AKT1_CAEEL
ID AKT1_CAEEL Reviewed; 541 AA.
AC Q17941; Q17942; Q8MQE0;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Serine/threonine-protein kinase akt-1;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase B akt-1;
DE Short=PKB akt-1;
GN Name=akt-1 {ECO:0000312|WormBase:C12D8.10a};
GN ORFNames=C12D8.10 {ECO:0000312|WormBase:C12D8.10a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, MUTAGENESIS OF
RP ALA-183, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9716402; DOI=10.1101/gad.12.16.2488;
RA Paradis S., Ruvkun G.;
RT "Caenorhabditis elegans Akt/PKB transduces insulin receptor-like signals
RT from AGE-1 PI3 kinase to the DAF-16 transcription factor.";
RL Genes Dev. 12:2488-2498(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=10364160; DOI=10.1101/gad.13.11.1438;
RA Paradis S., Ailion M., Toker A., Thomas J.H., Ruvkun G.;
RT "A PDK1 homolog is necessary and sufficient to transduce AGE-1 PI3 kinase
RT signals that regulate diapause in Caenorhabditis elegans.";
RL Genes Dev. 13:1438-1452(1999).
RN [4]
RP FUNCTION.
RX PubMed=11747825; DOI=10.1016/s0960-9822(01)00594-2;
RA Henderson S.T., Johnson T.E.;
RT "daf-16 integrates developmental and environmental inputs to mediate aging
RT in the nematode Caenorhabditis elegans.";
RL Curr. Biol. 11:1975-1980(2001).
RN [5]
RP FUNCTION.
RX PubMed=11381260; DOI=10.1038/88850;
RA Lin K., Hsin H., Libina N., Kenyon C.;
RT "Regulation of the Caenorhabditis elegans longevity protein DAF-16 by
RT insulin/IGF-1 and germline signaling.";
RL Nat. Genet. 28:139-145(2001).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH PDK-1; SGK-1; AKT-2 AND
RP DAF-16, AND DISRUPTION PHENOTYPE.
RX PubMed=15068796; DOI=10.1016/s1534-5807(04)00095-4;
RA Hertweck M., Goebel C., Baumeister R.;
RT "C. elegans SGK-1 is the critical component in the Akt/PKB kinase complex
RT to control stress response and life span.";
RL Dev. Cell 6:577-588(2004).
RN [7]
RP FUNCTION.
RX PubMed=16950159; DOI=10.1016/j.neuron.2006.07.024;
RA Tomioka M., Adachi T., Suzuki H., Kunitomo H., Schafer W.R., Iino Y.;
RT "The insulin/PI 3-kinase pathway regulates salt chemotaxis learning in
RT Caenorhabditis elegans.";
RL Neuron 51:613-625(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18782349; DOI=10.1111/j.1474-9726.2008.00435.x;
RA Evans E.A., Chen W.C., Tan M.-W.;
RT "The DAF-2 insulin-like signaling pathway independently regulates aging and
RT immunity in C. elegans.";
RL Aging Cell 7:879-893(2008).
RN [9]
RP FUNCTION.
RX PubMed=18358814; DOI=10.1016/j.cell.2008.01.030;
RA Tullet J.M., Hertweck M., An J.H., Baker J., Hwang J.Y., Liu S.,
RA Oliveira R.P., Baumeister R., Blackwell T.K.;
RT "Direct inhibition of the longevity-promoting factor SKN-1 by insulin-like
RT signaling in C. elegans.";
RL Cell 132:1025-1038(2008).
RN [10]
RP INTERACTION WITH CMD-1.
RX PubMed=17854888; DOI=10.1016/j.ceca.2007.07.008;
RA Shen X., Valencia C.A., Gao W., Cotten S.W., Dong B., Huang B.C., Liu R.;
RT "Ca(2+)/Calmodulin-binding proteins from the C. elegans proteome.";
RL Cell Calcium 43:444-456(2008).
RN [11]
RP INTERACTION WITH PPTR-1, TISSUE SPECIFICITY, AND PHOSPHORYLATION AT THR-350
RP AND SER-517.
