ID AASS_HUMAN Reviewed; 926 AA. AC Q9UDR5; O95462; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 17-JUN-2020, entry version 163. DE RecName: Full=Alpha-aminoadipic semialdehyde synthase, mitochondrial; DE AltName: Full=LKR/SDH; DE Includes: DE RecName: Full=Lysine ketoglutarate reductase; DE Short=LKR; DE Short=LOR; DE EC=1.5.1.8; DE Includes: DE RecName: Full=Saccharopine dehydrogenase; DE Short=SDH; DE EC=1.5.1.9; DE Flags: Precursor; GN Name=AASS; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND INVOLVEMENT IN HYPLYS1. RX PubMed=10775527; DOI=10.1086/302919; RA Sacksteder K.A., Biery B.J., Morrell J.C., Goodman B.K., Geisbrecht B.V., RA Cox R.P., Gould S.J., Geraghty M.T.; RT "Identification of the alpha-aminoadipic semialdehyde synthase gene, which RT is defective in familial hyperlysinemia."; RL Am. J. Hum. Genet. 66:1736-1743(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RA Papes F., Kemper E.L., Cord-Neto G., Langone F., Arruda P.; RT "Cloning and expression analysis of the LKR/SDH gene in human tissues."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP INVOLVEMENT IN HYPLYS1. RX PubMed=463877; RA Dancis J., Hutzler J., Cox R.P.; RT "Familial hyperlysinemia: enzyme studies, diagnostic methods, comments on RT terminology."; RL Am. J. Hum. Genet. 31:290-299(1979). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [6] RP INVOLVEMENT IN DECRD. RX PubMed=24847004; DOI=10.1093/hmg/ddu218; RA Houten S.M., Denis S., Te Brinke H., Jongejan A., van Kampen A.H., RA Bradley E.J., Baas F., Hennekam R.C., Millington D.S., Young S.P., RA Frazier D.M., Gucsavas-Calikoglu M., Wanders R.J.; RT "Mitochondrial NADP(H) deficiency due to a mutation in NADK2 causes RT dienoyl-CoA reductase deficiency with hyperlysinemia."; RL Hum. Mol. Genet. 23:5009-5016(2014). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Bifunctional enzyme that catalyzes the first two steps in CC lysine degradation. The N-terminal and the C-terminal contain lysine- CC ketoglutarate reductase and saccharopine dehydrogenase activity, CC respectively. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-saccharopine + NADP(+) = 2-oxoglutarate + H(+) + L- CC lysine + NADPH; Xref=Rhea:RHEA:19373, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:32551, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57951, ChEBI:CHEBI:58349; EC=1.5.1.8; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-saccharopine + NAD(+) = (S)-2-amino-6-oxohexanoate + CC H(+) + L-glutamate + NADH; Xref=Rhea:RHEA:24520, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, ChEBI:CHEBI:57951, ChEBI:CHEBI:58321; EC=1.5.1.9; CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine CC pathway; glutaryl-CoA from L-lysine: step 1/6. CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine CC pathway; glutaryl-CoA from L-lysine: step 2/6. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in all 16 tissues examined with highest CC expression in the liver. CC -!- INDUCTION: Induced by starvation. {ECO:0000250}. CC -!- DISEASE: Hyperlysinemia, 1 (HYPLYS1) [MIM:238700]: An autosomal CC recessive metabolic condition with variable clinical features. Some CC patients present with non-specific seizures, hypotonia, or mildly CC delayed psychomotor development, and increased serum lysine and CC pipecolic acid on laboratory analysis. However, about half of the CC probands are reported to be asymptomatic, and hyperlysinemia is CC generally considered to be a benign metabolic variant. CC {ECO:0000269|PubMed:10775527}. Note=The disease is caused by mutations CC affecting the gene represented in this entry. In hyperlysinemia 1, both CC enzymatic functions of AASS are defective and patients have increased CC serum lysine and possibly increased saccharopine. Some individuals, CC however, retain significant amounts of lysine-ketoglutarate reductase CC and present with saccharopinuria, a metabolic condition with few, if CC any, clinical manifestations. {ECO:0000305|PubMed:463877}. CC -!