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Large proline-rich protein BAG6 (BCL2-associated athanogene 6) (HLA-B-associated transcript 3)

 BAG6_RAT                Reviewed;        1146 AA.
Q6MG49; Q498N5; Q9WTN8;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
22-NOV-2017, entry version 107.
RecName: Full=Large proline-rich protein BAG6 {ECO:0000305};
AltName: Full=BCL2-associated athanogene 6 {ECO:0000312|RGD:71064};
AltName: Full=HLA-B-associated transcript 3 {ECO:0000303|PubMed:10390159};
Name=Bag6 {ECO:0000312|RGD:71064};
Synonyms=Bat3 {ECO:0000303|PubMed:10390159};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=10390159; DOI=10.1089/104454999315222;
Ozaki T., Hanaoka E., Naka M., Nakagawara A., Sakiyama S.;
"Cloning and characterization of rat BAT3 cDNA.";
DNA Cell Biol. 18:503-512(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15060004; DOI=10.1101/gr.1987704;
Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T.,
Inoko H., Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
"The genomic sequence and comparative analysis of the rat major
histocompatibility complex.";
Genome Res. 14:631-639(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-987 AND SER-1095, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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. Recruited to ribosomes, it
interacts with the transmembrane region of newly synthesized tail-
anchored proteins and together with SGTA and ASNA1 mediates their
delivery to the endoplasmic reticulum. Client proteins that cannot
be properly delivered to the endoplasmic reticulum are
ubiquitinated by RNF126, an E3 ubiquitin-protein ligase associated
with BAG6 and are sorted to the proteasome. SGTA which prevents
the recruitment of RNF126 to BAG6 may negatively regulate the
ubiquitination and the proteasomal degradation of client proteins.
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. BAG6 is also required for
selective ubiquitin-mediated degradation of defective nascent
chain polypeptides by the proteasome. In this context, it may
participate to the production of antigenic peptides and play a
role in antigen presentation in immune response. BAG6 is 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. BAG6 may ensure the proper degradation of these
proteins and thereby protects the endoplasmic reticulum from
protein overload upon stress. By inhibiting the polyubiquitination
and subsequent proteasomal degradation of HSPA2 it may also play a
role in the assembly of the synaptonemal complex during
spermatogenesis. Also positively regulates apoptosis by
interacting with and stabilizing the proapoptotic factor AIFM1.
{ECO:0000250|UniProtKB:P46379}.
-!- FUNCTION: Involved in DNA damage-induced apoptosis: following DNA
damage, accumulates in the nucleus and forms a complex with
p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation
leading to increase p53/TP53 transcriptional activity. When
nuclear, may also act as a component of some chromatin regulator
complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2).
{ECO:0000250|UniProtKB:P46379}.
-!- FUNCTION: Released extracellularly via exosomes, it is a ligand of
the natural killer/NK cells receptor NCR3 and stimulates NK cells
cytotoxicity. It may thereby trigger NK cells cytotoxicity against
neighboring tumor cells and immature myeloid dendritic cells (DC).
{ECO:0000250|UniProtKB:P46379}.
-!- FUNCTION: May mediate ricin-induced apoptosis.
{ECO:0000250|UniProtKB:P46379}.
-!- SUBUNIT: Component of the BAG6/BAT3 complex, also named BAT3
complex, at least composed of BAG6, UBL4A and GET4/TRC35.
Interacts with GET4; the interaction is direct and localizes BAG6
in the cytosol (By similarity). Interacts with AIFM1. Interacts
with HSPA2 (By similarity). Interacts with CTCFL. Interacts with
p300/EP300. Interacts (via ubiquitin-like domain) with RNF126;
required for BAG6-dependent ubiquitination of proteins
mislocalized to the cytosol. Interacts (via ubiquitin-like domain)
with SGTA; SGTA competes with RNF126 by binding the same region of
BAG6, thereby promoting deubiquitination of BAG6-target proteins
and rescuing them from degradation. Interacts with ricin A chain.
Interacts with VCP and AMFR; both form the VCP/p97-AMFR/gp78
complex. Interacts with SYVN1. Interacts with USP13; the
interaction is direct and may mediate UBL4A deubiquitination (By
similarity). {ECO:0000250|UniProtKB:P46379,
ECO:0000250|UniProtKB:Q9Z1R2}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P46379}. Nucleus
{ECO:0000250|UniProtKB:P46379}. Secreted, exosome
{ECO:0000250|UniProtKB:P46379}. Note=Normally localized in cytosol
and nucleus, it can also be released extracellularly, in exosomes,
by tumor and myeloid dendritic cells.
{ECO:0000250|UniProtKB:P46379}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6MG49-1; Sequence=Displayed;
Name=2;
IsoId=Q6MG49-2; Sequence=VSP_040420, VSP_040421;
-!- DOMAIN: The ubiquitin-like domain mediates interaction with the E3
ubiquitin-protein ligase RNF126 which is responsible for the BAG6-
dependent ubiquitination of client proteins. SGTA also binds this
domain and competes with RNF126 to antagonize client protein
ubiquitination and degradation. The ubiquitin-like domain also
mediates the interaction with USP13.
