ID ATM_ARATH Reviewed; 3856 AA.
AC Q9M3G7; F4JDV3; Q9M4D7;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 152.
DE RecName: Full=Serine/threonine-protein kinase ATM {ECO:0000303|PubMed:10734187};
DE EC=2.7.11.1;
DE AltName: Full=Ataxia telangiectasia mutated homolog {ECO:0000303|PubMed:10734187};
DE Short=AtATM {ECO:0000303|PubMed:10734187};
GN Name=ATM {ECO:0000303|PubMed:10734187};
GN OrderedLocusNames=At3g48190 {ECO:0000312|Araport:AT3G48190};
GN ORFNames=T24C20.70 {ECO:0000312|EMBL:CAB92122.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=10734187; DOI=10.1093/nar/28.8.1692;
RA Garcia V., Salanoubat M., Choisne N., Tissier A.;
RT "An ATM homologue from Arabidopsis thaliana: complete genomic organisation
RT and expression analysis.";
RL Nucleic Acids Res. 28:1692-1699(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12509526; DOI=10.1105/tpc.006577;
RA Garcia V., Bruchet H., Camescasse D., Granier F., Bouchez D., Tissier A.;
RT "AtATM is essential for meiosis and the somatic response to DNA damage in
RT plants.";
RL Plant Cell 15:119-132(2003).
RN [5]
RP FUNCTION.
RX PubMed=16166376; DOI=10.1101/gad.1333805;
RA Vespa L., Couvillion M., Spangler E., Shippen D.E.;
RT "ATM and ATR make distinct contributions to chromosome end protection and
RT the maintenance of telomeric DNA in Arabidopsis.";
RL Genes Dev. 19:2111-2115(2005).
RN [6]
RP FUNCTION.
RX PubMed=15772150; DOI=10.1091/mbc.e04-10-0890;
RA Friesner J.D., Liu B., Culligan K., Britt A.B.;
RT "Ionizing radiation-dependent gamma-H2AX focus formation requires ataxia
RT telangiectasia mutated and ataxia telangiectasia mutated and Rad3-
RT related.";
RL Mol. Biol. Cell 16:2566-2576(2005).
RN [7]
RP FUNCTION, INTERACTION WITH RUG3, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=28262819; DOI=10.1038/srep43897;
RA Su C., Zhao H., Zhao Y., Ji H., Wang Y., Zhi L., Li X.;
RT "RUG3 and ATM synergistically regulate the alternative splicing of
RT mitochondrial nad2 and the DNA damage response in Arabidopsis thaliana.";
RL Sci. Rep. 7:43897-43897(2017).
CC -!- FUNCTION: Serine/threonine protein kinase which activates checkpoint
CC signaling upon genotoxic stresses such as ionizing radiation (IR) or
CC DNA replication stalling. Plays a central role in the perception and
CC response to both stress-induced damage in somatic cells and
CC developmentally programmed DNA damage during meiosis. Recognizes the
CC substrate consensus sequence [ST]-Q. Phosphorylates histone variant
CC H2AX to form H2AXS139ph at double strand breaks (DSBs), thereby
CC regulating DNA damage response mechanism. Involved in transcriptional
CC regulation of RAD51, PARP1, GR1, and LIG4 in response to DNA double
CC strand breaks. Plays a dual role by activating the DNA damage response
CC at dysfunctional telomeres and yet preventing this activation at
CC functional telomeres. Not required for telomere length homeostasis.
CC Regulates DNA damage response (DDR) synergistically with RUG3. Together
CC with RUG3, involved in the splicing of the ND2/NAD2 mRNA
CC (PubMed:28262819). {ECO:0000269|PubMed:12509526,
CC ECO:0000269|PubMed:15772150, ECO:0000269|PubMed:16166376,
CC ECO:0000269|PubMed:28262819}.
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 -!- SUBUNIT: Interacts with RUG3. {ECO:0000269|PubMed:28262819}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels with slightly
CC higher levels in flower buds. {ECO:0000269|PubMed:10734187}.
