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Protein phosphatase 1 regulatory subunit 15A (Growth arrest and DNA damage-inducible protein GADD34) (Myeloid differentiation primary response protein MyD116 homolog) (Progression elevated gene 3 protein) (PEG-3)

 PR15A_RAT               Reviewed;         578 AA.
Q6IN02; O88344; Q7TQC2;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 2.
23-MAY-2018, entry version 78.
RecName: Full=Protein phosphatase 1 regulatory subunit 15A;
AltName: Full=Growth arrest and DNA damage-inducible protein GADD34;
AltName: Full=Myeloid differentiation primary response protein MyD116 homolog;
AltName: Full=Progression elevated gene 3 protein;
Short=PEG-3;
Name=Ppp1r15a; Synonyms=Gadd34, Myd116, Peg3;
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;
PubMed=9256446; DOI=10.1073/pnas.94.17.9125;
Su Z.-Z., Shi Y., Fisher P.B.;
"Subtraction hybridization identifies a transformation progression-
associated gene PEG-3 with sequence homology to a growth arrest and
DNA damage-inducible gene.";
Proc. Natl. Acad. Sci. U.S.A. 94:9125-9130(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT PEG-3.
STRAIN=Sprague-Dawley;
PubMed=12813455; DOI=10.1038/sj.onc.1206567;
Hollander M.C., Poola-Kella S., Fornace A.J. Jr.;
"Gadd34 functional domains involved in growth suppression and
apoptosis.";
Oncogene 22:3827-3832(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
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]
INDUCTION.
PubMed=8139541; DOI=10.1128/MCB.14.4.2361;
Zhan Q., Lord K.A., Alamo I. Jr., Hollander M.C., Carrier F., Ron D.,
Kohn K.W., Hoffman B., Liebermann D.A., Fornace A.J. Jr.;
"The gadd and MyD genes define a novel set of mammalian genes encoding
acidic proteins that synergistically suppress cell growth.";
Mol. Cell. Biol. 14:2361-2371(1994).
[5]
MUTANT PEG-3.
PubMed=10611347; DOI=10.1073/pnas.96.26.15115;
Su Z.-Z., Goldstein N.I., Jiang H., Wang M.-N., Duigou G.J.,
Young C.S.H., Fisher P.B.;
"PEG-3, a nontransforming cancer progression gene, is a positive
regulator of cancer aggressiveness and angiogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 96:15115-15120(1999).
[6]
FUNCTION, AND MUTANT PEG-3.
PubMed=15674324; DOI=10.1038/sj.onc.1208420;
Su Z.-Z., Emdad L., Sarkar D., Randolph A., Valerie K., Yacoub A.,
Dent P., Fisher P.B.;
"Potential molecular mechanism for rodent tumorigenesis: mutational
generation of Progression Elevated Gene-3 (PEG-3).";
Oncogene 24:2247-2255(2005).
-!- FUNCTION: Recruits the serine/threonine-protein phosphatase PP1 to
dephosphorylate the translation initiation factor eIF-2A/EIF2S1,
thereby reversing the shut-off of protein synthesis initiated by
stress-inducible kinases and facilitating recovery of cells from
stress. Down-regulates the TGF-beta signaling pathway by promoting
dephosphorylation of TGFB1 by PP1. May promote apoptosis by
inducing TP53 phosphorylation on 'Ser-15'.
{ECO:0000269|PubMed:15674324}.
-!- SUBUNIT: Interacts with PCNA. Interacts with LYN and KMT2A/MLL1.
Interacts with PP1, PPP1R1A and SMARCB1. Interacts with SMAD7.
Interacts with BAG1 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:O75807}.
Mitochondrion outer membrane; Peripheral membrane protein;
Cytoplasmic side {ECO:0000250|UniProtKB:O75807}. Note=Associates
with membranes via an N-terminal amphipathic intramembrane region.
{ECO:0000250|UniProtKB:O75807}.
-!- INDUCTION: By lipopolysaccharide. {ECO:0000269|PubMed:8139541}.
-!- PTM: Phosphorylated at multiple Ser/Thr residues. Phosphorylated
on tyrosine by LYN; which impairs its antiproliferative activity.
Phosphorylation at Tyr-236 enhances proteasomal degradation, this
position is dephosphorylated by PTPN2.
{ECO:0000250|UniProtKB:O75807}.
-!- PTM: Polyubiquitinated. Exhibits a rapid proteasomal degradation
with a half-life under 1 hour, ubiquitination depends on
endoplasmic reticulum association. {ECO:0000250|UniProtKB:O75807}.
-!- SIMILARITY: Belongs to the PPP1R15 family. {ECO:0000305}.
-!- CAUTION: The sequence described initially (PubMed:9256446)
corresponds to a mutant, frameshifted form named PEG-3 that
frequently arises during cell transformation and does not seem to
exist in normal cells. PEG-3 functions as a dominant negative of
GADD34-mediated pro-apoptotic pathway and promotes cancer
aggressiveness. {ECO:0000305|PubMed:9256446}.
-!- SEQUENCE CAUTION:
Sequence=AAC24980.1; Type=Frameshift; Positions=416, 504, 577; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF020618; AAC24980.1; ALT_FRAME; mRNA.
EMBL; AY128642; AAM77795.1; -; Genomic_DNA.
EMBL; BC072513; AAH72513.1; -; mRNA.
RefSeq; NP_598230.2; NM_133546.3.
UniGene; Rn.2232; -.
SMR; Q6IN02; -.
STRING; 10116.ENSRNOP00000048451; -.
