PTBP3_RAT
ID PTBP3_RAT Reviewed; 523 AA.
AC Q9Z118;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Polypyrimidine tract-binding protein 3;
DE AltName: Full=Regulator of differentiation 1;
DE Short=Rod1;
GN Name=Ptbp3; Synonyms=Rod1;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Kidney;
RX PubMed=10207106; DOI=10.1128/mcb.19.5.3829;
RA Yamamoto H., Tsukahara K., Kanaoka Y., Jinno S., Okayama H.;
RT "Isolation of a mammalian homologue of a fission yeast differentiation
RT regulator.";
RL Mol. Cell. Biol. 19:3829-3841(1999).
CC -!- FUNCTION: RNA-binding protein that mediates pre-mRNA alternative
CC splicing regulation. Plays a role in the regulation of cell
CC proliferation, differentiation and migration. Positive regulator of
CC EPO-dependent erythropoiesis. Participates in cell differentiation
CC regulation by repressing tissue-specific exons. Promotes Fas exon 6
CC skipping. Binds RNA, preferentially to both poly(G) and poly(U) (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with THBS4 (via the acidic amphipathic C-terminus).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected specifically in spleen, thymus, lungs, and
CC bone marrow. {ECO:0000269|PubMed:10207106}.
CC -!- DEVELOPMENTAL STAGE: At E18 and P1 expressed predominantly in thymus
CC and liver, and at lower levels in brain, muscle and kidney.
CC {ECO:0000269|PubMed:10207106}.
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DR EMBL; AB023966; BAA75465.1; -; mRNA.
DR RefSeq; NP_112636.1; NM_031346.1.
DR RefSeq; XP_006238268.1; XM_006238206.3.
DR AlphaFoldDB; Q9Z118; -.
DR SMR; Q9Z118; -.
DR STRING; 10116.ENSRNOP00000022107; -.
DR iPTMnet; Q9Z118; -.
DR PhosphoSitePlus; Q9Z118; -.
DR jPOST; Q9Z118; -.
DR PaxDb; Q9Z118; -.
DR PRIDE; Q9Z118; -.
DR GeneID; 83515; -.
DR KEGG; rno:83515; -.
DR UCSC; RGD:621671; rat.
DR CTD; 9991; -.
DR RGD; 621671; Ptbp3.
DR VEuPathDB; HostDB:ENSRNOG00000016334; -.
DR eggNOG; KOG1190; Eukaryota.
DR HOGENOM; CLU_015171_7_1_1; -.
DR InParanoid; Q9Z118; -.
DR PhylomeDB; Q9Z118; -.
DR TreeFam; TF319824; -.
DR PRO; PR:Q9Z118; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000016334; Expressed in ileum and 18 other tissues.
DR ExpressionAtlas; Q9Z118; baseline and differential.
DR Genevisible; Q9Z118; RN.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; NAS:RGD.
DR GO; GO:0043249; P:erythrocyte maturation; 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; ISO:RGD.
DR GO; GO:0033119; P:negative regulation of RNA splicing; ISO:RGD.
DR GO; GO:0045595; P:regulation of cell differentiation; IMP:RGD.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12779; RRM1_ROD1; 1.
DR CDD; cd12693; RRM2_PTBP1_like; 1.
DR CDD; cd12703; RRM4_ROD1; 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; IPR033110; PTBP3_RRM4.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034326; ROD1_RRM1.
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; Differentiation; Erythrocyte maturation; Isopeptide bond;
KW mRNA processing; mRNA splicing; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; RNA-binding; Ubl conjugation.
FT CHAIN 1..523
FT /note="Polypyrimidine tract-binding protein 3"
FT /id="PRO_0000081875"
FT DOMAIN 30..114
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 153..229
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 329..403
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 446..521
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 98
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT MOD_RES 394
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O95758"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95758"
FT CROSSLNK 36
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26599"
FT CROSSLNK 187
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26599"
SQ SEQUENCE 523 AA; 56716 MW; A2B9D5B427D316DE CRC64;
MNNSTSAGVY ANGNDNKKFK GDRPPCSPSR VLHLRKIPCD VTEAEVISLG LPFGKVTNLL
MLKGKSQAFL EMASEEAAVT MINYYTPVTP HLRSQPVYIQ YSNHRELKTD NLPNQARAQA
ALQAVSAVQS GNLSLPGATS NEGTLLPGQS PVLRIIIENL FYPVTLEVLH QIFSKFGTVL
KIITFTKNNQ FQALLQYADP VNAQYAKMAL DGQNIYNACC TLRIDFSKLT SLNVKYNNDK
SRDFTRLDLP TGDGQPSLEP PMAAAFGAPG IMSSPYAGAA GFAPAIAFPQ AAGLSVSAVP
GALGPLTLTS SAVSGRMAIP GASGIPGNSV LLVTNLNPDF ITPHGLFILF GVYGDVHRVK
IMFNKKENAL VQMADASQAQ IAMNHLSGQR LYGKVLRATL SKHQAVQLPR EGQEDQGLTK
DFSNSPLHRF KKPGSKNFQN IFPPSATLHL SNIPPSVTMD DLKNLFTEAG CSVKAFKFFQ
KDRKMALIQL GSVEEAIQAL IELHNHDLGE NHHLRVSFSK STI
