BAG1_RAT
ID BAG1_RAT Reviewed; 358 AA.
AC B0K019;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=BAG family molecular chaperone regulator 1;
DE Short=BAG-1;
DE AltName: Full=Bcl-2-associated athanogene 1;
GN Name=Bag1;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
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: 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. Inhibits the pro-apoptotic function of PPP1R15A,
CC and has anti-apoptotic activity. Markedly increases the anti-cell death
CC function of BCL2 induced by various stimuli.
CC {ECO:0000250|UniProtKB:Q99933}.
CC -!- SUBUNIT: Homodimer. Forms a heteromeric complex with HSP70/HSC70. Binds
CC to the ATPase domain of HSP/HSC70 chaperones. Interacts with NR3C1.
CC Interacts with the N-terminal region of STK19. Interacts with PPP1R15A.
CC Interacts with BCL2 in an ATP-dependent manner. Interacts with SIAH1,
CC SIAH2, HSPA8 (via NBD), HSPA1A (via NBD) and HSPA1B (via NBD).
CC {ECO:0000250|UniProtKB:Q60739, ECO:0000250|UniProtKB:Q99933}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its
CC subsequent proteasomal degradation. {ECO:0000250}.
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DR EMBL; BC159418; AAI59419.1; -; mRNA.
DR RefSeq; NP_001100117.2; NM_001106647.3.
DR RefSeq; NP_001243013.1; NM_001256084.1.
DR AlphaFoldDB; B0K019; -.
DR SMR; B0K019; -.
DR BioGRID; 255722; 6.
DR DIP; DIP-60384N; -.
DR IntAct; B0K019; 2.
DR STRING; 10116.ENSRNOP00000011455; -.
DR iPTMnet; B0K019; -.
DR PhosphoSitePlus; B0K019; -.
DR PaxDb; B0K019; -.
DR PeptideAtlas; B0K019; -.
DR GeneID; 297994; -.
DR KEGG; rno:297994; -.
DR UCSC; RGD:1305203; rat.
DR CTD; 573; -.
DR RGD; 1305203; Bag1.
DR eggNOG; ENOG502RN5W; Eukaryota.
DR InParanoid; B0K019; -.
DR OrthoDB; 1450573at2759; -.
DR PhylomeDB; B0K019; -.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR PRO; PR:B0K019; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR GO; GO:0014040; P:positive regulation of Schwann cell differentiation; IMP:RGD.
DR GO; GO:0070585; P:protein localization to mitochondrion; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:1901423; P:response to benzene; IEP:RGD.
DR GO; GO:0010226; P:response to lithium ion; IEP:RGD.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR Gene3D; 1.20.58.120; -; 1.
DR InterPro; IPR017093; BAG-1.
DR InterPro; IPR039773; BAG_chaperone_regulator.
DR InterPro; IPR036533; BAG_dom_sf.
DR InterPro; IPR003103; BAG_domain.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR12329; PTHR12329; 1.
DR PANTHER; PTHR12329:SF16; PTHR12329:SF16; 1.
DR Pfam; PF02179; BAG; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00264; BAG; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF63491; SSF63491; 1.
DR PROSITE; PS51035; BAG; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Chaperone; Cytoplasm; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..358
FT /note="BAG family molecular chaperone regulator 1"
FT /id="PRO_0000389100"
FT REPEAT 102..111
FT /note="1"
FT REPEAT 114..119
FT /note="2"
FT REPEAT 120..125
FT /note="3"
FT REPEAT 126..131
FT /note="4"
FT REPEAT 132..137
FT /note="5"
FT REPEAT 144..149
FT /note="6"
FT REPEAT 150..155
FT /note="7"
FT DOMAIN 157..237
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 259..339
FT /note="BAG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..212
FT /note="7 X 6 AA tandem repeat of E-E-X(4)"
FT REGION 136..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..232
FT /note="Interaction with HSPA8"
FT /evidence="ECO:0000250"
FT REGION 229..358
FT /note="Interaction with PPP1R15A"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 40160 MW; 7C39247930E3E198 CRC64;
MADRGGARRP RGDQEPLGPR LRAPRSARET RQSESRAERG LPPSQRSSVR SAASGHDRST
RGAASGACKP RVKKKVRPRS SQSEKVAHSK ELTRSKKLTR SKKVTGTQEA TQVEEVTTIE
EATQTEEITV AEEVTQTENM AQTEEMVQTE EMEPPTLSVV VTHSNERYDL LVTPQQGNSE
PIVQDLAQLV EEATGVPLPF QKLIFKGKSL KEMETPLSAL GMQNGCRVML IGEKSNPEEE
AELKKLKDLE VSVEKTANHL EELNKELSDI QQGFLAKELQ AEALCRLDRK IKATIEQFMK
ILEEIDTMVL PENFKDSRLK RKNLVKKVQV FLAECDTVEQ YICQETERLQ STNLALPE
