BAG6_MOUSE
ID BAG6_MOUSE Reviewed; 1154 AA.
AC Q9Z1R2; Q8SNA3;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Large proline-rich protein BAG6 {ECO:0000305};
DE AltName: Full=BAG family molecular chaperone regulator 6;
DE AltName: Full=BCL2-associated athanogene 6 {ECO:0000312|MGI:MGI:1919439};
DE Short=BAG-6 {ECO:0000303|PubMed:20713601};
DE AltName: Full=HLA-B-associated transcript 3 {ECO:0000303|PubMed:14656967};
DE AltName: Full=Protein Scythe {ECO:0000303|PubMed:16287848};
GN Name=Bag6 {ECO:0000312|MGI:MGI:1919439};
GN Synonyms=Bat3 {ECO:0000303|PubMed:14656967};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-1154.
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=16287848; DOI=10.1128/mcb.25.23.10329-10337.2005;
RA Desmots F., Russell H.R., Lee Y., Boyd K., McKinnon P.J.;
RT "The reaper-binding protein scythe modulates apoptosis and proliferation
RT during mammalian development.";
RL Mol. Cell. Biol. 25:10329-10337(2005).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=17403783; DOI=10.1101/gad.1534107;
RA Sasaki T., Gan E.C., Wakeham A., Kornbluth S., Mak T.W., Okada H.;
RT "HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated
RT acetylation of p53.";
RL Genes Dev. 21:848-861(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-995, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP FUNCTION, INTERACTION WITH AIFM1, AND SUBCELLULAR LOCATION.
RX PubMed=18056262; DOI=10.1074/jbc.m706419200;
RA Desmots F., Russell H.R., Michel D., McKinnon P.J.;
RT "Scythe regulates apoptosis-inducing factor stability during endoplasmic
RT reticulum stress-induced apoptosis.";
RL J. Biol. Chem. 283:3264-3271(2008).
RN [8]
RP FUNCTION, AND INTERACTION WITH HSPA2.
RX PubMed=18678708; DOI=10.1083/jcb.200802113;
RA Sasaki T., Marcon E., McQuire T., Arai Y., Moens P.B., Okada H.;
RT "Bat3 deficiency accelerates the degradation of Hsp70-2/HspA2 during
RT spermatogenesis.";
RL J. Cell Biol. 182:449-458(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-995, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION.
RX PubMed=20713601; DOI=10.1083/jcb.200908092;
RA Minami R., Hayakawa A., Kagawa H., Yanagi Y., Yokosawa H., Kawahara H.;
RT "BAG-6 is essential for selective elimination of defective proteasomal
RT substrates.";
RL J. Cell Biol. 190:637-650(2010).
RN [11]
RP INTERACTION WITH ZFAND2B.
RX PubMed=24160817; DOI=10.1042/bj20130710;
RA Glinka T., Alter J., Braunstein I., Tzach L., Wei Sheng C., Geifman S.,
RA Edelmann M.J., Kessler B.M., Stanhill A.;
RT "Signal-peptide-mediated translocation is regulated by a p97-AIRAPL
RT complex.";
RL Biochem. J. 457:253-261(2014).
RN [12]
RP INTERACTION WITH ZFAND2B.
RX PubMed=26337389; DOI=10.1091/mbc.e15-02-0085;
RA Braunstein I., Zach L., Allan S., Kalies K.U., Stanhill A.;
RT "Proteasomal degradation of preemptive quality control (pQC) substrates is
RT mediated by an AIRAPL-p97 complex.";
RL Mol. Biol. Cell 26:3719-3727(2015).
RN [13]
RP INTERACTION WITH ZFAND2B.
RX PubMed=26876100; DOI=10.1016/j.str.2015.12.017;
RA Rahighi S., Braunstein I., Ternette N., Kessler B., Kawasaki M., Kato R.,
RA Matsui T., Weiss T.M., Stanhill A., Wakatsuki S.;
RT "Selective Binding of AIRAPL Tandem UIMs to Lys48-Linked Tri-Ubiquitin
RT Chains.";
RL Structure 24:412-422(2016).
