NCOA6_MOUSE
ID NCOA6_MOUSE Reviewed; 2067 AA.
AC Q9JL19; Q9JLT9;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Nuclear receptor coactivator 6;
DE AltName: Full=Activating signal cointegrator 2;
DE Short=ASC-2;
DE AltName: Full=Amplified in breast cancer protein 3;
DE AltName: Full=Cancer-amplified transcriptional coactivator ASC-2;
DE AltName: Full=Nuclear receptor coactivator RAP250;
DE Short=NRC;
DE AltName: Full=Nuclear receptor-activating protein, 250 kDa;
DE AltName: Full=Peroxisome proliferator-activated receptor-interacting protein;
DE Short=PPAR-interacting protein;
DE AltName: Full=Thyroid hormone receptor-binding protein;
GN Name=Ncoa6; Synonyms=Aib3, Prip, Rap250, Trbp;
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 [MRNA] (ISOFORMS 1 AND 2), AND INTERACTION WITH PPARA;
RP PPARG; RARA; RXRA; ESR1; ESR2 AND THRB.
RC TISSUE=Liver;
RX PubMed=10788465; DOI=10.1074/jbc.275.18.13510;
RA Zhu Y.-J., Kan L., Qi C., Kanwar Y.S., Yeldandi A.V., Rao M.S., Reddy J.K.;
RT "Isolation and characterization of peroxisome proliferator-activated
RT receptor (PPAR) interacting protein (PRIP) as a coactivator for PPAR.";
RL J. Biol. Chem. 275:13510-13516(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 786-1142 (ISOFORM 1), INTERACTION WITH PPARA;
RP PPARG; ESR1; ESR2; THRA AND THRB, AND MUTAGENESIS OF 891-LEU--LEU-894.
RC TISSUE=Embryo;
RX PubMed=10681503; DOI=10.1074/jbc.275.8.5308;
RA Caira F., Antonson P., Pelto-Huikko M., Treuter E., Gustafsson J.-A.;
RT "Cloning and characterization of RAP250, a nuclear receptor coactivator.";
RL J. Biol. Chem. 275:5308-5317(2000).
RN [4]
RP INTERACTION WITH RBM39.
RX PubMed=11704680; DOI=10.1074/jbc.m110417200;
RA Jung D.-J., Na S.-Y., Na D.S., Lee J.W.;
RT "Molecular cloning and characterization of CAPER, a novel coactivator of
RT activating protein-1 and estrogen receptors.";
RL J. Biol. Chem. 277:1229-1234(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2022, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1822 AND LYS-1825, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-95; ARG-1050; ARG-1061 AND
RP ARG-1099, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Nuclear receptor coactivator that directly binds nuclear
CC receptors and stimulates the transcriptional activities in a hormone-
CC dependent fashion. Coactivates expression in an agonist- and AF2-
CC dependent manner. Involved in the coactivation of different nuclear
CC receptors, such as for steroids (GR and ERs), retinoids (RARs and
CC RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs).
CC Probably functions as a general coactivator, rather than just a nuclear
CC receptor coactivator. May also be involved in the coactivation of the
CC NF-kappa-B pathway. May coactivate expression via a remodeling of
CC chromatin and its interaction with histone acetyltransferase proteins.
CC Involved in placental, cardiac, hepatic and embryonic development.
CC -!- SUBUNIT: Monomer and homodimer. Interacts in vitro with the basal
CC transcription factors GTF2A and TBP, suggesting an autonomous
CC transactivation function. Interacts with NCOA1, CRSP3, RBM14, the
CC histone acetyltransferase proteins EP300 and CREBBP, and with
CC methyltransferase proteins NCOA6IP and PRMT2 (By similarity). Interacts
CC with RBM39. Component of the MLL2/3 complex (also named ASCOM complex),
CC at least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L, RBBP5, WDR5,
CC NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin (By
CC similarity). Interacts with ZNF335; may enhance ligand-dependent
CC transcriptional activation by nuclear hormone receptors (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JL19-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JL19-2; Sequence=VSP_003410;
CC -!- TISSUE SPECIFICITY: Widely expressed. High expression in testis and
CC weak expression in small intestine.
CC -!- DEVELOPMENTAL STAGE: Expressed at 9 dpc in placenta and at weaker level
CC in uterus. High expression in neural tube and in CNS throughout
CC development. High expression in sensory ganglia and retina from 11 dpc.
CC In the alimentary tract and olfactory epithelium expression was seen
CC from 13 dpc. Strong expression present in liver and kidney, from 11 dpc
CC and 13 dpc respectively, and then expression decreased at later stages
CC of development. Moderate expression in lung from 13 dpc, while it
CC decreases during postnatal life. Strong expression in thymus from 15
CC dpc onwards, and in spleen from 17 dpc and during early postnatal life,
CC then, the expression decreases.
