ATM_DROME
ID ATM_DROME Reviewed; 2767 AA.
AC Q5EAK6; Q0KI71; Q6TKQ1; Q8MZG4; Q9VFB1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Serine/threonine-protein kinase ATM;
DE EC=2.7.11.1;
DE AltName: Full=Telomere fusion protein;
GN Name=tefu; Synonyms=atm; ORFNames=CG6535;
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 [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 [2]
RP GENOME REANNOTATION.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1569-2767.
RX PubMed=14729967; DOI=10.1128/mcb.24.3.1219-1231.2004;
RA Brodsky M.H., Weinert B.T., Tsang G., Rong Y.S., McGinnis N.M., Golic K.G.,
RA Rio D.C., Rubin G.M.;
RT "Drosophila melanogaster MNK/Chk2 and p53 regulate multiple DNA repair and
RT apoptotic pathways following DNA damage.";
RL Mol. Cell. Biol. 24:1219-1231(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2183-2767.
RC STRAIN=Berkeley; TISSUE=Testis;
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 [5]
RP FUNCTION.
RX PubMed=15296750; DOI=10.1016/j.cub.2004.06.056;
RA Silva E., Tiong S., Pedersen M., Homola E., Royou A., Fasulo B.,
RA Siriaco G., Campbell S.D.;
RT "ATM is required for telomere maintenance and chromosome stability during
RT Drosophila development.";
RL Curr. Biol. 14:1341-1347(2004).
RN [6]
RP FUNCTION.
RX PubMed=15296751; DOI=10.1016/j.cub.2004.06.063;
RA Bi X., Wei S.-C.D., Rong Y.S.;
RT "Telomere protection without a telomerase; the role of ATM and Mre11 in
RT Drosophila telomere maintenance.";
RL Curr. Biol. 14:1348-1353(2004).
RN [7]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15296752; DOI=10.1016/j.cub.2004.06.064;
RA Song Y.-H., Mirey G., Betson M., Haber D.A., Settleman J.;
RT "The Drosophila ATM ortholog, dATM, mediates the response to ionizing
RT radiation and to spontaneous DNA damage during development.";
RL Curr. Biol. 14:1354-1359(2004).
RN [8]
RP IDENTIFICATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15256487; DOI=10.1101/gad.1202504;
RA Oikemus S.R., McGinnis N., Queiroz-Machado J., Tukachinsky H., Takada S.,
RA Sunkel C.E., Brodsky M.H.;
RT "Drosophila atm/telomere fusion is required for telomeric localization of
RT HP1 and telomere position effect.";
RL Genes Dev. 18:1850-1861(2004).
RN [9]
RP FUNCTION.
RX PubMed=16020777; DOI=10.1534/genetics.105.047720;
RA Bi X., Gong M., Srikanta D., Rong Y.S.;
RT "Drosophila ATM and Mre11 are essential for the G2/M checkpoint induced by
RT low-dose irradiation.";
RL Genetics 171:845-847(2005).
RN [10]
RP FUNCTION.
RX PubMed=16203987; DOI=10.1073/pnas.0504981102;
RA Bi X., Srikanta D., Fanti L., Pimpinelli S., Badugu R., Kellum R.,
RA Rong Y.S.;
RT "Drosophila ATM and ATR checkpoint kinases control partially redundant
RT pathways for telomere maintenance.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15167-15172(2005).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=22964637; DOI=10.1038/onc.2012.395;
RA Wang Y., Wang Z., Joshi B.H., Puri R.K., Stultz B., Yuan Q., Bai Y.,
RA Zhou P., Yuan Z., Hursh D.A., Bi X.;
RT "The tumor suppressor Caliban regulates DNA damage-induced apoptosis
RT through p53-dependent and -independent activity.";
RL Oncogene 32:3857-3866(2013).