CC -!- FUNCTION: ATP-independent molecular chaperone preventing the
CC aggregation of misfolded and hydrophobic patches-containing proteins
CC (PubMed:18056262, PubMed:18678708, PubMed:20713601). Functions as part
CC of a cytosolic protein quality control complex, the BAG6/BAT3 complex,
CC which maintains these client proteins in a soluble state and
CC participates in their proper delivery to the endoplasmic reticulum or
CC alternatively can promote their sorting to the proteasome where they
CC undergo degradation (PubMed:20713601). The BAG6/BAT3 complex is
CC involved in the post-translational delivery of tail-anchored/type II
CC transmembrane proteins to the endoplasmic reticulum membrane. Recruited
CC to ribosomes, it interacts with the transmembrane region of newly
CC synthesized tail-anchored proteins and together with SGTA and ASNA1
CC mediates their delivery to the endoplasmic reticulum. Client proteins
CC that cannot be properly delivered to the endoplasmic reticulum are
CC ubiquitinated by RNF126, an E3 ubiquitin-protein ligase associated with
CC BAG6 and are sorted to the proteasome. SGTA which prevents the
CC recruitment of RNF126 to BAG6 may negatively regulate the
CC ubiquitination and the proteasomal degradation of client proteins.
CC Similarly, the BAG6/BAT3 complex also functions as a sorting platform
CC for proteins of the secretory pathway that are mislocalized to the
CC cytosol either delivering them to the proteasome for degradation or to
CC the endoplasmic reticulum. The BAG6/BAT3 complex also plays a role in
CC the endoplasmic reticulum-associated degradation (ERAD), a quality
CC control mechanism that eliminates unwanted proteins of the endoplasmic
CC reticulum through their retrotranslocation to the cytosol and their
CC targeting to the proteasome. It maintains these retrotranslocated
CC proteins in an unfolded yet soluble state condition in the cytosol to
CC ensure their proper delivery to the proteasome (By similarity). BAG6 is
CC also required for selective ubiquitin-mediated degradation of defective
CC nascent chain polypeptides by the proteasome. In this context, it may
CC participate in the production of antigenic peptides and play a role in
CC antigen presentation in immune response (PubMed:20713601). BAG6 is also
CC involved in endoplasmic reticulum stress-induced pre-emptive quality
CC control, a mechanism that selectively attenuates the translocation of
CC newly synthesized proteins into the endoplasmic reticulum and reroutes
CC them to the cytosol for proteasomal degradation. BAG6 may ensure the
CC proper degradation of these proteins and thereby protects the
CC endoplasmic reticulum from protein overload upon stress (By
CC similarity). By inhibiting the polyubiquitination and subsequent
CC proteasomal degradation of HSPA2 it may also play a role in the
CC assembly of the synaptonemal complex during spermatogenesis
CC (PubMed:18678708). Also positively regulates apoptosis by interacting
CC with and stabilizing the proapoptotic factor AIFM1 (PubMed:18056262).
CC By controlling the steady-state expression of the IGF1R receptor,
CC indirectly regulates the insulin-like growth factor receptor signaling
CC pathway (By similarity). {ECO:0000250|UniProtKB:P46379,
CC ECO:0000269|PubMed:18056262, ECO:0000269|PubMed:18678708,
CC ECO:0000269|PubMed:20713601}.
CC -!- FUNCTION: Involved in DNA damage-induced apoptosis: following DNA
CC damage, accumulates in the nucleus and forms a complex with p300/EP300,
CC enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase
CC p53/TP53 transcriptional activity. When nuclear, may also act as a
CC component of some chromatin regulator complex that regulates histone 3
CC 'Lys-4' dimethylation (H3K4me2). {ECO:0000250|UniProtKB:P46379}.
