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mRNA decay activator protein ZFP36L1 (Butyrate response factor 1) (EGF-inducible protein CMG1) (TPA-induced sequence 11b) (Zinc finger protein 36, C3H1 type-like 1) (ZFP36-like 1)

 TISB_RAT                Reviewed;         338 AA.
P17431; Q6LAU8;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
07-NOV-2018, entry version 141.
RecName: Full=mRNA decay activator protein ZFP36L1 {ECO:0000305};
AltName: Full=Butyrate response factor 1 {ECO:0000250|UniProtKB:Q07352};
AltName: Full=EGF-inducible protein CMG1 {ECO:0000305};
AltName: Full=TPA-induced sequence 11b {ECO:0000250|UniProtKB:P23950};
AltName: Full=Zinc finger protein 36, C3H1 type-like 1 {ECO:0000312|RGD:62009};
Short=ZFP36-like 1 {ECO:0000312|RGD:62009};
Name=Zfp36l1 {ECO:0000312|RGD:62009};
Synonyms=Brf1 {ECO:0000250|UniProtKB:Q07352},
Cmg1 {ECO:0000303|PubMed:7575462},
Tis11b {ECO:0000303|PubMed:7575462};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
Gomperts M., Pascall J.C., Brown K.D.;
"The nucleotide sequence of a cDNA encoding an EGF-inducible gene
indicates the existence of a new family of mitogen-induced genes.";
Oncogene 5:1081-1083(1990).
PubMed=7575462; DOI=10.1042/bj3110251;
Corps A.N., Pascall J.C., Hadfield K.M., Brown K.D.;
"Identification of a functional promoter element in the 5'-flanking
region of the rat cMG1/TIS11b gene.";
Biochem. J. 311:251-258(1995).
PubMed=10751406; DOI=10.1074/jbc.M001696200;
Lai W.S., Carballo E., Thorn J.M., Kennington E.A., Blackshear P.J.;
"Interactions of CCCH zinc finger proteins with mRNA. Binding of
tristetraprolin-related zinc finger proteins to Au-rich elements and
destabilization of mRNA.";
J. Biol. Chem. 275:17827-17837(2000).
PubMed=11279239; DOI=10.1074/jbc.M100680200;
Lai W.S., Blackshear P.J.;
"Interactions of CCCH zinc finger proteins with mRNA: tristetraprolin-
mediated AU-rich element-dependent mRNA degradation can occur in the
absence of a poly(A) tail.";
J. Biol. Chem. 276:23144-23154(2001).
PubMed=12748283; DOI=10.1128/MCB.23.11.3798-3812.2003;
Lai W.S., Kennington E.A., Blackshear P.J.;
"Tristetraprolin and its family members can promote the cell-free
deadenylation of AU-rich element-containing mRNAs by poly(A)
Mol. Cell. Biol. 23:3798-3812(2003).
PubMed=15538381; DOI=10.1038/sj.emboj.7600477;
Schmidlin M., Lu M., Leuenberger S.A., Stoecklin G., Mallaun M.,
Gross B., Gherzi R., Hess D., Hemmings B.A., Moroni C.;
"The ARE-dependent mRNA-destabilizing activity of BRF1 is regulated by
protein kinase B.";
EMBO J. 23:4760-4769(2004).
-!- FUNCTION: Zinc-finger RNA-binding protein that destabilizes
several cytoplasmic AU-rich element (ARE)-containing mRNA
transcripts by promoting their poly(A) tail removal or
deadenylation, and hence provide a mechanism for attenuating
protein synthesis (PubMed:10751406, PubMed:12748283). Acts as a
3'-untranslated region (UTR) ARE mRNA-binding adapter protein to
communicate signaling events to the mRNA decay machinery
(PubMed:12748283). Functions by recruiting the CCR4-NOT
deadenylase complex and components of the cytoplasmic RNA decay
machinery to the bound ARE-containing mRNAs, and hence promotes
ARE-mediated mRNA deadenylation and decay processes
(PubMed:12748283). Induces also the degradation of ARE-containing
mRNAs even in absence of poly(A) tail (PubMed:11279239). Binds to
3'-UTR ARE of numerous mRNAs (PubMed:10751406). Positively
regulates early adipogenesis by promoting ARE-mediated mRNA decay
of immediate early genes (IEGs). Promotes ARE-mediated mRNA decay
of mineralocorticoid receptor NR3C2 mRNA in response to hypertonic
stress. Negatively regulates hematopoietic/erythroid cell
differentiation by promoting ARE-mediated mRNA decay of the
transcription factor STAT5B mRNA. Positively regulates
monocyte/macrophage cell differentiation by promoting ARE-mediated
mRNA decay of the cyclin-dependent kinase CDK6 mRNA. Promotes
degradation of ARE-containing pluripotency-associated mRNAs in
embryonic stem cells (ESCs), such as NANOG, through a fibroblast
growth factor (FGF)-induced MAPK-dependent signaling pathway, and
hence attenuates ESC self-renewal and positively regulates
mesendoderm differentiation. May play a role in mediating pro-
apoptotic effects in malignant B-cells by promoting ARE-mediated
mRNA decay of BCL2 mRNA. In association with ZFP36L2 maintains
quiescence on developing B lymphocytes by promoting ARE-mediated
decay of several mRNAs encoding cell cycle regulators that help B
cells progress through the cell cycle, and hence ensuring accurate
variable-diversity-joining (VDJ) recombination and functional
immune cell formation. Together with ZFP36L2 is also necessary for
thymocyte development and prevention of T-cell acute lymphoblastic
leukemia (T-ALL) transformation by promoting ARE-mediated mRNA
decay of the oncogenic transcription factor NOTCH1 mRNA.