CC -!- FUNCTION: Serine/threonine-protein kinase which recognizes the
CC substrate consensus sequence [ST]-Q. Required to suppress spontaneous
CC apoptosis of proliferating cells during development, and for their
CC proper differentiation. Required for female fertility. Protects
CC telomeres from fusion, maybe by recruiting or maintaining chromatin-
CC modifying complexes such as Su(var)205/HP1. May activate checkpoint
CC signaling in response to DNA double-stranded breaks induced by low-dose
CC ionizing radiation. May phosphorylate histone H2AV.
CC {ECO:0000269|PubMed:15256487, ECO:0000269|PubMed:15296750,
CC ECO:0000269|PubMed:15296751, ECO:0000269|PubMed:15296752,
CC ECO:0000269|PubMed:16020777, ECO:0000269|PubMed:16203987}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels throughout development and
CC at much higher levels in adult females compared to males.
CC {ECO:0000269|PubMed:15296752}.
CC -!- DISRUPTION PHENOTYPE: Flies die shortly before or after eclosion with a
CC rough eye phenotype, misshapen wings, and missing or abnormal bristles
CC (PubMed:15256487). Shows increased numbers of spontaneous tumors
CC (PubMed:15256487). Simultaneous knockout of tefu and Clbn/NEMF
CC increases the formation of spontaneous tumors (PubMed:22964637).
CC {ECO:0000269|PubMed:15256487, ECO:0000269|PubMed:22964637}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM29197.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014297; ABI31168.1; -; Genomic_DNA.
DR EMBL; AY395750; AAR89513.1; -; mRNA.
DR EMBL; AY113192; AAM29197.1; ALT_INIT; mRNA.
DR EMBL; BK004084; DAA04940.1; -; mRNA.
DR RefSeq; NP_001036712.1; NM_001043247.2.
DR SMR; Q5EAK6; -.
DR BioGRID; 66903; 25.
DR IntAct; Q5EAK6; 2.
DR STRING; 7227.FBpp0110174; -.
DR PaxDb; Q5EAK6; -.
DR PRIDE; Q5EAK6; -.
DR EnsemblMetazoa; FBtr0110874; FBpp0110174; FBgn0045035.
DR GeneID; 41839; -.
DR KEGG; dme:Dmel_CG6535; -.
DR CTD; 41839; -.
DR FlyBase; FBgn0045035; tefu.
DR VEuPathDB; VectorBase:FBgn0045035; -.
DR eggNOG; KOG0892; Eukaryota.
DR GeneTree; ENSGT00940000174195; -.
DR HOGENOM; CLU_227091_0_0_1; -.
DR InParanoid; Q5EAK6; -.
DR OMA; FPYFLCY; -.
DR OrthoDB; 80538at2759; -.
DR PhylomeDB; Q5EAK6; -.
DR Reactome; R-DME-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-DME-5693548; Sensing of DNA Double Strand Breaks.
DR Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-DME-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-DME-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DME-69473; G2/M DNA damage checkpoint.
DR Reactome; R-DME-69541; Stabilization of p53.
DR Reactome; R-DME-9664873; Pexophagy.
DR BioGRID-ORCS; 41839; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 41839; -.
DR PRO; PR:Q5EAK6; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0045035; Expressed in eye disc (Drosophila) and 24 other tissues.
DR ExpressionAtlas; Q5EAK6; baseline and differential.
DR Genevisible; Q5EAK6; DM.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035173; F:histone kinase activity; IDA:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0051276; P:chromosome organization; IMP:FlyBase.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IMP:FlyBase.
DR GO; GO:1990164; P:histone H2A phosphorylation; IDA:FlyBase.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR GO; GO:0000706; P:meiotic DNA double-strand break processing; IDA:FlyBase.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:FlyBase.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IGI:FlyBase.
DR GO; GO:0034351; P:negative regulation of glial cell apoptotic process; IMP:FlyBase.
DR GO; GO:0045824; P:negative regulation of innate immune response; IMP:FlyBase.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:FlyBase.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IBA:GO_Central.
