DEAF1_MOUSE
ID DEAF1_MOUSE Reviewed; 566 AA.
AC Q9Z1T5; C7SHZ9; Q3UJA4;
DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Deformed epidermal autoregulatory factor 1 homolog;
DE AltName: Full=Nuclear DEAF-1-related transcriptional regulator;
DE Short=NUDR;
GN Name=Deaf1;
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] (ISOFORM 1), INTERACTION WITH CLIM2; LMO2 AND
RP LMO4, AND TISSUE SPECIFICITY.
RC TISSUE=Pituitary, and Skin;
RX PubMed=9860983; DOI=10.1073/pnas.95.26.15418;
RA Sugihara T.M., Bach I., Kioussi C., Rosenfeld M.G., Andersen B.;
RT "Mouse deformed epidermal autoregulatory factor 1 recruits a LIM domain
RT factor, LMO-4, and CLIM coregulators.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15418-15423(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=NOD; TISSUE=Pancreas;
RX PubMed=19668219; DOI=10.1038/ni.1773;
RA Yip L., Su L., Sheng D., Chang P., Atkinson M., Czesak M., Albert P.R.,
RA Collier A.R., Turley S.J., Fathman C.G., Creusot R.J.;
RT "Deaf1 isoforms control the expression of genes encoding peripheral tissue
RT antigens in the pancreatic lymph nodes during type 1 diabetes.";
RL Nat. Immunol. 10:1026-1033(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [LARGE SCALE GENOMIC DNA].
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14966286; DOI=10.1128/mcb.24.5.2074-2082.2004;
RA Hahm K., Sum E.Y., Fujiwara Y., Lindeman G.J., Visvader J.E., Orkin S.H.;
RT "Defective neural tube closure and anteroposterior patterning in mice
RT lacking the LIM protein LMO4 or its interacting partner Deaf-1.";
RL Mol. Cell. Biol. 24:2074-2082(2004).
RN [6]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=18826651; DOI=10.1186/1471-213x-8-94;
RA Barker H.E., Smyth G.K., Wettenhall J., Ward T.A., Bath M.L.,
RA Lindeman G.J., Visvader J.E.;
RT "Deaf-1 regulates epithelial cell proliferation and side-branching in the
RT mammary gland.";
RL BMC Dev. Biol. 8:94-94(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172; SER-177 AND THR-180, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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 [8]
RP INTERACTION WITH LMO4, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-305.
RX PubMed=22723967; DOI=10.1371/journal.pone.0039218;
RA Cubeddu L., Joseph S., Richard D.J., Matthews J.M.;
RT "Contribution of DEAF1 structural domains to the interaction with the
RT breast cancer oncogene LMO4.";
RL PLoS ONE 7:E39218-E39218(2012).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24726472; DOI=10.1016/j.ajhg.2014.03.013;
RA Vulto-van Silfhout A.T., Rajamanickam S., Jensik P.J., Vergult S.,
RA de Rocker N., Newhall K.J., Raghavan R., Reardon S.N., Jarrett K.,
RA McIntyre T., Bulinski J., Ownby S.L., Huggenvik J.I., McKnight G.S.,
RA Rose G.M., Cai X., Willaert A., Zweier C., Endele S., de Ligt J.,
RA van Bon B.W., Lugtenberg D., de Vries P.F., Veltman J.A., van Bokhoven H.,
RA Brunner H.G., Rauch A., de Brouwer A.P., Carvill G.L., Hoischen A.,
RA Mefford H.C., Eichler E.E., Vissers L.E., Menten B., Collard M.W.,
RA de Vries B.B.;
RT "Mutations affecting the SAND domain of DEAF1 cause intellectual disability
RT with severe speech impairment and behavioral problems.";
RL Am. J. Hum. Genet. 94:649-661(2014).
CC -!- FUNCTION: Transcription factor that binds to sequence with multiple
CC copies of 5'-TTC[CG]G-3' present in its own promoter and that of the
CC HNRPA2B1 gene. Down-regulates transcription of these genes. Binds to
CC the retinoic acid response element (RARE) 5'-AGGGTTCACCGAAAGTTCA-3'.
CC Activates the proenkephalin gene independently of promoter binding,
CC probably through protein-protein interaction (By similarity). Regulates
CC epithelial cell proliferation and side-branching in the mammary gland.
CC Required for neural tube closure and skeletal patterning. Controls the
CC expression of peripheral tissue antigens in pancreatic lymph nodes.
CC Isoform 1 displays greater transcriptional activity than isoform 2.
