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BAG family molecular chaperone regulator 4 (BAG-4) (Bcl-2-associated athanogene 4) (Silencer of death domains)

 BAG4_MOUSE              Reviewed;         457 AA.
Q8CI61; Q3TRL9; Q91VT5; Q9CWG2;
09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
09-MAY-2003, sequence version 2.
23-MAY-2018, entry version 124.
RecName: Full=BAG family molecular chaperone regulator 4;
Short=BAG-4;
AltName: Full=Bcl-2-associated athanogene 4;
AltName: Full=Silencer of death domains;
Name=Bag4; Synonyms=Sodd;
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], MUTAGENESIS OF LEU-387; LEU-416 AND
ALA-441, AND INTERACTION WITH TNFRSF1A AND HSP70.
STRAIN=BALB/cJ; TISSUE=Testis;
PubMed=11909948; DOI=10.1128/MCB.22.8.2536-2543.2002;
Miki K., Eddy E.M.;
"Tumor necrosis factor receptor 1 is an ATPase regulated by silencer
of death domain.";
Mol. Cell. Biol. 22:2536-2543(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Diencephalon, and Embryonic stem cell;
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].
STRAIN=FVB/N; TISSUE=Brain, and Mammary gland;
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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-54, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by
promoting substrate release. Prevents constitutive TNFRSF1A
signaling (By similarity). Negative regulator of PRKN
translocation to damaged mitochondria (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds
to the death domain of TNFRSF12 (By similarity). Binds to the
death domain of TNFRSF1A in the absence of TNF and thereby
prevents binding of adapter molecules such as TRADD or TRAF2.
Interacts with PRKN (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SEQUENCE CAUTION:
Sequence=AAH37239.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF332863; AAL99586.1; -; mRNA.
EMBL; AK010765; BAB27167.1; -; mRNA.
EMBL; AK136899; BAE23161.1; -; mRNA.
EMBL; AK162658; BAE37009.1; -; mRNA.
EMBL; BC009102; AAH09102.1; -; mRNA.
EMBL; BC037239; AAH37239.1; ALT_INIT; mRNA.
EMBL; BC058518; AAH58518.1; -; mRNA.
CCDS; CCDS22201.1; -.
RefSeq; NP_080397.1; NM_026121.3.
UniGene; Mm.118400; -.
ProteinModelPortal; Q8CI61; -.
SMR; Q8CI61; -.
BioGrid; 212150; 2.
STRING; 10090.ENSMUSP00000044725; -.
iPTMnet; Q8CI61; -.
PhosphoSitePlus; Q8CI61; -.
EPD; Q8CI61; -.
MaxQB; Q8CI61; -.
PaxDb; Q8CI61; -.
PRIDE; Q8CI61; -.
Ensembl; ENSMUST00000038498; ENSMUSP00000044725; ENSMUSG00000037316.
GeneID; 67384; -.
KEGG; mmu:67384; -.
UCSC; uc009lgy.1; mouse.
CTD; 9530; -.
MGI; MGI:1914634; Bag4.
eggNOG; KOG4361; Eukaryota.
eggNOG; ENOG4111WNH; LUCA.
GeneTree; ENSGT00530000063256; -.
HOGENOM; HOG000290673; -.
HOVERGEN; HBG004809; -.
InParanoid; Q8CI61; -.
KO; K09558; -.
OMA; PAETTWP; -.
OrthoDB; EOG091G08LY; -.
PhylomeDB; Q8CI61; -.
TreeFam; TF102013; -.
Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-MMU-75893; TNF signaling.
PRO; PR:Q8CI61; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000037316; -.
CleanEx; MM_BAG4; -.
ExpressionAtlas; Q8CI61; baseline and differential.
Genevisible; Q8CI61; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0051087; F:chaperone binding; IEA:InterPro.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:UniProtKB.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
GO; GO:0090367; P:negative regulation of mRNA modification; IEA:Ensembl.
GO; GO:2001145; P:negative regulation of phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IDA:UniProtKB.
GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; ISO:MGI.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0097178; P:ruffle assembly; IMP:UniProtKB.
Gene3D; 1.20.58.120; -; 1.
InterPro; IPR036533; BAG_dom_sf.
InterPro; IPR003103; BAG_domain.
Pfam; PF02179; BAG; 1.
SMART; SM00264; BAG; 1.
SUPFAM; SSF63491; SSF63491; 1.
PROSITE; PS51035; BAG; 1.
1: Evidence at protein level;
Chaperone; Complete proteome; Cytoplasm; Methylation; Phosphoprotein;
Reference proteome.
CHAIN 1 457 BAG family molecular chaperone regulator
4.
/FTId=PRO_0000088871.
DOMAIN 379 456 BAG. {ECO:0000255|PROSITE-
ProRule:PRU00369}.
COMPBIAS 29 298 Pro-rich.
MOD_RES 7 7 Phosphoserine.
{ECO:0000250|UniProtKB:O95429}.
MOD_RES 41 41 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:O95429}.
MOD_RES 54 54 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 108 108 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:O95429}.
MOD_RES 185 185 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:O95429}.
MUTAGEN 387 387 L->P: Abolishes interaction with HSP70
and TNFRSF1A.
{ECO:0000269|PubMed:11909948}.
MUTAGEN 416 416 L->P: Abolishes interaction with HSP70
and TNFRSF1A.
{ECO:0000269|PubMed:11909948}.
MUTAGEN 441 441 A->P: Abolishes interaction with HSP70
and TNFRSF1A.
{ECO:0000269|PubMed:11909948}.
SEQUENCE 457 AA; 49095 MW; 5A70275BD42A6E20 CRC64;
MSALRRSGYG PSDGPSYGRY YGPGGGDVPV HVPPPLYPPL RPEPPQPPVS WRGRGGAPAE
TTWPGEGAGG DGYYPSGGAW AEASRAGGGH QEQPPYPGYN SNYWNSVRPR APYPGSYSVR
PELQGQSLNS YANGAYGPPY PPGPGASTAS YSGAYYVPGY TQSNYSTEVP NTYRSPGNSP
TPMSRWMYSQ QDCPTEAPPL RGQVPGYPAS QNPGMTLPHY PYGDGNRAVP QSGGTGRPQD
DAWASSAYGM GARYPWPSAA PSAPSAGSLY MTESASPWPG NSSPQPPPSP PPQQPKDPSY
SYNPSGQGLS RHSFPCSVHQ YESPGAVNND NSDLLDSQVQ YSAEPQLYGN ASSEHPSNQV
PSNNLPEECF SSDEGTPPSI KKIIHVLEKV QFLEQEVEEF VGKKTDKAYW LLEEMLTKEL
LELDSVETGG QDSVRQARKE AVCKIQAILE KLEKKGL


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