CC -!- FUNCTION: Released extracellularly via exosomes, it is a ligand of the
CC natural killer/NK cells receptor NCR3 and stimulates NK cells
CC cytotoxicity. It may thereby trigger NK cells cytotoxicity against
CC neighboring tumor cells and immature myeloid dendritic cells (DC).
CC {ECO:0000250|UniProtKB:P46379}.
CC -!- FUNCTION: May mediate ricin-induced apoptosis.
CC {ECO:0000250|UniProtKB:P46379}.
CC -!- SUBUNIT: Component of the BAG6/BAT3 complex, also named BAT3 complex,
CC at least composed of BAG6, UBL4A and GET4/TRC35. Interacts with GET4;
CC the interaction is direct and localizes BAG6 in the cytosol (By
CC similarity). Interacts with UBL4A; the interaction is direct and
CC required for UBL4A protein stability (By similarity). Interacts with
CC AIFM1 (PubMed:18056262). Interacts with HSPA2 (PubMed:18678708).
CC Interacts with CTCFL. Interacts with p300/EP300. Interacts (via
CC ubiquitin-like domain) with RNF126; required for BAG6-dependent
CC ubiquitination of proteins mislocalized to the cytosol. Interacts (via
CC ubiquitin-like domain) with SGTA; SGTA competes with RNF126 by binding
CC the same region of BAG6, thereby promoting deubiquitination of BAG6-
CC target proteins and rescuing them from degradation. Interacts with
CC ricin A chain. Interacts with VCP and AMFR; both form the VCP/p97-
CC AMFR/gp78 complex. Interacts with SYVN1. Interacts with USP13; the
CC interaction is direct and may mediate UBL4A deubiquitination (By
CC similarity). Interacts with ZFAND2B (PubMed:24160817, PubMed:26337389,
CC PubMed:26876100). Interacts with KPNA2 (By similarity). Interacts with
CC UBQLN4 (By similarity). {ECO:0000250|UniProtKB:P46379,
CC ECO:0000269|PubMed:18056262, ECO:0000269|PubMed:18678708,
CC ECO:0000269|PubMed:24160817, ECO:0000269|PubMed:26337389,
CC ECO:0000269|PubMed:26876100}.
CC -!- INTERACTION:
CC Q9Z1R2; P11798-2: Camk2a; NbExp=3; IntAct=EBI-644645, EBI-400402;
CC Q9Z1R2; O35305: Tnfrsf11a; NbExp=4; IntAct=EBI-644645, EBI-647362;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18056262}.
CC Nucleus {ECO:0000250|UniProtKB:P46379}. Secreted, extracellular exosome
CC {ECO:0000250|UniProtKB:P46379}. Note=Normally localized in cytosol and
CC nucleus, it can also be released extracellularly, in exosomes, by tumor
CC and myeloid dendritic cells. {ECO:0000250|UniProtKB:P46379}.
CC -!- DOMAIN: The ubiquitin-like domain mediates interaction with the E3
CC ubiquitin-protein ligase RNF126 which is responsible for the BAG6-
CC dependent ubiquitination of client proteins. SGTA also binds this
CC domain and competes with RNF126 to antagonize client protein
CC ubiquitination and degradation. The ubiquitin-like domain also mediates
CC the interaction with USP13. {ECO:0000250|UniProtKB:P46379}.
CC -!- PTM: Ricin can induce a cleavage by the caspase CASP3. The released C-
CC terminal peptide induces apoptosis. {ECO:0000250|UniProtKB:P46379}.
CC -!- DISRUPTION PHENOTYPE: Lethality associated with pronounced
CC developmental defects in the lung, kidney and brain. Lethality is
CC either embryonic consecutive to abnormal brain development or perinatal
CC associated with pronounced developmental defects in the lung and
CC kidney. These developmental defects were associated with widespread
CC aberrant apoptosis and proliferation. Lethality can be partially
CC rescued in an ICR genetic background: mice are slightly smaller in size
CC than their wild-type counterparts and show impaired genotoxic stress
CC responses. {ECO:0000269|PubMed:16287848, ECO:0000269|PubMed:17403783}.
