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Nucleolar protein 3 (Apoptosis repressor with CARD)

 NOL3_RAT                Reviewed;         221 AA.
Q62881;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
05-JUL-2017, entry version 100.
RecName: Full=Nucleolar protein 3;
AltName: Full=Apoptosis repressor with CARD;
Name=Nol3; Synonyms=Arc;
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=Sprague-Dawley; TISSUE=Brain, and Pheochromocytoma;
PubMed=8634331; DOI=10.1016/0167-4781(96)00036-X;
Geertman R., McMahon A., Sabban E.L.;
"Cloning and characterization of cDNAs for novel proteins with
glutamic acid-proline dipeptide tandem repeats.";
Biochim. Biophys. Acta 1306:147-152(1996).
[2]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=10590251; DOI=10.1161/01.RES.85.12.e70;
Ekhterae D., Lin Z., Lundberg M.S., Crow M.T., Brosius F.C. III,
Nunez G.;
"ARC inhibits cytochrome c release from mitochondria and protects
against hypoxia-induced apoptosis in heart-derived H9c2 cells.";
Circ. Res. 85:E70-E77(1999).
[3]
INTERACTION WITH TFPT.
PubMed=10644725; DOI=10.1074/jbc.275.4.2647;
Irie Y., Yamagata K., Gan Y., Miyamoto K., Do E., Kuo C.H., Taira E.,
Miki N.;
"Molecular cloning and characterization of Amida, a novel protein
which interacts with a neuron-specific immediate early gene product
arc, contains novel nuclear localization signals, and causes cell
death in cultured cells.";
J. Biol. Chem. 275:2647-2653(2000).
[4]
IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT THR-149,
MUTAGENESIS OF THR-149, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=12191471; DOI=10.1016/S1097-2765(02)00600-7;
Li P.F., Li J., Mueller E.C., Otto A., Dietz R., von Harsdorf R.;
"Phosphorylation by protein kinase CK2: a signaling switch for the
caspase-inhibiting protein ARC.";
Mol. Cell 10:247-258(2002).
[5]
FUNCTION, INTERACTION WITH FADD; FAS; CASP8 AND BAX, MUTAGENESIS OF
LEU-31 AND GLY-69, AND DOMAIN.
PubMed=15383280; DOI=10.1016/j.molcel.2004.08.020;
Nam Y.J., Mani K., Ashton A.W., Peng C.F., Krishnamurthy B.,
Hayakawa Y., Lee P., Korsmeyer S.J., Kitsis R.N.;
"Inhibition of both the extrinsic and intrinsic death pathways through
nonhomotypic death-fold interactions.";
Mol. Cell 15:901-912(2004).
[6]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CASP2; BAX AND PPM1G,
AND MUTAGENESIS OF THR-149.
PubMed=16639714; DOI=10.1002/jcb.20946;
Zhang Y.Q., Herman B.;
"ARC protects rat cardiomyocytes against oxidative stress through
inhibition of caspase-2 mediated mitochondrial pathway.";
J. Cell. Biochem. 99:575-588(2006).
[7]
FUNCTION.
PubMed=17292893; DOI=10.1016/j.febslet.2007.01.050;
Hunter A.L., Zhang J., Chen S.C., Si X., Wong B., Ekhterae D., Luo H.,
Granville D.J.;
"Apoptosis repressor with caspase recruitment domain (ARC) inhibits
myogenic differentiation.";
FEBS Lett. 581:879-884(2007).
[8]
UBIQUITINATION.
PubMed=17142834; DOI=10.1074/jbc.M609046200;
Foo R.S., Chan L.K., Kitsis R.N., Bennett M.R.;
"Ubiquitination and degradation of the anti-apoptotic protein ARC by
MDM2.";
J. Biol. Chem. 282:5529-5535(2007).
[9]
DEPHOSPHORYLATION BY CALCINEURIN, PHOSPHORYLATION AT THR-149, AND
MUTAGENESIS OF THR-149.
PubMed=19001025; DOI=10.1161/CIRCULATIONAHA.107.750869;
Tan W.Q., Wang J.X., Lin Z.Q., Li Y.R., Lin Y., Li P.F.;
"Novel cardiac apoptotic pathway: the dephosphorylation of apoptosis
repressor with caspase recruitment domain by calcineurin.";
Circulation 118:2268-2276(2008).
