BAG6_RAT
ID BAG6_RAT Reviewed; 1146 AA.
AC Q6MG49; Q498N5; Q9WTN8;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Large proline-rich protein BAG6 {ECO:0000305};
DE AltName: Full=BCL2-associated athanogene 6 {ECO:0000312|RGD:71064};
DE AltName: Full=HLA-B-associated transcript 3 {ECO:0000303|PubMed:10390159};
GN Name=Bag6 {ECO:0000312|RGD:71064};
GN Synonyms=Bat3 {ECO:0000303|PubMed:10390159};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10390159; DOI=10.1089/104454999315222;
RA Ozaki T., Hanaoka E., Naka M., Nakagawara A., Sakiyama S.;
RT "Cloning and characterization of rat BAT3 cDNA.";
RL DNA Cell Biol. 18:503-512(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-987 AND SER-1095, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Recruited to ribosomes,
CC it interacts with the transmembrane region of newly synthesized tail-
CC anchored proteins and together with SGTA and ASNA1 mediates their
CC delivery to the endoplasmic reticulum. Client proteins that cannot be
CC properly delivered to the endoplasmic reticulum are ubiquitinated by
CC RNF126, an E3 ubiquitin-protein ligase associated with BAG6 and are
CC sorted to the proteasome. SGTA which prevents the recruitment of RNF126
CC to BAG6 may negatively regulate the ubiquitination and the proteasomal
CC degradation of client proteins. Similarly, the BAG6/BAT3 complex also
CC functions as a sorting platform for proteins of the secretory pathway
CC that are mislocalized to the cytosol either delivering them to the
CC proteasome for degradation or to the endoplasmic reticulum. The
CC BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-
CC associated degradation (ERAD), a quality control mechanism that
CC eliminates unwanted proteins of the endoplasmic reticulum through their
CC 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. BAG6 is also required for selective
CC ubiquitin-mediated degradation of defective nascent chain polypeptides
CC by the proteasome. In this context, it may participate in the
CC production of antigenic peptides and play a role in antigen
CC presentation in immune response. BAG6 is also involved in endoplasmic
CC reticulum stress-induced pre-emptive quality control, a mechanism that
CC selectively attenuates the translocation of newly synthesized proteins
CC into the endoplasmic reticulum and reroutes them to the cytosol for
CC proteasomal degradation. BAG6 may ensure the proper degradation of
CC these proteins and thereby protects the endoplasmic reticulum from
CC protein overload upon stress. By inhibiting the polyubiquitination and
CC subsequent proteasomal degradation of HSPA2 it may also play a role in
CC the assembly of the synaptonemal complex during spermatogenesis. Also
CC positively regulates apoptosis by interacting with and stabilizing the
CC proapoptotic factor AIFM1. By controlling the steady-state expression
CC of the IGF1R receptor, indirectly regulates the insulin-like growth
CC factor receptor signaling pathway. {ECO:0000250|UniProtKB:P46379}.
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. Interacts
CC with UBL4A; the interaction is direct and required for UBL4A protein
CC stability. Interacts with AIFM1. Interacts with HSPA2. Interacts with
CC CTCFL. Interacts with p300/EP300. Interacts (via ubiquitin-like domain)
CC with RNF126; required for BAG6-dependent ubiquitination of proteins
CC mislocalized to the cytosol. Interacts (via ubiquitin-like domain) with
CC SGTA; SGTA competes with RNF126 by binding the same region of BAG6,
CC thereby promoting deubiquitination of BAG6-target proteins and rescuing
CC them from degradation. Interacts with ricin A chain. Interacts with VCP
CC and AMFR; both form the VCP/p97-AMFR/gp78 complex. Interacts with
CC SYVN1. Interacts with USP13; the interaction is direct and may mediate
CC UBL4A deubiquitination. Interacts with ZFAND2B. Interacts with KPNA2.
CC Interacts with UBQLN4 (By similarity). {ECO:0000250|UniProtKB:P46379,
CC ECO:0000250|UniProtKB:Q9Z1R2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P46379}. Nucleus {ECO:0000250|UniProtKB:P46379}.
CC Secreted, extracellular exosome {ECO:0000250|UniProtKB:P46379}.
CC Note=Normally localized in cytosol and nucleus, it can also be released
CC extracellularly, in exosomes, by tumor and myeloid dendritic cells.
