ID   BAG3_MOUSE              Reviewed;         577 AA.
AC   Q9JLV1; Q9CQL3; Q9JJC7;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=BAG family molecular chaperone regulator 3;
DE            Short=BAG-3;
DE   AltName: Full=Bcl-2-associated athanogene 3;
DE   AltName: Full=Bcl-2-binding protein Bis;
GN   Name=Bag3; Synonyms=Bis; ORFNames=MNCb-2243;
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].
RX   PubMed=10597216; DOI=10.1038/sj.onc.1203043;
RA   Lee J.H., Takahashi T., Yasuhara N., Inazawa J., Kamada S., Tsujimoto Y.;
RT   "Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing cell
RT   death.";
RL   Oncogene 18:6183-6190(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT   oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone, Pancreas, and Testis;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297 AND SER-390, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; THR-291; SER-297;
RP   SER-380; SER-382 AND SER-390, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen, and
RC   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   [7]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-141 AND ARG-267, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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).
RN   [8]
RP   STRUCTURE BY NMR OF 404-503.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the murine BAG domain of Bcl2-associated athanogene
RT   3.";
RL   Submitted (FEB-2004) to the PDB data bank.
CC   -!- FUNCTION: Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as
CC       a nucleotide-exchange factor (NEF) promoting the release of ADP from
CC       the HSP70 and HSC70 proteins thereby triggering client/substrate
CC       protein release. Nucleotide release is mediated via its binding to the
CC       nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate
CC       release is mediated via its binding to the substrate-binding domain
CC       (SBD) of HSPA8/HSC70. Has anti-apoptotic activity. Plays a role in the
CC       HSF1 nucleocytoplasmic transport. {ECO:0000250|UniProtKB:O95817}.
CC   -!- SUBUNIT: Binds to the ATPase domain of HSP70/HSC70 chaperones.
CC       Interacts with BCL2. Interacts with phospholipase C-gamma proteins.
CC       Interacts with DNAJB6. Interacts (via BAG domain) with HSF1; this
CC       interaction occurs in normal and heat-shocked cells. Interacts with
CC       HSPA8 (via NBD), HSPA1A (via NBD) and HSPA1B (via NBD). Interacts (via
CC       WW domain 1) with SYNPO2 (via PPPY motif).
CC       {ECO:0000250|UniProtKB:O95817}.
CC   -!- INTERACTION:
CC       Q9JLV1; Q8AZK7: EBNA-LP; Xeno; NbExp=2; IntAct=EBI-309231, EBI-1185167;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95817}. Cytoplasm
CC       {ECO:0000250|UniProtKB:O95817}. Note=Colocalizes with HSF1 to the
CC       nucleus upon heat stress. {ECO:0000250|UniProtKB:O95817}.
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DR   EMBL; AF130471; AAF26840.1; -; mRNA.
DR   EMBL; AB041583; BAA95066.1; -; mRNA.
DR   EMBL; AK007414; BAB25024.1; -; mRNA.
DR   EMBL; AK016510; BAB30278.1; -; mRNA.
DR   EMBL; AK036675; BAC29531.1; -; mRNA.
DR   EMBL; CH466531; EDL17651.1; -; Genomic_DNA.
DR   CCDS; CCDS21898.1; -.
DR   RefSeq; NP_038891.4; NM_013863.5.
DR   PDB; 1UK5; NMR; -; A=406-503.
DR   PDBsum; 1UK5; -.
DR   AlphaFoldDB; Q9JLV1; -.
DR   SMR; Q9JLV1; -.
DR   BioGRID; 205891; 71.
DR   IntAct; Q9JLV1; 5.
DR   MINT; Q9JLV1; -.
DR   STRING; 10090.ENSMUSP00000033136; -.
DR   GlyGen; Q9JLV1; 9 sites, 1 O-linked glycan (9 sites).
DR   iPTMnet; Q9JLV1; -.
DR   PhosphoSitePlus; Q9JLV1; -.
DR   SwissPalm; Q9JLV1; -.
DR   jPOST; Q9JLV1; -.
DR   MaxQB; Q9JLV1; -.
DR   PaxDb; 10090-ENSMUSP00000033136; -.
DR   ProteomicsDB; 265200; -.
DR   Pumba; Q9JLV1; -.
DR   Antibodypedia; 18850; 547 antibodies from 40 providers.
DR   DNASU; 29810; -.
DR   Ensembl; ENSMUST00000033136.9; ENSMUSP00000033136.8; ENSMUSG00000030847.9.
DR   GeneID; 29810; -.
DR   KEGG; mmu:29810; -.
DR   UCSC; uc009jzb.2; mouse.
DR   AGR; MGI:1352493; -.
DR   CTD; 9531; -.
DR   MGI; MGI:1352493; Bag3.
DR   VEuPathDB; HostDB:ENSMUSG00000030847; -.
DR   eggNOG; KOG0940; Eukaryota.
DR   eggNOG; KOG4361; Eukaryota.
DR   GeneTree; ENSGT00940000159204; -.
DR   HOGENOM; CLU_034378_0_0_1; -.
DR   InParanoid; Q9JLV1; -.
DR   OMA; QKGEPSM; -.
DR   OrthoDB; 5353777at2759; -.
DR   TreeFam; TF102013; -.
