BAG6_DANRE
ID BAG6_DANRE Reviewed; 1160 AA.
AC A3KPW9;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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};
GN ORFNames=si:ch211-215a10.6 {ECO:0000312|EMBL:CAM56392.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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; BX510301; CAM56392.1; -; Genomic_DNA.
DR RefSeq; NP_001315205.1; NM_001328276.1.
DR AlphaFoldDB; A3KPW9; -.
DR SMR; A3KPW9; -.
DR STRING; 7955.ENSDARP00000117226; -.
DR PaxDb; A3KPW9; -.
DR PeptideAtlas; A3KPW9; -.
DR Ensembl; ENSDART00000088760; ENSDARP00000083193; ENSDARG00000077531.
DR Ensembl; ENSDART00000135128; ENSDARP00000117226; ENSDARG00000077531.
DR GeneID; 751663; -.
DR KEGG; dre:751663; -.
DR CTD; 751663; -.
DR ZFIN; ZDB-GENE-060307-2; bag6l.
DR eggNOG; KOG4248; Eukaryota.
DR GeneTree; ENSGT00390000016199; -.
DR HOGENOM; CLU_012159_0_0_1; -.
DR InParanoid; A3KPW9; -.
DR OrthoDB; 1233552at2759; -.
DR PhylomeDB; A3KPW9; -.
DR TreeFam; TF328437; -.
DR PRO; PR:A3KPW9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000077531; Expressed in blastula and 20 other tissues.
DR ExpressionAtlas; A3KPW9; baseline.
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 3: Inferred from homology;
KW Apoptosis; Chaperone; Chromatin regulator; Cytoplasm; Nucleus;
KW Reference proteome; Secreted; Transport.
FT CHAIN 1..1160
FT /note="Large proline-rich protein BAG6"
FT /id="PRO_0000403752"
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 206..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..699
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1160 AA; 124121 MW; 11C550916176775A CRC64;
MEESGVIEVT VKTLDSQSRT FTVRGEWTVK QFKEHIAASV EISVDKQRLI YQGKVLQDER
TLTEYNVDGK VIHLVERPPP QSSQPGGGGG GVSGSSGAAD GGSSSSQSSA YTTSHDRNAN
NYVMLGTFNL PVNIMDPQQI QMSVQQMLAG VGEMGRNVRV STSTGSSGSV DVHINVDQSV
QSEPRMRLHL AENLLRETQA LIHRLEGQSS EPSQQETPPP QPSSSSFSAH PMDSSPPPPS
VSSSASQTEG ETQSGPNHPS PLELVEVLSE VRRVEERLRP FMERTHSILG AATSADYNNN
TQEREEDQRT LNLIGESLHL LGNTLVALSD LRCNLSAQPP RHLHVVRPMS HYTSPVMMQS
GLPHIPIPMN LGSTVTMTSN SRQTSDGQPQ PPHSSNQSDQ QGQAPPTPAN ESNQQTGHGQ
GTPRVIRITH QTMEPVVMMQ MNLDGTTVPL HVPGLPPEFM QAIMHQISQQ AVTMATAASA
GHQGQQQGTA GAGAQNGESP VPPPPQARVV ITRPTLSPRV PQPMGTRGTT INLRAAVPPP
SGQQTNQMVS GLVGQLLLPL HTGDQTSTTS SSHSFSFSTS SSTSSSSSFS SASPPLSSAN
TSGQTSTHTT STASVGQAQE SGPGDNLAQL LGSLLGGAAG AGGGVSGATP SITVTVPGVP
AFIQGLSEFI QSGQPVFPSP NQQPPPSQAT PPSAPSGPAP TTAPSGGAET LSPELFTGIV
QGVLSTMMGS LGAGQGNTES IAQFIQRLSQ TSNLFTPGAG DAVGFFGDLL SLVCQSFSMV
DMVLLLHGNP QPLSRIQPQL TAFFTEHYLQ GREPTDANIA SASEDLINEL EEYIAESFST
VTVREGVDII QTNMSFLRQQ FTRMATHILR CTDNTFGQRL LYLCTQGLFE CLALNLYCLR
GEQRALTTVI NHRIRRMSAE VNPSLVNWLT SMMSMRLHVI LEHNPVTEDQ IQHYVIYTQS
ESARRTEAGS QSSQQSQNMN VEEGLSPAPA TTAEEALRST GDTDGDEAPG RPSAEETRGA
VAMATTEREE STGEAEPWAA TVPPEWVPII RRDMLTQRKM KAQPPLSDAY MHGMPAKRRK
TAQGEGPHLS LTEAVSRAAR TAGVRPVTAP DSLQGELETP ELQEAYAQQV KSDIKKRLSD
DPDYNHQRFP NTHRVFSEDA
