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Endoribonuclease ZC3H12A (EC 3.1.-.-) (Monocyte chemotactic protein-induced protein 1) (MCP-induced protein 1) (MCPIP-1) (Regnase-1) (Reg1) (Zinc finger CCCH domain-containing protein 12A)

 ZC12A_RAT               Reviewed;         596 AA.
A0JPN4;
10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
12-DEC-2006, sequence version 1.
20-JUN-2018, entry version 74.
RecName: Full=Endoribonuclease ZC3H12A {ECO:0000305};
EC=3.1.-.- {ECO:0000250|UniProtKB:Q5D1E7};
AltName: Full=Monocyte chemotactic protein-induced protein 1 {ECO:0000250|UniProtKB:Q5D1E7};
Short=MCP-induced protein 1 {ECO:0000250|UniProtKB:Q5D1E7};
Short=MCPIP-1 {ECO:0000250|UniProtKB:Q5D1E7};
AltName: Full=Regnase-1 {ECO:0000250|UniProtKB:Q5D1E7};
Short=Reg1 {ECO:0000250|UniProtKB:Q5D1E7};
AltName: Full=Zinc finger CCCH domain-containing protein 12A {ECO:0000312|RGD:1306776};
Name=Zc3h12a {ECO:0000312|RGD:1306776};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1] {ECO:0000312|EMBL:AAI27517.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart {ECO:0000312|EMBL:AAI27517.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Endoribonuclease involved in various biological
functions such as cellular inflammatory response and immune
homeostasis, glial differentiation of neuroprogenitor cells, cell
death of cardiomyocytes, adipogenesis and angiogenesis. Functions
as an endoribonuclease involved in mRNA decay. Modulates the
inflammatory response by promoting the degradation of a set of
translationally active cytokine-induced inflammation-related
mRNAs, such as IL6 and IL12B, during the early phase of
inflammation. Prevents aberrant T-cell-mediated immune reaction by
degradation of multiple mRNAs controlling T-cell activation, such
as those encoding cytokines (IL6 and IL2), cell surface receptors
(ICOS, TNFRSF4 and TNFR2) and transcription factor (REL). Inhibits
cooperatively with ZC3H12A the differentiation of helper T cells
Th17 in lungs. They repress target mRNA encoding the Th17 cell-
promoting factors IL6, ICOS, REL, IRF4, NFKBID and NFKBIZ. The
cooperation requires RNA-binding by RC3H1 and the nuclease
activity of ZC3H12A (By similarity). Self regulates by
destabilizing its own mRNA. Cleaves mRNA harboring a stem-loop
(SL), often located in their 3'-UTRs, during the early phase of
inflammation in a helicase UPF1-dependent manner (By similarity).
Plays a role in the inhibition of microRNAs (miRNAs) biogenesis
(By similarity). Cleaves the terminal loop of a set of precursor
miRNAs (pre-miRNAs) important for the regulation of the
inflammatory response leading to their degradation, and thus
preventing the biosynthesis of mature miRNAs (By similarity).
Plays also a role in promoting angiogenesis in response to
inflammatory cytokines by inhibiting the production of
antiangiogenic microRNAs via its anti-dicer RNase activity (By
similarity). Affects the overall ubiquitination of cellular
proteins. Positively regulates deubiquitinase activity promoting
the cleavage at 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains
on TNF receptor-associated factors (TRAFs), preventing JNK and NF-
kappa-B signaling pathway activation, and hence negatively
regulating macrophage-mediated inflammatory response and immune
homeostasis (By similarity). Induces also deubiquitination of the
transcription factor HIF1A, probably leading to its stabilization
and nuclear import, thereby positively regulating the expression
of proangiogenic HIF1A-targeted genes. Involved in a TANK-
dependent negative feedback response to attenuate NF-kappaB
activation through the deubiquitination of IKBKG or TRAF6 in
response to interleukin-1-beta (IL1B) stimulation or upon DNA
damage (By similarity). Prevents stress granules (SGs) formation
and promotes macrophage apoptosis under stress conditions,
including arsenite-induced oxidative stress, heat shock, and
energy deprivation. Plays a role in the regulation of macrophage
polarization; promotes IL4-induced polarization of macrophages M1
into anti-inflammatory M2 state. May also act as a transcription
factor that regulates the expression of multiple genes involved in
inflammatory response, angiogenesis, adipogenesis and apoptosis
(By similarity). Functions as a positive regulator of glial
differentiation of neuroprogenitor cells through an amyloid
precursor protein (APP)-dependent signaling pathway (By
similarity). Attenuates septic myocardial contractile dysfunction
in response to lipopolysaccharide (LPS) by reducing I-kappa-B-
kinase (IKK)-mediated NF-kappa-B activation, and hence myocardial
proinflammatory cytokine production (By similarity).
