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Phorbol-12-myristate-13-acetate-induced protein 1 (Protein Noxa)

 APR_MOUSE               Reviewed;         103 AA.
Q9JM54;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 129.
RecName: Full=Phorbol-12-myristate-13-acetate-induced protein 1;
AltName: Full=Protein Noxa;
Name=Pmaip1; Synonyms=Noxa;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MCL1, SUBCELLULAR
LOCATION, FUNCTION, AND MUTAGENESIS OF LEU-27 AND LEU-78.
PubMed=10807576; DOI=10.1126/science.288.5468.1053;
Oda E., Ohki R., Murasawa H., Nemoto J., Shibue T., Yamashita T.,
Tokino T., Taniguchi T., Tanaka N.;
"Noxa, a BH3-only member of the Bcl-2 family and candidate mediator of
p53-induced apoptosis.";
Science 288:1053-1058(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Brain cortex, Dendritic cell, Kidney, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Limb;
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).
[4]
FUNCTION, AND INTERACTION WITH MCL1.
PubMed=15901672; DOI=10.1101/gad.1304105;
Willis S.N., Chen L., Dewson G., Wei A., Naik E., Fletcher J.I.,
Adams J.M., Huang D.C.S.;
"Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2,
until displaced by BH3-only proteins.";
Genes Dev. 19:1294-1305(2005).
[5]
FUNCTION, AND INTERACTION WITH MCL1.
PubMed=15694340; DOI=10.1016/j.molcel.2004.12.030;
Chen L., Willis S.N., Wei A., Smith B.J., Fletcher J.I., Hinds M.G.,
Colman P.M., Day C.L., Adams J.M., Huang D.C.S.;
"Differential targeting of prosurvival Bcl-2 proteins by their BH3-
only ligands allows complementary apoptotic function.";
Mol. Cell 17:393-403(2005).
[6]
FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=16822983; DOI=10.1523/JNEUROSCI.0196-06.2006;
Akhtar R.S., Geng Y., Klocke B.J., Latham C.B., Villunger A.,
Michalak E.M., Strasser A., Carroll S.L., Roth K.A.;
"BH3-only proapoptotic Bcl-2 family members Noxa and Puma mediate
neural precursor cell death.";
J. Neurosci. 26:7257-7264(2006).
[7]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 68-93 IN COMPLEX WITH MCL1,
STRUCTURE BY NMR OF 68-94 IN COMPLEX WITH MCL1, FUNCTION, INTERACTION
WITH MCL1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17389404; DOI=10.1073/pnas.0701297104;
Czabotar P.E., Lee E.F., van Delft M.F., Day C.L., Smith B.J.,
Huang D.C.S., Fairlie W.D., Hinds M.G., Colman P.M.;
"Structural insights into the degradation of Mcl-1 induced by BH3
domains.";
Proc. Natl. Acad. Sci. U.S.A. 104:6217-6222(2007).
-!- FUNCTION: Promotes activation of caspases and apoptosis. Promotes
mitochondrial membrane changes and efflux of apoptogenic proteins
from the mitochondria. Contributes to p53/TP53-dependent apoptosis
after radiation exposure. Promotes proteasomal degradation of
MCL1. Competes with BIM/BCL2L11 for binding to MCL1 and can
displace BIM/BCL2L11 from its binding site on MCL1 (By
similarity). Competes with BAK1 for binding to MCL1 and can
displace BAK1 from its binding site on MCL1. {ECO:0000250,
ECO:0000269|PubMed:10807576, ECO:0000269|PubMed:15694340,
ECO:0000269|PubMed:15901672, ECO:0000269|PubMed:16822983,
ECO:0000269|PubMed:17389404}.
-!- SUBUNIT: Interacts with MCL1, BCL2A1 and BAX. {ECO:0000250}.
-!- INTERACTION:
Q07820:MCL1 (xeno); NbExp=2; IntAct=EBI-709183, EBI-1003422;
P97287:Mcl1; NbExp=6; IntAct=EBI-709183, EBI-707292;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10807576}.
-!- TISSUE SPECIFICITY: Detected in thymocytes after irradiation with
X-rays. Not detectable in untreated thymocytes (at protein level).
Detected in embryonic neural precursor cells of the telencephalon
Constitutively expressed at low levels in adult brain, testis,
thymus, spleen, lung and kidney. {ECO:0000269|PubMed:16822983}.
-!- INDUCTION: Up-regulated after exposure to ionizing radiation and
other genotoxic agents. Up-regulation is mediated by p53.
{ECO:0000269|PubMed:16822983}.