CC -!- DISRUPTION PHENOTYPE: Plants show meiotic defects, hypersensitivity to
CC double strand breaks-inducing agents, and an inability to properly
CC induce IR-mediated transcription of several DNA repair genes. Augmented
CC DNA damage response (DDR) associated with increased intracellular
CC reactive oxygen species (ROS) levels in response to methyl
CC methanesulfonate (MMS) treatment (PubMed:28262819).
CC {ECO:0000269|PubMed:12509526, ECO:0000269|PubMed:28262819}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000305}.
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DR EMBL; AJ250248; CAB86487.1; -; mRNA.
DR EMBL; AL096856; CAB92122.1; -; Genomic_DNA.
DR EMBL; CP002686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T51174; T51174.
DR SMR; Q9M3G7; -.
DR BioGRID; 9294; 2.
DR STRING; 3702.Q9M3G7; -.
DR PaxDb; 3702-AT3G48190-1; -.
DR ProteomicsDB; 246584; -.
DR Araport; AT3G48190; -.
DR TAIR; AT3G48190; ATM.
DR eggNOG; KOG0892; Eukaryota.
DR HOGENOM; CLU_000201_1_0_1; -.
DR InParanoid; Q9M3G7; -.
DR PhylomeDB; Q9M3G7; -.
DR BioCyc; ARA:AT3G48190-MONOMER; -.
DR PRO; PR:Q9M3G7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M3G7; baseline and differential.
DR Genevisible; Q9M3G7; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA 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; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:DNA damage response; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IMP:UniProtKB.
DR CDD; cd05171; PIKKc_ATM; 1.
DR CDD; cd05162; PWWP; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR038980; ATM_plant.
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; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR044107; PIKKc_ATM.
DR InterPro; IPR000313; PWWP_dom.
DR PANTHER; PTHR37079; SERINE/THREONINE-PROTEIN KINASE ATM; 1.
DR PANTHER; PTHR37079:SF4; SERINE_THREONINE-PROTEIN KINASE ATM; 1.
DR Pfam; PF02259; FAT; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 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.
DR PROSITE; PS50812; PWWP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; DNA damage; DNA-binding; Kinase; Meiosis;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..3856
FT /note="Serine/threonine-protein kinase ATM"
FT /id="PRO_0000088843"
FT DOMAIN 108..162
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT DOMAIN 2727..3393
FT /note="FAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534"
FT DOMAIN 3499..3811