Participates in the delivery of target ARE-mRNAs to processing
bodies (PBs). In addition to its cytosolic mRNA-decay function,
plays a role in the regulation of nuclear mRNA 3'-end processing;
modulates mRNA 3'-end maturation efficiency of the DLL4 mRNA
through binding with an ARE embedded in a weak noncanonical
polyadenylation (poly(A)) signal in endothelial cells. Also
involved in the regulation of stress granule (SG) and P-body (PB)
formation and fusion. Plays a role in vasculogenesis and
endocardial development. Plays a role in the regulation of
keratinocyte proliferation, differentiation and apoptosis. Plays a
role in myoblast cell differentiation (By similarity).
{ECO:0000250|UniProtKB:P23950, ECO:0000250|UniProtKB:Q07352,
ECO:0000269|PubMed:10751406, ECO:0000269|PubMed:11279239,
-!- SUBUNIT: Associates with the cytoplasmic CCR4-NOT deadenylase and
RNA exosome complexes to trigger ARE-containing mRNA deadenylation
and decay processes. Interacts with CNOT1. Interacts (via N-
terminus) with CNOT6. Interacts with CNOT7; this interaction is
inhibited in response to phorbol 12-myristate 13-acetate (PMA)
treatment in a p38 MAPK-dependent manner. Interacts with DCP1A.
Interacts (via N-terminus) with DCP2. Interacts (via N-terminus)
with EXOSC2. Interacts with XRN1. Interacts (via phosphorylated
form) with YWHAB; this interaction occurs in a protein kinase
AKT1-dependent manner. Interacts (via phosphorylated form) with
YWHAZ; this interaction occurs in a p38 MAPK- and AKT-signaling
pathways. {ECO:0000250|UniProtKB:P23950,
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q07352}.
Cytoplasm {ECO:0000250|UniProtKB:Q07352}. Cytoplasmic granule
{ECO:0000250|UniProtKB:Q07352}. Cytoplasm, P-body
{ECO:0000250|UniProtKB:Q07352}. Note=Shuttles between the nucleus
and the cytoplasm in a XPO1/CRM1-dependent manner. Component of
cytoplasmic stress granules. Localizes in processing bodies (PBs).
{ECO:0000250|UniProtKB:P23950, ECO:0000250|UniProtKB:Q07352}.
-!- PTM: Phosphorylated. Phosphorylated by RPS6KA1 at Ser-334 upon
phorbol 12-myristate 13-acetate (PMA) treatment; this
phosphorylation results in dissociation of the CCR4-NOT
deadenylase complex and induces p38 MAPK-mediated stabilization of
the low-density lipoprotein receptor LDLR mRNA. Phosphorylated by
protein kinase AKT1 at Ser-92 and Ser-203 in response to insulin;
these phosphorylations stabilize ZFP36L1, increase the association
with 14-3-3 proteins and mediate ARE-containing mRNA
stabilization. AKT1-mediated phosphorylation at Ser-92 does not
impair ARE-containing RNA-binding. Phosphorylated at Ser-54, Ser-
92 and Ser-203 by MAPKAPK2; these phosphorylations increase the
association with 14-3-3 proteins and mediate ARE-containing mRNA
stabilization in a protein kinase AKT1-independent manner.
MAPKAPK2-mediated phosphorylations at Ser-54, Ser-92 and Ser-203
do not impair ARE-containing RNA-binding (By similarity).
Phosphorylations increase the association with 14-3-3 proteins and
mediate ARE-containing mRNA stabilization during early
adipogenesis in a p38 MAPK- and AKT-dependent manner (By
similarity). Phosphorylated by protein kinase AKT1 at Ser-92
(PubMed:15538381). {ECO:0000250|UniProtKB:P23950,
ECO:0000250|UniProtKB:Q07352, ECO:0000269|PubMed:15538381}.
-!- PTM: Ubiquitinated. Ubiquitination leads to proteasomal
degradation, a process inhibited by phosphorylations at Ser-90,
Ser-92 and Ser-203. {ECO:0000250|UniProtKB:Q07352}.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; X52590; CAA36826.1; -; mRNA.
EMBL; X86571; CAA60379.1; -; Genomic_DNA.
PIR; S10471; S10471.
RefSeq; NP_058868.1; NM_017172.1.
UniGene; Rn.6142; -.
ProteinModelPortal; P17431; -.
SMR; P17431; -.
MINT; P17431; -.
iPTMnet; P17431; -.
