DACT1_MOUSE
ID DACT1_MOUSE Reviewed; 778 AA.
AC Q8R4A3; Q80VG9; Q8BP49; Q9JK89;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Dapper homolog 1;
DE AltName: Full=Dapper antagonist of catenin 1;
DE AltName: Full=Frodo homolog;
DE AltName: Full=MDpr1;
DE AltName: Full=Thymus-expressed novel gene 3 protein;
GN Name=Dact1; Synonyms=Thyex3;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Cerebellum;
RX PubMed=11970895; DOI=10.1016/s1534-5807(02)00140-5;
RA Cheyette B.N.R., Waxman J.S., Miller J.R., Takemaru K., Sheldahl L.C.,
RA Khlebtsova N., Fox E.P., Earnest T.N., Moon R.T.;
RT "Dapper, a Dishevelled-associated antagonist of beta-catenin and JNK
RT signaling, is required for notochord formation.";
RL Dev. Cell 2:449-461(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-511, AND DEVELOPMENTAL STAGE.
RC STRAIN=FVB/N;
RX PubMed=16278878; DOI=10.1002/dvdy.20609;
RA Hunter N.L., Hikasa H., Dymecki S.M., Sokol S.Y.;
RT "Vertebrate homologues of Frodo are dynamically expressed during embryonic
RT development in tissues undergoing extensive morphogenetic movements.";
RL Dev. Dyn. 235:279-284(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-778.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 189-778.
RA Gong S., Qian X., Fu W., Chen W.;
RT "Cloning of a murine cDNA and its human homolog encoding transcription
RT factor-like proteins.";
RL Zhongguo Sheng Wu Hua Xue Yu Fen Zi Sheng Wu Xue Bao 17:280-287(2001).
RN [5]
RP INTERACTION WITH DVL1, AND DOMAIN.
RX PubMed=14636582; DOI=10.1016/s1097-2765(03)00427-1;
RA Wong H.C., Bourdelas A., Krauss A., Lee H.J., Shao Y., Wu D., Mlodzik M.,
RA Shi D.L., Zheng J.;
RT "Direct binding of the PDZ domain of Dishevelled to a conserved internal
RT sequence in the C-terminal region of Frizzled.";
RL Mol. Cell 12:1251-1260(2003).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16881060; DOI=10.1002/dvdy.20917;
RA Fisher D.A., Kivimaee S., Hoshino J., Suriben R., Martin P.-M., Baxter N.,
RA Cheyette B.N.R.;
RT "Three Dact gene family members are expressed during embryonic development
RT and in the adult brains of mice.";
RL Dev. Dyn. 235:2620-2630(2006).
RN [7]
RP FUNCTION.
RX PubMed=17197390; DOI=10.1096/fj.06-6246com;
RA Su Y., Zhang L., Gao X., Meng F., Wen J., Zhou H., Meng A., Chen Y.-G.;
RT "The evolutionally conserved activity of Dapper2 in antagonizing TGF-beta
RT signaling.";
RL FASEB J. 21:682-690(2007).
RN [8]
RP FUNCTION.
RX PubMed=19073771; DOI=10.2337/db08-1180;
RA Lagathu C., Christodoulides C., Virtue S., Cawthorn W.P., Franzin C.,
RA Kimber W.A., Nora E.D., Campbell M., Medina-Gomez G., Cheyette B.N.,
RA Vidal-Puig A.J., Sethi J.K.;
RT "Dact1, a nutritionally regulated preadipocyte gene, controls adipogenesis
RT by coordinating the Wnt/beta-catenin signaling network.";
RL Diabetes 58:609-619(2009).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19701191; DOI=10.1038/ng.435;
RA Suriben R., Kivimae S., Fisher D.A., Moon R.T., Cheyette B.N.;
RT "Posterior malformations in Dact1 mutant mice arise through misregulated
RT Vangl2 at the primitive streak.";
RL Nat. Genet. 41:977-985(2009).
RN [10]
RP FUNCTION, INTERACTION WITH DVL2 AND VANGL2, AND DISRUPTION PHENOTYPE.
