PTBP1_PIG
ID PTBP1_PIG Reviewed; 557 AA.
AC Q29099;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Polypyrimidine tract-binding protein 1;
DE Short=PTB;
DE AltName: Full=Heterogeneous nuclear ribonucleoprotein I;
DE Short=hnRNP I;
GN Name=PTBP1; Synonyms=PTB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8654585; DOI=10.1016/0014-5793(96)00509-1;
RA Niepmann M.;
RT "Porcine polypyrimidine tract-binding protein stimulates translation
RT initiation at the internal ribosome entry site of foot-and-mouth-disease
RT virus.";
RL FEBS Lett. 388:39-42(1996).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X93009; CAA63597.1; -; mRNA.
DR PIR; S68857; S68857.
DR RefSeq; NP_999396.1; NM_214231.1.
DR AlphaFoldDB; Q29099; -.
DR BMRB; Q29099; -.
DR SMR; Q29099; -.
DR IntAct; Q29099; 3.
DR STRING; 9823.ENSSSCP00000014270; -.
DR PaxDb; Q29099; -.
DR PeptideAtlas; Q29099; -.
DR PRIDE; Q29099; -.
DR GeneID; 397461; -.
DR KEGG; ssc:397461; -.
DR CTD; 5725; -.
DR eggNOG; KOG1190; Eukaryota.
DR InParanoid; Q29099; -.
DR OrthoDB; 1545178at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12777; RRM1_PTBP1; 1.
DR CDD; cd12693; RRM2_PTBP1_like; 1.
DR CDD; cd12695; RRM3_PTBP1; 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; IPR035001; PTBP1_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; 4.
DR SUPFAM; SSF54928; SSF54928; 3.
DR TIGRFAMs; TIGR01649; hnRNP-L_PTB; 1.
DR PROSITE; PS50102; RRM; 4.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..557
FT /note="Polypyrimidine tract-binding protein 1"
FT /id="PRO_0000081739"
FT DOMAIN 59..143
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 184..260
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 363..437
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 480..555
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 127
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT CROSSLNK 218
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26599"
SQ SEQUENCE 557 AA; 59855 MW; E323F8FBD6DAFF66 CRC64;
MDGIVPDIAV GTKRGSDELF SACVTNGPFI MSSNSASTAN GNDSKKFKGD NRSAGVPSRV
IHIRKLPSDV TEGEVISLGL PFGKVTNLLM LKGKNQAFIE MNTEEAANTM VNYYTSVTPV
LRGQPIYIQF SNHKELKTDS SPNQARAQAA LQAVNSVQSG NLALAASAAA VDAGMAMAGQ
SPVLRIIVEN LFYPVTLDVL HQIFSKFGTV LKIITFTKNN QFQALLQYAD PVSAQHAKLS
LDGQNIYNAC CTLRIDFSKL TSLNVKYNND KSRDYTRPDL PSGDNQPSLD QTMAAAFGAP
GIMSASPYAG AGFPPTFAIP QAATVSVPNV HGALAPLAIP SAAARAAAAG RIAIPGLAGA
GNSVLLVSNL NPERVTPQSL FILFGVYCDV QRVKILFNKK ENALVQMADG SQAQLAMSHL
NGHKLHGKPV RITLSKHQNV QLPREGQEDQ GLTKDYGNSP LHRFKKPGSK NFQNIFPPSA
TLHLSNIPPS ISEEDLKILF SSNGGIVKGF KFFQKDRKMA LIQMGSVEEA IQALIDLHNH
DLGENHHLRV SFSKSTI