{ECO:0000250|UniProtKB:P46379}.
-!- PTM: Ricin can induce a cleavage by the caspase CASP3. The
released C-terminal peptide induces apoptosis.
{ECO:0000250|UniProtKB:P46379}.
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EMBL; AB018791; BAA76607.1; -; mRNA.
EMBL; BX883045; CAE83997.1; -; Genomic_DNA.
EMBL; CH474121; EDL83534.1; -; Genomic_DNA.
EMBL; BC100141; AAI00142.1; -; mRNA.
RefSeq; NP_001029140.1; NM_001033968.1. [Q6MG49-1]
RefSeq; NP_446061.2; NM_053609.2. [Q6MG49-2]
UniGene; Rn.203343; -.
ProteinModelPortal; Q6MG49; -.
SMR; Q6MG49; -.
BioGrid; 250197; 2.
IntAct; Q6MG49; 2.
MINT; MINT-4566953; -.
STRING; 10116.ENSRNOP00000057557; -.
iPTMnet; Q6MG49; -.
PhosphoSitePlus; Q6MG49; -.
PaxDb; Q6MG49; -.
PRIDE; Q6MG49; -.
Ensembl; ENSRNOT00000001129; ENSRNOP00000001129; ENSRNOG00000000851. [Q6MG49-2]
Ensembl; ENSRNOT00000060832; ENSRNOP00000057557; ENSRNOG00000000851. [Q6MG49-1]
GeneID; 94342; -.
KEGG; rno:94342; -.
UCSC; RGD:71064; rat. [Q6MG49-1]
CTD; 7917; -.
RGD; 71064; Bag6.
eggNOG; KOG4248; Eukaryota.
eggNOG; ENOG410XS9P; LUCA.
GeneTree; ENSGT00390000016199; -.
HOGENOM; HOG000095177; -.
HOVERGEN; HBG002193; -.
InParanoid; Q6MG49; -.
OMA; LPVHVMT; -.
OrthoDB; EOG091G0XSR; -.
PhylomeDB; Q6MG49; -.
TreeFam; TF328437; -.
PRO; PR:Q6MG49; -.
Proteomes; UP000002494; Chromosome 20.
Bgee; ENSRNOG00000000851; -.
ExpressionAtlas; Q6MG49; baseline and differential.
Genevisible; Q6MG49; RN.
GO; GO:0071818; C:BAT3 complex; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; ISO:RGD.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0051787; F:misfolded protein binding; ISO:RGD.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
GO; GO:0070628; F:proteasome binding; ISS:UniProtKB.
GO; GO:0005102; F:receptor binding; ISO:RGD.
GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
GO; GO:0015643; F:toxic substance binding; ISO:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:RGD.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0007420; P:brain development; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0009790; P:embryo development; ISS:UniProtKB.
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:0002429; P:immune response-activating cell surface receptor signaling pathway; ISO:RGD.
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:1904378; P:maintenance of unfolded protein involved in ERAD pathway; ISO:RGD.
GO; GO:0030101; P:natural killer cell activation; ISO:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
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:1904294; P:positive regulation of ERAD pathway; ISO:RGD.
GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
GO; GO:0042127; P:regulation of cell proliferation; IEP:RGD.
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:0006810; P:transport; IEA:UniProtKB-KW.
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; IPR019954; Ubiquitin_CS.
InterPro; IPR000626; Ubiquitin_dom.
Pfam; PF12057; DUF3538; 1.
Pfam; PF00240; ubiquitin; 1.
SMART; SM00213; UBQ; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS00299; UBIQUITIN_1; 1.
PROSITE; PS50053; UBIQUITIN_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Apoptosis; Chaperone;
Chromatin regulator; Complete proteome; Cytoplasm; Differentiation;
Immunity; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Secreted; Spermatogenesis; Transport.
CHAIN 1 1146 Large proline-rich protein BAG6.
/FTId=PRO_0000114899.
DOMAIN 17 92 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
REPEAT 236 265 1. {ECO:0000250|UniProtKB:P46379}.
REPEAT 410 438 2. {ECO:0000250|UniProtKB:P46379}.
REPEAT 589 616 3. {ECO:0000250|UniProtKB:P46379}.
REPEAT 622 650 4. {ECO:0000250|UniProtKB:P46379}.
REGION 236 650 4 X 29 AA approximate repeats.
{ECO:0000250|UniProtKB:P46379}.
REGION 1036 1146 Mediates interaction with UBL4A and GET4
and is sufficient for the delivery of
client proteins to the endoplasmic
reticulum.
{ECO:0000250|UniProtKB:P46379}.
