BAG6B_XENLA
ID BAG6B_XENLA Reviewed; 1116 AA.
AC Q6PA26;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Large proline-rich protein bag6-B {ECO:0000305};
DE AltName: Full=BCL2-associated athanogene 6 {ECO:0000250|UniProtKB:P46379};
DE AltName: Full=HLA-B-associated transcript 3-B {ECO:0000305};
GN Name=Bag6-b {ECO:0000305}; Synonyms=bat3-b {ECO:0000305};
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 [LARGE SCALE MRNA].
RC TISSUE=Lung;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) 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; BC060479; AAH60479.1; -; mRNA.
DR RefSeq; NP_001083439.1; NM_001089970.1.
DR AlphaFoldDB; Q6PA26; -.
DR SMR; Q6PA26; -.
DR PRIDE; Q6PA26; -.
DR DNASU; 398926; -.
DR GeneID; 398926; -.
DR KEGG; xla:398926; -.
DR CTD; 398926; -.
DR Xenbase; XB-GENE-865204; bag6.S.
DR OrthoDB; 1233552at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 398926; Expressed in testis 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..1116
FT /note="Large proline-rich protein bag6-B"
FT /id="PRO_0000403754"
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 170..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 533..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..383
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..676
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1065..1079
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1116 AA; 119354 MW; 08F9042F20677EA0 CRC64;
MAANEKMDVT VKTLDSQTRT FTVEAEILVK EFKAHISSAV GITPEKQRLI YQGRVLQEDK
KLNEYNVDGK VIHLVERAPP QTQTSTSGPS TSSSTSPSSS NAAPVPGAPE RNGNSYVMVG
TFNLPHVMSG LGEASRGPSV STISGSEPRV RLVLAQNILQ DIQRNLDRLE GQPGNEQAAE
PMDTAESEGE ASSRETLPQT TQNADGQSNS TPTSHPSPSE YVEVLQSLSR VEERLAPFMQ
RYREILSSAT SDTYENQERE QSQRIINLVG ESLRLLGNAL VAVSDLRCNL SSASPRHLHV
VRPMSHYSGP MLLQQAAIPI QINVGTTVST TGNGTHAGHV PSDGNATPST NTSEHQRSNS
ENQPPPSGER PASDAPPNSV PHPHPRVIRI THQTVEPVMM MHMNIQDSAS GGPTNIPPPT
AGHGGSAHIH MPGLPPEFMQ AISNQITQQA MAAASGQQIP GFQAPPRFVF TRPAAPSFNF
QPGAAATTPP APGGATTTAP GATVGPAGNA SLAQMISGLV GQLLMHPVVV AQGGSSTSST
TSTSTSTSTS SSTSSSSSTV PTSTTTTTST SFPNVSSVPS AQLPPGTDQH LSQLLGSLLG
TASSGMSNLT MGSPSITVTV PGMPAFLQGV TDILQATQTV PVSTSPPQSA SQAPPPPSSP
APPAHSAPPP AAAPESLPPE FFTSVVQGVL SSMLGSLSAA DQSGTESIAD FIQRLSGSHN
IFQPDAEGPG GFFGDLLTLI CHNFSLVDMV MLLHGHSQPL QNLQPQLRSF FLQEYLHQAD
PTPNNIQMAS RNLTNGLEEY IRESFASVTV RDDVDITRTN LEFLQDQFNR ITTHILHCAD
STFGQRLLEM CNQSLFEWLA LNLYCLRGDQ NALTSVINER IRRLSLDVSP VLVSWVTSVL
SLRLQVLLGQ MPVTEGEIQR HVRRVGDASQ VPEPSSQEQP METMPVDFQQ NGAASPVPAT
TVEEVLFLPP QSSVPTICPD SEHPTQGDSV SEQWTASVPP EWVPVIRQDL QNQRKIKQQP
PLSDAYLSGM PAKRRKTMQG EGPHLSLSEA VSRAMKVTGA KPESSTECVK RELDNSEAQG
EYKEQLCQDI QEILQDDESY TAQRFPNTHR AFRGDP