-!- DOMAIN: The BH3 motif is essential for pro-apoptotic activity.
-!- SIMILARITY: Belongs to the PMAIP1 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AB041230; BAA95781.1; -; mRNA.
EMBL; AK043856; BAC31682.1; -; mRNA.
EMBL; AK088556; BAC40421.1; -; mRNA.
EMBL; AK143990; BAE25650.1; -; mRNA.
EMBL; AK169914; BAE41454.1; -; mRNA.
EMBL; BC050821; AAH50821.1; -; mRNA.
CCDS; CCDS29315.1; -.
RefSeq; NP_067426.1; NM_021451.2.
UniGene; Mm.271878; -.
PDB; 2JM6; NMR; -; A=68-93.
PDB; 2NLA; X-ray; 2.80 A; B=68-93.
PDB; 2ROD; NMR; -; B=17-42.
PDBsum; 2JM6; -.
PDBsum; 2NLA; -.
PDBsum; 2ROD; -.
ProteinModelPortal; Q9JM54; -.
SMR; Q9JM54; -.
BioGrid; 208439; 2.
DIP; DIP-45232N; -.
ELM; Q9JM54; -.
IntAct; Q9JM54; 4.
MINT; MINT-7965607; -.
STRING; 10090.ENSMUSP00000025399; -.
iPTMnet; Q9JM54; -.
PhosphoSitePlus; Q9JM54; -.
PaxDb; Q9JM54; -.
PRIDE; Q9JM54; -.
Ensembl; ENSMUST00000025399; ENSMUSP00000025399; ENSMUSG00000024521.
GeneID; 58801; -.
KEGG; mmu:58801; -.
UCSC; uc008fft.1; mouse.
CTD; 5366; -.
MGI; MGI:1930146; Pmaip1.
eggNOG; ENOG410J6XT; Eukaryota.
eggNOG; ENOG4111AWA; LUCA.
GeneTree; ENSGT00530000065105; -.
HOGENOM; HOG000034021; -.
HOVERGEN; HBG095669; -.
InParanoid; Q9JM54; -.
KO; K10131; -.
OMA; ADLKDEC; -.
OrthoDB; EOG091G1040; -.
TreeFam; TF339379; -.
Reactome; R-MMU-111448; Activation of NOXA and translocation to mitochondria.
Reactome; R-MMU-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
ChiTaRS; Pmaip1; mouse.
EvolutionaryTrace; Q9JM54; -.
PRO; PR:Q9JM54; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000024521; -.
Genevisible; Q9JM54; MM.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; ISO:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IMP:UniProtKB.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:MGI.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:ParkinsonsUK-UCL.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:MGI.
GO; GO:0010917; P:negative regulation of mitochondrial membrane potential; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
GO; GO:0043517; P:positive regulation of DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:MGI.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; IMP:MGI.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:UniProtKB.
GO; GO:0009411; P:response to UV; IMP:MGI.
GO; GO:0010165; P:response to X-ray; IMP:MGI.
GO; GO:0043029; P:T cell homeostasis; IMP:UniProtKB.
Gene3D; 1.10.437.10; -; 1.
InterPro; IPR036834; Blc2-like_sf.
InterPro; IPR024140; Noxa.
PANTHER; PTHR14299; PTHR14299; 1.
Pfam; PF15150; PMAIP1; 2.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Mitochondrion;
Reference proteome; Repeat.
CHAIN 1 103 Phorbol-12-myristate-13-acetate-induced
protein 1.
/FTId=PRO_0000333230.
REGION 90 99 Required for mitochondrial location.
{ECO:0000250}.
MOTIF 27 35 BH3 1.
MOTIF 78 86 BH3 2.
MUTAGEN 27 27 L->A: Loss of pro-apoptotic activity and
of targeting to mitochondria; when
associated with A-78.
{ECO:0000269|PubMed:10807576}.
MUTAGEN 78 78 L->A: Loss of pro-apoptotic activity and
of targeting to mitochondria; when
associated with A-27.
{ECO:0000269|PubMed:10807576}.
HELIX 22 39 {ECO:0000244|PDB:2ROD}.
HELIX 77 90 {ECO:0000244|PDB:2NLA}.
SEQUENCE 103 AA; 11566 MW; 9B9A5B04D5535E30 CRC64;
MPGRKARRNA PVNPTRAELP PEFAAQLRKI GDKVYCTWSA PDITVVLAQM PGKSQKSRMR
SPSPTRVPAD LKDECAQLRR IGDKVNLRQK LLNLISKLFN LVT


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