CC -!- DOMAIN: Contains two Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Only motif 1
CC is essential for the association with nuclear receptors.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: Acts as a dominant negative repressor.
CC {ECO:0000305}.
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DR EMBL; AF216186; AAF35860.1; -; mRNA.
DR EMBL; BC031113; AAH31113.1; -; mRNA.
DR EMBL; AF135169; AAF35973.1; -; mRNA.
DR AlphaFoldDB; Q9JL19; -.
DR DIP; DIP-61283N; -.
DR ELM; Q9JL19; -.
DR IntAct; Q9JL19; 2.
DR STRING; 10090.ENSMUSP00000105295; -.
DR iPTMnet; Q9JL19; -.
DR PhosphoSitePlus; Q9JL19; -.
DR EPD; Q9JL19; -.
DR MaxQB; Q9JL19; -.
DR PaxDb; Q9JL19; -.
DR PeptideAtlas; Q9JL19; -.
DR PRIDE; Q9JL19; -.
DR ProteomicsDB; 287456; -. [Q9JL19-1]
DR ProteomicsDB; 287457; -. [Q9JL19-2]
DR MGI; MGI:1929915; Ncoa6.
DR eggNOG; ENOG502QQMS; Eukaryota.
DR InParanoid; Q9JL19; -.
DR Reactome; R-MMU-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR ChiTaRS; Ncoa6; mouse.
DR PRO; PR:Q9JL19; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JL19; protein.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0044666; C:MLL3/4 complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; ISO:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; ISO:MGI.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; ISO:MGI.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISS:UniProtKB.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; ISO:MGI.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; ISO:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:MGI.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
DR GO; GO:0030099; P:myeloid cell differentiation; ISS:UniProtKB.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0002793; P:positive regulation of peptide secretion; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR InterPro; IPR026638; NCOA6.
DR InterPro; IPR032715; NCOA6_TRADD-N.
DR PANTHER; PTHR15690; PTHR15690; 2.
DR Pfam; PF13820; Nucleic_acid_bd; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..2067
FT /note="Nuclear receptor coactivator 6"
FT /id="PRO_0000094414"
FT REGION 1..1314
FT /note="NCOA1-binding region"
FT /evidence="ECO:0000250"
FT REGION 1..1060
FT /note="CREBBP-binding region"
FT /evidence="ECO:0000250"
FT REGION 1..932
FT /note="TBP/GTF2A-binding region"
FT /evidence="ECO:0000250"
FT REGION 181..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..931
FT /note="NCOA6IP-binding region"
FT /evidence="ECO:0000250"
FT REGION 903..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1424..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1497..1581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1644..2067
FT /note="EP300/CRSP3-binding region"
FT /evidence="ECO:0000250"
FT REGION 1769..1822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1840..1911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1957..2067
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 891..895
FT /note="LXXLL motif 1"
FT MOTIF 1495..1499
FT /note="LXXLL motif 2"
FT COMPBIAS 182..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..1026
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1232
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1424..1447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1867..1909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2007..2021
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2043..2057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 95
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14686"
FT MOD_RES 1050
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1061
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1099
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1822
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1825
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 2022
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 458..2067
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10788465,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_003410"
FT MUTAGEN 891..894
FT /note="LVNL->AVNA: Abolishes interaction with nuclear
FT receptors."
