BAG5_BOVIN
ID BAG5_BOVIN Reviewed; 447 AA.
AC Q2TA08;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 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 [MRNA].
RC TISSUE=Placenta;
RA Ushizawa K., Takahashi T., Hosoe M., Hashizume K.;
RT "Expression of BAG5 in bovine placenta.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds PRKN
CC (By similarity). {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; AB211978; BAE94654.1; -; mRNA.
DR EMBL; BC111177; AAI11178.1; -; mRNA.
DR RefSeq; NP_001035634.1; NM_001040544.2.
DR RefSeq; XP_005222261.1; XM_005222204.3.
DR RefSeq; XP_010815554.1; XM_010817252.2.
DR AlphaFoldDB; Q2TA08; -.
DR SMR; Q2TA08; -.
DR STRING; 9913.ENSBTAP00000023084; -.
DR PaxDb; Q2TA08; -.
DR PRIDE; Q2TA08; -.
DR GeneID; 522854; -.
DR KEGG; bta:522854; -.
DR CTD; 9529; -.
DR eggNOG; KOG4361; Eukaryota.
DR HOGENOM; CLU_579940_0_0_1; -.
DR InParanoid; Q2TA08; -.
DR OrthoDB; 902874at2759; -.
DR TreeFam; TF102014; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
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..447
FT /note="BAG family molecular chaperone regulator 5"
FT /id="PRO_0000282860"
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; 50954 MW; E9811887ACDF9C48 CRC64;
MEMGNQHPSI SRLQEIQKEV KSIEQQVLGF SGLSDDKNYK KLERILTKQL FEIDSVDTEG
KGDIQQARKR AAQETERLLK ELEQNANHPH RLEIQNIFQE AQALVKEKVV PFYNGGNCVT
DEFEEGIQDV ILRLTHVKTG GKVSLRKARY HTLTKICAVQ EIIENCMKKQ PSLPLSEDAH
PSVAKINSVM CEVNKTRGTL IALLMGVNNK ETCRHLSCVL SGLMADLDAL DVCGHTEIRN
YRKEVVEDIN QLLRYLDLEE EADTTHAFDL GQNHSILKIE KVLKRMREIK TELLQAQNPP
ELYLSAKTEL QGLIGQLDEV SLEKNPCIRE ARRRAVIEVQ TLITYIDLKE ALEKRKLLAC
EEHPSHKAVW DVLGNLSEIQ GEVLSFDGNR TDKNYIRLEE LLTKQLLALD AVDPQGEEKC
KAARKQAVKL AQNILSYLDL KSDEWEY