DR GO; GO:0030717; P:oocyte karyosome formation; IDA:FlyBase.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; IMP:FlyBase.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:FlyBase.
DR GO; GO:0000723; P:telomere maintenance; IMP:FlyBase.
DR CDD; cd05171; PIKKc_ATM; 1.
DR Gene3D; 1.10.1070.11; -; 1.
DR InterPro; IPR015519; ATM/Tel1.
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; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR044107; PIKKc_ATM.
DR PANTHER; PTHR11139:SF72; PTHR11139:SF72; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Chromatin regulator; Chromosome;
KW Developmental protein; DNA damage; Kinase; Nucleotide-binding; Nucleus;
KW Reference proteome; Serine/threonine-protein kinase; Telomere; Transferase.
FT CHAIN 1..2767
FT /note="Serine/threonine-protein kinase ATM"
FT /id="PRO_0000225627"
FT DOMAIN 1713..2317
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 2419..2734
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 2735..2767
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 2425..2431
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2601..2609
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 2621..2645
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT CONFLICT 2733
FT /note="T -> P (in Ref. 4; AAM29197)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2767 AA; 317991 MW; F354E55FA1B35570 CRC64;
MSALLNEIQR ILGDLQSGKA ASRNKGIQQL DEKLSSCRED LDKLFLSKTS DISWTTIFEA
SKEALFKQAG NLEDVNEKVF KTLAGKNYLY DNVLEKITQF NLEAGSQTSG NGHFLAKTSI
FSAFEDGIKM RVVVKYFGDR ILSLLEKGIY SSVSYVRDLK INEYSRILSY LFELNVDMDE
VLRTRILKCI TRTVSLAKDR VQLHVDLVEY LPELSSFALS AFGARKTEIV RVYLIFASEL
AVNYNHQLNV HMQEILPKLC EYHDEDAFRD DTRNLFFQCV SKSLHSMYLK MDMCDFNTLG
VPVHEKWPQT LLRLKTIVNV EIRKNSWARC KNALLSNNKF SDPFIKMSAL AMYIVLWHLE
TKKADENGEG DAPKKIPKPA DKMETIFSLI DKKENTFNDV WLAIFTEILQ LSSVILNVAN
YQMALTTVAE IMQMYGNAKN LRNLRLCLAH LLTKEQELLH SKSIREDFLG ELWSQMANQL
ISETTTNSEE IKEKQLVLQM LIRHNKLNQK LSSTLLNNII SNEMLKRNEC LATIREIFIH
ADKCGQDKAS ADLEPIIAWA YGSADRFIAA QMIHNIDSID AQLQADTFAI SIINFLDVQQ
LRQISQSEHI VPSTERNLLA YKYNEQLICF DKDYATPFES ITHIQSETKN CLIQSNYDCL
MRGLNFEIAK ENKPAAIIKN LNSLLKLICT MERLLHYKVF DADTYTGCPL IKRIGLYLSH
IEFQLKANGA EILDKSDLPE ILRLEIYVLD VFRTNLVLLD YLERQPIEML VEFVGAALKL
