BAG6A_XENLA
ID BAG6A_XENLA Reviewed; 1135 AA.
AC Q9YHD3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Large proline-rich protein bag6-A {ECO:0000305};
DE AltName: Full=BCL2-associated athanogene 6 {ECO:0000250|UniProtKB:P46379};
DE AltName: Full=HLA-B-associated transcript 3-A {ECO:0000305|PubMed:9799223};
DE AltName: Full=Protein Scythe {ECO:0000303|PubMed:9799223};
GN Name=Bag6-a {ECO:0000305}; Synonyms=bat3-a {ECO:0000305|PubMed:9799223};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9799223; DOI=10.1093/emboj/17.21.6135;
RA Thress K., Henzel W., Shillinglaw W., Kornbluth S.;
RT "Scythe: a novel reaper-binding apoptotic regulator.";
RL EMBO J. 17:6135-6143(1998).
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 similarity). By stabilizing a large spectrum of proteins,
CC may indirectly affect different biological processes including
CC apoptosis (PubMed:9799223). By controlling the steady-state expression
CC of the IGF1R receptor, indirectly regulates the insulin-like growth
CC factor receptor signaling pathway (By similarity).
CC {ECO:0000250|UniProtKB:P46379, ECO:0000269|PubMed:9799223}.
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; AF098511; AAC83822.1; -; mRNA.
DR PIR; T30561; T30561.
DR RefSeq; NP_001080008.1; NM_001086539.1.
DR AlphaFoldDB; Q9YHD3; -.
DR SMR; Q9YHD3; -.
DR BioGRID; 97941; 4.
DR DNASU; 379698; -.
DR GeneID; 379698; -.
DR KEGG; xla:379698; -.
DR CTD; 379698; -.
DR Xenbase; XB-GENE-6255172; bag6.L.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 379698; Expressed in pancreas and 19 other tissues.
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: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: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..1135
FT /note="Large proline-rich protein bag6-A"
FT /id="PRO_0000403753"
FT DOMAIN 7..82
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 76..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..696
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1098
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1135 AA; 121641 MW; DA75677109AC1017 CRC64;
MAANEKMEVT VKTLDSQTRT FTVETEISVK DFKAHISSDV GISPEKQRLI YQGRVLQEDK
KLKEYNVDGK VIHLVERAPP QTQPSTGGPS TSSSTSPTSS NAAPVPGAPE RNGNSYVMVG
TFNLPHVMSG LVRQQRPSVS TVNGNDGSTL DVHINLDQQL PVQSEPRVRL VLAQHILQDI
QRILDRLEGQ AVNEQAAEPM DTAESEGEAS SRETLPQTTQ NTDGQSNTTP TSHPSPSEYV
EVLQSLSRVE ERLAPFMQRY REILSSATSD AYENQEEREQ SQRIINLVGE SLRLLGNALV
AVSDLRCNLS SASPRHLHVV RPMSHYSGPM LLQQAAIPIQ INVGTTVTAT GNGTHAGHMP
SDGNAAQPPS TNTSEPQRPN TENQPPSNGE RPASDAPPTS VPHPHPRVIR ITHQTVEPVM
MMHMNIQDSA SGGPTTIPPP TAGHGGSAHI HMPGLPPEFM QAISHQITQQ AMAAASGQQI
PGFQAPPRFV FTRPAAPSFQ FQPGTATTPP GPGGATTTVP GATVGPAGNA SLAQMISGLV
GQLLMHPVVV AQGGSSTSSS TSSSTFTSTS SSASSSSSTD TTSTTTTSST ANPTVSSVPS
SQPPPGTDQH LSQLLGSLLG TASSGMSNIT MGSPSITVTV PGMPAFLQGV TDILQATQTV
PVSTAPTQSA SQAPPPSSPP PPPAHSSPPP AAAPESLPPE FFTSVVQGVL SSMLGSLSAA
DQSGTESIAA FIQRLSGTHN IFQPDAEGPG GFFGDLLTLI CHNFSLVDMV MLLHGHSQPL
QNLQPQLRSF FLQEYLHQVD PTPNNIQMAS RNLTNGLEEY IRESFASVTV RDDVDITRTN
IEFLQDQFNR ITTHILHCAD STFGQRLLEM CNQSLFEWLA LNLYCLRGDQ NALTSVINER
IRRLSLDVSP VLVSWVTSVL SLRLQVLLGQ MPVTEGEIQR HVRRVGDAPQ VPEPSSQEQP
METMPVDCQN GAASPVLATH SGGVLFLPPQ SSVPTICPDS DHPTQEDGGS EQWAASVPPE
WVPVIRQDMQ NQRKIKQQPP LSDAYLSGMP AKRRKTMQGE GPHLSLSEAV SRAMKATGAK
PESSAECVRR ELDNSEAQGR YREQLCQDIQ KTLQDNESYS AQRFPNTQRA FRGDP
