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   16-SEP-2015, entry version 129.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; 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.,
RA   Tsujimoto Y.;
RT   "Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing
RT   cell death.";
RL   Oncogene 18:6183-6190(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
RA   Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library
RT   made by 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   STRUCTURE BY NMR OF 404-503.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the murine BAG domain of Bcl2-associated
RT   athanogene 3.";
RL   Submitted (FEB-2004) to the PDB data bank.
CC   -!- FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by
CC       promoting substrate release. Has anti-apoptotic activity.
CC   -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds
CC       to Bcl-2 and PLC-gamma (By similarity). Interacts with DNAJB6 (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8AZK7:EBNA-LP (xeno); NbExp=2; IntAct=EBI-309231, EBI-1185167;
CC   -!- SIMILARITY: Contains 1 BAG domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00369}.
CC   -!- SIMILARITY: Contains 2 WW domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00224}.
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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   UniGene; Mm.84073; -.
DR   PDB; 1UK5; NMR; -; A=406-503.
DR   PDBsum; 1UK5; -.
DR   ProteinModelPortal; Q9JLV1; -.
DR   SMR; Q9JLV1; 18-57, 401-503.
DR   BioGrid; 205891; 6.
DR   IntAct; Q9JLV1; 4.
DR   MINT; MINT-4124913; -.
DR   STRING; 10090.ENSMUSP00000033136; -.
DR   PhosphoSite; Q9JLV1; -.
DR   MaxQB; Q9JLV1; -.
DR   PaxDb; Q9JLV1; -.
DR   PRIDE; Q9JLV1; -.
DR   Ensembl; ENSMUST00000033136; ENSMUSP00000033136; ENSMUSG00000030847.
DR   GeneID; 29810; -.
DR   KEGG; mmu:29810; -.
DR   UCSC; uc009jzb.2; mouse.
DR   CTD; 9531; -.
DR   MGI; MGI:1352493; Bag3.
DR   eggNOG; NOG238690; -.
DR   GeneTree; ENSGT00530000063256; -.
DR   HOGENOM; HOG000050234; -.
DR   HOVERGEN; HBG003419; -.
DR   InParanoid; Q9JLV1; -.
DR   KO; K09557; -.
DR   OMA; VYPQLRP; -.
DR   OrthoDB; EOG75B85S; -.
DR   TreeFam; TF102013; -.
DR   Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR   EvolutionaryTrace; Q9JLV1; -.
DR   NextBio; 306958; -.
DR   PRO; PR:Q9JLV1; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; Q9JLV1; -.
DR   CleanEx; MM_BAG3; -.
DR   Genevisible; Q9JLV1; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0032403; F:protein complex binding; IDA:MGI.
DR   GO; GO:0007420; P:brain development; IEA:Ensembl.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:MGI.
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:0010664; P:negative regulation of striated muscle cell apoptotic process; IMP:MGI.
DR   GO; GO:0050821; P:protein stabilization; IMP:MGI.
DR   GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR   Gene3D; 1.20.58.120; -; 1.
DR   InterPro; IPR003103; BAG_domain.
DR   InterPro; IPR001202; WW_dom.
DR   Pfam; PF02179; BAG; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00264; BAG; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF51045; SSF51045; 1.
DR   PROSITE; PS51035; BAG; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Apoptosis; Chaperone; Complete proteome;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:O95817}.
FT   CHAIN         2    577       BAG family molecular chaperone regulator
FT                                3.
FT                                /FTId=PRO_0000088869.
FT   DOMAIN       22     56       WW 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00224}.
FT   DOMAIN      126    157       WW 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00224}.
FT   DOMAIN      426    503       BAG. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00369}.
FT   COMPBIAS    186    193       Poly-Ser.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000250|UniProtKB:O95817}.
FT   MOD_RES     138    138       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     204    204       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O95817}.
FT   MOD_RES     280    280       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O95817}.
FT   MOD_RES     281    281       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O95817}.
FT   MOD_RES     285    285       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O95817}.
FT   MOD_RES     291    291       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     297    297       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     380    380       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     382    382       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     390    390       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   CONFLICT     74     74       D -> N (in Ref. 1; AAF26840).
FT                                {ECO:0000305}.
FT   CONFLICT    527    527       Q -> P (in Ref. 1; AAF26840).
FT                                {ECO:0000305}.
FT   CONFLICT    539    539       K -> E (in Ref. 2; BAA95066).
FT                                {ECO:0000305}.
FT   STRAND      417    420       {ECO:0000244|PDB:1UK5}.
FT   HELIX       425    445       {ECO:0000244|PDB:1UK5}.
FT   STRAND      451    453       {ECO:0000244|PDB:1UK5}.
FT   HELIX       454    471       {ECO:0000244|PDB:1UK5}.
FT   HELIX       479    503       {ECO:0000244|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
//