BAG6_XENTR
ID BAG6_XENTR Reviewed; 1129 AA.
AC A4IH17;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Large proline-rich protein bag6 {ECO:0000305};
DE AltName: Full=BCL2-associated athanogene 6 {ECO:0000250|UniProtKB:P46379};
DE AltName: Full=HLA-B-associated transcript 3 {ECO:0000250|UniProtKB:P46379};
GN Name=Bag6 {ECO:0000250|UniProtKB:P46379};
GN Synonyms=bat3 {ECO:0000250|UniProtKB:P46379};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-independent molecular chaperone preventing the
CC aggregation of misfolded and hydrophobic patches-containing proteins.
CC Functions as part of a cytosolic protein quality control complex, the
CC bag6/bat3 complex, which maintains these client proteins in a soluble
CC state and participates in their proper delivery to the endoplasmic
CC reticulum or alternatively can promote their sorting to the proteasome
CC where they undergo degradation. The bag6/bat3 complex is involved in
CC the post-translational delivery of tail-anchored/type II transmembrane
CC proteins to the endoplasmic reticulum membrane. Similarly, the
CC bag6/bat3 complex also functions as a sorting platform for proteins of
CC the secretory pathway that are mislocalized to the cytosol either
CC delivering them to the proteasome for degradation or to the endoplasmic
CC reticulum. The bag6/bat3 complex also plays a role in the endoplasmic
CC reticulum-associated degradation (ERAD), a quality control mechanism
CC that eliminates unwanted proteins of the endoplasmic reticulum through
CC their retrotranslocation to the cytosol and their targeting to the
CC proteasome. It maintains these retrotranslocated proteins in an
CC unfolded yet soluble state condition in the cytosol to ensure their
CC proper delivery to the proteasome. Also required for selective
CC ubiquitin-mediated degradation of defective nascent chain polypeptides
CC by the proteasome. Also involved in endoplasmic reticulum stress-
CC induced pre-emptive quality control, a mechanism that selectively
CC attenuates the translocation of newly synthesized proteins into the
CC endoplasmic reticulum and reroutes them to the cytosol for proteasomal
CC degradation. May ensure the proper degradation of these proteins and
CC thereby protects the endoplasmic reticulum from protein overload upon
CC stress. By stabilizing a large spectrum of proteins, may indirectly
CC affect different biological processes including apoptosis. By
CC controlling the steady-state expression of the IGF1R receptor,
CC indirectly regulates the insulin-like growth factor receptor signaling
CC pathway. {ECO:0000250|UniProtKB:P46379}.
CC -!- FUNCTION: When nuclear, may also act as a component of some chromatin
CC regulator complex. {ECO:0000250|UniProtKB:P46379}.
CC -!- SUBUNIT: Component of the bag6/bat3 complex.
CC {ECO:0000250|UniProtKB:P46379}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P46379}. Nucleus {ECO:0000250|UniProtKB:P46379}.
CC Secreted, extracellular exosome {ECO:0000250|UniProtKB:P46379}.
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DR EMBL; BC135335; AAI35336.1; -; mRNA.
DR RefSeq; NP_001090878.2; NM_001097409.2.
DR AlphaFoldDB; A4IH17; -.
DR SMR; A4IH17; -.
DR GeneID; 100038304; -.
DR KEGG; xtr:100038304; -.
DR CTD; 7917; -.
DR Xenbase; XB-GENE-478689; bag6.
DR eggNOG; KOG4248; Eukaryota.
DR InParanoid; A4IH17; -.
DR OrthoDB; 1233552at2759; -.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0071818; C:BAT3 complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0061857; P:endoplasmic reticulum stress-induced pre-emptive quality control; ISS:UniProtKB.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISS:UniProtKB.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; ISS:UniProtKB.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0030324; P:lung development; ISS:UniProtKB.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0045861; P:negative regulation of proteolysis; ISS:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:0007130; P:synaptonemal complex assembly; ISS:UniProtKB.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR InterPro; IPR021925; BAG6.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF12057; BAG6; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Chaperone; Chromatin regulator; Cytoplasm; Nucleus;
KW Reference proteome; Secreted; Transport.
FT CHAIN 1..1129
FT /note="Large proline-rich protein bag6"
FT /id="PRO_0000403755"
FT DOMAIN 1..76
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 69..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 942..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 987..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..504
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..967
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1006
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1129 AA; 120785 MW; 024D658610148D1B CRC64;
MEVTVKTLDS QTRTFTVDAE ITVKEFKTHI SSDVGISPEK QRLIYQGRVL QEDKKLKEYN
VDGKVIHLVE RAPPQTQPST GGPSTSSSTS PSSSNAANVP GAGAPERNGN SYVMVGTFNL
PHVMSGLGEA SRGPRVSTVS GNDGSTLDVH INLDQQLPVQ SEPRVRLVLA QQILQDIQRI
LDRLEGQPVN EQTAEPMDTA VSEGEASSRE TLPQTTQNTD GQSNTAPTSH PSPSEYVEVL
QSLSRVEERL APFMQRYREI LSSATSDAYE NQEEREQSQR IINLVGESLR LLGNALVAVS
DLRCNLSSAS PRHLHVVRPM SHYTGPMLLQ QAAIPIQINV GTTVTMTGNG THAGQMPSDG
NAAHTPTNTS EPQRSNSDNQ PPSSGERPAS EIPPTSVPHP HPRVVRITHQ TVEPVMMMHM
NIQDSGPGGP TNIPPPTAGH GGSAHIHMPG LPPEFMQAIS HQITQQAVAA ASGQQIPGFQ
APPRFVFTRP AAPSFPPQPG VATTPPGPGG ATTAVPGATV GPAGNASLAQ MISGLVGQLL
MHPVIVAQGG SNTPSSTSTP TSTSSSSSSS SSTVTTSTTT TSSTSFPTVS SGPSPQPPPG
TDQHLSQLLG SLLGTAGSGM SNFAMGSPSI TVTVPGMPAF LQGVTDILQA TQTVPVSTSP
PQSASQAPPP SSPSPPPAHS SPPPAAAPES LPPEFFTSVV QGVLSSMLGS LSAADQSGTE
SIAAFIQRLS GSHNIFQPDA EGPGGFFGDL LTLICHNFSL VDMVMLLHGH SQPLQNLQPQ
LRSFFLQEYL HQADPTPNNI QMASRNLTNG LEEYIRESFA SVTVRDDVDI TRTNLEFLQD
QFNRITTHIL HCADSTFGQR LLEMCNQSLF EWLALNLYCL RGDQSALTSV INERIRRLSL
DVSPVLVSWV TSVLSLRLQV LLGQMPVTEG EIQRHIRRVG DVPQAPEASS QDQPMETTPV
DCQNGAASPV PATTVEEVLF LPPQSSVPTI CTDSEHPTQE DTGSEQWAAS VPPEWVPVIR
QDMQNQRKMK QQPPLSDAYL SGMPAKRRKT MQGEGPHLSL SEAVSRAMKA TGAKPESSTD
CVRRELDNSE AQGRYREQLC QDIQNILQDN ESYSAQRFPN TQRAFRGDP
