BAG4_MOUSE
ID BAG4_MOUSE Reviewed; 457 AA.
AC Q8CI61; Q3TRL9; Q91VT5; Q9CWG2;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=BAG family molecular chaperone regulator 4;
DE Short=BAG-4;
DE AltName: Full=Bcl-2-associated athanogene 4;
DE AltName: Full=Silencer of death domains;
GN Name=Bag4; Synonyms=Sodd;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LEU-387; LEU-416 AND ALA-441,
RP AND INTERACTION WITH TNFRSF1A AND HSP70.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=11909948; DOI=10.1128/mcb.22.8.2536-2543.2002;
RA Miki K., Eddy E.M.;
RT "Tumor necrosis factor receptor 1 is an ATPase regulated by silencer of
RT death domain.";
RL Mol. Cell. Biol. 22:2536-2543(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Embryonic stem cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-54, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting
CC substrate release. Prevents constitutive TNFRSF1A signaling (By
CC similarity). Negative regulator of PRKN translocation to damaged
CC mitochondria (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds to
CC the death domain of TNFRSF12 (By similarity). Binds to the death domain
CC of TNFRSF1A in the absence of TNF and thereby prevents binding of
CC adapter molecules such as TRADD or TRAF2. Interacts with PRKN (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37239.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF332863; AAL99586.1; -; mRNA.
DR EMBL; AK010765; BAB27167.1; -; mRNA.
DR EMBL; AK136899; BAE23161.1; -; mRNA.
DR EMBL; AK162658; BAE37009.1; -; mRNA.
DR EMBL; BC009102; AAH09102.1; -; mRNA.
DR EMBL; BC037239; AAH37239.1; ALT_INIT; mRNA.
DR EMBL; BC058518; AAH58518.1; -; mRNA.
DR CCDS; CCDS22201.1; -.
DR RefSeq; NP_080397.1; NM_026121.3.
DR AlphaFoldDB; Q8CI61; -.
DR SMR; Q8CI61; -.
DR BioGRID; 212150; 16.
DR STRING; 10090.ENSMUSP00000044725; -.
DR iPTMnet; Q8CI61; -.
DR PhosphoSitePlus; Q8CI61; -.
DR EPD; Q8CI61; -.
DR MaxQB; Q8CI61; -.
DR PaxDb; Q8CI61; -.
DR PRIDE; Q8CI61; -.
DR ProteomicsDB; 265201; -.
DR Antibodypedia; 4434; 416 antibodies from 43 providers.
DR DNASU; 67384; -.
DR Ensembl; ENSMUST00000038498; ENSMUSP00000044725; ENSMUSG00000037316.
DR GeneID; 67384; -.
DR KEGG; mmu:67384; -.
DR UCSC; uc009lgy.1; mouse.
DR CTD; 9530; -.
DR MGI; MGI:1914634; Bag4.
DR VEuPathDB; HostDB:ENSMUSG00000037316; -.
DR eggNOG; KOG4361; Eukaryota.
DR GeneTree; ENSGT00940000158936; -.
DR HOGENOM; CLU_051025_0_0_1; -.
DR InParanoid; Q8CI61; -.
DR OMA; YQPKDQQ; -.
DR OrthoDB; 1392346at2759; -.
DR PhylomeDB; Q8CI61; -.
DR TreeFam; TF102013; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-75893; TNF signaling.
DR BioGRID-ORCS; 67384; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Bag4; mouse.
DR PRO; PR:Q8CI61; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8CI61; protein.
DR Bgee; ENSMUSG00000037316; Expressed in primary oocyte and 246 other tissues.
DR ExpressionAtlas; Q8CI61; baseline and differential.
DR Genevisible; Q8CI61; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
DR GO; GO:2001145; P:negative regulation of phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IDA:UniProtKB.
DR GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; ISO:MGI.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0097178; P:ruffle assembly; IMP:UniProtKB.
DR Gene3D; 1.20.58.120; -; 1.
DR InterPro; IPR039773; BAG_chaperone_regulator.
DR InterPro; IPR036533; BAG_dom_sf.
DR InterPro; IPR003103; BAG_domain.
DR PANTHER; PTHR12329; PTHR12329; 1.
DR Pfam; PF02179; BAG; 1.
DR SMART; SM00264; BAG; 1.
DR SUPFAM; SSF63491; SSF63491; 1.
DR PROSITE; PS51035; BAG; 1.
PE 1: Evidence at protein level;
KW Chaperone; Cytoplasm; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..457
FT /note="BAG family molecular chaperone regulator 4"
FT /id="PRO_0000088871"
FT DOMAIN 379..456
FT /note="BAG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..51
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95429"
FT MOD_RES 41
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O95429"
FT MOD_RES 54
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 108
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O95429"
FT MOD_RES 185
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O95429"
FT MUTAGEN 387
FT /note="L->P: Abolishes interaction with HSP70 and
FT TNFRSF1A."
FT /evidence="ECO:0000269|PubMed:11909948"
FT MUTAGEN 416
FT /note="L->P: Abolishes interaction with HSP70 and
FT TNFRSF1A."
FT /evidence="ECO:0000269|PubMed:11909948"
FT MUTAGEN 441
FT /note="A->P: Abolishes interaction with HSP70 and
FT TNFRSF1A."
FT /evidence="ECO:0000269|PubMed:11909948"
SQ 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