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT DOMAIN 3824..3856
FT /note="FATC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00534,
FT ECO:0000255|PROSITE-ProRule:PRU00535"
FT REGION 648..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3505..3511
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 3678..3686
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 3698..3722
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT MOTIF 3233..3249
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 648..664
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 3640
FT /note="P -> S (in Ref. 1; CAB86487)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3856 AA; 435114 MW; 934D08DC3C67A180 CRC64;
MKLQNPDKKT LREGFSQESS VVALDSGVLA MSGLKCDGKF PVKDVLMEEG GDKVRKIQVS
GGNISLVVDF SGARTSSNNF FESNASCVNE NLVKGNGYRE DETQEFLVGN LVWVMTKYKK
WWPGEVVDFK ADAKESFMVR SIGQSHLVSW FASSKLKPFK ESFEQVLNQR NDNGFFDALQ
KAMSLLSNSL KLDMTCSCIA DGNGIVSAQN ITTRKNKPLI LREFSVDRLE PKEFVTQLKN
IAKCVLNAGV LESTVMQSQL SAFYTLFGHK QIPMAQLHEN EGRKSFTAKM SDSKFIGSPS
ICAGNSRKRF RKEWFRKFVS EVDNVSARDD LVNVPPSDLI SKLKLLAVGY NCSEETENIG
LFEWFFSKFR ISVYHDENAY KMQLANMAGF KDLMLATNAN RGTVQKTLKS KKIGKSKMEP
LNGVSVADTE QKTFELQISK KSNIESLNGV SVADTEQKTF ELQILEKSNI ESLNGVSTPN
IDHEASKSNN SGKTKINHII GHSNFPSSVA KVQLAKDFQD KLLVQAPDRK AMTADTLSRP
AAILVPDLNS GGNALGTAEF DHMQRPETLI QHNVCPQEEK TPRSTILNFQ VTAHQGVSGT
QFVSSQPTSY KHFTSADLFT YSGKKKRGRK RKNAEELPIV AHASATTGIP DLNGTNTEPT
LVLPQVEPTQ RRRRRKKEES PNGLTRGITI LFLKFSSQVS MPSRDDLTST FSAFGPLDSS
ETHVSEEFSG AQVAFVSSAD AIEAVKSLEK ANPFGETLVN FRLQQKLITV QRNIAPRMPV
ISHVSPVPKP NNIPTSMDAM RQNLLMMTAM LEKSGDSLSR ETKAKLKSEI TGLLEKDGVK
LLNTWLEGER SITFCRFLSQ NTAKLKLDEI PNAETWPFLV KLLLQCVSME VSGSKRRMPK
PTFAKTLRVV VQRTEETKFP GVQFPLLSMA KTLFTHVHDI LSNTPSFQSE YGTILRHLLE
IKEYRFQMRK RTYSSLVLLY MERAETGFCE KNSGQHSQKE EAFRYILTLQ SLLENSPGDF
PDDLREEIVN GLIHIFSSVR DEGKLSRKLI ECVNTFLLKD GPNLGSLSLE IHNAVEQFVF
RCWLTTHDKN LKEILVSYGR LQLNLTRDSS ESSSLVEQLL DVVTRELDLG SSSSSASWGD
TTKDEKLGAL SSYQNSLVEL AAHVFYRACV NTSRPSLSEK RARRQHIAMR MVDALTEGKW
LWCAAFGCLV RNYCARINMD LLIYWFEAIC TNFQRLLEDA SMRRSYDGLL WTLRSLQGLS
SGLSLPDITM DISKSSASSS ELDRGWQSIW SSLIHGLATF SSMSVIVDAV LVLLGSIISS
NHITVKILPQ EVWDHQLFRH IPSEPALYFI ACYFSRMGCQ GNLQDDLHLR RNLLRAVCAP
LSWKVRLTLD ERMVQLLPAA AFSLCAGFKV SLPLPKEHLP TPSQWDVCEQ IDDVDRERNF
GLFECSVEAL TRICSNSSKI SGCQVPDVVQ LPLVLRDPLL HDMDIYFLSI IPEVKEKGPL
SDIFMGCALL CHFMHGSYIT RKGKGSSSFF LKACQYLLEG LDHAVESVSK SLNDLQRRGS
LGFGSDFNEK GSIIVSLRSF TQSPVFSNRR DQNLLGASYD FVIHSLENLL RSFAKVYEEY
