SMG1_DROME
ID SMG1_DROME Reviewed; 3218 AA.
AC Q70PP2; Q6NP14; Q9W3V6;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Serine/threonine-protein kinase Smg1;
DE EC=2.7.11.1;
GN Name=nonC; Synonyms=Smg1; ORFNames=CG32743;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RX PubMed=12881430; DOI=10.1093/emboj/cdg371;
RA Gatfield D., Ciccarelli F.D., Bork P., Izaurralde E.;
RT "Nonsense-mediated mRNA decay in Drosophila: at the intersection of the
RT yeast and mammalian pathways.";
RL EMBO J. 22:3960-3970(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2062-3218 (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP POSSIBLE LACK OF INVOLVEMENT IN NONSENSE-MEDIATED MRNA DECAY.
RX PubMed=15965240; DOI=10.1534/genetics.105.045674;
RA Chen Z., Smith K.R., Batterham P., Robin C.;
RT "Smg1 nonsense mutations do not abolish nonsense-mediated mRNA decay in
RT Drosophila melanogaster.";
RL Genetics 171:403-406(2005).
RN [6]
RP FUNCTION.
RX PubMed=16199763; DOI=10.1261/rna.2160905;
RA Rehwinkel J., Letunic I., Raes J., Bork P., Izaurralde E.;
RT "Nonsense-mediated mRNA decay factors act in concert to regulate common
RT mRNA targets.";
RL RNA 11:1530-1544(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Serine/threonine protein kinase involved in mRNA
CC surveillance. Recognizes the substrate consensus sequence [ST]-Q.
CC Involved in nonsense-mediated decay (NMD) of mRNAs containing premature
CC stop codons, probably by phosphorylating Upf1.
CC {ECO:0000269|PubMed:12881430, ECO:0000269|PubMed:16199763}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of a post-splicing multiprotein NMD complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A;
CC IsoId=Q70PP2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q70PP2-2; Sequence=VSP_017754, VSP_017755;
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
CC -!- CAUTION: According to some authors (PubMed:15965240) it may not be
CC directly involved in NMD, as mutants do not abolish NMD. However, other
CC data clearly show its involvement in NMD (PubMed:12881430 and
CC PubMed:16199763). {ECO:0000305|PubMed:15965240}.
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DR EMBL; AJ556818; CAD89223.1; -; mRNA.
DR EMBL; AE014298; AAF46207.2; -; Genomic_DNA.
DR EMBL; BT011117; AAR82784.1; -; mRNA.
DR RefSeq; NP_001284967.1; NM_001298038.1. [Q70PP2-1]
DR RefSeq; NP_727132.1; NM_167095.3. [Q70PP2-1]
DR BioGRID; 58110; 3.
DR STRING; 7227.FBpp0070933; -.
DR iPTMnet; Q70PP2; -.
DR PaxDb; Q70PP2; -.
DR PRIDE; Q70PP2; -.
DR EnsemblMetazoa; FBtr0070972; FBpp0070933; FBgn0263968. [Q70PP2-1]
DR EnsemblMetazoa; FBtr0343321; FBpp0309979; FBgn0263968. [Q70PP2-1]
DR GeneID; 31625; -.
DR KEGG; dme:Dmel_CG32743; -.
DR CTD; 31625; -.
DR FlyBase; FBgn0263968; nonC.
DR VEuPathDB; VectorBase:FBgn0263968; -.
DR eggNOG; KOG0891; Eukaryota.
DR HOGENOM; CLU_000316_0_0_1; -.
DR InParanoid; Q70PP2; -.
DR OMA; EAIIMRH; -.
DR PhylomeDB; Q70PP2; -.
DR SignaLink; Q70PP2; -.
DR BioGRID-ORCS; 31625; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 31625; -.
DR PRO; PR:Q70PP2; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0263968; Expressed in spermathecum and 22 other tissues.
DR ExpressionAtlas; Q70PP2; baseline and differential.
DR Genevisible; Q70PP2; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IDA:FlyBase.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:FlyBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0050808; P:synapse organization; IDA:FlyBase.
DR GO; GO:0048489; P:synaptic vesicle transport; IDA:FlyBase.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR CDD; cd05170; PIKKc_SMG1; 1.
DR Gene3D; 1.10.1070.11; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR031559; SMG1.
