ID MLS1_YEAST Reviewed; 554 AA. AC P30952; B0KZR8; B0KZS7; B0KZU5; B0KZY1; B0L026; D6W165; Q4KQ64; Q4KQ91; AC Q4KQC3; Q4KQC4; Q4KQC8; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 27-MAR-2024, entry version 181. DE RecName: Full=Malate synthase 1 {ECO:0000303|PubMed:1454530}; DE EC=2.3.3.9 {ECO:0000250|UniProtKB:Q9LZC3}; GN Name=MLS1 {ECO:0000303|PubMed:1454530}; OrderedLocusNames=YNL117W; GN ORFNames=N1921; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION RP PHENOTYPE. RX PubMed=1454530; DOI=10.1093/nar/20.21.5677; RA Hartig A., Simon M.M., Schuster T., Daugherty J.R., Yoo H.S., Cooper T.G.; RT "Differentially regulated malate synthase genes participate in carbon and RT nitrogen metabolism of S. cerevisiae."; RL Nucleic Acids Res. 20:5677-5686(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-217; SER-253; ASP-310 RP AND VAL-541. RC STRAIN=ATCC 200060 / W303, S103, SK1, V1-09, YJM 1129, YJM 269, YJM RC 270, YJM 320, YJM 326, YJM 339, YJM 627, and YJM230; RX PubMed=18780730; DOI=10.1534/genetics.108.092932; RA Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S., RA Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H., RA Steinmetz L.M.; RT "Sequential elimination of major-effect contributors identifies additional RT quantitative trait loci conditioning high-temperature growth in yeast."; RL Genetics 180:1661-1670(2008). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9090055; RX DOI=10.1002/(sici)1097-0061(19970315)13:3<261::aid-yea64>3.0.co;2-l; RA de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D., RA Pallavicini A., Lanfranchi G., Valle G.; RT "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces RT cerevisiae reveals an unusually high number of overlapping open reading RT frames."; RL Yeast 13:261-266(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169873; RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F., RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its RT evolutionary implications."; RL Nature 387:93-98(1997). RN [5] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-282, AND VARIANTS THR-118; VAL-199 RP AND SER-253. RC STRAIN=AKU-4011, ATCC 204508 / S288c, ATCC 9804 / CBS 400 / DSM 70478 RC / IFO 0210 / JCM 2220, Awamori-1, Cote des blancs, I14, K1, K10, K5, RC K9, Lalvin 71B, Lalvin BM45, Lalvin CY-3079, Levuline ALS, M1, M11, RC M12, M13, M15, M17, M19, M2, M20, M21, M24, M29, M3, M30, M31, M32, RC M33, M34, M4, M5, M6, M7, M8, M9, NRIC 1413, NRIC 1685, NRIC 23, NRRL RC Y-1438, NRRL Y-1532, NRRL Y-1546, NRRL Y-2411, NRRL Y-390, NRRL RC Y-5997, NRRL Y-7567, NRRL YB-1952, Pasteur Red, UCD 175, UCD 2120, UCD RC 529, UCD 612, UCD 762, UCD 765, UCD 781, UCD 820, UCD51, YJM 145, YJM RC 269, YJM 270, YJM 280, YJM 320, YJM 326, YJM 339, YJM 421, YJM 627, RC YJM1129 YPS163, YJM308, YJM434, YJM436, YJM440, YJM454, YPS1000, RC YPS1009, Zymaflore F15, and Zymaflore VL3; RX PubMed=16103919; DOI=10.1371/journal.pgen.0010005; RA Fay J.C., Benavides J.A.; RT "Evidence for domesticated and wild populations of Saccharomyces RT cerevisiae."; RL PLoS Genet. 