TEHAWNTHSD TVPSKSLAPD SPEVGRIVDM DLDLAEDTKE RDIIAAGGKA VPGLPVSMGN
WKLGMVSLIS CFSPVLQFPT WDVLYNLLEK ESDPKVLENI LYHLCKLSCL TSIPKVDDLV
IFLDGMLSTQ VKMKRNCLNI VTALHVLLHT LSSSRRDSSG VEKNCGLSLK EAESFQVFVQ
LGAMVNKVSE FGLLGWFGRV KLINCICDLV LLNPQTGQTM IERLLLMLSD SDYRVRFVLA
RQIGILFQTW DGHEALFQDI CSSFGIKLVT SSKEKLVTAK DVLAVGPQPR QKMETVIITL
MHLAYHSENI ELQAVFMMCA VSAKDPCQRE LIIAALDNLS AQLHYPSRFK YLEELLGPIL
FHWIASGVSL AGLIETSQLF IPNAEPKYFI HFCSHWLLPA LLLHEDHTNL DWVAKMAGQP
VVVLVKENFV PIFSICMGLH CSKTSECDKG AMVLQNSILY VGETSENERD KLIKQNMVSI
VSFILSCASS SPEPPVPTFS RDTISLAVQT VVDGFLENTD YPKNAAITDR INIFRPDRVF
MFITEMHYRM SAACHHRHTR HHLAALEELT ILLGHRALVP SSLNYIFNLV GQFIGYPSLQ
DQCCSIASCL LDLFKSNPAK EIVSVLGDQL QFLVSKLVTC CIDAEADTKI SGAKSSQLVN
LLHKLVVSSD SSLNEDIRDL EPLPDLKYFQ VIRESHIRIC EAYSPRNHLL KVEHSTFLIY
IFLEILSLSN FLFLSCSTIQ QCSRRSNYLP PRFLSRSLQA LHNKLIASEV SQEDTNGETA
ETFWQSDDEI VNAVWTLVRV SASDEADSMR LLVSDFLSRI GIRDPHTVVF HLPGNLVSMH
GLQGFGHNTG SKVRSLTENG ISDETLITLL NFLKKYLLDD SVKIIDVTSQ TLRGILSTER
GQQALSSFDS CERALIEVHG RGVNLDIVEK ILLDSQKQFK AEKFSLETPE VWSTDNKNFD
RWICQLVYCM IALCEDVPIR LCQNIALLKA EISELLFPSV VVSLAGRIGM DINLHDLITS
QVKEHIFTDS NKLTKSKQVM LNTLNELRMC YVLERSIFSG QTKREKNSRS CSTAAKIRDV
ESGSNGMAAS ITTNWEKVYW LSIDYLVVAG SAVVCGAYLT ASMYVEYWCE EKFGNLSLGD
PDFSYHDKLP DHVEILVSAI TRINEPDSLY GVIHSNKLSA QIITFEHEGN WTRALEYYDL
QARSQKMVVP SSLSENLEVE QFQPTTSARH SVFGEGEVQR QPFKGLIRSL QQTGCMHVLD
LYCRGLTSRE GCFQYDPEFI ELQYEAAWRA GKWDFSLLYP QTHCQPLQHA KNNNYHESLH
CCLRALQEGD YDGFYGKLKD TKKELVLSIS RASEESTEFI YSTVVKLQIL HHLGLVWDLR
WTTSSHQSVH GYLVKQMACV DPVIPTMDQL SWLNKDWNSI ITQTQLHMTL LEPFIAFRRV
LLQILGCEKC TMQHLLQSAS LLRKGTRFSH AAASLHEFKF LCARSNGQQP VPDWLGKLEE
AKLLHAQGRH EVSISLANYI LHNYQLKEEA SDIYRVIGKW LAETRSSNSR TILEKYLRPA
VSLAEEQSSK ICKRLVDRQS QTWFHLAHYA DALFKSYEER LSSSEWQAAL RLRKHKTKEL
EVFIKRFKSS KKAEQSDYSL KIQDLQKQLT MDKEEAEKLQ VDRDNFLKLA LEGYKRCLEI
GDKYDVRVVF RQVSMWFSLA SQKNVIDNML STIKEVQSYK FIPLVYQIAS RLGSSKDESG
SNSFQSALVS LIRKMAIDHP YHTILQLLAL ANGDRIKDNQ RSRNSFVVDM DKKLAAEHLL
QDVSHYHGPM IRQMKQLVDI YIKLAELETR REDTNRKVAL PREIRSVKQL ELVPVVTATI
PVDRSCQYNE GSFPFFRGLS DSVTVMNGIN APKVVECFGS DGQKYKQLAK SGNDDLRQDA
VMEQFFGLVN TFLHNNRDTW KRRLAVRTYK VIPFTPSAGV LEWVDGTIPL GDYLIGSSRS
EGAHGRYGIG NWKYPKCREH MSSAKDKRKA FVDVCTNFRP VMHYFFLEKF LQPADWFVKR
LAYTRSVAAS SMVGYIVGLG DRHAMNILID QATAEVVHID LGVAFEQGLM LKTPERVPFR
LTRDIIDGMG ITGVEGVFRR CCEETLSVMR TNKEALLTIV EVFIHDPLYK WALSPLKALQ
RQKETEDYDG MNLEGLQEEF EGNKDATRAL MRVKQKLDGY EGGEMRSIHG QAQQLIQDAI
DTDRLSHMFP GWGAWM
//