DR InterPro; IPR039414; SMG1_PIKKc.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF15785; SMG1; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Manganese;
KW Metal-binding; Nonsense-mediated mRNA decay; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..3218
FT /note="Serine/threonine-protein kinase Smg1"
FT /id="PRO_0000229795"
FT DOMAIN 1289..1692
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT REPEAT 1643..1678
FT /note="HEAT"
FT DOMAIN 1897..2232
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 3186..3218
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 32..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1903..1909
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2101..2109
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2121..2145
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 34..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 2159..2162
FT /note="GPFR -> KRCS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12881430"
FT /id="VSP_017754"
FT VAR_SEQ 2163..3218
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12881430"
FT /id="VSP_017755"
SQ SEQUENCE 3218 AA; 361587 MW; BE6ADBB9A38DA3CA CRC64;
MKNAIHPENC NGAGTEEEAS SAFHAEIDRV LLNNNGNHGD SSNEGGGGNG SGRGGATGSG
NIAGLGGSES MWSPGGGKSH DVAQAFANAL LLRNMNHVVG KGQPVVQNHR KAYQCKGDTI
NPMANGEDLR LSKIIRRLIN ENNPTVSLEL CSKLDQAVRT PINMGYMTCS FVWILDNMLT
LYKQCPPPVL EECSKTLGLI GFINRKSYPI YEEFIVKNYK SSKRMQKYMI MALRATLSCD
TKCELHMYAD KIMLLLKDFL ENAESADIFI VVSNTLVQFA ASYAETFECH FTDVVDIVIG
WQLEAGQPTD LKTHCAQVLE QLTPFFSKQI DFSYGLLDQF VEDITTLEEG EPANTAERVG
AFVGAFNTLL KCLARMQIFV GMPTCECIVK MAVDHLIKIM PTLHLNTEAL VNINELICIC
LLNNFTGLDP ILLEQVLLDQ VKRMISLTEL QRQSVLYLLL CTVRRLRARL TPSLVHFIFQ
SNPYMTKVRL RSPGETSYKL LLRTCQETLL IRNVPLLQQA YKYLVDDIDA CLEKLLITAP
RSKARKASVL LVFHLSALAA LAKQTSSIIG MYACKPSILE LLLTNCRAHE LKFWSKYPAA
QQAIFGLLVV HCQANHNFRT NSSLLRDQEL SAENTSPTAN SFASILRFLD SVLGQAHQLA
PQNLRVLLQW IQMLLRECRE KIDLLMEQEN FRGICRNIAA TASKLVPLES AACIQTVLDY
GLERLEKYPK LLILYRDTAL QQLQMLSTNY HAPYFQIYAQ LPLHLTLTGG ESSMPGMASR
RVSVWQQRIS QYSAVRDNVF RDFFDRVQKP EQDSLIHCLR ELFVRSCQVA PQDERQMNLS
QCTKRCQRLA IAWLQFEAAR YCVDQRLRTT VGKPQETFLG FEAIIMRHAR LLSGCAKEIE
RSALDDLSLE ELLSMQSNLS LLLGFLDALE KLIYNAAEGS AFALRPPEKQ VAAFFRLNNP
TCQSWFNRIR IGVVIIAMHV QQPELVIRYA QQILVNSKTQ DPTYSQAIVY MAWSLVSCQE
ADSLRGLRLW ARGKSCKSYK WLKYAADQAA GKRESALAGY RTILAEKELQ SELEPHTRQF