PaxDb; Q6IN02; -.
PRIDE; Q6IN02; -.
GeneID; 171071; -.
KEGG; rno:171071; -.
CTD; 23645; -.
RGD; 621526; Ppp1r15a.
eggNOG; ENOG410ITE6; Eukaryota.
eggNOG; ENOG410Y1YJ; LUCA.
HOGENOM; HOG000060154; -.
HOVERGEN; HBG052542; -.
InParanoid; Q6IN02; -.
KO; K14019; -.
PhylomeDB; Q6IN02; -.
TreeFam; TF105547; -.
PRO; PR:Q6IN02; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0008157; F:protein phosphatase 1 binding; IDA:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0071236; P:cellular response to antibiotic; IEP:RGD.
GO; GO:0072732; P:cellular response to calcium ion starvation; IEP:RGD.
GO; GO:0071322; P:cellular response to carbohydrate stimulus; IEP:RGD.
GO; GO:1904310; P:cellular response to cordycepin; IEP:RGD.
GO; GO:1904308; P:cellular response to desipramine; IEP:RGD.
GO; GO:0035690; P:cellular response to drug; IEP:RGD.
GO; GO:1904312; P:cellular response to gold(3+); IEP:RGD.
GO; GO:1904314; P:cellular response to methamphetamine hydrochloride; IEP:RGD.
GO; GO:0072703; P:cellular response to methyl methanesulfonate; IEP:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0090650; P:cellular response to oxygen-glucose deprivation; IEP:RGD.
GO; GO:0034644; P:cellular response to UV; IEP:RGD.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEP:RGD.
GO; GO:0060548; P:negative regulation of cell death; IMP:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:RGD.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IMP:RGD.
GO; GO:0010955; P:negative regulation of protein processing; IMP:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:RGD.
GO; GO:0045765; P:regulation of angiogenesis; IMP:RGD.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0042220; P:response to cocaine; IEP:RGD.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:RGD.
GO; GO:0090648; P:response to environmental enrichment; IEP:RGD.
GO; GO:0035902; P:response to immobilization stress; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
InterPro; IPR019523; Prot_Pase1_reg-su15A/B_C.
Pfam; PF10488; PP1c_bdg; 1.
2: Evidence at transcript level;
Apoptosis; Complete proteome; Endoplasmic reticulum; Membrane;
Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
Reference proteome; Repeat; Stress response; Translation regulation;
Ubl conjugation.
CHAIN 1 578 Protein phosphatase 1 regulatory subunit
15A.
/FTId=PRO_0000320519.
TOPO_DOM 1 21 Cytoplasmic.
{ECO:0000250|UniProtKB:O75807}.
INTRAMEM 22 39 Helical. {ECO:0000250|UniProtKB:O75807}.
TOPO_DOM 40 578 Cytoplasmic.
{ECO:0000250|UniProtKB:O75807}.
REPEAT 279 318 1.
REPEAT 319 357 2.
REPEAT 358 375 3.
REGION 1 165 Required for localization in the
endoplasmic reticulum. {ECO:0000250}.
REGION 279 375 3 X approximate repeats.
REGION 319 417 Interaction with SMAD7. {ECO:0000250}.
REGION 363 462 Interaction with KMT2A/MLL1.
{ECO:0000250}.
REGION 443 490 Interaction with SMARCB1. {ECO:0000250}.
COMPBIAS 294 297 Poly-Glu.
COMPBIAS 534 537 Poly-Ser.
MOD_RES 236 236 Phosphotyrosine.
{ECO:0000250|UniProtKB:O75807}.
MOD_RES 365 365 Phosphotyrosine.
{ECO:0000250|UniProtKB:O75807}.
MOD_RES 419 419 Phosphotyrosine.
{ECO:0000250|UniProtKB:O75807}.
CONFLICT 347 348 AS -> TA (in Ref. 3; AAH72513).
{ECO:0000305}.
CONFLICT 453 453 D -> G (in Ref. 1; AAC24980).
{ECO:0000305}.
SEQUENCE 578 AA; 63570 MW; 923EC49921C0BC61 CRC64;
MAPSPRPQHV LHWKEAHSFY LLSPLMGFLS RAWSRLRGPE VSEAWLAETV AGANQIEADA
LLTPPPVSEN HLPLRETEGN GTPEWSKAAQ RLCLDVEAQS SPPKTWGLSD IDEHNGKPGQ
DGLREQEVEH TAGLPTLQPL HLQGADKKVG EVVAREEGVS ELAYPTSHWE GGPAEDEEDT
ETVKKAHQAS AASIAPGYKP STSVYCPGEA EHRATEEKGT DNKAEPSGSH SRVWEYHTRE
RPKQEGETKP EQHRAGQSHP CQNAEAEEGG PETSVCSGSA FLKAWVYRPG EDTEEEEDSD
LDSAEEDTAH TCTTPHTSAF LKAWVYRPGE DTEEEDDGDW DSAEEDASQS CTTPHTSAFL
KAWVYRPGED TEEEDDSENV APVDSETVDS CQSTQHCLPV EKTKGCGEAE PPPFQVAFYL
PGQKPAPPWA APKLPLRLQK RLRSFKAPAR NQDPEIPLKG RKVHFSEKVT VHFLAVWAGP
AQAARRGPWE QFARDRSRFA RRIAQAEEQL GPYLTPAFRA RAWTRLRNLP LPLSSSSLPL
PEPCSSTEAT PLSQDVTTPS PLPSEIPPPS LDLGGRRG


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