ID ODP1_ECOLI Reviewed; 887 AA. AC P0AFG8; P06958; P78049; Q53382; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 04-NOV-2026, entry version 171. DE RecName: Full=Pyruvate dehydrogenase E1 component; DE Short=PDH E1 component; DE EC=1.2.4.1; GN Name=aceE; OrderedLocusNames=b0114, JW0110; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=6343085; DOI=10.1111/j.1432-1033.1983.tb07441.x; RA Stephens P.E., Darlison M.G., Lewis H.M., Guest J.R.; RT "The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide RT sequence encoding the pyruvate dehydrogenase component."; RL Eur. J. Biochem. 133:155-162(1983). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8202364; DOI=10.1093/nar/22.9.1637; RA Fujita N., Mori H., Yura T., Ishihama A.; RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4- RT 4.1 min (110,917-193,643 bp) region."; RL Nucleic Acids Res. 22:1637-1639(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 145 RP AND 275. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23. RC STRAIN=K12; RX PubMed=8262214; DOI=10.1016/0014-5793(93)81605-y; RA Haydon D.J., Quail M.A., Guest J.R.; RT "A mutation causing constitutive synthesis of the pyruvate dehydrogenase RT complex in Escherichia coli is located within the pdhR gene."; RL FEBS Lett. 336:43-47(1993). RN [6] RP PROTEIN SEQUENCE OF 2-13. RC STRAIN=K12 / EMG2; RX PubMed=9298646; DOI=10.1002/elps.1150180807; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded in the RT genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [7] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-716, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076; RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200; RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., RA Grishin N.V., Zhao Y.; RT "Lysine acetylation is a highly abundant and evolutionarily conserved RT modification in Escherichia coli."; RL Mol. Cell. Proteomics 8:215-225(2009). RN [9] RP INTERACTION WITH CEDA. RX PubMed=28818726; DOI=10.1016/j.ijbiomac.2017.08.073; RA Sharma P., Tomar A.K., Kundu B.; RT "Identification of functional interactome of a key cell division regulatory RT protein CedA of E.coli."; RL Int. J. Biol. Macromol. 106:763-767(2018). RN [10] RP X-RAY CRYSTALLOGRAPHY, AND SUBUNIT. RX PubMed=11955070; DOI=10.1021/bi0118557; RA Arjunan P., Nemeria N., Brunskill A., Chandrasekhar K., Sax M., Yan Y., RA Jordan F., Guest J.R., Furey W.; RT "Structure of the pyruvate dehydrogenase multienzyme complex E1 component RT from Escherichia coli at 1.85 A resolution."; RL Biochemistry 41:5213-5221(2002). CC -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that CC catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + pyruvate + H(+) = N(6)- CC [(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein] + CO2; CC Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10478, CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC -!- SUBUNIT: Homodimer (PubMed:11955070). Part of the PDH complex, CC consisting of multiple copies of pyruvate dehydrogenase (E1), CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase CC (E3) (Probable). In pull-down experiments interacts with CedA CC (PubMed:28818726). {ECO:0000269|PubMed:11955070, CC ECO:0000269|PubMed:28818726, ECO:0000305|PubMed:11955070, CC ECO:0000305|PubMed:6343085}. CC -!