1:66-71(2005). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF 552-SER--LEU-554, RP AND DISRUPTION PHENOTYPE. RX PubMed=11846793; DOI=10.1046/j.0014-2956.2001.02727.x; RA Kunze M., Kragler F., Binder M., Hartig A., Gurvitz A.; RT "Targeting of malate synthase 1 to the peroxisomes of Saccharomyces RT cerevisiae cells depends on growth on oleic acid medium."; RL Eur. J. Biochem. 269:915-922(2002). RN [8] RP INTERACTION WITH PEX9, AND SUBCELLULAR LOCATION. RX PubMed=27678487; DOI=10.1242/jcs.195271; RA Effelsberg D., Cruz-Zaragoza L.D., Schliebs W., Erdmann R.; RT "Pex9p is a new yeast peroxisomal import receptor for PTS1-containing RT proteins."; RL J. Cell Sci. 129:4057-4066(2016). CC -!- FUNCTION: Malate synthase which takes part in the glyoxylate cycle CC (PubMed:1454530). MLS1 activity is essential for cells to grow on oleic CC acid as a sole carbon source (PubMed:11846793). Two steps of the CC glyoxylate cycle take place in the cytosol, the splitting of isocitrate CC into succinate and glyoxylate, and the dehydrogenation of malate to CC oxaloacetate (PubMed:1454530). However, the formation of malate from CC glyoxylate and acetyl-CoA undertaken MLS1, occurs in the peroxisomes CC when cells are grown on oleic acid (Probable). The source of acetyl-CoA CC being either peroxisomal when breaking down fatty acids, or cytosolic CC when extra-cellular two-carbon substrates are used, therefore, although CC not strictly essential, the peroxisomal localization of MLS1 appears to CC be advantageous for cells growing on oleic acid, in that acetyl-CoA CC production and utilization are thereby intimately compartmentalized CC together to increase efficiency (Probable). CC {ECO:0000269|PubMed:11846793, ECO:0000269|PubMed:1454530, CC ECO:0000305|PubMed:1454530}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); CC Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288; EC=2.3.3.9; CC Evidence={ECO:0000250|UniProtKB:Q9LZC3}; CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from CC isocitrate: step 2/2. {ECO:0000250|UniProtKB:Q9LZC3}. CC -!- SUBUNIT: Interacts with PEX9. {ECO:0000269|PubMed:27678487}. CC -!- INTERACTION: CC P30952; P33203: PRP40; NbExp=2; IntAct=EBI-10428, EBI-701; CC P30952; P39940: RSP5; NbExp=3; IntAct=EBI-10428, EBI-16219; CC -!- SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:11846793, CC ECO:0000269|PubMed:27678487}. Note=Imported in peroxisome via CC recognition by the peroxisomal targeting signal receptor PEX9 in an CC oleate-dependent manner. {ECO:0000269|PubMed:27678487}. CC -!- INDUCTION: Expression is sensitive to carbon catabolite repression, but CC nearly insensitive to nitrogen catabolite repression. CC {ECO:0000269|PubMed:1454530}. CC -!- DISRUPTION PHENOTYPE: Strongly decreases the growth rate on ethanol or CC acetate medium. {ECO:0000269|PubMed:11846793, CC ECO:0000269|PubMed:1454530}. CC -!