ID TTP_RAT Reviewed; 320 AA. AC P47973; Q54AH1; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 29-OCT-2014, entry version 108. DE RecName: Full=Tristetraprolin; DE Short=TTP; DE AltName: Full=Protein TIS11A; DE Short=TIS11; DE AltName: Full=Zinc finger protein 36; DE Short=Zfp-36; GN Name=Zfp36; Synonyms=Tis11a; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1511903; DOI=10.1016/0378-1119(92)90202-Z; RA Kaneda N., Oshima M., Chung S.Y., Guroff G.; RT "Sequence of a rat TIS11 cDNA, an immediate early gene induced by RT growth factors and phorbol esters."; RL Gene 118:289-291(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11129950; DOI=10.1023/A:1007172316657; RA Kaneda N., Murata T., Niimi Y., Minamiyama M.; RT "Cloning and characterization of the rat TIS11 gene."; RL Mol. Cell. Biochem. 213:119-126(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pituitary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: mRNA-binding protein involved in post-transcriptional CC regulation of AU-rich element (ARE)-containing mRNAs. Acts by CC specifically binding ARE-containing mRNAs and promoting their CC degradation. Recruits deadenylase CNOT7 (and probably the CCR4-NOT CC complex) via association with CNOT1. Plays a key role in the post- CC transcriptional regulation of tumor necrosis factor (TNF). Plays a CC key role in the post-transcriptional regulation of tumor necrosis CC factor (TNF) (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with CNOT1. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm CC {ECO:0000250}. Note=Localizes to stress granules upon energy CC starvation. phosphorylation by MAPKAPK2 promotes exclusion from CC stress granules (By similarity). {ECO:0000250}. CC -!- PTM: Phosphorylation by MAPKAPK2 increases its stability and CC binding to 14-3-3 proteins, leading to reduce its ARE affinity CC leading to inhibition of degradation of ARE-containing CC transcripts. Phosphorylated upon mitogen stimulation (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Contains 2 C3H1-type zinc fingers. CC {ECO:0000255|PROSITE-ProRule:PRU00723}. 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; X63369; CAA44970.1; -; mRNA. DR EMBL; AB025017; BAB12432.1; -; Genomic_DNA. DR EMBL; BC060308; AAH60308.1; -; mRNA. DR PIR; JC1255; JC1255. DR RefSeq; NP_579824.2; NM_133290.3. DR UniGene; Rn.82737; -. DR ProteinModelPortal; P47973; -. DR SMR; P47973; 94-163. DR STRING; 10116.ENSRNOP00000026661; -. DR PhosphoSite; P47973; -. DR PaxDb; P47973; -. DR PRIDE; P47973; -. DR GeneID; 79426; -. DR KEGG; rno:79426; -. DR UCSC; RGD:620722; rat. DR CTD; 7538; -. DR RGD; 620722; Zfp36. DR eggNOG; COG5063; -. DR HOGENOM; HOG000233479; -. DR HOVERGEN; HBG008483; -. DR InParanoid; P47973; -. DR KO; K15308; -. DR PhylomeDB; P47973; -. DR Reactome; REACT_196431; Tristetraprolin (TTP) destabilizes mRNA. DR NextBio; 614778; -. DR PRO; PR:P47973; -. DR ExpressionAtlas; P47973; baseline and differential. DR Genevestigator; P47973; -. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB. DR GO; GO:0017091; F:AU-rich element binding; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IEA:Ensembl. DR GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISS:UniProtKB. DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl. DR GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB. DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl. DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl. DR GO; GO:0035278; P:negative regulation of translation involved in gene silencing by miRNA; ISS:UniProtKB. DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IEA:Ensembl. DR GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISS:UniProtKB. DR GO; GO:0060213; P:positive regulation of nuclear-transcribed mRNA poly(A) tail shortening; ISS:UniProtKB. DR GO; GO:0032680; P:regulation of tumor necrosis factor production; ISS:UniProtKB. DR GO; GO:0042594; P:response to starvation; ISS:UniProtKB. DR GO; GO:0050779; P:RNA destabilization; IEA:Ensembl. DR Gene3D; 4.10.1000.10; -; 2. DR InterPro; IPR000571; Znf_CCCH. DR Pfam; PF00642; zf-CCCH; 2. DR SMART; SM00356; ZnF_C3H1; 2. DR PROSITE; PS50103; ZF_C3H1; 2. PE 2: Evidence at transcript level; KW Complete proteome; Cytoplasm; DNA-binding; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger. FT CHAIN 1 320 Tristetraprolin. FT /FTId=PRO_0000089165. FT REPEAT 64 68 P-P-P-P-G. FT REPEAT 191 195 P-P-P-P-G. FT REPEAT 212 216 P-P-P-P-G. FT ZN_FING 96 124 C3H1-type 1. {ECO:0000255|PROSITE- FT ProRule:PRU00723}. FT ZN_FING 134 162 C3H1-type 2. {ECO:0000255|PROSITE- FT ProRule:PRU00723}. FT REGION 306 320 Interaction with CNOT1. {ECO:0000250}. FT MOD_RES 53 53 Phosphoserine; by MAPKAPK2. FT {ECO:0000250}. FT MOD_RES 59 59 Phosphoserine. {ECO:0000250}. FT MOD_RES 81 81 Phosphoserine. {ECO:0000250}. FT MOD_RES 83 83 Phosphoserine. {ECO:0000250}. FT MOD_RES 85 85 Phosphothreonine. {ECO:0000250}. FT MOD_RES 86 86 Phosphoserine. {ECO:0000250}. FT MOD_RES 179 179 Phosphoserine; by MAPKAPK2. FT {ECO:0000250}. FT MOD_RES 190 190 Phosphoserine. {ECO:0000250}. FT MOD_RES 211 211 Phosphoserine. {ECO:0000250}. FT MOD_RES 221 221 Phosphoserine. {ECO:0000250}. FT MOD_RES 251 251 Phosphothreonine. {ECO:0000250}. FT MOD_RES 270 270 Phosphoserine. {ECO:0000250}. FT MOD_RES 290 290 Phosphoserine. {ECO:0000250}. FT MOD_RES 317 317 Phosphoserine. {ECO:0000250}. SQ SEQUENCE 320 AA; 33654 MW; CFC597F3C7E5CA76 CRC64; MDLSAIYESL MSMSHDLSPD HGGTESSGGL WNINSSDSIP SGVTSRLTGR STSLVEGRSC SWVPPPPGFA PLAPRPGPEL SPSPTSPTAT PTTSSRYKTE LCRTYSESGR CRYGAKCQFA HGPGELRQAN RHPKYKTELC HKFYLQGRCP YGSRCHFIHN PTEDLALPGQ PHVLRQSISF SGLPSGRRTS PPPPGFSGPS LSSCSFSPSS SPPPPGDLPL SPSAFSAAPG TPVSRRDPTP ACCPSCRRST TPSTIWGPLG GLARSPSAHS LGSDPDDYAS SGSSLGGSDS PVFEAGVFGP PQPPAPPRRL PIFNRISVSE //