PhosphoSitePlus; P17431; -.
PRIDE; P17431; -.
Ensembl; ENSRNOT00000083677; ENSRNOP00000075412; ENSRNOG00000058646.
GeneID; 29344; -.
KEGG; rno:29344; -.
UCSC; RGD:62009; rat.
CTD; 677; -.
RGD; 62009; Zfp36l1.
GeneTree; ENSGT00530000063262; -.
HOGENOM; HOG000233479; -.
HOVERGEN; HBG008483; -.
InParanoid; P17431; -.
KO; K18753; -.
OrthoDB; EOG091G0957; -.
PhylomeDB; P17431; -.
Reactome; R-RNO-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
PRO; PR:P17431; -.
Proteomes; UP000002494; Chromosome 6.
Bgee; ENSRNOG00000058646; Expressed in 9 organ(s), highest expression level in spleen.
Genevisible; P17431; RN.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0000932; C:P-body; ISS:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0071889; F:14-3-3 protein binding; ISS:UniProtKB.
GO; GO:0017091; F:AU-rich element binding; IMP:RGD.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
GO; GO:0003729; F:mRNA binding; IDA:MGI.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISS:UniProtKB.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; ISS:UniProtKB.
GO; GO:0097403; P:cellular response to raffinose; ISS:UniProtKB.
GO; GO:0071472; P:cellular response to salt stress; ISS:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISS:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
GO; GO:0060710; P:chorio-allantoic fusion; IEA:Ensembl.
GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
GO; GO:0048382; P:mesendoderm development; ISS:UniProtKB.
GO; GO:0006402; P:mRNA catabolic process; IDA:MGI.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0051028; P:mRNA transport; ISS:UniProtKB.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISS:UniProtKB.
GO; GO:1901991; P:negative regulation of mitotic cell cycle phase transition; ISS:UniProtKB.
GO; GO:0021915; P:neural tube development; IEA:Ensembl.
GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IEA:Ensembl.
GO; GO:0031086; P:nuclear-transcribed mRNA catabolic process, deadenylation-independent decay; IDA:UniProtKB.
GO; GO:0038066; P:p38MAPK cascade; ISS:UniProtKB.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:1904582; P:positive regulation of intracellular mRNA localization; ISS:UniProtKB.
GO; GO:0045657; P:positive regulation of monocyte differentiation; ISS:UniProtKB.
GO; GO:1900153; P:positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:UniProtKB.
GO; GO:0003342; P:proepicardium development; IEA:Ensembl.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0045577; P:regulation of B cell differentiation; ISS:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
GO; GO:1902172; P:regulation of keratinocyte apoptotic process; ISS:UniProtKB.
GO; GO:0045616; P:regulation of keratinocyte differentiation; ISS:UniProtKB.
GO; GO:0010837; P:regulation of keratinocyte proliferation; ISS:UniProtKB.
GO; GO:0031440; P:regulation of mRNA 3'-end processing; IEA:Ensembl.
GO; GO:0043488; P:regulation of mRNA stability; IDA:UniProtKB.
GO; GO:0045661; P:regulation of myoblast differentiation; ISS:UniProtKB.
GO; GO:0072091; P:regulation of stem cell proliferation; ISS:UniProtKB.
GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
GO; GO:0060712; P:spongiotrophoblast layer development; IEA:Ensembl.
GO; GO:0033077; P:T cell differentiation in thymus; ISS:UniProtKB.
GO; GO:0001570; P:vasculogenesis; IEA:Ensembl.
InterPro; IPR007635; Tis11B_N.
InterPro; IPR000571; Znf_CCCH.
InterPro; IPR036855; Znf_CCCH_sf.
Pfam; PF04553; Tis11B_N; 1.
Pfam; PF00642; zf-CCCH; 2.
SMART; SM00356; ZnF_C3H1; 2.
SUPFAM; SSF90229; SSF90229; 2.
PROSITE; PS50103; ZF_C3H1; 2.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Developmental protein; DNA-binding;
Metal-binding; mRNA processing; mRNA transport; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
RNA-binding; Transport; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 338 mRNA decay activator protein ZFP36L1.
ZN_FING 114 142 C3H1-type 1. {ECO:0000255|PROSITE-
ZN_FING 152 180 C3H1-type 2. {ECO:0000255|PROSITE-
REGION 1 111 Necessary and sufficient for the
association with mRNA decay enzymes and
mRNA decay activation.
REGION 185 338 Necessary for mRNA decay activation.
COMPBIAS 307 316 Poly-Ser.
MOD_RES 54 54 Phosphoserine; by MAPKAPK2.
MOD_RES 90 90 Phosphoserine; by PKB/AKT1.
MOD_RES 92 92 Phosphoserine; by PKB/AKT1 and MAPKAPK2.
MOD_RES 203 203 Phosphoserine; by PKB/AKT1 and MAPKAPK2.
MOD_RES 318 318 Phosphoserine.
MOD_RES 334 334 Phosphoserine; by RPS6KA1.
SEQUENCE 338 AA; 36399 MW; A1547C8BF566196C CRC64;

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