- SIMILARITY: Belongs to the malate synthase family. {ECO:0000305}. 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; X64407; CAA45750.1; -; Genomic_DNA. DR EMBL; EF125216; ABN58540.1; -; Genomic_DNA. DR EMBL; EF125217; ABN58549.1; -; Genomic_DNA. DR EMBL; EF125218; ABN58558.1; -; Genomic_DNA. DR EMBL; EF125219; ABN58567.1; -; Genomic_DNA. DR EMBL; EF125220; ABN58575.1; -; Genomic_DNA. DR EMBL; EF125221; ABN58585.1; -; Genomic_DNA. DR EMBL; EF125222; ABN58594.1; -; Genomic_DNA. DR EMBL; EF125223; ABN58603.1; -; Genomic_DNA. DR EMBL; EF125224; ABN58612.1; -; Genomic_DNA. DR EMBL; EF125225; ABN58621.1; -; Genomic_DNA. DR EMBL; EF125226; ABN58630.1; -; Genomic_DNA. DR EMBL; EF125228; ABN58648.1; -; Genomic_DNA. DR EMBL; Z69382; CAA93390.1; -; Genomic_DNA. DR EMBL; Z71393; CAA95997.1; -; Genomic_DNA. DR EMBL; AY942279; AAY22671.1; -; Genomic_DNA. DR EMBL; AY942280; AAY22672.1; -; Genomic_DNA. DR EMBL; AY942281; AAY22673.1; -; Genomic_DNA. DR EMBL; AY942282; AAY22674.1; -; Genomic_DNA. DR EMBL; AY942283; AAY22675.1; -; Genomic_DNA. DR EMBL; AY942284; AAY22676.1; -; Genomic_DNA. DR EMBL; AY942285; AAY22677.1; -; Genomic_DNA. DR EMBL; AY942286; AAY22678.1; -; Genomic_DNA. DR EMBL; AY942287; AAY22679.1; -; Genomic_DNA. DR EMBL; AY942288; AAY22680.1; -; Genomic_DNA. DR EMBL; AY942289; AAY22681.1; -; Genomic_DNA. DR EMBL; AY942290; AAY22682.1; -; Genomic_DNA. DR EMBL; AY942291; AAY22683.1; -; Genomic_DNA. DR EMBL; AY942292; AAY22684.1; -; Genomic_DNA. DR EMBL; AY942293; AAY22685.1; -; Genomic_DNA. DR EMBL; AY942294; AAY22686.1; -; Genomic_DNA. DR EMBL; AY942295; AAY22687.1; -; Genomic_DNA. DR EMBL; AY942296; AAY22688.1; -; Genomic_DNA. DR EMBL; AY942297; AAY22689.1; -; Genomic_DNA. DR EMBL; AY942298; AAY22690.1; -; Genomic_DNA. DR EMBL; AY942299; AAY22691.1; -; Genomic_DNA. DR EMBL; AY942300; AAY22692.1; -; Genomic_DNA. DR EMBL; AY942301; AAY22693.1; -; Genomic_DNA. DR EMBL; AY942302; AAY22694.1; -; Genomic_DNA. DR EMBL; AY942303; AAY22695.1; -; Genomic_DNA. DR EMBL; AY942304; AAY22696.1; -; Genomic_DNA. DR EMBL; AY942305; AAY22697.1; -; Genomic_DNA. DR EMBL; AY942306; AAY22698.1; -; Genomic_DNA. DR EMBL; AY942307; AAY22699.1; -; Genomic_DNA. DR EMBL; AY942308; AAY22700.1; -; Genomic_DNA. DR EMBL; AY942309; AAY22701.1; -; Genomic_DNA. DR EMBL; AY942310; AAY22702.1; -; Genomic_DNA. DR EMBL; AY942311; AAY22703.1; -; Genomic_DNA. DR EMBL; AY942312; AAY22704.1; -; Genomic_DNA. DR EMBL; AY942313; AAY22705.1; -; Genomic_DNA. DR EMBL; AY942314; AAY22706.1; -; Genomic_DNA. DR EMBL; AY942315; AAY22707.1; -; Genomic_DNA. DR EMBL; AY942316; AAY22708.1; -; Genomic_DNA. DR EMBL; AY942317; AAY22709.1; -; Genomic_DNA. DR EMBL; AY942318; AAY22710.1; -; Genomic_DNA. DR EMBL; AY942319; AAY22711.1; -; Genomic_DNA. DR EMBL; AY942320; AAY22712.1; -; Genomic_DNA. DR EMBL; AY942321; AAY22713.1; -; Genomic_DNA. DR EMBL; AY942322; AAY22714.1; -; Genomic_DNA. DR EMBL; AY942323; AAY22715.1; -; Genomic_DNA. DR EMBL; AY942324; AAY22716.1; -; Genomic_DNA. DR