ID   BAG5_CHICK              Reviewed;         450 AA.
AC   Q5F486;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=BAG family molecular chaperone regulator 5;
DE            Short=BAG-5;
DE   AltName: Full=Bcl-2-associated athanogene 5;
GN   Name=BAG5; ORFNames=RCJMB04_2e5;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: May function as a nucleotide exchange factor for HSP/HSP70,
CC       promoting ADP release, and activating Hsp70-mediated refolding.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The fifth BAG domain is responsible for the interaction with
CC       HSP70 nucleotide-binding domain. {ECO:0000250}.
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DR   EMBL; AJ851414; CAH65048.1; -; mRNA.
DR   RefSeq; NP_001026382.1; NM_001031211.1.
DR   AlphaFoldDB; Q5F486; -.
DR   SMR; Q5F486; -.
DR   STRING; 9031.ENSGALP00000018771; -.
DR   PaxDb; Q5F486; -.
DR   GeneID; 423482; -.
DR   KEGG; gga:423482; -.
DR   CTD; 9529; -.
DR   VEuPathDB; HostDB:geneid_423482; -.
DR   eggNOG; KOG4361; Eukaryota.
DR   InParanoid; Q5F486; -.
DR   OrthoDB; 902874at2759; -.
DR   PhylomeDB; Q5F486; -.
DR   PRO; PR:Q5F486; -.
DR   Proteomes; UP000000539; Unplaced.
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:0051087; F:chaperone binding; IBA:GO_Central.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR   GO; GO:0090083; P:regulation of inclusion body assembly; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Chaperone; Reference proteome; Repeat.
FT   CHAIN           1..450
FT                   /note="BAG family molecular chaperone regulator 5"
FT                   /id="PRO_0000088875"
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   450 AA;  51167 MW;  FBE35BC8D73572C5 CRC64;
     MDMGNQHPSI KRLHEIQKEV KEIEQQVAVF SGLSTDRDYK KLERSLTKQL FEIDSVDTEG
     KGDIQQARKR AAQETERLLK ELEQNANHPR RLEIEAIFKE AQALVEREIT PFYQGGNCVN
     EEFEEGIQDV VLRLTQVKTG GKVSLRKARY RTLTKVCAVQ EIIESCAKRQ LSLPLSNDAH
     PSVSKINSVM CEVNKARGTL IALLMGVSSN DTCRHLACVL TGLVADLDAL DVCGRTEIRN
     YRKEVVEEIN KLQKYLDLDE EANSTHAYDL AQNHSILKIE EIRKKLKEVN SLLLKTENAS
     DLYLGSKAEL QGLIAQLDEV SLGKNPCIRE ARRRAVIEVQ TLITYIDLKE ALGKRQMYAE
     QTAAEHQSHK AVWTVLGNLS QIQQEVISFD GNKTDKNYMR LEELLTKQLL ALDAVDPQGD
     ERCKAARKQA VKLAQNILYY LDMKTDEWEY