ID   BAG2_BOVIN              Reviewed;         211 AA.
AC   Q3ZBG5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=BAG family molecular chaperone regulator 2;
DE            Short=BAG-2;
DE   AltName: Full=Bcl-2-associated athanogene 2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:O95816}.
CC   -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. May
CC       interact with NWD1. Interacts with HSPA1A (via NBD), HSPA1B (via NBD)
CC       and HSPA8. May interact with DNJC9; the interaction seems to be
CC       histone-dependent (By similarity). {ECO:0000250|UniProtKB:O95816}.
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DR   EMBL; BC103308; AAI03309.1; -; mRNA.
DR   RefSeq; NP_001029436.1; NM_001034264.1.
DR   AlphaFoldDB; Q3ZBG5; -.
DR   SMR; Q3ZBG5; -.
DR   STRING; 9913.ENSBTAP00000007039; -.
DR   PaxDb; Q3ZBG5; -.
DR   PRIDE; Q3ZBG5; -.
DR   Ensembl; ENSBTAT00000007039; ENSBTAP00000007039; ENSBTAG00000005355.
DR   GeneID; 506107; -.
DR   KEGG; bta:506107; -.
DR   CTD; 9532; -.
DR   VEuPathDB; HostDB:ENSBTAG00000005355; -.
DR   VGNC; VGNC:26406; BAG2.
DR   eggNOG; KOG3633; Eukaryota.
DR   GeneTree; ENSGT00390000017590; -.
DR   HOGENOM; CLU_072417_2_0_1; -.
DR   InParanoid; Q3ZBG5; -.
DR   OMA; EMIHNIQ; -.
DR   OrthoDB; 1268987at2759; -.
DR   TreeFam; TF102012; -.
DR   Reactome; R-BTA-3371453; Regulation of HSF1-mediated heat shock response.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000005355; Expressed in myometrium and 105 other tissues.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0101031; C:chaperone complex; IEA:Ensembl.
DR   GO; GO:1901588; C:dendritic microtubule; IEA:Ensembl.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0048156; F:tau protein binding; IEA:Ensembl.
DR   GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR   GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IEA:Ensembl.
DR   GO; GO:0010954; P:positive regulation of protein processing; IEA:Ensembl.
DR   GO; GO:0019538; P:protein metabolic process; IEA:Ensembl.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR   InterPro; IPR037689; BAG2.
DR   InterPro; IPR003103; BAG_domain.
DR   PANTHER; PTHR12334; PTHR12334; 1.
DR   SMART; SM00264; BAG; 1.
DR   PROSITE; PS51035; BAG; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chaperone; Coiled coil; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O95816"
FT   CHAIN           2..211
FT                   /note="BAG family molecular chaperone regulator 2"
FT                   /id="PRO_0000282938"
FT   DOMAIN          109..189
FT                   /note="BAG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT   COILED          20..61
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:O95816"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95816"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95816"
FT   MOD_RES         73
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95816"
SQ   SEQUENCE   211 AA;  23649 MW;  727D6613B6F48A10 CRC64;
     MAQARISAKA NEGRFCRSSS MADRSSRLLE SLDQLELRVE ALREAATAVE QEKEVLLEMI
     HSIQNSQDMR QISDGEREEL NLTANRLMGR TLTVEVSVET IRSPQQQESL KHATRIIDEV
     VSKFLDDLGN ARSHLMSLYS ACSSEVPAGP VDQKFQSIVI GCALEDQKKI KRRLETLLRN
     IENADKAIKL LEHSKGAASK TLQQNAEARF N