VVSQMMQCLQ DLGQWSQLVE LKQQQMTRPE DRELNPFLQR SNVEVNALER LLAKSEESCS
SMDALGGVFQ QLSLWPSNWD ESVSSSGLSE RASFSSIHMR QRTEDIVLHK LLEDRCVPDQ
AKNLLDTQWR DSLLNPSFDQ RSCKELTLLR HIVQGVSGGQ ELSLLPVSSG RCQNRSKFIS
SAILMRCLAW TQLLRQHCAP GSWETLCLDA AAAAREEGNL QLAETLLTQF FGQPIGEIAA
LFSLEQGVQT DNPEMLRGYS ELVKCLHLQQ QQSQTHSGDL SSSIDVCAAL CLNIQKSNNQ
PAAGADLLLN LADWIAVRTC NGLTTNQSPV LIQLLDQLPE CPLTCDSSQP LAIPQAERMV
ARLVHSCLQQ RPNYAEALIA YGNWCYRWGK KVADSCCVLT QADATAISQA LDIPQPLESE
KLDELLQALS TEQPPANCVE VCPDAARARD DEAAKNRLRR LTFLADKTPE ALDAILQIWR
RAIANTYDYY KDAARSYFQY LSFKSGSGPE KPEGEGVVSQ RERLHVDDSN LVTTTLRLLR
LIVKHASGLQ EVLEQGLHTT PIAPWKVIIP QLFSRLNHHE PYVRKSVCDL LCRLAKSRPQ
LVIFPAVVGA NREQQDATAP PATARPTTED ACCYGYLLGE LSKQAPEAVQ HVKLMVKELR
RVCLLWDEYW IHSLAHIYNT YVSRVSALAT DFRPDDHEGK NNRFNVWRPQ LLADLEALVA
VTSRPPETTY ERSFRKRFDA PIRLTVDALR HRRYPEAWDK LKQLYHILQS NMIRGSGSTL
KMQSISPVLC GIGRMRISMP GLDAHGPDGD QVYIESVESS VCVLPTKTKP KKVAFYGSNG
QRYTFLFKGM EDLHLDERIM QFLSISNAIM ACRSDAPGNG CYRAHHYSVI PLGPQSGLIS
WVDGVTPVFA LYKKWQQRRS QVAGNAGAGA VANVPRRFTD LFYNKLSPLL AKHNMQVSDP
RRQWPISVLL QVLDELSQET PNDLLARELW CQAGNAAEWR QSVRRFVRCM SVMSMIGYVI
GLGDRHLDNV LINLGSGDIV HIDYNVCFEK GRTLRIPEKV PFRLTQNLVQ AMGITGIEGP
FRLGCEYVLK VMRKERETLL TLLEAFVYDP LVDWTTNDDA QALRRSLNAK LQESADGGGA
GGLGVGDLKY HKKDKNKGKP LDSDVKRQPF LSKLGMLQKY WSTNKTELMP QLEEMEQEVG
NLQAAQAKQV VAEEELVKLN QRSALIAEIK SLGTAIESHS FNTASLRNAV RRGHSEALAL
LSTERLPDFG RVQCILRSYG QCLQLYHLLD LQGQLVKLQM ESNSENAREF SALTEALQLS
GLDSMRSQLN ELLGRMDMVA QKSSKHLQEY AGVMNFYPEQ SHRQNLFVRF HDSFATYIQN
GYTADSTTNT NSPSSSIICK ADVVGVAEAM EYSWERLGCQ LHEASKLYAA NQAQALTLGA
PTTALLSMIV QSGCSQLLLK ASLVRTLDRA GGAFAAYEQV ALASHDDGLL HHQLLFIHLV
RTMLQGVLVM TKEEDQHLAQ LESLLSALSH LKKMFEYDLP ANLYRLLLLQ PNLGKLSALC
HLSASSLAQL FLEATMENGH KPPDQFPVER RFLLTLQPVY DQFLLASTSL DSLVSSMQSM
LEDVHDVQTQ QIMELGLMRS CHTELNDECF FGLVSEALES SRTCDVREMA RPMLGFIHRL
QVEKLAGLLP ILTRNFYTAV GPQCLPTASC GDPAQADHLC ESLFISLQSD GALLQQQAEI
ALLSQQVDLH TLAASAQYWA YSEALGSQLR CGPHIVSRPK LTAAIGECWL ELDQKLTALQ
QLQAGLESQL SQLQTQRSNW NRNHIDNLLR MEQCNKQRTM SHVALLQKMT DGAGAVARLE
QNAIVVGEEG QALVDHLEQW LAAHGQWQAS SSRISAVEQS MVELLDPEGA IDHYWLENVQ
GLLEEQTCKV HREIAAIEGE QQSKHRFICT LLKETLRLLE NMPRFHVQSL CSEAQAQGQG
KMEYANVQLL SDHLREGQGL MQSLYMRLQE LRKDICSDRR VLQPSMLQNW RHQLEMILTL
AKQEVNEFFK GLEDFMQHAG ETDSYEIFTH AKGSGNVHEQ KRNAYGVSVW KKIRMKLEGR
DPDSNQRSTV AEQVDYVIRE ACNPENLAVL YEGWTPWV
