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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.
22-NOV-2017, entry version 134.
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.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar;
PubMed=1695727;
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).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
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).
[3]
FUNCTION, RNA-BINDING, AND INDUCTION.
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).
[4]
FUNCTION.
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).
[5]
FUNCTION, AND RNA-BINDING.
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)
ribonuclease.";
Mol. Cell. Biol. 23:3798-3812(2003).
[6]
PHOSPHORYLATION AT SER-92.
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,
ECO:0000269|PubMed:12748283}.
-!- 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,
ECO:0000250|UniProtKB:Q07352}.
-!- 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}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
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; MINT-1210346; -.
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; -.
OMA; LQHSYSF; -.
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; -.
Genevisible; P17431; RN.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0000932; C:P-body; 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:0003729; F:mRNA binding; IDA:MGI.
GO; GO:0003723; F:RNA binding; ISO:RGD.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
GO; GO:0006915; P:apoptotic process; ISO:RGD.
GO; GO:0008283; P:cell proliferation; ISO:RGD.
GO; GO:0071320; P:cellular response to cAMP; ISO:RGD.
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:1904628; P:cellular response to phorbol 13-acetate 12-myristate; 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; ISO:RGD.
GO; GO:0048568; P:embryonic organ development; ISO:RGD.
GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0007507; P:heart development; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
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:0006417; P:regulation of translation; ISO:RGD.
GO; GO:0009611; P:response to wounding; ISS:UniProtKB.
GO; GO:0060712; P:spongiotrophoblast layer development; ISO:RGD.
GO; GO:0033077; P:T cell differentiation in thymus; ISS:UniProtKB.
GO; GO:0001570; P:vasculogenesis; ISO:RGD.
Gene3D; 4.10.1000.10; -; 2.
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.
/FTId=PRO_0000089169.
ZN_FING 114 142 C3H1-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
ZN_FING 152 180 C3H1-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
REGION 1 111 Necessary and sufficient for the
association with mRNA decay enzymes and
mRNA decay activation.
{ECO:0000250|UniProtKB:Q07352}.
REGION 185 338 Necessary for mRNA decay activation.
{ECO:0000250|UniProtKB:Q07352}.
COMPBIAS 307 316 Poly-Ser.
MOD_RES 54 54 Phosphoserine; by MAPKAPK2.
{ECO:0000250|UniProtKB:Q07352}.
MOD_RES 90 90 Phosphoserine; by PKB/AKT1.
{ECO:0000250|UniProtKB:Q07352}.
MOD_RES 92 92 Phosphoserine; by PKB/AKT1 and MAPKAPK2.
{ECO:0000269|PubMed:15538381}.
MOD_RES 203 203 Phosphoserine; by PKB/AKT1 and MAPKAPK2.
{ECO:0000250|UniProtKB:Q07352}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000250|UniProtKB:Q07352}.
MOD_RES 334 334 Phosphoserine; by RPS6KA1.
{ECO:0000250|UniProtKB:Q07352}.
SEQUENCE 338 AA; 36399 MW; A1547C8BF566196C CRC64;
MTTTLVSATI FDLSEVLCKG NKMLNYSTPS AGGCLLDRKA VGTPAGGGFP RRHSVTLPSS
KFHQNQLLSS LKGEPAPTLS SRDSRFRDRS FSEGGERLLP TQKQPGSGQV NSSRYKTELC
RPFEENGACK YGDKCQFAHG IHELRSLTRH PKYKTELCRT FHTIGFCPYG PRCHFIHNAE
ERRALAGGRD LSADRPRLQH SFSFAGFPSA AATAAATGLL DSPTSITPPP ILSADDLLGS
PTLPDGTNNP FAFSSQELAS LFAPSMGLPG GGSPTTFLFR PMSESPHMFD SPPSPQDSLS
DHEGYLSSSS SSHSGSDSPT LDNSRRLPIF SRLSISDD


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