RX PubMed=20145239; DOI=10.1074/jbc.m109.085381;
RA Wen J., Chiang Y.J., Gao C., Xue H., Xu J., Ning Y., Hodes R.J., Gao X.,
RA Chen Y.G.;
RT "Loss of Dact1 disrupts planar cell polarity signaling by altering
RT dishevelled activity and leads to posterior malformation in mice.";
RL J. Biol. Chem. 285:11023-11030(2010).
RN [11]
RP PHOSPHORYLATION, SELF-ASSOCIATION, AND INTERACTION WITH DACT2; DACT3;
RP CSNK1D; CSNK2A1; PKA; PKC; CSNK2B; GSK3B; DVL1; DLV2; DVL3; VANGL1; VANGL2;
RP CTNND1 AND HDAC1.
RX PubMed=21718540; DOI=10.1186/1471-2091-12-33;
RA Kivimae S., Yang X.Y., Cheyette B.N.;
RT "All Dact (Dapper/Frodo) scaffold proteins dimerize and exhibit conserved
RT interactions with Vangl, Dvl, and serine/threonine kinases.";
RL BMC Biochem. 12:33-33(2011).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20335472; DOI=10.1523/jneurosci.0354-10.2010;
RA Okerlund N.D., Kivimae S., Tong C.K., Peng I.F., Ullian E.M.,
RA Cheyette B.N.;
RT "Dact1 is a postsynaptic protein required for dendrite, spine, and
RT excitatory synapse development in the mouse forebrain.";
RL J. Neurosci. 30:4362-4368(2010).
CC -!- FUNCTION: Involved in regulation of intracellular signaling pathways
CC during development. Specifically thought to play a role in canonical
CC and/or non-canonical Wnt signaling pathways through interaction with
CC DSH (Dishevelled) family proteins. The activation/inhibition of Wnt
CC signaling may depend on the phosphorylation status. Proposed to
CC regulate the degradation of CTNNB1/beta-catenin, thereby modulating the
CC transcriptional activation of target genes of the Wnt signaling
CC pathway. Its function in stabilizing CTNNB1 may involve inhibition of
CC GSK3B activity. Promotes the membrane localization of CTNNB1. The
CC cytoplasmic form can induce DVL2 degradation via a lysosome-dependent
CC mechanism; the function is inhibited by PKA-induced binding to 14-3-3
CC proteins, such as YWHAB (By similarity). Seems to be involved in
CC morphogenesis at the primitive streak by regulating VANGL2 and DVL2;
CC the function seems to be independent of canonical Wnt signaling and
CC rather involves the non-canonical Wnt/planar cell polarity (PCP)
CC pathway. The nuclear form may prevent the formation of LEF1:CTNNB1
CC complex and recruit HDAC1 to LEF1 at target gene promoters to repress
CC transcription thus antagonizing Wnt signaling (By similarity). May be
CC involved in positive regulation of fat cell differentiation. During
CC neuronal differentiation may be involved in excitatory synapse
CC organization, and dendrite formation and establishment of spines.
CC {ECO:0000250, ECO:0000269|PubMed:17197390, ECO:0000269|PubMed:19073771,
CC ECO:0000269|PubMed:19701191, ECO:0000269|PubMed:20145239,
CC ECO:0000269|PubMed:20335472}.
CC -!- SUBUNIT: Can form homodimers and heterodimers with DACT2 or DACT3.
CC Interacts with CSNK1D, PKA catalytic subunit, PKC-type kinase, CSNK2A1,
CC CSNK2B, DVL1, DLV2, DVAL3, VANGL1, VANGL2, CTNND1 and HDAC1. Interacts
CC with GSK3B; the interaction is indicative for an association of DACT1
CC with the beta-catenin destruction complex. Interacts with GSK3A.