CC Isoform 2 may inhibit transcriptional activity of isoform 1 by
CC interacting with it and retaining it in the cytoplasm. Transcriptional
CC activator of EIF4G3 (By similarity). May also involved in behavior
CC (PubMed:24726472). {ECO:0000250|UniProtKB:O75398,
CC ECO:0000269|PubMed:14966286, ECO:0000269|PubMed:18826651,
CC ECO:0000269|PubMed:19668219, ECO:0000269|PubMed:24726472}.
CC -!- SUBUNIT: Homodimer (By similarity). Isoform 1 and isoform 2 may form a
CC heterodimer. May interact with the corepressors NCOR1 and NCRO2 (By
CC similarity). Identified in a complex with XRCC5 and XRCC6. Interacts
CC (via the SAND domain) with the DNA-PK complex subunit XRCC6; the
CC interaction is direct with XRCC6 and may be inhibited by DNA-binding
CC (By similarity). Interacts with LMO4; LMO4 blocks export from nucleus.
CC Interacts with LMO2 and CLIM2. {ECO:0000250,
CC ECO:0000269|PubMed:22723967, ECO:0000269|PubMed:9860983}.
CC -!- INTERACTION:
CC Q9Z1T5; Q9Z2D6: Mecp2; NbExp=2; IntAct=EBI-2364863, EBI-1188816;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. Cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus. Note=Displays
CC some nuclear localization when expressed with isoform 1, suggesting
CC that it may heterodimerize with isoform 1 and shuttle to the nucleus
CC using the nuclear localization signal of isoform 1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=DF1;
CC IsoId=Q9Z1T5-1; Sequence=Displayed;
CC Name=2; Synonyms=DF1-VAR1;
CC IsoId=Q9Z1T5-2; Sequence=VSP_038703, VSP_038704, VSP_038705;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed during embryogenesis, with
CC higher expression in regions of the central nervous system, dorsal root
CC ganglia, submandibular gland, epidermis and breast. In 12-week-old NOD
CC mice, expression of isoform 2 is sevenfold higher in lymph node stromal
CC elements than in T-cells and tenfold higher than in B-cells.
CC {ECO:0000269|PubMed:9860983}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages of mammary gland
CC development with slightly higher levels observed during pregnancy and
CC lactation. At 4 weeks, expression levels of isoform 1 and isoform 2 do
CC not differ in pancreatic lymph nodes of nonobese diabetic (NOD) mice
CC compared to NOD.B10 mice which do not develop diabetes. However, at 12
CC weeks, expression of isoform 1 is down-regulated while expression of
CC isoform 2 is up-regulated in NOD mice but not in NOD.B10. There is no
CC difference in expression levels at 12 weeks in spleen.
CC {ECO:0000269|PubMed:18826651, ECO:0000269|PubMed:19668219}.
CC -!- PTM: May be phosphorylated by DNA-PK complex in a DNA independent
CC manner (in vitro). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Exencephaly and skeletal abnormalities in the rib
CC cage and cervical vertebrae but no presphenoid bone or cranial nerve
CC defects. DEAF1 homozygous mice neonates die 100% of the time and DEAF1
CC heterozygous mice survived in a 2:1 ratio.
CC {ECO:0000269|PubMed:14966286, ECO:0000269|PubMed:24726472}.
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DR EMBL; AF102818; AAC98511.1; -; mRNA.
DR EMBL; FJ377318; ACN61629.1; -; mRNA.
DR EMBL; FJ377319; ACN61630.1; -; mRNA.
DR EMBL; AK146546; BAE27251.1; -; mRNA.
DR EMBL; CH466531; EDL18044.1; -; Genomic_DNA.
DR CCDS; CCDS40185.1; -. [Q9Z1T5-1]
DR RefSeq; NP_058570.1; NM_016874.3. [Q9Z1T5-1]
DR PDB; 2MBV; NMR; -; A=404-418.
DR PDBsum; 2MBV; -.
DR AlphaFoldDB; Q9Z1T5; -.
DR BMRB; Q9Z1T5; -.
DR SMR; Q9Z1T5; -.
DR BioGRID; 207558; 25.
DR IntAct; Q9Z1T5; 3.
DR MINT; Q9Z1T5; -.
DR STRING; 10090.ENSMUSP00000079395; -.
DR iPTMnet; Q9Z1T5; -.
DR PhosphoSitePlus; Q9Z1T5; -.
DR jPOST; Q9Z1T5; -.
DR MaxQB; Q9Z1T5; -.
DR PaxDb; Q9Z1T5; -.
DR PRIDE; Q9Z1T5; -.
DR ProteomicsDB; 277973; -. [Q9Z1T5-1]
DR ProteomicsDB; 277974; -. [Q9Z1T5-2]
DR Antibodypedia; 9854; 339 antibodies from 30 providers.
