Nol3
entrez
85383
canonical
uniprot
Q62881
canonical
ensembl
ENSRNOG00000015588
resolver
ensp
ENSRNOP00000020908
resolver
genesymbol
Nol3
resolver
genesymbol_syn
Arc
resolver
uniprot_entry
NOL3_RAT
resolver
amino_acid_sequence
MGNMQERPSETIDRERKRLVETLQADSGLLLDALVARGVLTGPEYEALDALPDAERRVRRLLLLVQSKGEAACQELLRCAQQTVSMPDPAWDWQHVGPGYRDRSYDPPCPGHWTPEAPSSGTTCPGLPRASEEEEIGGPEDSEAVQPRTPEEPELEAEATKGDEPDLEQEMEPEPEPEVEPEPEPEPEPEPEPEPEPEPEPEPEREPDFQEGDESEGCENT
uniprot
proteins
function
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}.
uniprot
proteins
mass_dalton
24577
uniprot
proteins
mutagenesis
MUTAGEN 31; /note="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."; /evidence="ECO:0000269|PubMed:15383280"; MUTAGEN 69; /note="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."; /evidence="ECO:0000269|PubMed:15383280"; MUTAGEN 149; /note="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."; /evidence="ECO:0000269|PubMed:12191471, ECO:0000269|PubMed:16639714, ECO:0000269|PubMed:19001025"; MUTAGEN 149; /note="T->D: Significantly enhances resistance against hydrogen peroxide- and induced by isoproterenol or aldosterone-induced cell death."; /evidence="ECO:0000269|PubMed:16639714, ECO:0000269|PubMed:19001025
uniprot
proteins
post_translational_modification
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}.
uniprot
proteins
pubmed
10590251
uniprot
proteins
pubmed
10644725
uniprot
proteins
pubmed
12191471
uniprot
proteins
pubmed
15383280
uniprot
proteins
pubmed
16639714
uniprot
proteins
pubmed
17142834
uniprot
proteins
pubmed
17292893
uniprot
proteins
pubmed
17998337
uniprot
proteins
pubmed
19001025
uniprot
proteins
pubmed
22082675
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
23382383
uniprot
proteins
pubmed
8634331
uniprot
proteins
sequence_length
221
uniprot
proteins
subcellular_location
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}.
uniprot
proteins