DR   Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR   BioGRID-ORCS; 29810; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Bag3; mouse.
DR   EvolutionaryTrace; Q9JLV1; -.
DR   PRO; PR:Q9JLV1; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q9JLV1; Protein.
DR   Bgee; ENSMUSG00000030847; Expressed in cardiac muscle of left ventricle and 213 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0101031; C:protein folding chaperone complex; ISO:MGI.
DR   GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR   GO; GO:0051087; F:protein-folding chaperone binding; ISO:MGI.
DR   GO; GO:0000045; P:autophagosome assembly; IEA:Ensembl.
DR   GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:MGI.
DR   GO; GO:0034620; P:cellular response to unfolded protein; ISO:MGI.
DR   GO; GO:0061684; P:chaperone-mediated autophagy; IEA:Ensembl.
DR   GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
DR   GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:BHF-UCL.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; ISO:MGI.
DR   GO; GO:0010664; P:negative regulation of striated muscle cell apoptotic process; IMP:MGI.
DR   GO; GO:1905337; P:positive regulation of aggrephagy; ISO:MGI.
DR   GO; GO:0046827; P:positive regulation of protein export from nucleus; ISS:UniProtKB.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IMP:MGI.
DR   GO; GO:0010658; P:striated muscle cell apoptotic process; IMP:MGI.
DR   CDD; cd00201; WW; 1.
DR   Gene3D; 2.20.70.10; -; 1.
DR   Gene3D; 1.20.58.120; BAG domain; 1.
DR   InterPro; IPR039773; BAG_chaperone_regulator.
DR   InterPro; IPR036533; BAG_dom_sf.
DR   InterPro; IPR003103; BAG_domain.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR12329:SF12; BAG FAMILY MOLECULAR CHAPERONE REGULATOR 3; 1.
DR   PANTHER; PTHR12329; BCL2-ASSOCIATED ATHANOGENE; 1.
DR   Pfam; PF02179; BAG; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00264; BAG; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF63491; BAG domain; 1.
DR   SUPFAM; SSF51045; WW domain; 1.
DR   PROSITE; PS51035; BAG; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
DR   Genevisible; Q9JLV1; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Apoptosis; Chaperone; Cytoplasm;
KW   Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O95817"
FT   CHAIN           2..577
FT                   /note="BAG family molecular chaperone regulator 3"
FT                   /id="PRO_0000088869"
FT   DOMAIN          22..56
FT                   /note="WW 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          126..157
FT                   /note="WW 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT   DOMAIN          426..503
FT                   /note="BAG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          524..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..339
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..390
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95817"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         141
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         179
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95817"
FT   MOD_RES         204
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95817"
FT   MOD_RES         267
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         280
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95817"
FT   MOD_RES         281
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95817"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95817"
FT   MOD_RES         291
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         297
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         380
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         382
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         390
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   CROSSLNK        450
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O95817"
FT   CROSSLNK        450
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O95817"
FT   CONFLICT        74
FT                   /note="D -> N (in Ref. 1; AAF26840)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        527
FT                   /note="Q -> P (in Ref. 1; AAF26840)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        539
FT                   /note="K -> E (in Ref. 2; BAA95066)"
FT                   /evidence="ECO:0000305"
FT   STRAND          417..420
FT                   /evidence="ECO:0007829|PDB:1UK5"
FT   HELIX           425..445
FT                   /evidence="ECO:0007829|PDB:1UK5"
FT   STRAND          451..453
FT                   /evidence="ECO:0007829|PDB:1UK5"
FT   HELIX           454..471
FT                   /evidence="ECO:0007829|PDB:1UK5"
FT   HELIX           479..503
FT                   /evidence="ECO:0007829|PDB:1UK5"
SQ   SEQUENCE   577 AA;  61860 MW;  7BBF296A4A2EF7E3 CRC64;
     MSAATQSPMM QMASGNGASD RDPLPPGWEI KIDPQTGWPF FVDHNSRTTT WNDPRVPPEG
     PKDTASSANG PSRDGSRLLP IREGHPIYPQ LRPGYIPIPV LHEGSENRQP HLFHAYSQPG
     VQRFRTEAAA ATPQRSQSPL RGGMTEAAQT DKQCGQMPAT ATTAAAQPPT AHGPERSQSP
     AASDCSSSSS SASLPSSGRS SLGSHQLPRG YIPIPVIHEQ NITRPAAQPS FHQAQKTHYP
     AQQGEYQPQQ PVYHKIQGDD WEPRPLRAAS PFRSPVRGAS SREGSPARSG TPVHCPSPIR
     VHTVVDRPQP MTHREPPPVT QPENKPESKP GPAGPDLPPG HIPIQVIRRE ADSKPVSQKS
     PPPAEKVEVK VSSAPIPCPS PSPAPSAVPS PPKNVAAEQK AAPSPAPAEP AAPKSGEAET
     PPKHPGVLKV EAILEKVQGL EQAVDSFEGK KTDKKYLMIE EYLTKELLAL DSVDPEGRAD
     VRQARRDGVR KVQTILEKLE QKAIDVPGQV QVYELQPSNL EAEQPLQEIM GAVVADKDKK
     GPENKDPQTE SQQLEAKAAT PPNPSNPADS AGNLVAP
//