- INTERACTION: CC P0AFG8; P0AFG8: aceE; NbExp=2; IntAct=EBI-542683, EBI-542683; CC P0AFG8; P0A8N7: epmA; NbExp=2; IntAct=EBI-542683, EBI-562598; CC P0AFG8; P77439: fryA; NbExp=2; IntAct=EBI-542683, EBI-545399; CC P0AFG8; P46889: ftsK; NbExp=2; IntAct=EBI-542683, EBI-550795; CC P0AFG8; P0A6F5: groEL; NbExp=3; IntAct=EBI-542683, EBI-543750; CC P0AFG8; P0AEV9: hycI; NbExp=2; IntAct=EBI-542683, EBI-552628; CC P0AFG8; P0AB83: nth; NbExp=3; IntAct=EBI-542683, EBI-555213; CC P0AFG8; P0AB89: purB; NbExp=2; IntAct=EBI-542683, EBI-556534; CC P0AFG8; P0AG40: ribF; NbExp=2; IntAct=EBI-542683, EBI-542969; CC P0AFG8; P05100: tag; NbExp=2; IntAct=EBI-542683, EBI-558722; CC P0AFG8; P26602: ubiC; NbExp=2; IntAct=EBI-542683, EBI-559360; CC P0AFG8; P0A9U1: ybhF; NbExp=3; IntAct=EBI-542683, EBI-547696; CC P0AFG8; P0A8L7: yciU; NbExp=3; IntAct=EBI-542683, EBI-544511; CC P0AFG8; P76049: ycjY; NbExp=2; IntAct=EBI-542683, EBI-544654; CC P0AFG8; P76170: ynfB; NbExp=2; IntAct=EBI-542683, EBI-544774; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; V01498; CAA24740.1; -; Genomic_DNA. DR EMBL; U00096; AAC73225.1; -; Genomic_DNA. DR EMBL; AP009048; BAB96684.2; -; Genomic_DNA. DR EMBL; S67363; AAB29357.1; -; Genomic_DNA. DR PIR; B64734; DEECPV. DR RefSeq; NP_414656.1; NC_000913.3. DR RefSeq; WP_000003820.1; NZ_CP009789.1. DR PDB; 1L8A; X-ray; 1.85 A; A/B=2-887. DR PDB; 1RP7; X-ray; 2.09 A; A/B=2-887. DR PDB; 2G25; X-ray; 2.10 A; A/B=2-887. DR PDB; 2G28; X-ray; 1.85 A; A/B=2-887. DR PDB; 2G67; X-ray; 2.32 A; A/B=2-887. DR PDB; 2IEA; X-ray; 1.85 A; A/B=2-887. DR PDB; 2QTA; X-ray; 1.85 A; A/B=2-887. DR PDB; 2QTC; X-ray; 1.77 A; A/B=2-887. DR PDB; 9H1N; X-ray; 1.54 A; B/C=2-50. DR AlphaFoldDB; P0AFG8; -. DR MDposit; P0AFG8; -. DR MDRepo; P0AFG8; -. DR SMR; P0AFG8; -. DR BioGRID; 4261303; 40. DR BioGRID; 849234; 3. DR ComplexPortal; CPX-3943; Pyruvate dehydrogenase complex. DR DIP; DIP-9039N; -. DR FunCoup; P0AFG8; 788. DR IntAct; P0AFG8; 104. DR STRING; 511145.b0114; -. DR DrugBank; DB01987; Cocarboxylase. DR DrugBank; DB00152; Thiamine. DR CarbonylDB; P0AFG8; -. DR iPTMnet; P0AFG8; -. DR jPOST; P0AFG8; -. DR PaxDb; 511145-b0114; -. DR EnsemblBacteria; AAC73225; AAC73225; b0114. DR GeneID; 75170013; -. DR GeneID; 75202071; -. DR GeneID; 944834; -. DR KEGG; ecj:JW0110; -. DR KEGG; eco:b0114; -. DR KEGG; ecoc:C3026_00475; -. DR PATRIC; fig|1411691.4.peg.2168; -. DR EchoBASE; EB0023; -. DR eggNOG; COG2609; Bacteria. DR HOGENOM; CLU_009154_2_0_6; -. DR InParanoid; P0AFG8; -. DR OMA; AACDHKG; -. DR OrthoDB; 9759664at2; -. DR PhylomeDB; P0AFG8; -. DR BioCyc; EcoCyc:E1P-MONOMER; -. DR BioCyc; MetaCyc:E1P-MONOMER; -. DR BRENDA; 1.2.1.104; 2026. DR BRENDA; 1.2.4.1; 2026. DR SABIO-RK; P0AFG8; -. DR EvolutionaryTrace; P0AFG8; -. DR PRO; PR:P0AFG8; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P0AFG8; -. DR GO; GO:0005829; C:cytosol; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0045254; C:pyruvate dehydrogenase complex; NAS:ComplexPortal. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0000287; F:magnesium ion binding; IDA:CAFA. DR GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt. DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA. DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC. DR GO; GO:0036094; F:small molecule binding; EXP:DisProt. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IDA:CAFA. DR GO; GO:0042867; P:pyruvate catabolic process; NAS:ComplexPortal. DR CDD; cd02017; TPP_E1_EcPDC_like; 1. DR DisProt; DP00427; -. DR FunFam; 3.40.50.920:FF:000005; Pyruvate dehydrogenase E1 component; 1. DR FunFam; 3.40.50.970:FF:000009; Pyruvate dehydrogenase E1 component; 1. DR FunFam; 3.40.50.970:FF:000011; Pyruvate dehydrogenase E1 component; 1. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 2. DR InterPro; IPR035807; PDC_E1_N. DR InterPro; IPR051157; PDH/Transketolase. DR InterPro; IPR004660; PDH_E1. DR InterPro; IPR041621; PDH_E1_M. DR InterPro; IPR060495; PDH_E1_N. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR InterPro; IPR055152; Transketolase-like_C_2. DR InterPro; IPR005474; Transketolase_N. DR NCBIfam; TIGR00759; aceE; 1. DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1. DR PANTHER; PTHR43825:SF3; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1. DR Pfam; PF17831; PDH_E1_M; 1. DR Pfam; PF28598; PDH_E1_N; 1. DR Pfam; PF22613; Transketolase_C_1; 1. DR Pfam; PF00456; Transketolase_N; 1. DR PIRSF; PIRSF000156; Pyruvate_dh_E1; 1. DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2. DR SUPFAM; SSF52922; TK C-terminal domain-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Magnesium; KW Metal-binding; Oxidoreductase; Pyruvate; Reference proteome; KW Thiamine pyrophosphate. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9298646" FT CHAIN 2..887 FT /note="Pyruvate dehydrogenase E1 component" FT /id="PRO_0000162243" FT BINDING 231 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 261 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT BINDING 263 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT MOD_RES 716 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:18723842" FT CONFLICT 146 FT /note="P -> R (in Ref. 1; CAA24740)" FT /evidence="ECO:0000305" FT CONFLICT 276 FT /note="Missing (in Ref. 1; CAA24740)" FT /evidence="ECO:0000305" FT HELIX 11..28 FT /evidence="ECO:0007829|PDB:9H1N" FT HELIX 30..47 FT /evidence="ECO:0007829|PDB:9H1N" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 69..72 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 76..99 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 109..124 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 126..129 FT /evidence="ECO:0007829|PDB:2IEA" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 142..144 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 145..154 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 160..163 FT /evidence="ECO:0007829|PDB:2QTC" FT TURN 181..183 FT /evidence="ECO:0007829|PDB:2QTC" FT TURN 185..187 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 197..214 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 225..230 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 232..235 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 237..240 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 243..248 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 254..260 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 262..264 FT /evidence="ECO:0007829|PDB:1L8A" FT STRAND 265..269 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 275..285 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 289..293 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 299..305 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 310..317 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 320..326 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 331..337 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 339..341 FT /evidence="ECO:0007829|PDB:1L8A" FT HELIX 343..346 FT /evidence="ECO:0007829|PDB:2QTC" FT TURN 347..351 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 354..358 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 363..365 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 367..379 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 385..390 FT /evidence="ECO:0007829|PDB:2QTC" FT TURN 393..396 FT /evidence="ECO:0007829|PDB:2QTC" FT TURN 398..400 FT /evidence="ECO:0007829|PDB:2QTA" FT TURN 401..403 FT /evidence="ECO:0007829|PDB:2G25" FT HELIX 407..409 FT /evidence="ECO:0007829|PDB:2G25" FT HELIX 416..424 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 431..434 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 447..458 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 