ADAR_DROME
ID ADAR_DROME Reviewed; 676 AA.
AC Q9NII1; O96834; Q8IRX2; Q8MSQ9; Q9BJ37; Q9NII2; Q9W562;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Double-stranded RNA-specific editase Adar;
DE EC=3.5.-.-;
DE AltName: Full=Adenosine deaminase that act on RNA;
DE AltName: Full=Pre-mRNA adenosine deaminase;
DE AltName: Full=RNA-editing deaminase 1;
DE AltName: Full=RNA-editing enzyme 1;
DE AltName: Full=dADAR;
DE AltName: Full=dsRNA adenosine deaminase;
GN Name=Adar {ECO:0000312|EMBL:AAF63702.1};
GN Synonyms=hypnos-2 {ECO:0000303|PubMed:11254668}; ORFNames=CG12598;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF63702.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A; C; D; E; F AND G), FUNCTION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND RNA EDITING OF POSITION 437.
RC STRAIN=Canton-S {ECO:0000312|EMBL:AAF63702.1};
RX PubMed=10917596; DOI=10.1017/s1355838200000248;
RA Palladino M.J., Keegan L.P., O'Connell M.A., Reenan R.A.;
RT "dADAR, a Drosophila double-stranded RNA-specific adenosine deaminase is
RT highly developmentally regulated and is itself a target for RNA editing.";
RL RNA 6:1004-1018(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAK26850.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11254668; DOI=10.1172/jci11625;
RA Ma E., Gu X.-Q., Wu X., Xu T., Haddad G.G.;
RT "Mutation in pre-mRNA adenosine deaminase markedly attenuates neuronal
RT tolerance to O(2) deprivation in Drosophila melanogaster.";
RL J. Clin. Invest. 107:685-693(2001).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAF45665.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAF45665.2}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5] {ECO:0000305, ECO:0000312|EMBL:CAA22774.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R {ECO:0000269|PubMed:10731137};
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAM50022.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=10966106; DOI=10.1016/s0092-8674(00)00049-0;
RA Palladino M.J., Keegan L.P., O'Connell M.A., Reenan R.A.;
RT "A-to-I pre-mRNA editing in Drosophila is primarily involved in adult
RT nervous system function and integrity.";
RL Cell 102:437-449(2000).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=12756328; DOI=10.1261/rna.2120703;
RA Peters N.T., Rohrbach J.A., Zalewski B.A., Byrkett C.M., Vaughn J.C.;
RT "RNA editing and regulation of Drosophila 4f-rnp expression by sas-10
RT antisense readthrough mRNA transcripts.";
RL RNA 9:698-710(2003).
CC -!- FUNCTION: Has A-to-I RNA editing activity on extended dsRNA: edits RNA-
CC binding protein Rnp4F. A-to-I editing of pre-mRNAs acts predominantly
CC through nervous system targets to affect adult nervous system
CC integrity, function and behavior. Essential for adaptation to
CC environmental stresses, such as oxygen deprivation, and for the
CC prevention of premature neuronal degeneration, through the editing of
CC ion channels as targets. {ECO:0000269|PubMed:10917596,
CC ECO:0000269|PubMed:10966106, ECO:0000269|PubMed:11254668,
CC ECO:0000269|PubMed:12756328}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=7;
CC Name=C {ECO:0000269|PubMed:10917596}; Synonyms=b
CC {ECO:0000303|PubMed:10917596};
CC IsoId=Q9NII1-1; Sequence=Displayed;
CC Name=A {ECO:0000269|PubMed:10917596}; Synonyms=a
CC {ECO:0000303|PubMed:10917596};
CC IsoId=Q9NII1-2; Sequence=VSP_051651;
CC Name=B {ECO:0000303|PubMed:10731132};
CC IsoId=Q9NII1-3; Sequence=VSP_051649, VSP_051651;
CC Name=D {ECO:0000269|PubMed:10917596};
CC IsoId=Q9NII1-4; Sequence=VSP_051648;
CC Name=F {ECO:0000269|PubMed:10917596};
CC IsoId=Q9NII1-5; Sequence=VSP_051650;
CC Name=G {ECO:0000269|PubMed:10917596};
CC IsoId=Q9NII1-6; Sequence=VSP_051650, VSP_051651;
CC Name=E;
CC IsoId=Q9NII1-7; Sequence=VSP_018700;
CC -!- TISSUE SPECIFICITY: Expressed in embryonic nervous system; late stage
CC 13 sees ventral nerve cord expression which spreads to brain by stage
CC 16. Expression is maintained through to adulthood.