RX PubMed=19249087; DOI=10.1016/j.cell.2009.01.025;
RA Padmanabhan S., Mukhopadhyay A., Narasimhan S.D., Tesz G., Czech M.P.,
RA Tissenbaum H.A.;
RT "A PP2A regulatory subunit regulates C. elegans insulin/IGF-1 signaling by
RT modulating AKT-1 phosphorylation.";
RL Cell 136:939-951(2009).
RN [12]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF ALA-183 AND LYS-222.
RX PubMed=25383666; DOI=10.1038/nsmb.2915;
RA Nakagawa A., Sullivan K.D., Xue D.;
RT "Caspase-activated phosphoinositide binding by CNT-1 promotes apoptosis by
RT inhibiting the AKT pathway.";
RL Nat. Struct. Mol. Biol. 21:1082-1090(2014).
RN [13]
RP FUNCTION.
RX PubMed=30779740; DOI=10.1371/journal.pgen.1007945;
RA Peymen K., Watteyne J., Borghgraef C., Van Sinay E., Beets I., Schoofs L.;
RT "Myoinhibitory peptide signaling modulates aversive gustatory learning in
RT Caenorhabditis elegans.";
RL PLoS Genet. 15:E1007945-E1007945(2019).
CC -!- FUNCTION: Acts downstream of PI3 kinase age-1 and kinase pdk-1 in the
CC daf-2/insulin receptor-like transduction pathway. Phosphorylates
CC Forkhead-related daf-16 and the longevity-promoting skn-1 transcription
CC factors, which inhibits their entry into the nucleus and antagonizes
CC their functions (PubMed:9716402, PubMed:11747825, PubMed:11381260,
CC PubMed:15068796, PubMed:18358814). Has an essential role in regulating
CC developmental arrest at the dauer stage (PubMed:10364160). Plays a role
CC in immune function and pathogen resistance (PubMed:18782349). Regulates
CC salt chemotaxis learning (PubMed:16950159, PubMed:30779740). Downstream
CC of age-1 and together with akt-2 and sgk-1, promotes cell survival
CC during embryonic development (PubMed:25383666).
CC {ECO:0000269|PubMed:10364160, ECO:0000269|PubMed:11381260,
CC ECO:0000269|PubMed:11747825, ECO:0000269|PubMed:15068796,
CC ECO:0000269|PubMed:16950159, ECO:0000269|PubMed:18358814,
CC ECO:0000269|PubMed:18782349, ECO:0000269|PubMed:25383666,
CC ECO:0000269|PubMed:30779740, ECO:0000269|PubMed:9716402}.
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=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Phosphorylated and activated by pdk-1.
CC {ECO:0000269|PubMed:15068796}.
CC -!- SUBUNIT: Interacts with pdk-1, sgk-1, akt-2 and daf-16
CC (PubMed:15068796). Part of a complex containing sgk-1, akt-1 and akt-2
CC (PubMed:15068796). Interacts with cmd-1 in the presence of Ca(2+)
CC (PubMed:17854888). Interacts with let-92 phosphatase regulatory subunit
CC pptr-1 (PubMed:19249087). {ECO:0000269|PubMed:15068796,
CC ECO:0000269|PubMed:17854888, ECO:0000269|PubMed:19249087}.
CC -!- INTERACTION:
CC Q17941; Q9XTG7: akt-2; NbExp=2; IntAct=EBI-1770718, EBI-320656;
CC Q17941; O16850: daf-16; NbExp=3; IntAct=EBI-1770718, EBI-324028;
CC Q17941; G5EFM0: mdf-1; NbExp=2; IntAct=EBI-1770718, EBI-316684;
CC Q17941; O18178: pptr-1; NbExp=3; IntAct=EBI-1770718, EBI-2298122;
CC Q17941; Q2PJ68: sgk-1; NbExp=3; IntAct=EBI-1770718, EBI-1770776;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:C12D8.10a};
CC IsoId=Q17941-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C12D8.10b};
CC IsoId=Q17941-2; Sequence=VSP_017044, VSP_017045, VSP_017046;
CC Name=c {ECO:0000312|WormBase:C12D8.10c};
CC IsoId=Q17941-3; Sequence=VSP_038163;
CC -!- TISSUE SPECIFICITY: Expressed in neurons, muscle cells of the pharynx,
CC rectal gland cells, vulva and spermatheca.