CC Interacts with YWHAB; the interaction is enhanced by PKA
CC phosphorylating DACT1 at Ser-769. Interacts with CTNNB1 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8R4A3; Q0PHV7: Dact3; NbExp=2; IntAct=EBI-3870250, EBI-6392520;
CC Q8R4A3; P51141: Dvl1; NbExp=4; IntAct=EBI-3870250, EBI-1538407;
CC Q8R4A3; Q60838: Dvl2; NbExp=3; IntAct=EBI-3870250, EBI-641940;
CC Q8R4A3; Q91ZD4: Vangl2; NbExp=3; IntAct=EBI-3870250, EBI-1750744;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Synapse {ECO:0000269|PubMed:20335472}. Note=Shuttles between the
CC nucleus and the cytoplasm. Seems to be nuclear in the absence of Wnt
CC signaling and to translocate to the cytoplasm in its presence (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in multiple tissues including brain,
CC heart, kidney, liver and testis. {ECO:0000269|PubMed:11970895,
CC ECO:0000269|PubMed:16881060}.
CC -!- DEVELOPMENTAL STAGE: Expression strongly increases from 9.5 dpc, peaks
CC between 11.5 dpc and 13.5 dpc and diminishes slowly thereafter.
CC Expressed in the somites during segmentation, limb bud mesenchyme, and
CC developing central nervous system. Expressed in primitive streak
CC mesoderm, neuroectoderm, neural crest, presomitic mesoderm and somites.
CC {ECO:0000269|PubMed:16278878, ECO:0000269|PubMed:16881060}.
CC -!- DOMAIN: The C-terminal PDZ-binding motif mediates interaction with the
CC PDZ domains of DSH (Dishevelled) family proteins.
CC {ECO:0000269|PubMed:14636582}.
CC -!- DISRUPTION PHENOTYPE: Mice die within a day of birth with malformations
CC involving the spine, genitourinary system and distal digestive tract
CC due to disrupted germ-layer morphogenesis at the primitive streak where
CC cells undergo an epithelial-mesenchymal transition. Urogenital defects
CC due to impaired hindgut formation start at embryonic day 8.25. Dvl2 and
CC Vangl2 are found increased at the primitive streak, associated with
CC abnormal distribution of E-cadherin. {ECO:0000269|PubMed:19701191,
CC ECO:0000269|PubMed:20145239}.
CC -!- SIMILARITY: Belongs to the dapper family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF65568.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC36958.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF488775; AAM12547.1; -; mRNA.
DR EMBL; AY208970; AAO49712.1; -; mRNA.
DR EMBL; AK077691; BAC36958.1; ALT_SEQ; mRNA.
DR EMBL; AF251078; AAF65568.1; ALT_INIT; mRNA.
DR CCDS; CCDS25963.1; -.
DR RefSeq; NP_067507.2; NM_021532.4.
DR AlphaFoldDB; Q8R4A3; -.
DR SMR; Q8R4A3; -.
DR BioGRID; 208502; 11.
DR IntAct; Q8R4A3; 20.
DR STRING; 10090.ENSMUSP00000117169; -.
DR iPTMnet; Q8R4A3; -.
DR PhosphoSitePlus; Q8R4A3; -.
DR PaxDb; Q8R4A3; -.
DR PRIDE; Q8R4A3; -.
DR ProteomicsDB; 279153; -.
DR Antibodypedia; 66; 160 antibodies from 24 providers.
DR DNASU; 59036; -.
DR Ensembl; ENSMUST00000061273; ENSMUSP00000058943; ENSMUSG00000044548.
DR GeneID; 59036; -.
DR KEGG; mmu:59036; -.
DR UCSC; uc007nup.2; mouse.
DR CTD; 51339; -.
DR MGI; MGI:1891740; Dact1.
DR VEuPathDB; HostDB:ENSMUSG00000044548; -.
DR eggNOG; ENOG502QVXB; Eukaryota.
DR GeneTree; ENSGT00950000183181; -.
DR HOGENOM; CLU_021211_1_0_1; -.
DR InParanoid; Q8R4A3; -.
DR PhylomeDB; Q8R4A3; -.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR BioGRID-ORCS; 59036; 4 hits in 70 CRISPR screens.
DR PRO; PR:Q8R4A3; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8R4A3; protein.