[10]
INDUCTION, AND INTERACTION WITH BBC3 AND BAD.
PubMed=17998337; DOI=10.1128/MCB.00738-07;
Li Y.Z., Lu D.Y., Tan W.Q., Wang J.X., Li P.F.;
"p53 initiates apoptosis by transcriptionally targeting the
antiapoptotic protein ARC.";
Mol. Cell. Biol. 28:564-574(2008).
[11]
INDUCTION.
PubMed=22082675; DOI=10.1161/CIRCULATIONAHA.111.034512;
Zaiman A.L., Damico R., Thoms-Chesley A., Files D.C., Kesari P.,
Johnston L., Swaim M., Mozammel S., Myers A.C., Halushka M.,
El-Haddad H., Shimoda L.A., Peng C.F., Hassoun P.M., Champion H.C.,
Kitsis R.N., Crow M.T.;
"A critical role for the protein apoptosis repressor with caspase
recruitment domain in hypoxia-induced pulmonary hypertension.";
Circulation 124:2533-2542(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-149, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[13]
FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
PubMed=23382383; DOI=10.1074/jbc.M112.442061;
Lu D., Liu J., Jiao J., Long B., Li Q., Tan W., Li P.;
"Transcription factor Foxo3a prevents apoptosis by regulating calcium
through the apoptosis repressor with caspase recruitment domain.";
J. Biol. Chem. 288:8491-8504(2013).
-!- FUNCTION: Apoptosis repressor that blocks multiple modes of cell
death. Inhibits extrinsic apoptotic pathways through two different
ways. Firstly by interacting with FAS and FADD upon FAS activation
blocking death-inducing signaling complex (DISC) assembly
(PubMed:15383280). Secondly by interacting with CASP8 in a
mitochondria localization- and phosphorylation-dependent manner,
limiting the amount of soluble CASP8 available for DISC-mediated
activation (PubMed:12191471). Inhibits intrinsic apoptotic pathway
in response to a wide range of stresses, through its interaction
with BAX resulting in BAX inactivation, preventing mitochondrial
dysfunction and release of pro-apoptotic factors
(PubMed:15383280). Inhibits calcium-mediated cell death by
functioning as a cytosolic calcium buffer, dissociating its
interaction with CASP8 and maintaining calcium homeostasis
(PubMed:23382383). Negatively regulates oxidative stress-induced
apoptosis by phosphorylation-dependent suppression of the
mitochondria-mediated intrinsic pathway, by blocking CASP2
activation and BAX translocation (PubMed:16639714). Negatively
regulates hypoxia-induced apoptosis in part by inhibiting the
release of cytochrome c from mitochondria in a caspase-independent
manner (PubMed:10590251). Also inhibits TNF-induced necrosis by
preventing TNF-signaling pathway through TNFRSF1A interaction
abrogating the recruitment of RIPK1 to complex I (By similarity).
Finally through its role as apoptosis repressor, promotes vascular
remodeling through inhibition of apoptosis and stimulation of
proliferation, in response to hypoxia (By similarity). Inhibits
too myoblast differentiation through caspase inhibition
(PubMed:17292893). {ECO:0000250|UniProtKB:O60936,
ECO:0000250|UniProtKB:Q9D1X0, ECO:0000269|PubMed:10590251,
ECO:0000269|PubMed:12191471, ECO:0000269|PubMed:15383280,
ECO:0000269|PubMed:16639714, ECO:0000269|PubMed:17292893,
ECO:0000269|PubMed:23382383}.
-!- SUBUNIT: Oligomerizes (via CARD doamin) (By similarity). Interacts
(via CARD domain) with CASP2; inhibits CASP2 activity in a
phosphorylation-dependent manner. Interacts with CASP8; decreases
CASP8 activity in a mitochondria localization- and
phosphorylation-dependent manner and this interaction is
dissociated by calcium. Interacts with TFPT; translocates NOL3
into the nucleus and negatively regulated TFPT-induced cell death.
