 57
FT /note="S -> T (in Ref. 2; CAA52653)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="A -> R (in Ref. 2; CAA52653)"
FT /evidence="ECO:0000305"
FT CONFLICT 311..320
FT /note="VPSHLCHPSR -> GFPPTFAIPQA (in Ref. 2; CAA52653)"
FT /evidence="ECO:0000305"
FT CONFLICT 542..549
FT /note="ENHHLRVS -> LGDNHHKR (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 555 AA; 59354 MW; E73F22B54467117F CRC64;
MDGIVPDIAV GTKRGSDELF STCVSNGPFI MSSSASAANG NDSKKFKGDN RSTGVPSRVI
HVRKLPSDVT EGEVISLGLP FGKVTNLLML KGKNQAFIEM STEEAANTMV NYYTSVAPVL
RGQPIYIQFS NHKELKTDSS PNQARAQAAL QAVNSVQSGN LALAASAAAV DAGMAMAGQS
PVLRIIVENL FYPVTLDVLH QIFSKFGTVL KIITFTKNNQ FQALLQYADP VSAQHAKLSL
DGQNIYNACC TLRIDFSKLT SLNVKYNNDK SRDYTRPDLP SGDSQPSLDQ TMAAAFGAPG
IMSASPYAGA VPSHLCHPSR AGLSVPNVHG ALAPLAIPSA AAAAAAAGRI AIPGLAGAGN
SVLLVSNLNP ERVTPQSLFI LFGVYGDVQR VKILFNKKEN ALVEMADGSQ AQLAMSHLNG
HKLHGKSVRI TLSKHQSVQL PREGQEDQGL TKDYGSSPLH RFKKPGSKNF QNIFPPSATL
HLSNIPPSVS EDDLKSLFSS NGGVVKGFKF FQKDRKMALI QMGSVEEAVQ ALIELHNHDL
GENHHLRVSF SKSTI