479..482 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 483..486 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 495..506 FT /evidence="ECO:0007829|PDB:2QTC" FT TURN 510..515 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 516..522 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 525..527 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 530..536 FT /evidence="ECO:0007829|PDB:2QTC" FT TURN 549..552 FT /evidence="ECO:0007829|PDB:2G25" FT STRAND 553..555 FT /evidence="ECO:0007829|PDB:2G25" FT STRAND 565..567 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 572..583 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 585..588 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 594..600 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 601..603 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 605..617 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 623..628 FT /evidence="ECO:0007829|PDB:2QTC" FT TURN 631..633 FT /evidence="ECO:0007829|PDB:2QTC" FT TURN 635..637 FT /evidence="ECO:0007829|PDB:2QTC" FT TURN 639..641 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 646..650 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 656..659 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 664..679 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 687..691 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 700..703 FT /evidence="ECO:0007829|PDB:2QTC" FT TURN 704..706 FT /evidence="ECO:0007829|PDB:1L8A" FT HELIX 707..712 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 715..720 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 723..731 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 733..735 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 736..750 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 752..758 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 762..778 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 783..787 FT /evidence="ECO:0007829|PDB:2G28" FT HELIX 788..792 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 798..801 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 807..810 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 813..815 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 817..819 FT /evidence="ECO:0007829|PDB:2QTA" FT STRAND 821..824 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 835..841 FT /evidence="ECO:0007829|PDB:2QTC" FT HELIX 846..860 FT /evidence="ECO:0007829|PDB:2QTC" FT STRAND 861..863 FT /evidence="ECO:0007829|PDB:2G67" FT HELIX 865..874 FT /evidence="ECO:0007829|PDB:2QTC" FT TURN 884..886 FT /evidence="ECO:0007829|PDB:2QTC" SQ SEQUENCE 887 AA; 99668 MW; 7FB3811DE11BDD02 CRC64; MSERFPNDVD PIETRDWLQA IESVIREEGV ERAQYLIDQL LAEARKGGVN VAAGTGISNY INTIPVEEQP EYPGNLELER RIRSAIRWNA IMTVLRASKK DLELGGHMAS FQSSATIYDV CFNHFFRARN EQDGGDLVYF QGHISPGVYA RAFLEGRLTQ EQLDNFRQEV HGNGLSSYPH PKLMPEFWQF PTVSMGLGPI GAIYQAKFLK YLEHRGLKDT SKQTVYAFLG DGEMDEPESK GAITIATREK LDNLVFVINC NLQRLDGPVT GNGKIINELE GIFEGAGWNV IKVMWGSRWD ELLRKDTSGK LIQLMNETVD GDYQTFKSKD GAYVREHFFG KYPETAALVA DWTDEQIWAL NRGGHDPKKI YAAFKKAQET KGKATVILAH TIKGYGMGDA AEGKNIAHQV KKMNMDGVRH IRDRFNVPVS DADIEKLPYI TFPEGSEEHT YLHAQRQKLH GYLPSRQPNF TEKLELPSLQ DFGALLEEQS KEISTTIAFV RALNVMLKNK SIKDRLVPII ADEARTFGME GLFRQIGIYS PNGQQYTPQD REQVAYYKED EKGQILQEGI NELGAGCSWL AAATSYSTNN LPMIPFYIYY SMFGFQRIGD LCWAAGDQQA RGFLIGGTSG RTTLNGEGLQ HEDGHSHIQS LTIPNCISYD PAYAYEVAVI MHDGLERMYG EKQENVYYYI TTLNENYHMP AMPEGAEEGI RKGIYKLETI EGSKGKVQLL GSGSILRHVR EAAEILAKDY GVGSDVYSVT SFTELARDGQ DCERWNMLHP LETPRVPYIA QVMNDAPAVA STDYMKLFAE QVRTYVPADD YRVLGTDGFG RSDSRENLRH HFEVDASYVV VAALGELAKR GEIDKKVVAD AIAKFNIDAD KVNPRLA //