MLS1_YEAST
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 03-AUG-2022, entry version 174.
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 270,
RC 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,
RC ATCC 9804 / CBS 400 / DSM 70478 / IFO 0210 / JCM 2220, Awamori-1,
RC Cote des blancs, I14, K1, K10, K5, K9, Lalvin 71B, Lalvin BM45,
RC Lalvin CY-3079, Levuline ALS, M1, M11, M12, M13, M15, M17, M19, M2, M20,
RC M21, M24, M29, M3, M30, M31, M32, M33, M34, M4, M5, M6, M7, M8, M9,
RC NRIC 1413, NRIC 1685, NRIC 23, NRRL Y-1438, NRRL Y-1532, NRRL Y-1546,
RC NRRL Y-2411, NRRL Y-390, NRRL Y-5997, NRRL Y-7567, NRRL YB-1952,
RC Pasteur Red, UCD 175, UCD 2120, UCD 529, UCD 612, UCD 762, UCD 765,
RC UCD 781, UCD 820, UCD51, YJM 145, YJM 269, YJM 270, YJM 280, YJM 320,
RC YJM 326, YJM 339, YJM 421, YJM 627, YJM1129 YPS163, YJM308, YJM434, YJM436,
RC YJM440, YJM454, YPS1000, 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}.
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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; 44.
DR IntAct; P30952; 9.
DR STRING; 4932.YNL117W; -.
DR MaxQB; P30952; -.
DR PaxDb; P30952; -.
DR PRIDE; P30952; -.
DR TopDownProteomics; P30952; -.
DR EnsemblFungi; YNL117W_mRNA; YNL117W; YNL117W.
DR GeneID; 855606; -.
DR KEGG; sce:YNL117W; -.
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 BioCyc; MetaCyc:YNL117W-MON; -.
DR BioCyc; YEAST:YNL117W-MON; -.
DR UniPathway; UPA00703; UER00720.
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; 1.20.1220.12; -; 1.
DR Gene3D; 3.20.20.360; -; 1.
DR InterPro; IPR044856; Malate_synth_C_sf.
DR InterPro; IPR011076; Malate_synth_sf.
DR InterPro; IPR006252; Malate_synthA.
DR InterPro; IPR001465; Malate_synthase.
DR InterPro; IPR019830; Malate_synthase_CS.
DR InterPro; IPR046363; MS_N_TIM-barrel_dom.
DR PANTHER; PTHR42902; PTHR42902; 1.
DR Pfam; PF01274; Malate_synthase; 1.
DR PIRSF; PIRSF001363; Malate_synth; 1.
DR SUPFAM; SSF51645; SSF51645; 1.
DR TIGRFAMs; TIGR01344; malate_syn_A; 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, NRRL Y-1438, NRRL YB-1952, NRRL Y-2411, Pasteur
FT Red, UCD 51, UCD 2120, UCD 175, UCD 529, UCD 765, UCD 781,
FT UCD 820, UCD 762, YJM269, YJM270, YJM308, YJM326, YJM434
FT and 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