COMPBIAS 196 268 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
COMPBIAS 389 711 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
SITE 1015 1016 Cleavage; by CASP3.
{ECO:0000250|UniProtKB:P46379}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P46379}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000250|UniProtKB:P46379}.
MOD_RES 117 117 Phosphothreonine.
{ECO:0000250|UniProtKB:P46379}.
MOD_RES 978 978 Phosphoserine.
{ECO:0000250|UniProtKB:P46379}.
MOD_RES 987 987 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1067 1067 Phosphothreonine.
{ECO:0000250|UniProtKB:P46379}.
MOD_RES 1095 1095 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 1131 1131 Phosphoserine.
{ECO:0000250|UniProtKB:P46379}.
VAR_SEQ 522 522 Missing (in isoform 2).
{ECO:0000303|PubMed:10390159}.
/FTId=VSP_040420.
VAR_SEQ 1067 1115 Missing (in isoform 2).
{ECO:0000303|PubMed:10390159}.
/FTId=VSP_040421.
CONFLICT 4 4 S -> N (in Ref. 1; BAA76607).
{ECO:0000305}.
CONFLICT 11 11 M -> V (in Ref. 1; BAA76607).
{ECO:0000305}.
CONFLICT 47 47 A -> R (in Ref. 1; BAA76607).
{ECO:0000305}.
CONFLICT 74 74 D -> E (in Ref. 1; BAA76607).
{ECO:0000305}.
CONFLICT 93 93 Q -> H (in Ref. 1; BAA76607).
{ECO:0000305}.
CONFLICT 114 114 L -> C (in Ref. 1; BAA76607).
{ECO:0000305}.
CONFLICT 189 189 T -> N (in Ref. 1; BAA76607).
{ECO:0000305}.
CONFLICT 264 265 NH -> TQ (in Ref. 1; BAA76607).
{ECO:0000305}.
CONFLICT 567 567 T -> TAQ (in Ref. 1; BAA76607).
{ECO:0000305}.
SEQUENCE 1146 AA; 120012 MW; 9CAA4CD9C04F3C29 CRC64;
MEPSDSTSTA MEEPDSLEVL VKTLDSQTRT FIVGAQMNVK EFKEHIAASV SIPSEKQRLI
YQGRVLQDDK KLQDYNVGGK VIHLVERAPP QTQLPSGASS GTGSASATHG GGPLPGTRGP
GASGHDRNAN SYVMVGTFNL PSDGSAVDVH INMEQAPIQS EPRVRLVMAQ HMIRDIQTLL
SRMECRGGTQ AQASQPPPQT PTVASETVAL NSQTSEPVES EAPPREPMES EEMEERPPTQ
TPELPPSGPA PAGPAPAPET NAPNHPSPAE HVEVLQELQR LQRRLQPFLQ RYCEVLGAAA
TTDYNNNHEG REEDQRLINL VGESLRLLGN TFVALSDLRC NLACAPPRHL HVVRPMSHYT
TPMVLQQAAI PIQINVGTTV TMTGNGARPP PAPGAEAASP GSGQASSLPP SSATVDSSTE
GAPPPGPAPP PATSHPRVIR ISHQSVEPVV MMHMNIQDSG AQPGGVPSAP TGPLGPPGHG
QSLGQQVPGF PTAPTRVVIA RPTPPQARPS HPGGPPVSGA LQGAGLGTNT SLAQMVSGLV
GQLLMQPVLV AQGTPGMAPA SASAPATAQA QAPAPAPAPA PAPATASASA GTTNTATTAG
PAPGGPAQPP PPQPSAADLQ FSQLLGNLLG PAGPGAGGPS LASPTITVAV PGVPAFLQGM
TEFLQASQAA PPPPPPPPPP PPAPEQQTTP PPGSPSGGTA SPGGLGPESL PPEFFTSVVQ
GVLSSLLGSL GARAGSSESI AAFIQRLSGS SNIFEPGADG ALGFFGALLS LLCQNFSMVD
VVMLLHGHFQ PLQRLQPQLR SFFHQHYLGG QEPTSSNIRM ATHTLITGLE EYVRESFSLV
QVQPGVDIIR TNLEFLQEQF NSIAAHVLHC TDSGFGARLL ELCNQGLFEC LALNLHCLGG
QQMELAAVIN GRIRRMSRGV NPSLVSWLTT MMGLRLQVVL EHMPVGPDAI LRYVRRIGDP
PQALPEEPME VQGAERTSPE PQREDASPAP GTTAEEAMSR GPPPAPEGGS RDEQDGASAD
AEPWAAAVPP EWVPIIQQDI QSQRKVKPQP PLSDAYLSGM PAKRRKTMQG EGPQLLLSEA
VSRAAKAAGA RPLTSPESLS RDLEAPEVQE SYRQQLRSDI QKRLQEDPNY SPQRFPNAHR
AFADDP


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