CC {ECO:0000269|PubMed:10917596, ECO:0000269|PubMed:10966106,
CC ECO:0000303|PubMed:11254668}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development, highest
CC expression is during pupal stage. Isoforms A, C and D have lowest
CC expression levels. {ECO:0000269|PubMed:10917596}.
CC -!- RNA EDITING: Modified_positions=437 {ECO:0000269|PubMed:10917596};
CC Note=Partially edited. Editing is low in embryos and pupae and
CC increases dramatically upon eclosion. {ECO:0000269|PubMed:10917596};
CC -!- DISRUPTION PHENOTYPE: Adult flies are morphologically wild-type but
CC exhibit extreme behavioral defects including temperature-sensitive
CC paralysis, locomotor uncoordination, and tremors which increase in
CC severity with age. {ECO:0000269|PubMed:10966106}.
CC -!- MISCELLANEOUS: [Isoform E]: Produced by alternative initiation at Met-8
CC of isoform C. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM50022.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF208535; AAF63702.1; -; Genomic_DNA.
DR EMBL; AF208535; AAF63703.1; -; Genomic_DNA.
DR EMBL; AF343579; AAK26850.1; -; mRNA.
DR EMBL; AE014298; AAF45665.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09057.2; -; Genomic_DNA.
DR EMBL; AL035207; CAA22774.1; -; Genomic_DNA.
DR EMBL; AY118653; AAM50022.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001245469.1; NM_001258540.1.
DR RefSeq; NP_569940.2; NM_130584.4.
DR RefSeq; NP_726761.2; NM_166903.3. [Q9NII1-3]
DR PDB; 2LJH; NMR; -; A=48-140.
DR PDBsum; 2LJH; -.
DR AlphaFoldDB; Q9NII1; -.
DR BMRB; Q9NII1; -.
DR SMR; Q9NII1; -.
DR BioGRID; 57679; 7.
DR IntAct; Q9NII1; 1.
DR STRING; 7227.FBpp0300329; -.
DR PaxDb; Q9NII1; -.
DR DNASU; 31130; -.
DR EnsemblMetazoa; FBtr0070300; FBpp0070287; FBgn0026086. [Q9NII1-3]
DR EnsemblMetazoa; FBtr0305499; FBpp0293951; FBgn0026086. [Q9NII1-6]
DR EnsemblMetazoa; FBtr0339272; FBpp0308381; FBgn0026086. [Q9NII1-7]
DR GeneID; 31130; -.
DR KEGG; dme:Dmel_CG12598; -.
DR CTD; 103; -.
DR FlyBase; FBgn0026086; Adar.
DR VEuPathDB; VectorBase:FBgn0026086; -.
DR eggNOG; KOG2777; Eukaryota.
DR GeneTree; ENSGT00940000168020; -.
DR InParanoid; Q9NII1; -.
DR PhylomeDB; Q9NII1; -.
DR BRENDA; 3.5.4.37; 1994.
DR Reactome; R-DME-75102; C6 deamination of adenosine.
DR Reactome; R-DME-77042; Formation of editosomes by ADAR proteins.
DR BioGRID-ORCS; 31130; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31130; -.
DR PRO; PR:Q9NII1; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0026086; Expressed in saliva-secreting gland and 27 other tissues.
DR ExpressionAtlas; Q9NII1; baseline and differential.
DR Genevisible; Q9NII1; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; HDA:FlyBase.
DR GO; GO:0003726; F:double-stranded RNA adenosine deaminase activity; IDA:FlyBase.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IBA:GO_Central.
DR GO; GO:0006382; P:adenosine to inosine editing; IDA:UniProtKB.
DR GO; GO:0030534; P:adult behavior; IMP:FlyBase.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0007626; P:locomotory behavior; IMP:FlyBase.
DR GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
DR GO; GO:0016556; P:mRNA modification; IDA:FlyBase.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0042752; P:regulation of circadian rhythm; IDA:FlyBase.
DR GO; GO:0042391; P:regulation of membrane potential; IMP:FlyBase.
DR GO; GO:0060964; P:regulation of miRNA-mediated gene silencing; IMP:FlyBase.