DR DNASU; 54006; -.
DR Ensembl; ENSMUST00000080553; ENSMUSP00000079395; ENSMUSG00000058886. [Q9Z1T5-1]
DR GeneID; 54006; -.
DR KEGG; mmu:54006; -.
DR UCSC; uc009kkn.2; mouse. [Q9Z1T5-1]
DR CTD; 10522; -.
DR MGI; MGI:1858496; Deaf1.
DR VEuPathDB; HostDB:ENSMUSG00000058886; -.
DR eggNOG; KOG4333; Eukaryota.
DR GeneTree; ENSGT00940000159701; -.
DR HOGENOM; CLU_039056_1_0_1; -.
DR InParanoid; Q9Z1T5; -.
DR OMA; KDHQHSC; -.
DR OrthoDB; 662933at2759; -.
DR PhylomeDB; Q9Z1T5; -.
DR TreeFam; TF325664; -.
DR BioGRID-ORCS; 54006; 2 hits in 78 CRISPR screens.
DR ChiTaRS; Deaf1; mouse.
DR PRO; PR:Q9Z1T5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9Z1T5; protein.
DR Bgee; ENSMUSG00000058886; Expressed in embryonic brain and 251 other tissues.
DR ExpressionAtlas; Q9Z1T5; baseline and differential.
DR Genevisible; Q9Z1T5; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0001662; P:behavioral fear response; IMP:UniProtKB.
DR GO; GO:0048706; P:embryonic skeletal system development; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
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; ISO:MGI.
DR GO; GO:0033599; P:regulation of mammary gland epithelial cell proliferation; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0008542; P:visual learning; IMP:UniProtKB.
DR Gene3D; 3.10.390.10; -; 1.
DR InterPro; IPR010919; SAND-like_dom_sf.
DR InterPro; IPR000770; SAND_dom.
DR InterPro; IPR024119; TF_DEAF-1.
DR InterPro; IPR002893; Znf_MYND.
DR PANTHER; PTHR10237; PTHR10237; 2.
DR Pfam; PF01342; SAND; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SMART; SM00258; SAND; 1.
DR SUPFAM; SSF63763; SSF63763; 1.
DR PROSITE; PS50864; SAND; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein;
KW DNA-binding; Metal-binding; Neurogenesis; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..566
FT /note="Deformed epidermal autoregulatory factor 1 homolog"
FT /id="PRO_0000074085"
FT DOMAIN 194..274
FT /note="SAND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00185"
FT ZN_FING 505..541
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 33..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..479
FT /note="Interaction with LMO4"
FT MOTIF 300..306
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 40..54
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 505
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 508
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 516
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 519
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 529
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 537
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 541
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT MOD_RES 172
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 433
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75398"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88450"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88450"
FT VAR_SEQ 19..32
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19668219"
FT /id="VSP_038703"
FT VAR_SEQ 292..308
FT /note="SGPVRLFVPYKRRKKEN -> AGVSLFSFPWPTSLLRI (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:19668219"
FT /id="VSP_038704"
FT VAR_SEQ 309..566
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19668219"
FT /id="VSP_038705"
FT MUTAGEN 305
FT /note="K->T: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:22723967"
SQ SEQUENCE 566 AA; 59633 MW; 6CC4B10E914EFD83 CRC64;
MEDSDSAAKQ LGLAEAAAVA AAAAVAAAAA AAAESEAEEP VLSRDEDSEE DADSEAERET
RRVTAVAVMA AESGHMDMGT EALPSPDEAA AAAAAFAEVT TVTVANVGSS ADNVFTTSVA
NAASISGHVL SGRTALQIGD SLNTEKATLI VVHTDGSIVE TTGLKGPAAP LTPGPQSPPT
PLAPGQEKGG TKYNWDPSVY DSELPVRCRN ISGTLYKSRL GSGGRGRCIK QGENWYSPTE
FEAMAGRASS KDWKRSIRYA GRPLQCLIQD GILNPHAASC TCAACCDDMT LSGPVRLFVP
YKRRKKENEL PTTPVKKDSP KNITLLPATA ATTFTVTPSG QITTSGALTF DRASTVEATA
VISESPAQGD VFAGATVQEA GVQPPCRVGH PEPHYPGYQD SCQIAPFPEA ALPTSHPKIV
LTSLPALAVP PSTPTKAVSP TVVSGLEMSE HRSWLYLEEM VNSLLNTAQQ LKTLFEQAKQ
ASSCREAAVT QARMQVDTER KEQSCVNCGR EAMSECTGCH KVNYCSTFCQ RKDWKDHQHV
CGQSASVTVQ ADDVHVEESV IEKVAV