FT /evidence="ECO:0000269|PubMed:10681503"
FT CONFLICT 39
FT /note="G -> S (in Ref. 2; AAH31113)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="W -> R (in Ref. 2; AAH31113)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="M -> I (in Ref. 2; AAH31113)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="Q -> QQ (in Ref. 2; AAH31113)"
FT /evidence="ECO:0000305"
FT CONFLICT 1014
FT /note="P -> L (in Ref. 3; AAF35973)"
FT /evidence="ECO:0000305"
FT CONFLICT 1141..1142
FT /note="SE -> RS (in Ref. 3; AAF35973)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2067 AA; 219663 MW; C855F8777167AD48 CRC64;
MVLDDLPNFE DIYTSLCSST MGDSEVEFDS GLEDDDTKGD SILEDSTIFV AFKGNIDDKD
FKWKLDAILK NVPNLLHMES SKLKVQKVEP WNSVRVTFNI PREAAERLWI LAQSNNQQLR
DLGILSVQIE GEGAINLALG QNRSQDVRMN GPVASGNSVR MEAGFPMASG PGLIRMTSPA
AVMTPQGGNM SSSMMAPGPN PELQPRTPRP ASQSDAMDPL LSGLHIQQQS HPSGSLPPAH
HSMQPVPVNR QMNPANFPQL QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ LQTRPLQQHQ
QQPQGIRPQF TAPTQVPVPP GWNQLPSGAL QPPPAQGSLG TMTTNQGWKK APLPSPMQAQ
LQARPSLATV QTPSHPPPPY PFGSQQASQA HTNFPQMSNP GQFTAPQMKG LQGGPSRVPT
PLQQPHLTNK SPASSPSSFQ QGSPASSPTV NQTQQQMGPR PPQNNPLSQG FQQPVSSPGR
NPMVQQGNVP PNFMVMQQQP PNQGPQSLHP GLGGMPKRLP PGFSAGQANP NFMQGQVPST
TAATPGNSGA LQLQANQNVQ HAGGQGAGPP QNQMQVSHGP PNMMQPSLMG IHGNINNQQA
GSSGVPQVTL GNMQGQPQQG PPSQLMGMHQ QIVPSQGQMA QQQGTLNPQN PMILSRAQLM
PQGQMMVNAQ NQNLGPSPQR MTPPKQMLPQ QGPQMMAPHN QMMGPQGQVL LQQNPMIEQI
MTNQMQGNKA QFNSQNQSNV MPGPAQIMRG PTPNMQGNMV QFTGQMSGQM LPQQGPVNNS
PSQVMGIQGQ VLRPPGPSPH MAQQHTDPVT TANNDVNLSQ MMPDVSMQQA SMVPPHVQSM
QGNSASGSHF SGHGVSFNAP FGGAPNGSQM SCGQNPGFPV NKDVTLTSPL LVNLLQSDIS
AGHFGVNNKQ NNTNANKPKK KKPPRKKKNC HQDLNTPDNR PTGLEEVDQQ SLPGEQGINL
DTTGPKLPDF SNRPPGYPTQ PVEQRPLPQM PPQLMQHVAP PPQPPQQQPQ PQLPQQQQPP
PPSQPQSQQQ QQQQQMMMML MMQQDPKSIR LPVSQNVHPP RGPLNPDSQR MPVQQSGNVP
VMVGLQGPAS VPPSPDKQRM PMSVNTPMGS NSRKMVYQEN PQNSSSSPLG EMSSLPEASG
SEVPSVAGGP NNMPSHLVVS QNQLMMTGPK PGPSPLSATQ GATPQQPPVN SLPSSHGHHF
PNVAAPTQTS RPKTPNRASP RPYYPQTPNN RPPSTEPSEI SLSPERLNAS IAGLFPPQIN
IPLPPRPNLN RGFDQQGLNP TTLKAIGQAP SNLTITNPPN FAAPQAHKLD SVVVNSGKQS
NPGTTKRASP SNSRRSSPGS SRKTTPSPGR QNSKAPKLTL ASQTSTTMLQ NMELPRNVLV
GPTPLANPPL PGSFPNNTGL NPQNPTVPVP AMGTVLEDNK ESVNIPQDSD CQNAQGRKEQ
VNTELKVVPT QEAKMAVPED QSKKDGQPLD PNKLPSVEEN KNLMSPAMRE APTSLSQLLD
NSGAPNVTIK PPGLTDLEVT PPVVSGEDLR KASVIPTLQD PPSKEPSTSL SSPHSSEPCS
TLARSELSEV SSNAAPSIPP VMSRPVSSSS ISTPLPPNQI TVFVTSNPIT TSSNTSAALP
THLQSALMST VVTMPNVGNK VMVSEGQSAA QSNARPQFIT PVFINSSSII QVMKGSQPST
IPATPLTTNS GLMPPSVAVV GPLHIPQNIK FSSAPVTPNV PSSSPAPNIQ TGRPLVLSSR
ATPVQLPSPP CTSSPVVAPN PSVQQVKELN PDEASPQTNT SADQSTLPPS QPTTVVSSLL
TNSPGSSANR RSPVSSSKGK GKVDKIGQIL LTKACKKVTG SLEKGEEQYG ADGETEGPGL
EITTPGLMGT EQCSTELDSK TPTPSAPTLL KMTSSPMAPS STSTGPILPG GALPTSVRSI
VTTLVPSELI STAPTTKGNH GGVTSEPLAG GLVEEKVGSH PELLPSIAPS QNLAPKETPA
TALQGSVARP ELEANAAIAS GQSCEPKEIV EKSKTLTSRR NSRTEEPTMA SESVENGHRK
RSSRPASASS STKDITGAVQ SKRRKSK