CC {ECO:0000269|PubMed:19249087, ECO:0000269|PubMed:9716402}.
CC -!- DEVELOPMENTAL STAGE: Expressed in late stage embryos and throughout
CC life. {ECO:0000269|PubMed:9716402}.
CC -!- DOMAIN: The PH domain binds to phosphatidylinositol 3,4,5-trisphosphate
CC (PtdIns(3,4,5)P3) resulting in its targeting to the plasma membrane.
CC {ECO:0000269|PubMed:25383666}.
CC -!- DISRUPTION PHENOTYPE: Increased resistance to pathogens. Simultaneous
CC knockdown of akt-1 and akt-2 result in dauer formation and a weak
CC extension to life span. {ECO:0000269|PubMed:15068796,
CC ECO:0000269|PubMed:18782349}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. RAC subfamily. {ECO:0000305}.
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DR EMBL; AF072379; AAC62466.1; -; mRNA.
DR EMBL; AF072380; AAC62467.1; -; mRNA.
DR EMBL; BX284605; CAA98238.1; -; Genomic_DNA.
DR EMBL; BX284605; CAA98240.1; -; Genomic_DNA.
DR EMBL; BX284605; CAD44085.1; -; Genomic_DNA.
DR PIR; T43232; T43232.
DR PIR; T43233; T43233.
DR RefSeq; NP_001023645.1; NM_001028474.4. [Q17941-1]
DR RefSeq; NP_001023646.1; NM_001028475.2. [Q17941-2]
DR RefSeq; NP_001023647.1; NM_001028476.3. [Q17941-3]
DR AlphaFoldDB; Q17941; -.
DR SMR; Q17941; -.
DR BioGRID; 44454; 13.
DR ComplexPortal; CPX-1129; Atk-1/Akt-2/Sgk-1 protein kinase complex.
DR IntAct; Q17941; 9.
DR MINT; Q17941; -.
DR STRING; 6239.C12D8.10b; -.
DR iPTMnet; Q17941; -.
DR EPD; Q17941; -.
DR PaxDb; Q17941; -.
DR PeptideAtlas; Q17941; -.
DR EnsemblMetazoa; C12D8.10a.1; C12D8.10a.1; WBGene00000102. [Q17941-1]
DR EnsemblMetazoa; C12D8.10b.1; C12D8.10b.1; WBGene00000102. [Q17941-2]
DR EnsemblMetazoa; C12D8.10c.1; C12D8.10c.1; WBGene00000102. [Q17941-3]
DR GeneID; 179424; -.
DR KEGG; cel:CELE_C12D8.10; -.
DR UCSC; C12D8.10b.1; c. elegans. [Q17941-1]
DR CTD; 179424; -.
DR WormBase; C12D8.10a; CE15612; WBGene00000102; akt-1. [Q17941-1]
DR WormBase; C12D8.10b; CE05274; WBGene00000102; akt-1. [Q17941-2]
DR WormBase; C12D8.10c; CE31304; WBGene00000102; akt-1. [Q17941-3]
DR eggNOG; KOG0690; Eukaryota.
DR GeneTree; ENSGT00940000168810; -.
DR InParanoid; Q17941; -.
DR OMA; CIDNERR; -.
DR OrthoDB; 614710at2759; -.
DR PhylomeDB; Q17941; -.
DR Reactome; R-CEL-1257604; PIP3 activates AKT signaling.
DR Reactome; R-CEL-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-CEL-165158; Activation of AKT2.
DR Reactome; R-CEL-165159; MTOR signalling.
DR Reactome; R-CEL-198323; AKT phosphorylates targets in the cytosol.
DR Reactome; R-CEL-198693; AKT phosphorylates targets in the nucleus.
DR Reactome; R-CEL-199418; Negative regulation of the PI3K/AKT network.
DR Reactome; R-CEL-203615; eNOS activation.
DR Reactome; R-CEL-211163; AKT-mediated inactivation of FOXO1A.
DR Reactome; R-CEL-354192; Integrin signaling.
DR Reactome; R-CEL-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-CEL-389513; CTLA4 inhibitory signaling.