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DR EMBL; AF109719; AAC82479.1; -; Genomic_DNA.
DR EMBL; CR974444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026647; AAH26647.1; -; mRNA.
DR CCDS; CCDS28688.1; -.
DR RefSeq; NP_476512.1; NM_057171.2.
DR AlphaFoldDB; Q9Z1R2; -.
DR SMR; Q9Z1R2; -.
DR BioGRID; 230309; 21.
DR ComplexPortal; CPX-133; BAT3 complex.
DR DIP; DIP-49391N; -.
DR IntAct; Q9Z1R2; 8.
DR MINT; Q9Z1R2; -.
DR STRING; 10090.ENSMUSP00000025250; -.
DR iPTMnet; Q9Z1R2; -.
DR PhosphoSitePlus; Q9Z1R2; -.
DR EPD; Q9Z1R2; -.
DR jPOST; Q9Z1R2; -.
DR MaxQB; Q9Z1R2; -.
DR PaxDb; Q9Z1R2; -.
DR PRIDE; Q9Z1R2; -.
DR ProteomicsDB; 273649; -.
DR Antibodypedia; 27346; 307 antibodies from 37 providers.
DR Ensembl; ENSMUST00000025250; ENSMUSP00000025250; ENSMUSG00000024392.
DR GeneID; 224727; -.
DR KEGG; mmu:224727; -.
DR UCSC; uc008cgb.2; mouse.
DR CTD; 7917; -.
DR MGI; MGI:1919439; Bag6.
DR VEuPathDB; HostDB:ENSMUSG00000024392; -.
DR eggNOG; KOG4248; Eukaryota.
DR GeneTree; ENSGT00390000016199; -.
DR HOGENOM; CLU_012159_0_0_1; -.
DR InParanoid; Q9Z1R2; -.
DR OMA; SFPNEWL; -.
DR OrthoDB; 1233552at2759; -.
DR PhylomeDB; Q9Z1R2; -.
DR TreeFam; TF328437; -.
DR BioGRID-ORCS; 224727; 14 hits in 74 CRISPR screens.
DR ChiTaRS; Bag6; mouse.
DR PRO; PR:Q9Z1R2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9Z1R2; protein.
DR Bgee; ENSMUSG00000024392; Expressed in embryonic brain and 266 other tissues.
DR ExpressionAtlas; Q9Z1R2; baseline and differential.
DR Genevisible; Q9Z1R2; MM.
DR GO; GO:0071818; C:BAT3 complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0051787; F:misfolded protein binding; ISO:MGI.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:MGI.
DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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:0002429; P:immune response-activating cell surface receptor signaling pathway; ISO:MGI.
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; IMP:UniProtKB.
DR GO; GO:0001822; P:kidney development; IMP:UniProtKB.
DR GO; GO:0030324; P:lung development; IMP:UniProtKB.
DR GO; GO:1904378; P:maintenance of unfolded protein involved in ERAD pathway; ISO:MGI.
DR GO; GO:0030101; P:natural killer cell activation; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0045861; P:negative regulation of proteolysis; IMP:UniProtKB.
DR GO; GO:1904294; P:positive regulation of ERAD pathway; ISO:MGI.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR GO; GO:0007130; P:synaptonemal complex assembly; IMP: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; IMP:UniProtKB.
DR InterPro; IPR021925; BAG6.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR Pfam; PF12057; BAG6; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Chaperone; Chromatin regulator; Cytoplasm;
KW Differentiation; Immunity; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Spermatogenesis; Transport.