DR GO; GO:0009408; P:response to heat; IMP:FlyBase.
DR GO; GO:0001666; P:response to hypoxia; IMP:FlyBase.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0009451; P:RNA modification; IDA:FlyBase.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR InterPro; IPR002466; A_deamin.
DR InterPro; IPR014720; dsRBD_dom.
DR Pfam; PF02137; A_deamin; 1.
DR Pfam; PF00035; dsrm; 2.
DR SMART; SM00552; ADEAMc; 1.
DR SMART; SM00358; DSRM; 2.
DR PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
DR PROSITE; PS50137; DS_RBD; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative splicing; Hydrolase;
KW Metal-binding; mRNA processing; Reference proteome; Repeat; RNA editing;
KW Zinc.
FT CHAIN 1..676
FT /note="Double-stranded RNA-specific editase Adar"
FT /id="PRO_0000004790"
FT DOMAIN 61..127
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 197..272
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 348..672
FT /note="A to I editase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 374
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P78563,
FT ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P78563,
FT ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 493
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P78563,
FT ECO:0000255|PROSITE-ProRule:PRU00240"
FT VAR_SEQ 1..28
FT /note="Missing (in isoform F and isoform G)"
FT /evidence="ECO:0000303|PubMed:10917596"
FT /id="VSP_051650"
FT VAR_SEQ 1..19
FT /note="MKFDSRVMLNSANNNSPQH -> MTLCRYSE (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10731132"
FT /id="VSP_051649"
FT VAR_SEQ 1..19
FT /note="MKFDSRVMLNSANNNSPQH -> MKFECFSLYCTVLK (in isoform
FT D)"
FT /evidence="ECO:0000303|PubMed:10917596"
FT /id="VSP_051648"
FT VAR_SEQ 1..7
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000305"
FT /id="VSP_018700"
FT VAR_SEQ 154..191
FT /note="GIENLSSSKMFEIIQTMLTEKLSNPTSLEQPTFCMSQN -> D (in
FT isoform A, isoform B and isoform G)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:10917596, ECO:0000303|PubMed:11254668"
FT /id="VSP_051651"
FT VARIANT 437
FT /note="S -> G (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:10917596"
FT CONFLICT 346
FT /note="V -> VSPQPAKHCETNYNAKPILDQV (in Ref. 5; CAA22774)"
FT /evidence="ECO:0000305"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:2LJH"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:2LJH"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2LJH"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:2LJH"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:2LJH"
FT HELIX 110..125
FT /evidence="ECO:0007829|PDB:2LJH"
SQ SEQUENCE 676 AA; 74978 MW; 6570D16D25D1C9F4 CRC64;
MKFDSRVMLN SANNNSPQHP VSAPSDINMN GYNRKLPQKR GYEMPKYSDP KKKMCKERIP
QPKNTVAMLN ELRHGLIYKL ESQTGPVHAP LFTISVEVDG QKYLGQGRSK KVARIEAAAT
ALRSFIQFKD GAVLSPLKPA GNLDFTSDEH LENGIENLSS SKMFEIIQTM LTEKLSNPTS
LEQPTFCMSQ NVSKSAITVD GQKKVPDKGP VMLLYELFND VNFECINIDG AQNNCRFKMT
VTINEKKFDG TGPSKKTAKN AAAKAALASL CNISYSPMVV PQKNVPLPID DKSSSMELPQ
IHADTIGRLV LEKFMEVIKG QEAYSRRKVL AGIVMTENMN FCEAKVISVS TGTKCVSGEH
MSVNGAVLND SHAEIVSRRC LLKYLYAQLD LQCNQATAYQ SIFVRNTDGQ YPYKLKSGVH
FHLYINTAPC GDARIFSPHE NDTGVDKHPN RKARGQLRTK IESGEGTIPV KSSDGIQTWD
GVLQGQRLLT MSCSDKIARW NIVGIQGSLL SSIIEPVYLH SIVLGSLLHP EHMYRAVCGR
IEKSIQGLPP PYHLNKPRLA LVTSAEPRNQ AKAPNFGINW TIGDTELEVV NSLTGRTIGG
QVSRITKQAF FVKYGFLMAN LPGILVRKVT TDYGQTKANV KDYQIAKLEL FSAFKREDLG
SWLKKPIEQD EFGLAE