DR Reactome; R-CEL-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-CEL-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-CEL-450604; KSRP (KHSRP) binds and destabilizes mRNA.
DR Reactome; R-CEL-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-CEL-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-CEL-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-CEL-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-CEL-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR Reactome; R-CEL-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-CEL-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-CEL-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-CEL-9607240; FLT3 Signaling.
DR Reactome; R-CEL-9614399; Regulation of localization of FOXO transcription factors.
DR Reactome; R-CEL-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR Reactome; R-CEL-9755511; KEAP1-NFE2L2 pathway.
DR SignaLink; Q17941; -.
DR PRO; PR:Q17941; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00000102; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:1902911; C:protein kinase complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:WormBase.
DR GO; GO:0004672; F:protein kinase activity; IDA:WormBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:WormBase.
DR GO; GO:0007635; P:chemosensory behavior; IGI:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IGI:UniProtKB.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IMP:WormBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:CACAO.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:WormBase.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
DR GO; GO:0010468; P:regulation of gene expression; IDA:ComplexPortal.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IGI:UniProtKB.
DR GO; GO:1902074; P:response to salt; IGI:UniProtKB.
DR CDD; cd01241; PH_PKB; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039026; PH_PKB.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Calmodulin-binding;
KW Developmental protein; Immunity; Innate immunity; Kinase; Lipid-binding;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..541
FT /note="Serine/threonine-protein kinase akt-1"
FT /id="PRO_0000085615"
FT DOMAIN 15..118
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 193..450
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 451..528
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ACT_SITE 316
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 199..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 350
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19249087"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19249087"
FT VAR_SEQ 255..541
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_038163"
FT VAR_SEQ 262..287
FT /note="EQHYLCFVMQFANGGELFTHVRKCGT -> TNDRLCFVMEFAIGGDLYYHLN
FT REVQMNKEG (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9716402"
FT /id="VSP_017044"
FT VAR_SEQ 298
FT /note="A -> S (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9716402"
FT /id="VSP_017045"
FT VAR_SEQ 309..317
FT /note="RCDIVYRDM -> ANSIVYRDL (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9716402"
FT /id="VSP_017046"
FT MUTAGEN 183
FT /note="A->T: In mg144; causes a delay in apoptosis during
FT embryonic development. Suppresses the dauer arrest
FT phenotype of the age-1(mg44) null mutant."
FT /evidence="ECO:0000269|PubMed:25383666,
FT ECO:0000269|PubMed:9716402"
FT MUTAGEN 222
FT /note="K->M: Probable loss of kinase activity. Increased
FT apoptosis during embryonic development in an akt-2 tm1075
FT mutant background."
FT /evidence="ECO:0000269|PubMed:25383666"
SQ SEQUENCE 541 AA; 62200 MW; 17FEDD1109926950 CRC64;
MSMTSLSTKS RRQEDVVIEG WLHKKGEHIR NWRPRYFMIF NDGALLGFRA KPKEGQPFPE
PLNDFMIKDA ATMLFEKPRP NMFMVRCLQW TTVIERTFYA ESAEVRQRWI HAIESISKKY
KGTNANPQEE LMETNQQPKI DEDSEFAGAA HAIMGQPSSG HGDNCSIDFR ASMISIADTS
EAAKRDKITM EDFDFLKVLG KGTFGKVILC KEKRTQKLYA IKILKKDVII AREEVAHTLT
ENRVLQRCKH PFLTELKYSF QEQHYLCFVM QFANGGELFT HVRKCGTFSE PRARFYGAEI
VLALGYLHRC DIVYRDMKLE NLLLDKDGHI KIADFGLCKE EISFGDKTST FCGTPEYLAP
EVLDDHDYGR CVDWWGVGVV MYEMMCGRLP FYSKDHNKLF ELIMAGDLRF PSKLSQEART
LLTGLLVKDP TQRLGGGPED ALEICRADFF RTVDWEATYR KEIEPPYKPN VQSETDTSYF
DNEFTSQPVQ LTPPSRSGAL ATVDEQEEMQ SNFTQFSFHN VMGSINRIHE ASEDNEDYDM
G