{ECO:0000250|UniProtKB:Q5D1E7, ECO:0000250|UniProtKB:Q5D1E8}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q5D1E7};
Note=Mg(2+) is required for RNase activity.
{ECO:0000250|UniProtKB:Q5D1E7};
-!- SUBUNIT: Oligomer. Found in a deubiquitination complex with TANK,
USP10 and ZC3H12A; this complex inhibits genotoxic stress- or
interleukin-1-beta-mediated NF-kappaB activation by promoting
IKBKG or TRAF6 deubiquitination. Interacts with IKBKG; this
interaction increases in response to DNA damage. Interacts with
TANK; this interaction increases in response to DNA damage and
serves as a bridge to anchor both TANK and USP10 into a
deubiquitinating complex. Interacts with TRAF6; this interaction
increases in response to DNA damage and is stimulated by TANK.
Interacts with USP10; this interaction increases in response to
DNA damage and serves as a bridge to anchor both TANK and USP10
into a deubiquitinating complex. Interacts with ZC3H12D. Interacts
with TNRC6A. Interacts with IKBKB/IKKB. Interacts with IKBKB/IKKB.
Interacts with IKBKB/IKKB. Interacts with BTRC; the interaction
occurs when ZC3H12A is phosphorylated in a IKBKB/IKKB-dependent
manner. Interacts with IRAK1; this interaction increases the
interaction between ZC3H12A and IKBKB/IKKB. Interacts with UPF1;
this interaction occurs in a mRNA translationally active- and
termination-dependent manner and is essential for ZC3H12A-mediated
degradation of target mRNAs. Associates with ribosomes. Interacts
with ubiquitin. {ECO:0000250|UniProtKB:Q5D1E7,
ECO:0000250|UniProtKB:Q5D1E8}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5D1E7}.
Cytoplasm {ECO:0000250|UniProtKB:Q5D1E7}. Rough endoplasmic
reticulum membrane {ECO:0000250|UniProtKB:Q5D1E7}; Peripheral
membrane protein {ECO:0000250|UniProtKB:Q5D1E7}; Cytoplasmic side
{ECO:0000250|UniProtKB:Q5D1E7}. Cytoplasmic granule
{ECO:0000250|UniProtKB:Q5D1E7}. Cytoplasm, P-body
{ECO:0000250|UniProtKB:Q5D1E8}. Note=Predominantly localized in
the cytoplasm. Colocalizes with GW182 on many granule-like
structures, probably corresponding to cytoplasmic GW bodies
(GWBs), also called processing bodies (P bodies). Colocalizes with
calnexin on the surface of the rough endoplasmic reticulum (RER)
membrane and with translationally active polysomes. Colocalizes
with ZC3H12D in cytoplasmic mRNA processing P-body, also known as
GW bodies (GWBs). {ECO:0000250|UniProtKB:Q5D1E7,
ECO:0000250|UniProtKB:Q5D1E8}.
-!- DOMAIN: The C3H1-type zinc finger domain and C-terminal region are
necessary for pre-miRNA binding. The C-terminal region and
proline-rich domain are necessary for oligomerization.
{ECO:0000250|UniProtKB:Q5D1E8}.
-!- PTM: Phosphorylated by IRAK1; phosphorylation is necessary for
subsequent phosphorylation by the I-kappa-B-kinase (IKK) complex.
