BAG1_CAEEL
ID BAG1_CAEEL Reviewed; 210 AA.
AC O44739;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=BAG family molecular chaperone regulator 1;
GN Name=bag-1; ORFNames=F57B10.11;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9873016; DOI=10.1074/jbc.274.2.781;
RA Takayama S., Xie Z., Reed J.C.;
RT "An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone
RT regulators.";
RL J. Biol. Chem. 274:781-786(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 74-210, AND SUBUNIT.
RX PubMed=15333932; DOI=10.1107/s0907444904017603;
RA Symersky J., Zhang Y., Schormann N., Li S., Bunzel R., Pruett P.,
RA Luan C.-H., Luo M.;
RT "Structural genomics of Caenorhabditis elegans: structure of the BAG
RT domain.";
RL Acta Crystallogr. D 60:1606-1610(2004).
CC -!- FUNCTION: May inhibit the chaperone activity of HSP70/HSC70 by
CC promoting substrate release in an ATP-dependent manner. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000269|PubMed:15333932}.
CC -!- INTERACTION:
CC O44739; Q9XWX7: CELE_Y43F8B.2; NbExp=3; IntAct=EBI-323218, EBI-323231;
CC -!- DOMAIN: The BAG domain probably mediates direct interaction with HSP70.
CC {ECO:0000250}.
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DR EMBL; AF095788; AAD16125.1; -; mRNA.
DR EMBL; FO081416; CCD71479.1; -; Genomic_DNA.
DR PIR; T43666; T43666.
DR RefSeq; NP_491893.1; NM_059492.5.
DR PDB; 1T7S; X-ray; 2.80 A; A/B=74-210.
DR PDBsum; 1T7S; -.
DR AlphaFoldDB; O44739; -.
DR SMR; O44739; -.
DR BioGRID; 37824; 14.
DR DIP; DIP-27094N; -.
DR IntAct; O44739; 3.
DR STRING; 6239.F57B10.11; -.
DR EPD; O44739; -.
DR PaxDb; O44739; -.
DR PeptideAtlas; O44739; -.
DR PRIDE; O44739; -.
DR EnsemblMetazoa; F57B10.11.1; F57B10.11.1; WBGene00000236.
DR GeneID; 172373; -.
DR KEGG; cel:CELE_F57B10.11; -.
DR UCSC; F57B10.11; c. elegans.
DR CTD; 172373; -.
DR WormBase; F57B10.11; CE11318; WBGene00000236; bag-1.
DR eggNOG; ENOG502S5YF; Eukaryota.
DR GeneTree; ENSGT00450000040296; -.
DR HOGENOM; CLU_1316430_0_0_1; -.
DR InParanoid; O44739; -.
DR OMA; AGFKMLM; -.
DR OrthoDB; 1262293at2759; -.
DR PhylomeDB; O44739; -.
DR Reactome; R-CEL-3371453; Regulation of HSF1-mediated heat shock response.
DR EvolutionaryTrace; O44739; -.
DR PRO; PR:O44739; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00000236; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0001671; F:ATPase activator activity; IDA:WormBase.
DR GO; GO:0051087; F:chaperone binding; ISS:WormBase.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISS:WormBase.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
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 PIRSF; PIRSF037029; BAG_1; 1.
DR SMART; SM00264; BAG; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF63491; SSF63491; 1.
DR PROSITE; PS51035; BAG; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Reference proteome.
FT CHAIN 1..210
FT /note="BAG family molecular chaperone regulator 1"
FT /id="PRO_0000088877"
FT DOMAIN 8..85
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 108..194
FT /note="BAG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1T7S"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1T7S"
FT HELIX 88..121
FT /evidence="ECO:0007829|PDB:1T7S"
FT HELIX 126..155
FT /evidence="ECO:0007829|PDB:1T7S"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1T7S"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1T7S"
FT HELIX 170..200
FT /evidence="ECO:0007829|PDB:1T7S"
SQ SEQUENCE 210 AA; 24010 MW; 1F72FD2C2CF3B157 CRC64;
MKVNVSCSSV QTTIDILEEN QGEDESILTL GQLRDRIATD NDVDVETMKL LHRGKFLQGA
DDVSLSTLNF KENDKIIVMG GKNALVDDAG FKMLMQYEKH NLSNLQKAYD LNLRDVADLE
RGFLEKPKQV EMGKKLEKKV KYFNEEAERH LETLDGMNII TETTPENQAK RNREKRKTLV
NGIQTLLNQN DALLRRLQEY QSVLNGDIPE