Interacts directly (via CARD domain) with FAS and FADD (via DED
domain); inhibits death-inducing signaling complex (DISC) assembly
by inhibiting the increase in FAS-FADD binding induced by FAS
activation. Interacts (via CARD domain) with BAX (via a C-terminal
33 residues); inhibits BAX activation and translocation and
consequently cytochrome c release from mitochondria. Interacts
with PPM1G; may dephosphorylate NOL3. Interacts (via CARD domain)
with BBC3 (via BH3 domain); preventing the association of BBC3
with BCL2 and resulting in activation of CASP8. Interacts (via
CARD domain) with BAD(via BH3 domain); preventing the association
of BAD with BCL2. Interacts directly (via CARD domain) with
TNFRSF1A; inhibits TNF-signaling pathway (By similarity).
{ECO:0000250|UniProtKB:O60936, ECO:0000250|UniProtKB:Q9D1X0,
ECO:0000269|PubMed:10644725, ECO:0000269|PubMed:15383280,
ECO:0000269|PubMed:16639714, ECO:0000269|PubMed:17998337,
ECO:0000305|PubMed:16639714}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60936,
ECO:0000269|PubMed:10590251, ECO:0000269|PubMed:12191471}.
Mitochondrion {ECO:0000269|PubMed:10590251,
ECO:0000269|PubMed:12191471, ECO:0000269|PubMed:16639714}.
Sarcoplasmic reticulum {ECO:0000269|PubMed:23382383}. Membrane
{ECO:0000250|UniProtKB:O60936}; Lipid-anchor
{ECO:0000250|UniProtKB:O60936}. Note=Phosphorylation at Thr-149
results in translocation to mitochondria (PubMed:12191471).
Colocalized with mitochondria in response to oxidative stress
(PubMed:16639714). {ECO:0000269|PubMed:12191471,
ECO:0000269|PubMed:16639714}.
-!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart and
medulla. {ECO:0000269|PubMed:10590251}.
-!- INDUCTION: Increased by chronic hypoxia (PubMed:22082675).
Activated by FOXO3 (PubMed:23382383). Negatively regulated by TP53
(PubMed:17998337). {ECO:0000269|PubMed:17998337,
ECO:0000269|PubMed:22082675, ECO:0000269|PubMed:23382383}.
-!- DOMAIN: CARD is critical for both extrinsic and intrinsic
apoptotic pathways (PubMed:15383280). CARD domain mediates a
protective effect against myocardial ischemia/reperfusion,
oxidative stress and TNF-induced necrosis (By similarity). The
calcium binding domain plays a protective role in calcium-mediated
cell death (By similarity). {ECO:0000250|UniProtKB:O60936,
ECO:0000250|UniProtKB:Q9D1X0, ECO:0000269|PubMed:15383280}.
-!- PTM: Phosphorylation at Thr-149 is required for its antiapoptotic
effect by blocking death-inducing signaling complex (DISC)
activity through the control of interaction with CASP8.
Phosphorylation at Thr-149 results in translocation to
mitochondria and this translocation enables the binding to CASP8
(PubMed:12191471). Dephosphorylated at Thr-149 by calcineurin;
doesn't inhibit the association between FADD and CASP8 and the
consequent apoptosis (PubMed:19001025).
{ECO:0000269|PubMed:12191471, ECO:0000269|PubMed:19001025}.
-!- PTM: Polyubiquitinated by MDM2; promoting proteasomal-dependent
degradation in response to apoptotic stimuli.
{ECO:0000250|UniProtKB:O60936, ECO:0000269|PubMed:17142834}.
-----------------------------------------------------------------------
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EMBL; U40627; AAB05667.1; -; mRNA.
PIR; S70009; S70009.
RefSeq; NP_445968.2; NM_053516.2.
UniGene; Rn.86956; -.
ProteinModelPortal; Q62881; -.
SMR; Q62881; -.
IntAct; Q62881; 1.
iPTMnet; Q62881; -.
PhosphoSitePlus; Q62881; -.
PaxDb; Q62881; -.
PRIDE; Q62881; -.
GeneID; 85383; -.
KEGG; rno:85383; -.
UCSC; RGD:708558; rat.
CTD; 8996; -.