EMBL; AY942325; AAY22717.1; -; Genomic_DNA. DR EMBL; AY942326; AAY22718.1; -; Genomic_DNA. DR EMBL; AY942327; AAY22719.1; -; Genomic_DNA. DR EMBL; AY942328; AAY22720.1; -; Genomic_DNA. DR EMBL; AY942329; AAY22721.1; -; Genomic_DNA. DR EMBL; AY942330; AAY22722.1; -; Genomic_DNA. DR EMBL; AY942331; AAY22723.1; -; Genomic_DNA. DR EMBL; AY942332; AAY22724.1; -; Genomic_DNA. DR EMBL; AY942333; AAY22725.1; -; Genomic_DNA. DR EMBL; AY942334; AAY22726.1; -; Genomic_DNA. DR EMBL; AY942335; AAY22727.1; -; Genomic_DNA. DR EMBL; AY942336; AAY22728.1; -; Genomic_DNA. DR EMBL; AY942337; AAY22729.1; -; Genomic_DNA. DR EMBL; AY942338; AAY22730.1; -; Genomic_DNA. DR EMBL; AY942339; AAY22731.1; -; Genomic_DNA. DR EMBL; AY942340; AAY22732.1; -; Genomic_DNA. DR EMBL; AY942341; AAY22733.1; -; Genomic_DNA. DR EMBL; AY942342; AAY22734.1; -; Genomic_DNA. DR EMBL; AY942343; AAY22735.1; -; Genomic_DNA. DR EMBL; AY942344; AAY22736.1; -; Genomic_DNA. DR EMBL; AY942345; AAY22737.1; -; Genomic_DNA. DR EMBL; AY942346; AAY22738.1; -; Genomic_DNA. DR EMBL; AY942347; AAY22739.1; -; Genomic_DNA. DR EMBL; AY942348; AAY22740.1; -; Genomic_DNA. DR EMBL; AY942349; AAY22741.1; -; Genomic_DNA. DR EMBL; AY942350; AAY22742.1; -; Genomic_DNA. DR EMBL; AY942351; AAY22743.1; -; Genomic_DNA. DR EMBL; AY942352; AAY22744.1; -; Genomic_DNA. DR EMBL; AY942353; AAY22745.1; -; Genomic_DNA. DR EMBL; AY942354; AAY22746.1; -; Genomic_DNA. DR EMBL; AY942355; AAY22747.1; -; Genomic_DNA. DR EMBL; BK006947; DAA10431.1; -; Genomic_DNA. DR PIR; S26645; S26645. DR RefSeq; NP_014282.1; NM_001182955.1. DR AlphaFoldDB; P30952; -. DR SMR; P30952; -. DR BioGRID; 35709; 90. DR IntAct; P30952; 9. DR STRING; 4932.YNL117W; -. DR MaxQB; P30952; -. DR PaxDb; 4932-YNL117W; -. DR PeptideAtlas; P30952; -. DR TopDownProteomics; P30952; -. DR EnsemblFungi; YNL117W_mRNA; YNL117W; YNL117W. DR GeneID; 855606; -. DR KEGG; sce:YNL117W; -. DR AGR; SGD:S000005061; -. DR SGD; S000005061; MLS1. DR VEuPathDB; FungiDB:YNL117W; -. DR eggNOG; KOG1261; Eukaryota. DR GeneTree; ENSGT00940000174673; -. DR HOGENOM; CLU_018928_3_0_1; -. DR InParanoid; P30952; -. DR OMA; DGSWIAH; -. DR OrthoDB; 177378at2759; -. DR BioCyc; MetaCyc:YNL117W-MONOMER; -. DR BioCyc; YEAST:YNL117W-MONOMER; -. DR UniPathway; UPA00703; UER00720. DR BioGRID-ORCS; 855606; 0 hits in 10 CRISPR screens. DR PRO; PR:P30952; -. DR Proteomes; UP000002311; Chromosome XIV. DR RNAct; P30952; Protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0005782; C:peroxisomal matrix; IDA:SGD. DR GO; GO:0005777; C:peroxisome; IDA:SGD. DR GO; GO:0004474; F:malate synthase activity; IMP:SGD. DR GO; GO:0006097; P:glyoxylate cycle; IMP:SGD. