PTBP1_BOVIN
ID PTBP1_BOVIN Reviewed; 531 AA.
AC Q8WN55;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Polypyrimidine tract-binding protein 1;
DE Short=PTB;
GN Name=PTBP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holstein; TISSUE=Skin;
RA Guibert S., Julien R., Oulmouden A.;
RT "Cloning and characterization of bovine mRNA encoding polypyrimidine-tract
RT binding protein (PTB).";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
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DR EMBL; AF445640; AAL38169.1; -; mRNA.
DR RefSeq; NP_776867.1; NM_174442.3.
DR AlphaFoldDB; Q8WN55; -.
DR BMRB; Q8WN55; -.
DR SMR; Q8WN55; -.
DR STRING; 9913.ENSBTAP00000054889; -.
DR PaxDb; Q8WN55; -.
DR PeptideAtlas; Q8WN55; -.
DR PRIDE; Q8WN55; -.
DR Ensembl; ENSBTAT00000066209; ENSBTAP00000054889; ENSBTAG00000045828.
DR GeneID; 282018; -.
DR KEGG; bta:282018; -.
DR CTD; 5725; -.
DR VEuPathDB; HostDB:ENSBTAG00000045828; -.
DR VGNC; VGNC:52809; PTBP1.
DR eggNOG; KOG1190; Eukaryota.
DR GeneTree; ENSGT01050000244924; -.
DR HOGENOM; CLU_015171_7_1_1; -.
DR InParanoid; Q8WN55; -.
DR OrthoDB; 1545178at2759; -.
DR TreeFam; TF319824; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000045828; Expressed in parenchyma of mammary gland and 105 other tissues.
DR ExpressionAtlas; Q8WN55; baseline and differential.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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: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 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; 4.
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..531
FT /note="Polypyrimidine tract-binding protein 1"
FT /id="PRO_0000232931"
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 337..411
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 454..529
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 411..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 433
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 531 AA; 57105 MW; 99CF43EDA6238133 CRC64;
MDGIVPDIAV GTKRGSDELF SACVTNGPFI MSGTSASTAN GNDSKKFKGD SRSAGVPSRV
IHIRKLPGDV TEGEVISLGL PFGKVTNLLM LKGKNQAFIE MHTEEAANTM VNYYTSVTPV
LRGQPIYIQF SNHKELKTDS SPNQARAQAA LQAVNSVQSG NLALAASAAA VDAGMAMAGQ
SPVLRIIVEN LFYPVTLDVL HQIFSKFGTV LKIITFTKNN QFQALLQYAD PVSAQHAKLS
LDGQNIYNAC CTLRIDFSKL TSLNVKYNND KSRDYTRPDL PSGDSQPSLD QTMAAAFGLS
VPNVHGALAP LAIPSAAAAA AAAGRIAIPG LAGAGNSVLL VSNLNPERVT PQSLFILFGV
YGDVQRVKVL FNKKENALVQ MADGSQAQLA MSHLNGHKLH GKPVRITLSK HQSVQLPREG
QEDQGLTKDY GNSPLHRFKK PGSKNFQNIF PPSATLHLSN IPPSISEDDL KILFSSNGGI
VKGFKFFQKD RKMALIQMGS VEEAIQALID LHNHDLGENH HLRVSFSKST I