HSMQRERSVD ADHGTITRLC LNILAGLCAY NSHRDEAFEH IVKVTMRWHP QDVLIVTKML
CSCQTISEAS SSWLVSKLKT LFQQHHQDAE LMDKVVQHMP TIFYFVRHKE NHLDDMLMAL
NSLLRIAIKK SYTSNLTAKI VRCVGLIAQR CPDIYLLENF AVICKSTAKF ITMPTLEVRF
ATLFTFTILL ESNCVTSDAI GHSRTHWDFC QELYESIEFK KLTYNNEDAI QNSNALIVQM
LIAIFLRSSF HQEIALKELL HHCALRRLTE REFISLQSMS SCHRQTVRDL IRPFAAILLH
HWSSKRWPIS KFPYFLCYST KSEFRKTHAS EIMAYTFLYG KTEDIERCSK SISEELALPI
LASFLLIKNS SCSESEGQNF KEHLQLLSEN LSYSQLNATD VDLDLDILCY VISMLHDPQE
MMRLFGSLAI CNRTASWYSL SGESLFKCLN FHIDPEMRPS MDSRIQSMTT LQTKHSRVLV
DIFGRLKTNC YSASFSSQAL HDFFLYCEVA DAVYDAARKN ETIVTQCSFF VRDIWFFVVR
LLIHTKFIRV QMAALTFLEL LLNKHNFRLD DYQNHFGDIA KLLSNFQLCC EAKEVREKTM
SIVMYILESK KGHINLNSFL EETTDCEFLK PLREDCKSSQ PNIDRADVAN YLRSFLLSPT
PERLRDLRTY IAEHKDKVQE HEKLLFGVIN KLIQMTRDAH NKTTSIDSLK CLAQIGPLKI
STVSYYFQTD FEAFEKSNGE PMEAFLGVVC HSLDTSLFQF DPKTHEGLVS VAIQVVNSKP
GSNIMERYKN LRIFADKSTA STFLHSNKQI RRIDWLSILK ATKSLSYEPW MCAFVSKVFQ
MCGWLGFDKL AATSFAFAKT CLLPFIKLLL ENSLEHVESL SQMLDYFFEG FTSSTAPNSQ
EIFRNKRAIK KFLHICEYIR IFNNWTIPIN LSNVVMASNH CQAYFLSIMY LELWACSESP
KSKADFLDNE CFQDGAKKAY ESIGCLDAIP GFVNPMRSRL DFLGHGSNLS TILLESDHLD
RASGQLCIDI MKGNGLWSFA KLQQHQNIEP DYEIFWRLGQ WDSLTDPKHQ QNQTVVRTSL
DLEQEFKRHH FVALRSIGQR EEENSLSAIE QAYSCVRDIL MEISVECLQS VYKYLTWLCS
LQQAEDFCQI QFGTQLDPAS TTKIFRKWQT ELELKYGNFS CKEYVIAHQI ALLKLAGTRA
SRRMSEFYQK DPISTYLMKG IEECKSAGKL NLAAKYTATL RELPNIRESI KISVLLEDAE
INLKMGNQQI AKAILDYVTN NNEFVYCVQR VPALRMQGEF LLDCNAETLS WVQSHKFNNS
LKLIDDFVQH RQTLSEKYRD IFDWHQLDAY ASKQRTAAYA TIAKYADREY QQLHDYRHSQ
EYQTLKDIIE QNRQTAEKVT QRENQDRRVI SVQMKRYASL DEQQLNQIEE KLTEYLRLAL
TNYMAYCRLD SGFSSAAIYR IISLWFTNAT SKQCQECIKD EILTVPSYKF ICAANQLTAR
LNSKNTSLLK GLTDLLVQCG KDHPYHTFYQ LYPLVFAHLD GENSNTERSG IARKIIAMIC
EKNGTAGECS KQLESLLPAL ITFANEGKTN DNRPVSDSVR NKQFDKVRRW RNLNAVHCPT
LELPVMPSKE YSIISVVKWT NETTQCGGLN APVKIMCVCS DGKIRAQLVK GKDDLRQDAV
MQQVFGIVNE LLNQDSEFIE RKLKLRTYKV TPLSMRSGIL EWCTNSVPVG HYLVVEGKGG
AHARYRPNDW NNNKCRKLSS DHLKSPKETR YAIYKKICEN IKPVFHYFLL EKFPIPGVWF
ERRLAYTNSV ATTSMVGYVL GLGDRHTQNI LVDQQTAEVI HIDFGIAFEQ GKIQTTPETV
PFRLTRDFVA PMGICGTKGV FAKSCEATMH ILRRYKSVFT TILEVLLYDP LFIWGVLKKK
QSPQQSGEES VNLVAQRALL LVQNKLDGRE AGTMGDSNVE AQVERLINEA TLPSNLCMLF
PGWDPHL