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR CDD; cd00727; malate_synt_A; 1. DR Gene3D; 3.20.20.360; Malate synthase, domain 3; 1. DR Gene3D; 1.20.1220.12; Malate synthase, domain III; 1. DR InterPro; IPR044856; Malate_synth_C_sf. DR InterPro; IPR011076; Malate_synth_sf. DR InterPro; IPR006252; Malate_synthA. DR InterPro; IPR019830; Malate_synthase_CS. DR InterPro; IPR001465; Malate_synthase_TIM. DR InterPro; IPR048355; MS_C. DR InterPro; IPR048356; MS_N. DR InterPro; IPR046363; MS_N_TIM-barrel_dom. DR NCBIfam; TIGR01344; malate_syn_A; 1. DR PANTHER; PTHR42902; MALATE SYNTHASE; 1. DR PANTHER; PTHR42902:SF1; MALATE SYNTHASE 1-RELATED; 1. DR Pfam; PF20659; MS_C; 1. DR Pfam; PF20656; MS_N; 1. DR Pfam; PF01274; MS_TIM-barrel; 1. DR PIRSF; PIRSF001363; Malate_synth; 1. DR SUPFAM; SSF51645; Malate synthase G; 1. DR PROSITE; PS00510; MALATE_SYNTHASE; 1. PE 1: Evidence at protein level; KW Glyoxylate bypass; Peroxisome; Reference proteome; Transferase; KW Tricarboxylic acid cycle. FT CHAIN 1..554 FT /note="Malate synthase 1" FT /id="PRO_0000166864" FT MOTIF 552..554 FT /note="SKL peroxisome targeting motif" FT /evidence="ECO:0000269|PubMed:11846793" FT ACT_SITE 177 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:Q9LZC3" FT ACT_SITE 457 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q9LZC3" FT VARIANT 118 FT /note="A -> T (in strain: Awamori-1, AKU-4011, K1, K5, NRIC FT 23, NRIC 1413 and NRIC 1685)" FT /evidence="ECO:0000269|PubMed:16103919" FT VARIANT 199 FT /note="I -> V (in strain: Pasteur Red)" FT /evidence="ECO:0000269|PubMed:16103919" FT VARIANT 217 FT /note="G -> C (in strain: YJM326)" FT /evidence="ECO:0000269|PubMed:18780730" FT VARIANT 253 FT /note="T -> S (in strain: Levuline ALS, Lalvin CY-3079, FT Cote des Blancs, I14, M1, M11, M12, M13, M15, M2, M20, M21, FT M22, M24, M29, M3, M30, M31, M32, M33, M34, M4, M5, M6, M7, FT M8, M9, NRRLY-1438, NRRLYB-1952, NRRLY-2411, Pasteur Red, FT UCD 51, UCD 2120, UCD 175, UCD 529, UCD 765, UCD 781, UCD FT 820, UCD 762, YJM269, YJM270, YJM308, YJM326, YJM434 and FT YJM1129)" FT /evidence="ECO:0000269|PubMed:16103919, FT ECO:0000269|PubMed:18780730" FT VARIANT 310 FT /note="N -> D (in strain: SK1, V1-09, YJM269, YJM270, FT YJM280, YJM320, YJM326, YJM339, YJM627 and YJM1129)" FT /evidence="ECO:0000269|PubMed:18780730" FT VARIANT 541 FT /note="I -> V (in strain: YJM269 and YJM270)" FT /evidence="ECO:0000269|PubMed:18780730" FT MUTAGEN 552..554 FT /note="Missing: Impairs the peroxisomal localitation and FT leads to both nuclear and cytosolic localization." FT /evidence="ECO:0000269|PubMed:11846793" SQ SEQUENCE 554 AA; 62791 MW; 98E698E86E59C480 CRC64; MVKVSLDNVK LLVDVDKEPF FKPSSTTVGD ILTKDALEFI VLLHRTFNNK RKQLLENRQV VQKKLDSGSY HLDFLPETAN IRNDPTWQGP ILAPGLINRS TEITGPPLRN MLINALNAPV NTYMTDFEDS ASPTWNNMVY GQVNLYDAIR NQIDFDTPRK SYKLNGNVAN LPTIIVRPRG WHMVEKHLYV DDEPISASIF DFGLYFYHNA KELIKLGKGP YFYLPKMEHH LEAKLWNDVF CVAQDYIGIP RGTIRATVLI ETLPAAFQME EIIYQLRQHS SGLNCGRWDY IFSTIKRLRN DPNHILPNRN QVTMTSPFMD AYVKRLINTC HRRGVHAMGG MAAQIPIKDD PAANEKAMTK VRNDKIRELT NGHDGSWVAH PALAPICNEV FINMGTPNQI YFIPENVVTA ANLLETKIPN GEITTEGIVQ NLDIGLQYME AWLRGSGCVP INNLMEDAAT AEVSRCQLYQ WVKHGVTLKD TGEKVTPELT EKILKEQVER LSKASPLGDK NKFALAAKYF LPEIRGEKFS EFLTTLLYDE IVSTKATPTD LSKL //