BAG5_MOUSE
ID BAG5_MOUSE Reviewed; 447 AA.
AC Q8CI32; Q3TVA8; Q8K175; Q9DAU0;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=BAG family molecular chaperone regulator 5;
DE Short=BAG-5;
DE AltName: Full=Bcl-2-associated athanogene 5;
GN Name=Bag5;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, 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 [4]
RP STRUCTURE BY NMR OF 1-86.
RX PubMed=20223214; DOI=10.1016/j.str.2010.01.004;
RA Arakawa A., Handa N., Ohsawa N., Shida M., Kigawa T., Hayashi F.,
RA Shirouzu M., Yokoyama S.;
RT "The C-terminal BAG domain of BAG5 induces conformational changes of the
RT Hsp70 nucleotide-binding domain for ADP-ATP exchange.";
RL Structure 18:309-319(2010).
CC -!- FUNCTION: May function as a nucleotide exchange factor for HSP/HSP70,
CC promoting ADP release, and activating Hsp70-mediated refolding.
CC Inhibits both auto-ubiquitination of PRKN and ubiquitination of target
CC proteins by PRKN (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds PRKN
CC (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The fifth BAG domain is responsible for the interaction with
CC HSP70 nucleotide-binding domain. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH27827.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB24105.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK005534; BAB24105.1; ALT_FRAME; mRNA.
DR EMBL; AK160246; BAE35711.1; -; mRNA.
DR EMBL; BC027827; AAH27827.1; ALT_INIT; mRNA.
DR EMBL; BC037642; AAH37642.1; -; mRNA.
DR CCDS; CCDS26185.1; -.
DR RefSeq; NP_001311409.1; NM_001324480.1.
DR RefSeq; NP_001311410.1; NM_001324481.1.
DR RefSeq; NP_001311411.1; NM_001324482.1.
DR RefSeq; NP_081680.1; NM_027404.2.
DR RefSeq; XP_006516280.1; XM_006516217.3.
DR PDB; 1UGO; NMR; -; A=1-86.
DR PDBsum; 1UGO; -.
DR AlphaFoldDB; Q8CI32; -.
DR SMR; Q8CI32; -.
DR BioGRID; 214005; 9.
DR IntAct; Q8CI32; 4.
DR STRING; 10090.ENSMUSP00000051049; -.
DR iPTMnet; Q8CI32; -.
DR PhosphoSitePlus; Q8CI32; -.
DR EPD; Q8CI32; -.
DR MaxQB; Q8CI32; -.
DR PaxDb; Q8CI32; -.
DR PeptideAtlas; Q8CI32; -.
DR PRIDE; Q8CI32; -.
DR ProteomicsDB; 277105; -.
DR Antibodypedia; 36; 561 antibodies from 36 providers.
DR DNASU; 70369; -.
DR Ensembl; ENSMUST00000054636; ENSMUSP00000051049; ENSMUSG00000049792.
DR Ensembl; ENSMUST00000160576; ENSMUSP00000125183; ENSMUSG00000049792.
DR GeneID; 70369; -.
DR KEGG; mmu:70369; -.
DR UCSC; uc007pdr.3; mouse.
DR CTD; 9529; -.
DR MGI; MGI:1917619; Bag5.
DR VEuPathDB; HostDB:ENSMUSG00000049792; -.
DR eggNOG; KOG4361; Eukaryota.
DR GeneTree; ENSGT00940000158888; -.
DR HOGENOM; CLU_579940_0_0_1; -.
DR InParanoid; Q8CI32; -.
DR OMA; VWDVLGN; -.
DR OrthoDB; 902874at2759; -.
DR PhylomeDB; Q8CI32; -.
DR TreeFam; TF102014; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR BioGRID-ORCS; 70369; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Bag5; mouse.
DR EvolutionaryTrace; Q8CI32; -.
DR PRO; PR:Q8CI32; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8CI32; protein.
DR Bgee; ENSMUSG00000049792; Expressed in seminiferous tubule of testis and 241 other tissues.
DR ExpressionAtlas; Q8CI32; baseline and differential.
DR Genevisible; Q8CI32; MM.
DR GO; GO:0005829; C:cytosol; ISS:ParkinsonsUK-UCL.
DR GO; GO:0016234; C:inclusion body; ISS:BHF-UCL.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005634; C:nucleus; ISS:ParkinsonsUK-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; ISS:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0007030; P:Golgi organization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:ParkinsonsUK-UCL.
DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:ParkinsonsUK-UCL.
DR GO; GO:0061084; P:negative regulation of protein refolding; ISS:BHF-UCL.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:ParkinsonsUK-UCL.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; ISS:BHF-UCL.
DR GO; GO:0070997; P:neuron death; ISS:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0090083; P:regulation of inclusion body assembly; ISS:BHF-UCL.
DR Gene3D; 1.20.58.120; -; 5.
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; 4.
DR SMART; SM00264; BAG; 4.
DR SUPFAM; SSF63491; SSF63491; 4.
DR PROSITE; PS51035; BAG; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Reference proteome; Repeat.
FT CHAIN 1..447
FT /note="BAG family molecular chaperone regulator 5"
FT /id="PRO_0000088873"
FT DOMAIN 9..86
FT /note="BAG 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT DOMAIN 95..167
FT /note="BAG 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT DOMAIN 182..260
FT /note="BAG 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT DOMAIN 275..350
FT /note="BAG 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT DOMAIN 365..442
FT /note="BAG 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT CONFLICT 6
FT /note="Q -> H (in Ref. 1; BAB24105)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="I -> K (in Ref. 1; BAB24105)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="D -> E (in Ref. 1; BAB24105)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="E -> G (in Ref. 1; BAB24105)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="K -> E (in Ref. 1; BAB24105)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="A -> S (in Ref. 1; BAB24105)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="I -> T (in Ref. 2; AAH27827)"
FT /evidence="ECO:0000305"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:1UGO"
FT HELIX 24..28
FT /evidence="ECO:0007829|PDB:1UGO"
FT HELIX 38..55
FT /evidence="ECO:0007829|PDB:1UGO"
FT HELIX 62..86
FT /evidence="ECO:0007829|PDB:1UGO"
SQ SEQUENCE 447 AA; 50943 MW; 72E2C5472DA95416 CRC64;
MDMGNQHPSI SRLQEIQREV KAIEPQVVGF SGLSDDKNYK RLERILTKQL FEIDSVDTEG
KGDIQQARKR AAQETERLLK ELEQNANHPH RIEIQNIFKE AQALVKDKIV PFYSGGNCVT
DEFEEGIQDI ILRLTHVKTG GKVSLRKARY RTLTKICAVQ EVIEDCMKKQ PSLPLSEDVH
PSVAKINSVM CEVNKARGTL IALLMGVDSS ETCRHLSCVL SGLIADLDAL DVCGRTEIRN
YRREVVEDIN KLLKYLDLEE EADSTHAFDL GQNHSIIKIE NVLKRMREIK NELLQAQSPP
ELYLRAKTEL QGLIGQLDEV SLEKNPCIRE ARRRAVIEVQ ILITYLDLKE ALEKRKLFPC
EEHPPHKAVW EILGNLSEIL GEVLSFGGNR TDKNYIRLEE LLTKQLLALD AVDPQGEEKC
KAARKQAVKL AQNILSYLDM KSDEWEY
