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Large proline-rich protein bag6-A (BCL2-associated athanogene 6) (HLA-B-associated transcript 3-A) (Protein Scythe)

 BAG6A_XENLA             Reviewed;        1135 AA.
Q9YHD3;
11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
18-JUL-2018, entry version 71.
RecName: Full=Large proline-rich protein bag6-A {ECO:0000305};
AltName: Full=BCL2-associated athanogene 6 {ECO:0000250|UniProtKB:P46379};
AltName: Full=HLA-B-associated transcript 3-A {ECO:0000305|PubMed:9799223};
AltName: Full=Protein Scythe {ECO:0000303|PubMed:9799223};
Name=Bag6-a {ECO:0000305};
Synonyms=bat3-a {ECO:0000305|PubMed:9799223};
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=9799223; DOI=10.1093/emboj/17.21.6135;
Thress K., Henzel W., Shillinglaw W., Kornbluth S.;
"Scythe: a novel reaper-binding apoptotic regulator.";
EMBO J. 17:6135-6143(1998).
-!- FUNCTION: ATP-independent molecular chaperone preventing the
aggregation of misfolded and hydrophobic patches-containing
proteins. Functions as part of a cytosolic protein quality control
complex, the bag6/bat3 complex, which maintains these client
proteins in a soluble state and participates to their proper
delivery to the endoplasmic reticulum or alternatively can promote
their sorting to the proteasome where they undergo degradation.
The bag6/bat3 complex is involved in the post-translational
delivery of tail-anchored/type II transmembrane proteins to the
endoplasmic reticulum membrane. Similarly, the bag6/bat3 complex
also functions as a sorting platform for proteins of the secretory
pathway that are mislocalized to the cytosol either delivering
them to the proteasome for degradation or to the endoplasmic
reticulum. The bag6/bat3 complex also plays a role in the
endoplasmic reticulum-associated degradation (ERAD), a quality
control mechanism that eliminates unwanted proteins of the
endoplasmic reticulum through their retrotranslocation to the
cytosol and their targeting to the proteasome. It maintains these
retrotranslocated proteins in an unfolded yet soluble state
condition in the cytosol to ensure their proper delivery to the
proteasome. Also required for selective ubiquitin-mediated
degradation of defective nascent chain polypeptides by the
proteasome. Also involved in endoplasmic reticulum stress-induced
pre-emptive quality control, a mechanism that selectively
attenuates the translocation of newly synthesized proteins into
the endoplasmic reticulum and reroutes them to the cytosol for
proteasomal degradation. May ensure the proper degradation of
these proteins and thereby protects the endoplasmic reticulum from
protein overload upon stress (By similarity). By stabilizing a
large spectrum of proteins, may indirectly affect different
biological processes including apoptosis (PubMed:9799223). By
controlling the steady-state expression of the IGF1R receptor,
indirectly regulates the insulin-like growth factor receptor
signaling pathway (By similarity). {ECO:0000250|UniProtKB:P46379,
ECO:0000269|PubMed:9799223}.
-!- FUNCTION: When nuclear, may also act as a component of some
chromatin regulator complex. {ECO:0000250|UniProtKB:P46379}.
-!- SUBUNIT: Component of the bag6/bat3 complex.
{ECO:0000250|UniProtKB:P46379}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P46379}. Nucleus
{ECO:0000250|UniProtKB:P46379}. Secreted, exosome
{ECO:0000250|UniProtKB:P46379}.
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EMBL; AF098511; AAC83822.1; -; mRNA.
PIR; T30561; T30561.
RefSeq; NP_001080008.1; NM_001086539.1.
UniGene; Xl.422; -.
ProteinModelPortal; Q9YHD3; -.
SMR; Q9YHD3; -.
BioGrid; 97941; 3.
PRIDE; Q9YHD3; -.
GeneID; 379698; -.
KEGG; xla:379698; -.
CTD; 379698; -.
Xenbase; XB-GENE-6255172; bag6.
HOVERGEN; HBG002193; -.
GO; GO:0071818; C:BAT3 complex; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
GO; GO:0070628; F:proteasome binding; ISS:UniProtKB.
GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
GO; GO:0007420; P:brain development; ISS:UniProtKB.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0061857; P:endoplasmic reticulum stress-induced pre-emptive quality control; ISS:UniProtKB.
GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISS:UniProtKB.
GO; GO:0018393; P:internal peptidyl-lysine acetylation; ISS:UniProtKB.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISS:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0001822; P:kidney development; ISS:UniProtKB.
GO; GO:0030324; P:lung development; ISS:UniProtKB.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0045861; P:negative regulation of proteolysis; ISS:UniProtKB.
GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
GO; GO:0007130; P:synaptonemal complex assembly; ISS:UniProtKB.
GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; ISS:UniProtKB.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
InterPro; IPR021925; BAG6.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR000626; Ubiquitin_dom.
Pfam; PF12057; DUF3538; 1.
Pfam; PF00240; ubiquitin; 1.
SMART; SM00213; UBQ; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50053; UBIQUITIN_2; 1.
2: Evidence at transcript level;
Apoptosis; Chaperone; Chromatin regulator; Cytoplasm; Nucleus;
Secreted; Transport.
CHAIN 1 1135 Large proline-rich protein bag6-A.
/FTId=PRO_0000403753.
DOMAIN 7 82 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
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


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