Phosphorylated by I-kappa-B-kinases (IKKs) at Ser-435 and Ser-439
upon lipopolysaccharide (LPS) or IL1B stimulation in macrophages
through the MyD88-dependent signaling pathway; these
phosphorylations promote rapid ubiquitin proteasome-mediated
degradation of ZC3H12A in macrophages and hence allows its target
mRNAs, such as IL6, to escape from degradation and accumulate
during the inflammatory response. {ECO:0000250|UniProtKB:Q5D1E7}.
-!- PTM: Ubiquitinated; ubiquitination is induced in response to
interleukin IL1 receptor stimuli in a IKBKB/IKKB and IRAK1-
dependent manner, leading to proteasome-mediated degradation.
{ECO:0000250|UniProtKB:Q5D1E7}.
-!- PTM: Proteolytically cleaved between Arg-111 and Arg-214 by MALT1
in activated T-cells; cleavage at Arg-111 is critical for
promoting ZC3H12A degradation in response to T-cell receptor (TCR)
stimulation, and hence is necessary for prolonging the stability
of a set of mRNAs controlling T-cell activation and Th17 cell
differentiation. {ECO:0000250|UniProtKB:Q5D1E7}.
-!- SIMILARITY: Belongs to the ZC3H12 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BC127516; AAI27517.1; -; mRNA.
RefSeq; NP_001071139.1; NM_001077671.1.
UniGene; Rn.234344; -.
SMR; A0JPN4; -.
STRING; 10116.ENSRNOP00000012314; -.
iPTMnet; A0JPN4; -.
PhosphoSitePlus; A0JPN4; -.
PaxDb; A0JPN4; -.
PRIDE; A0JPN4; -.
Ensembl; ENSRNOT00000012314; ENSRNOP00000012314; ENSRNOG00000009131.
GeneID; 313587; -.
KEGG; rno:313587; -.
UCSC; RGD:1306776; rat.
CTD; 80149; -.
RGD; 1306776; Zc3h12a.
eggNOG; KOG3777; Eukaryota.
eggNOG; ENOG410ZNK1; LUCA.
GeneTree; ENSGT00750000117218; -.
HOGENOM; HOG000060218; -.
HOVERGEN; HBG108758; -.
InParanoid; A0JPN4; -.
KO; K18668; -.
OMA; FPPREYW; -.
OrthoDB; EOG091G03B2; -.
PhylomeDB; A0JPN4; -.
PRO; PR:A0JPN4; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000009131; -.
Genevisible; A0JPN4; RN.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0000932; C:P-body; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
GO; GO:0004532; F:exoribonuclease activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; ISS:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
GO; GO:0004518; F:nuclease activity; ISS:UniProtKB.
GO; GO:0043022; F:ribosome binding; IEA:Ensembl.
GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:Ensembl.
GO; GO:0061158; P:3'-UTR-mediated mRNA destabilization; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:1990869; P:cellular response to chemokine; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
GO; GO:1904637; P:cellular response to ionomycin; ISS:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
GO; GO:1903936; P:cellular response to sodium arsenite; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
GO; GO:0002757; P:immune response-activating signal transduction; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0044828; P:negative regulation by host of viral genome replication; IEA:Ensembl.
GO; GO:0055118; P:negative regulation of cardiac muscle contraction; ISS:UniProtKB.
GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:1902714; P:negative regulation of interferon-gamma secretion; ISS:UniProtKB.
GO; GO:0050713; P:negative regulation of interleukin-1 beta secretion; ISS:UniProtKB.
GO; GO:1900165; P:negative regulation of interleukin-6 secretion; ISS:UniProtKB.
GO; GO:0010656; P:negative regulation of muscle cell apoptotic process; ISS:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISS:UniProtKB.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; ISS:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:2000320; P:negative regulation of T-helper 17 cell differentiation; ISS:UniProtKB.
