BAG5_RAT
ID BAG5_RAT Reviewed; 447 AA.
AC Q5QJC9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH THE HSP70 COMPLEX
RP AND PRKN, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=15603737; DOI=10.1016/j.neuron.2004.11.026;
RA Kalia S.K., Lee S., Smith P.D., Liu L., Crocker S.J., Thorarinsdottir T.E.,
RA Glover J.R., Fon E.A., Park D.S., Lozano A.M.;
RT "BAG5 inhibits parkin and enhances dopaminergic neuron degeneration.";
RL Neuron 44:931-945(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
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. {ECO:0000250, ECO:0000269|PubMed:15603737}.
CC -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds
CC PRKN.
CC -!- TISSUE SPECIFICITY: Detected in brain, lung, stomach, liver, kidney and
CC testis. {ECO:0000269|PubMed:15603737}.
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; AY366364; AAR13081.1; -; mRNA.
DR EMBL; BC088418; AAH88418.1; -; mRNA.
DR RefSeq; NP_001008526.1; NM_001008526.2.
DR RefSeq; XP_006240663.1; XM_006240601.2.
DR RefSeq; XP_006240664.1; XM_006240602.2.
DR RefSeq; XP_006240665.1; XM_006240603.3.
DR RefSeq; XP_008763199.1; XM_008764977.2.
DR RefSeq; XP_008763200.1; XM_008764978.2.
DR RefSeq; XP_008763201.1; XM_008764979.2.
DR RefSeq; XP_008763202.1; XM_008764980.2.
DR RefSeq; XP_008774543.1; XM_008776321.1.
DR RefSeq; XP_008774544.1; XM_008776322.1.
DR RefSeq; XP_008774545.1; XM_008776323.2.
DR AlphaFoldDB; Q5QJC9; -.
DR SMR; Q5QJC9; -.
DR BioGRID; 266094; 1.
DR IntAct; Q5QJC9; 1.
DR STRING; 10116.ENSRNOP00000015333; -.
DR jPOST; Q5QJC9; -.
DR PaxDb; Q5QJC9; -.
DR PRIDE; Q5QJC9; -.
DR Ensembl; ENSRNOT00000085594; ENSRNOP00000071757; ENSRNOG00000058841.
DR GeneID; 366734; -.
DR KEGG; rno:366734; -.
DR UCSC; RGD:1310847; rat.
DR CTD; 9529; -.
DR RGD; 1310847; Bag5.
DR eggNOG; KOG4361; Eukaryota.
DR GeneTree; ENSGT00940000158888; -.
DR HOGENOM; CLU_579940_0_0_1; -.
DR InParanoid; Q5QJC9; -.
DR OMA; VWDVLGN; -.
DR OrthoDB; 902874at2759; -.
DR PhylomeDB; Q5QJC9; -.
DR TreeFam; TF102014; -.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR PRO; PR:Q5QJC9; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000011527; Expressed in testis and 18 other tissues.
DR Genevisible; Q5QJC9; RN.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
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; IDA:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
DR GO; GO:0007030; P:Golgi organization; ISO:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0061084; P:negative regulation of protein refolding; IMP:BHF-UCL.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:BHF-UCL.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IDA:BHF-UCL.
DR GO; GO:0070997; P:neuron death; IDA:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0090083; P:regulation of inclusion body assembly; IDA: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 Chaperone; Reference proteome; Repeat.
FT CHAIN 1..447
FT /note="BAG family molecular chaperone regulator 5"
FT /id="PRO_0000088874"
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"
SQ SEQUENCE 447 AA; 51030 MW; 3248480576409C0A CRC64;
MDMGNQHPSI SRLQEIQREV KSIEQQVVGF SGLSDDKNYK RLERILTKQL FEIDSVDTEG
KGDIQQARKR AAQDTERLLK ELEQNANHPH RIEIKNIFQE AQALVKEKTV PFYSGSNCVT
SEFEEAIQDI ILRLTHVKTG GKISLRKARY HTLTKICAVQ EIIEDCVRKQ PSLPLSEDVH
PSVAKINSVM CEVNKARGTL IALLMGVDSS ETCRHLSCVL SGLMADLDAL DVCGRTEIRN
YRREVVEDIN KLLKYLDLEE EADNTHAFDL GQNHSIIKIE NVLKRMREMK NELLQAQSPP
ELYLRSKTEL QGLIGQLDEV SLEKNPCIRE ARRRAVIEVQ TLITYLDLKE ALEKRKLFPC
EETPPHKAVW NVLGNLSEIQ GEVLSFGGNR TDKNYIRLEE LLTKQLLTLD AVDPLGEEKC
KAARKQAVKL AQNILSYLDM KSDEWEY