CC {ECO:0000250|UniProtKB:P46379}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6MG49-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6MG49-2; Sequence=VSP_040420, VSP_040421;
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}.
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DR EMBL; AB018791; BAA76607.1; -; mRNA.
DR EMBL; BX883045; CAE83997.1; -; Genomic_DNA.
DR EMBL; CH474121; EDL83534.1; -; Genomic_DNA.
DR EMBL; BC100141; AAI00142.1; -; mRNA.
DR RefSeq; NP_001029140.1; NM_001033968.1. [Q6MG49-1]
DR RefSeq; NP_446061.2; NM_053609.2. [Q6MG49-2]
DR AlphaFoldDB; Q6MG49; -.
DR SMR; Q6MG49; -.
DR BioGRID; 250197; 3.
DR IntAct; Q6MG49; 2.
DR MINT; Q6MG49; -.
DR STRING; 10116.ENSRNOP00000057557; -.
DR iPTMnet; Q6MG49; -.
DR PhosphoSitePlus; Q6MG49; -.
DR jPOST; Q6MG49; -.
DR PaxDb; Q6MG49; -.
DR PRIDE; Q6MG49; -.
DR GeneID; 94342; -.
DR KEGG; rno:94342; -.
DR UCSC; RGD:71064; rat. [Q6MG49-1]
DR CTD; 7917; -.
DR RGD; 71064; Bag6.
DR VEuPathDB; HostDB:ENSRNOG00000000851; -.
DR eggNOG; KOG4248; Eukaryota.
DR HOGENOM; CLU_012159_0_0_1; -.
DR InParanoid; Q6MG49; -.
DR OMA; SFPNEWL; -.
DR OrthoDB; 1233552at2759; -.
DR PhylomeDB; Q6MG49; -.
DR TreeFam; TF328437; -.
DR PRO; PR:Q6MG49; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Proteomes; UP000234681; Chromosome 20.
DR Bgee; ENSRNOG00000000851; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q6MG49; baseline and differential.
DR Genevisible; Q6MG49; RN.
DR GO; GO:0071818; C:BAT3 complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:RGD.
DR GO; GO:0051787; F:misfolded protein binding; ISO:RGD.
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:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS: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:RGD.
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:1904378; P:maintenance of unfolded protein involved in ERAD pathway; ISO:RGD.
DR GO; GO:0030101; P:natural killer cell activation; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
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:1904294; P:positive regulation of ERAD pathway; ISO:RGD.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEP:RGD.
DR GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
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 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; Alternative splicing; Apoptosis; Chaperone;
KW Chromatin regulator; Cytoplasm; Differentiation; Immunity; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Spermatogenesis;
KW Transport.
FT CHAIN 1..1146
FT /note="Large proline-rich protein BAG6"
FT /id="PRO_0000114899"
FT DOMAIN 17..92
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REPEAT 236..265
FT /note="1"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT REPEAT 410..438
FT /note="2"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT REPEAT 589..616
FT /note="3"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT REPEAT 622..650
FT /note="4"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT REGION 87..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..650
FT /note="4 X 29 AA approximate repeats"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT REGION 381..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 961..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1054
FT /note="Required for interaction with GET4"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT REGION 1036..1146
FT /note="Sufficient for the delivery of client proteins to
FT the endoplasmic reticulum"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT REGION 1072..1129
FT /note="BAG-similar domain, required and sufficient for
FT interaction with UBL4A"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT MOTIF 1026..1068
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..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..263
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..697
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1015..1016
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 978
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1067
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT MOD_RES 1095
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46379"
FT VAR_SEQ 522
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10390159"
FT /id="VSP_040420"
FT VAR_SEQ 1067..1115
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10390159"
FT /id="VSP_040421"
FT CONFLICT 4
FT /note="S -> N (in Ref. 1; BAA76607)"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="M -> V (in Ref. 1; BAA76607)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="A -> R (in Ref. 1; BAA76607)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="D -> E (in Ref. 1; BAA76607)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="Q -> H (in Ref. 1; BAA76607)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="L -> C (in Ref. 1; BAA76607)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="T -> N (in Ref. 1; BAA76607)"
FT /evidence="ECO:0000305"
FT CONFLICT 264..265
FT /note="NH -> TQ (in Ref. 1; BAA76607)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="T -> TAQ (in Ref. 1; BAA76607)"
FT /evidence="ECO:0000305"
SQ 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