RGD; 708558; Nol3.
eggNOG; ENOG410J0R1; Eukaryota.
eggNOG; ENOG4111BHK; LUCA.
HOGENOM; HOG000113820; -.
HOVERGEN; HBG029007; -.
InParanoid; Q62881; -.
PhylomeDB; Q62881; -.
PRO; PR:Q62881; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0016529; C:sarcoplasmic reticulum; IDA:UniProtKB.
GO; GO:0089720; F:caspase binding; IPI:UniProtKB.
GO; GO:0035877; F:death effector domain binding; IPI:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019902; F:phosphatase binding; IPI:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
GO; GO:0097340; P:inhibition of cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0045445; P:myoblast differentiation; IDA:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IMP:UniProtKB.
GO; GO:1903073; P:negative regulation of death-inducing signaling complex assembly; IDA:UniProtKB.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:UniProtKB.
GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IDA:UniProtKB.
GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; IDA:UniProtKB.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0051562; P:negative regulation of mitochondrial calcium ion concentration; IDA:UniProtKB.
GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; IDA:UniProtKB.
GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; TAS:RGD.
GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IMP:UniProtKB.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0048659; P:smooth muscle cell proliferation; IMP:UniProtKB.
InterPro; IPR001315; CARD.
InterPro; IPR011029; DEATH-like_dom.
Pfam; PF00619; CARD; 1.
SMART; SM00114; CARD; 1.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50209; CARD; 1.
1: Evidence at protein level;
Calcium; Complete proteome; Cytoplasm; Lipoprotein; Membrane;
Metal-binding; Mitochondrion; mRNA processing; Myristate;
Phosphoprotein; Reference proteome; Sarcoplasmic reticulum;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O60936}.
CHAIN 2 221 Nucleolar protein 3.
/FTId=PRO_0000144101.
DOMAIN 4 95 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
REGION 20 70 Essential for interaction with BAX.
{ECO:0000269|PubMed:15383280}.
COMPBIAS 107 219 Glu/Pro-rich.
MOD_RES 149 149 Phosphothreonine; by CK2.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:12191471}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000250|UniProtKB:O60936}.
MUTAGEN 31 31 L->F: Failed to protect against extrinsic
and intrinsic apoptotic pathways; when
associated with R-69. Not interferes with
death-inducing signaling complex (DISC)
assembly; when associated with R-69.
Promotes BAX activation; when associated
with R-69. {ECO:0000269|PubMed:15383280}.
MUTAGEN 69 69 G->R: Failed to protect against extrinsic
and intrinsic apoptotic pathways; when
associated with F-31. Not interferes with
DISC assembly; when associated with F-31.
Promotes BAX activation; when associated
with F-31. {ECO:0000269|PubMed:15383280}.
MUTAGEN 149 149 T->A: Not phosphorylated by CK2. Loses
the ability to block CASP8-, FAS-, or
TNFRSF1A-induced apoptosis. Prevents
translocation to mitochondria.
Significantly decreases resistance to
hydrogen peroxide-induced cell death.
Doesn't interact with PPM1G, BAX and
CASP2. Doesn't inhibit CASP2 and CASP3
activation. Doesn't was inhibit CASP8-
induced apoptosis.
{ECO:0000269|PubMed:12191471,
ECO:0000269|PubMed:16639714,
ECO:0000269|PubMed:19001025}.
MUTAGEN 149 149 T->D: Significantly enhances resistance
against hydrogen peroxide- and induced by
isoproterenol or aldosterone-induced cell
death. {ECO:0000269|PubMed:16639714,
ECO:0000269|PubMed:19001025}.
SEQUENCE 221 AA; 24577 MW; A7661C9040B2CD4D CRC64;
MGNMQERPSE TIDRERKRLV ETLQADSGLL LDALVARGVL TGPEYEALDA LPDAERRVRR
LLLLVQSKGE AACQELLRCA QQTVSMPDPA WDWQHVGPGY RDRSYDPPCP GHWTPEAPSS
GTTCPGLPRA SEEEEIGGPE DSEAVQPRTP EEPELEAEAT KGDEPDLEQE MEPEPEPEVE
PEPEPEPEPE PEPEPEPEPE PEPEREPDFQ EGDESEGCEN T


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