GO; GO:1904468; P:negative regulation of tumor necrosis factor secretion; ISS:UniProtKB.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0000294; P:nuclear-transcribed mRNA catabolic process, endonucleolytic cleavage-dependent decay; IEA:Ensembl.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
GO; GO:0010942; P:positive regulation of cell death; ISS:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IEA:Ensembl.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IEA:Ensembl.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0010884; P:positive regulation of lipid storage; IEA:Ensembl.
GO; GO:2000627; P:positive regulation of miRNA catabolic process; ISS:UniProtKB.
GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISS:UniProtKB.
GO; GO:1900745; P:positive regulation of p38MAPK cascade; IEA:Ensembl.
GO; GO:1903003; P:positive regulation of protein deubiquitination; ISS:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IEA:Ensembl.
GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; ISS:UniProtKB.
GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; ISS:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
InterPro; IPR021869; RNase_Zc3h12_NYN.
Pfam; PF11977; RNase_Zc3h12a; 1.
2: Evidence at transcript level;
Angiogenesis; Apoptosis; Complete proteome; Cytoplasm;
Developmental protein; Differentiation; DNA damage; DNA-binding;
Endonuclease; Endoplasmic reticulum; Hydrolase; Immunity;
Inflammatory response; Magnesium; Membrane; Metal-binding;
Neurogenesis; Nuclease; Nucleus; Phosphoprotein; Reference proteome;
RNA-binding; Stress response; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 596 Endoribonuclease ZC3H12A.
/FTId=PRO_0000341514.
ZN_FING 301 324 C3H1-type.
REGION 42 87 Ubiquitin association domain.
{ECO:0000250|UniProtKB:Q5D1E7}.
REGION 81 150 Necessary for interaction with TANK.
{ECO:0000250|UniProtKB:Q5D1E8}.
REGION 112 281 RNase. {ECO:0000250|UniProtKB:Q5D1E8}.
REGION 214 220 RNA binding.
{ECO:0000250|UniProtKB:Q5D1E8}.
REGION 301 454 Necessary for interaction with ZC3H12D.
{ECO:0000250|UniProtKB:Q5D1E8}.
COMPBIAS 496 533 Pro-rich. {ECO:0000255}.
METAL 226 226 Magnesium.
{ECO:0000250|UniProtKB:Q5D1E8}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000250|UniProtKB:Q5D1E8}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000250|UniProtKB:Q5D1E8}.
MOD_RES 435 435 Phosphoserine.
{ECO:0000250|UniProtKB:Q5D1E7}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000250|UniProtKB:Q5D1E7}.
SEQUENCE 596 AA; 65927 MW; C2BBA6DF323432AE CRC64;
MSDPCGKKLV QEISPTMSLW GLEDRHSCQG QPQPDQDPVA KEASASELQM KVDFFRKLGY
SSSEIHSALQ KLGVQADTNT VLGELVKHGS ATERECQAST DPCPQPPLVP RGGSTPKPST
VEPSLPEEDK ESSDLRPVVI DGSNVAMSHG NKEVFSCRGI LLAVNWFLER GHTDITVFVP
SWRKEQPRPD VPITDQHILR ELEKKKILVF TPSRRVGGKR VVCYDDRFIV KLAYESDGVV
VSNDTYRDLQ GERQEWKRFI EERLLMYSFV NDKFMPPDDP LGRHGPSLDN FLRKKPLPSE
HRKQPCPYGR KCTYGIKCRF FHPERPSRPQ RSVADELRAN ALLSPPRTPV KDKSSQRPSP
ASQPNSMSLE AEPGSPDGKK LGTRSSPGPH QEGSTQTCAP AGRSLPVSGG SFGPTEWLPH
TLDSLPYTSQ ECLDSGIGSL ESQMSELWGL RGGSPGESGP TRGPYTGYQT YGSKLPAAPA
FSPFRQAIGT GHFSVPTDYV PPPPTYPARE YWSEPYPLPP PTPVLQEPQR PRPRASGDPW
GRVSDLAKER AGVYTKLCGV FPPHLVEAVM GRFPQLLDPQ QLAAEILSYK SQHLSE


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