DR Bgee; ENSMUSG00000044548; Expressed in presomitic mesoderm and 259 other tissues.
DR ExpressionAtlas; Q8R4A3; baseline and differential.
DR Genevisible; Q8R4A3; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030877; C:beta-catenin destruction complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
DR GO; GO:0070097; F:delta-catenin binding; IDA:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0051018; F:protein kinase A binding; IDA:UniProtKB.
DR GO; GO:0005080; F:protein kinase C binding; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR GO; GO:0048619; P:embryonic hindgut morphogenesis; IMP:UniProtKB.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:MGI.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR GO; GO:1904864; P:negative regulation of beta-catenin-TCF complex assembly; ISO:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0046329; P:negative regulation of JNK cascade; IDA:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0021915; P:neural tube development; ISO:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IMP:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:2000095; P:regulation of Wnt signaling pathway, planar cell polarity pathway; IMP:UniProtKB.
DR GO; GO:0050808; P:synapse organization; IMP:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR024848; Dact1.
DR InterPro; IPR024843; Dapper.
DR PANTHER; PTHR15919; PTHR15919; 2.
DR PANTHER; PTHR15919:SF12; PTHR15919:SF12; 2.
DR Pfam; PF15268; Dapper; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Developmental protein; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Synapse; Wnt signaling pathway.
FT CHAIN 1..778
FT /note="Dapper homolog 1"
FT /id="PRO_0000191354"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..149
FT /note="Required for self-association"
FT REGION 305..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 85..149
FT /evidence="ECO:0000255"
FT MOTIF 125..134
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOTIF 551..564
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 768..778
FT /note="PDZ-binding"
FT COMPBIAS 19..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 769
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9NYF0"
FT CONFLICT 18..19
FT /note="AE -> SN (in Ref. 2; AAO49712)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="C -> F (in Ref. 2; AAO49712)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="G -> V (in Ref. 4; AAF65568)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="M -> I (in Ref. 2; AAO49712)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="A -> G (in Ref. 4; AAF65568)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="R -> S (in Ref. 2; AAO49712)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="V -> G (in Ref. 4; AAF65568)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 778 AA; 84306 MW; 31EAD7E9BBA77DE7 CRC64;
MKPDAAREPE PLSPGRGAEA EGRWRERGEA DTERQRTRER QEATLAGLAE LGYLRQRQEL
LVRGALRCSG TVGTVAPRSG ELRGDAAQRS RLEEKFLEEN ILLLRRQLNC LRRRDAGLLN
QLQELDKQIS DLRLDVEKTS EEHLETDSRP SSGFYELSDG ASGSLSNSSN SVFSECLSSC
HSSTCFCSPL EAALTISDGC PKSADVNPKY QCDLVSKNGN DVYRYPSPLH AVAVQSPMFL
LCLTGNTLRE EEGLGSHASD ICIGSELNAT KTDNSLPSPS SLWSASHPAS SKKMDGYILS
LVQKKTHPVR TNKPRTSVNA DPTKGLLRNG SVCVRAPSGV PPGSSVNFKN TKQMCLPAGG
ITSLENGPFS PPKQRSKDSK TDQLESKRLA LPESCSAGAA MEPQSKHVPK AAKAASQELT
RCQAGLGESM KESNQASAVS PKTSPGRGPV APAESKALQL PKKMSQKNSL QAVPALDRPA
LDFKSEGSSQ SLEEGHLVKA QFIPGQQAAA RPHRAHRNPG VARSATLKAR GQAAMEHGLP
TVREKPRAAG KKCRFPDDSD TNKKFRKTSA KGRRSGGLQD AGLPGRALGT GGHRAGSRAH
AHGREPVVAK PKHKRTDYRR WKSSAEVSYE EALRRARRAR REHGAAYRVA VALPYASPYA
YVPSDSEYSA ECESLFHSTV VDTSEDEQSN YTTNCFGDSE SSVSEGDFVG ESTTTSDSEE
SGGLIWSQFV QTLPIQTVTA PDLHTRPTKT FVKIKASHNL KKKILRFRSG SLKLMTTV