FT CHAIN 1..1154
FT /note="Large proline-rich protein BAG6"
FT /id="PRO_0000114898"
FT DOMAIN 17..92
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REPEAT 237..271
FT /note="1"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT REPEAT 416..444
FT /note="2"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT REPEAT 597..624
FT /note="3"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT REPEAT 630..658
FT /note="4"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT REGION 87..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..658
FT /note="4 X 29 AA approximate repeats"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT REGION 387..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1062
FT /note="Required for interaction with GET4"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT REGION 1044..1154
FT /note="Sufficient for the delivery of client proteins to
FT the endoplasmic reticulum"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT REGION 1080..1137
FT /note="BAG-similar domain, required and sufficient for
FT interaction with UBL4A"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT MOTIF 1034..1076
FT /note="Nuclear localization site"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT COMPBIAS 92..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..705
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1023..1024
FT /note="Cleavage; by CASP3"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT MOD_RES 986
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT MOD_RES 995
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1075
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT MOD_RES 1103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT MOD_RES 1139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT CONFLICT 528
FT /note="Missing (in Ref. 3; AAH26647)"
FT /evidence="ECO:0000305"
FT CONFLICT 1012
FT /note="P -> S (in Ref. 3; AAH26647)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1154 AA; 121037 MW; 7F3FD14DF5AC1211 CRC64;
MEPSDSASTA MEEPDSLEVL VKTLDSQTRT FIVGAQMNVK EFKEHIAASV SIPSEKQRLI
YQGRVLQDDK KLQEYNVGGK VIHLVERAPP QTQLPSGASS GTGSASATHG GAPLPGTRGP
GASVHDRNAN SYVMVGTFNL PSDGSAVDVH INMEQAPIQS EPRVRLVMAQ HMIRDIQTLL
SRMECRGGTQ AQASQPPPQT PQTVASETVA LNSQTSEPVE SEAPPREPME SEEMEERPPT
QTPELAPSGP APAGPAPAGP APAPETNAPN HPSPAEHVEV LQELQRLQRR LQPFLQRYCE
VLGAAATTDY NNNHEGREED QRLINLVGES LRLLGNTFVA LSDLRCNLAC APPRHLHVVR
PMSHYTTPMV LQQAAIPIQI NVGTTVTMTG NGARPPPAPG AEAATPGSAQ ATSLPPSSTT
VDSSTEGAPP PGPAPPPASS HPRVIRISHQ SVEPVVMMHM NIQDSGAQPG GVPSAPTGPL
GPPGHGQTLG QQVPGFPTAP TRVVIARPTP PQARPSHPGG PPVSGALQGA GLGTNTSLAQ
MVSGLVGQLL MQPVLVAQGT PGMAQAQAQA QAQAQAQAQA PAPAPAPAPA PATASASAGT
TNTATTAGPA PGGPAQPPPP QPSAADLQFS QLLGNLLGPA GPGAGGPGMA SPTITVAMPG
VPAFLQGMTD FLQASQTAPP PPPPPPPPPP APEQQSTPPP GSPSGGTASP GGLGPESLPP
EFFTSVVQGV LSSLLGSLGA RAGSSESIAA FIQRLSGSSN IFEPGADGAL GFFGALLSLL
CQNFSMVDVV MLLHGHFQPL QRLQPQLRSF FHQHYLGGQE PTPSNIRMAT HTLITGLEEY
VRESFSLVQV QPGVDIIRTN LEFLQEQFNS IAAHVLHCTD SGFGARLLEL CNQGLFECLA
LNLHCLGGQQ MELAAVINGR IRRMSRGVNP SLVSWLTTMM GLRLQVVLEH MPVGPDAILR
YVRRVGDPPQ TLPEEPMEVQ GAERTSPEPQ RENASPAPGT TAEEAMSRGP PPAPEGGSRD
EQDGASADAE PWAAAVPPEW VPIIQQDIQS QRKVKPQPPL SDAYLSGMPA KRRKTMQGEG
PQLLLSEAVS RAAKAAGARP LTSPESLSRD LEAPEVQESY RQQLRSDIQK RLQEDPNYSP
QRFPNAHRAF ADDP