- DISEASE: 2,4-dienoyl-CoA reductase deficiency (DECRD) [MIM:616034]: A CC rare, autosomal recessive, inborn error of polyunsaturated fatty acids CC and lysine metabolism, resulting in mitochondrial dysfunction. Affected CC individuals have a severe encephalopathy with neurologic and metabolic CC abnormalities beginning in early infancy. Laboratory studies show CC increased C10:2 carnitine levels and hyperlysinemia. CC {ECO:0000269|PubMed:24847004}. Note=The protein represented in this CC entry is involved in disease pathogenesis. A selective decrease in CC mitochondrial NADP(H) levels due to NADK2 mutations causes a deficiency CC of NADPH-dependent mitochondrial enzymes, such as DECR1 and AASS. CC {ECO:0000269|PubMed:24847004}. CC -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the saccharopine CC dehydrogenase 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; AF229180; AAF44328.1; -; mRNA. DR EMBL; AJ007714; CAA07619.2; -; mRNA. DR EMBL; AC006020; AAF03526.1; -; Genomic_DNA. DR CCDS; CCDS5783.1; -. DR RefSeq; NP_005754.2; NM_005763.3. DR PDB; 5L76; X-ray; 2.57 A; A=455-926. DR PDB; 5L78; X-ray; 2.68 A; A/B=455-926. DR PDB; 5O1N; X-ray; 2.28 A; A=455-926. DR PDB; 5O1O; X-ray; 2.48 A; A/B=455-926. DR PDB; 5O1P; X-ray; 1.90 A; A=455-926. DR PDBsum; 5L76; -. DR PDBsum; 5L78; -. DR PDBsum; 5O1N; -. DR PDBsum; 5O1O; -. DR PDBsum; 5O1P; -. DR SMR; Q9UDR5; -. DR BioGRID; 115459; 33. DR IntAct; Q9UDR5; 9. DR MINT; Q9UDR5; -. DR STRING; 9606.ENSP00000377040; -. DR DrugBank; DB00142; Glutamic acid. DR DrugBank; DB04207; N-(5-Amino-5-Carboxypentyl)Glutamic Acid. DR DrugBank; DB00157; NADH. DR DrugBank; DB02338; Nadph Dihydro-Nicotinamide-Adenine-Dinucleotidephosphate. DR CarbonylDB; Q9UDR5; -. DR iPTMnet; Q9UDR5; -. DR MetOSite; Q9UDR5; -. DR PhosphoSitePlus; Q9UDR5; -. DR BioMuta; AASS; -. DR DMDM; 46396032; -. DR EPD; Q9UDR5; -. DR jPOST; Q9UDR5; -. DR MassIVE; Q9UDR5; -. DR MaxQB; Q9UDR5; -. DR PaxDb; Q9UDR5; -. DR PeptideAtlas; Q9UDR5; -. DR PRIDE; Q9UDR5; -. DR ProteomicsDB; 84114; -. DR Antibodypedia; 17598; 193 antibodies. DR Ensembl; ENST00000393376; ENSP00000377040; ENSG00000008311. DR Ensembl; ENST00000417368; ENSP00000403768; ENSG00000008311. DR GeneID; 10157; -. DR KEGG; hsa:10157; -. DR UCSC; uc003vka.4; human. DR CTD; 10157; -. DR DisGeNET; 10157; -. DR EuPathDB; HostDB:ENSG00000008311.14; -. DR GeneCards; AASS; -. DR HGNC; HGNC:17366; AASS. DR HPA; ENSG00000008311; Low tissue specificity. DR MalaCards; AASS; -. DR MIM; 238700; phenotype. DR MIM; 605113; gene. DR MIM; 616034; phenotype. DR neXtProt; NX_Q9UDR5; -. DR OpenTargets; ENSG00000008311; -. DR Orphanet; 2203; Hyperlysinemia. DR Orphanet; 3124; Saccharopinuria. DR PharmGKB; PA24369; -. DR eggNOG; KOG0172; Eukaryota. DR eggNOG; COG1748; LUCA. DR GeneTree; ENSGT00390000013249; -. DR HOGENOM; CLU_005231_0_1_1; -. DR InParanoid; Q9UDR5; -. DR KO; K14157; -. DR OMA; KMEGRSE; -. DR OrthoDB; 498994at2759; -. DR PhylomeDB; Q9UDR5; -. DR TreeFam; TF105728; -. DR BioCyc; MetaCyc:HS00244-MONOMER; -. DR Reactome; R-HSA-71064; Lysine catabolism. DR SABIO-RK; Q9UDR5; -. DR UniPathway; UPA00868; UER00835. DR UniPathway; UPA00868; UER00836. DR BioGRID-ORCS; 10157; 7 hits in 787 CRISPR screens. DR ChiTaRS; AASS; human. DR GeneWiki; AASS; -. DR GenomeRNAi; 10157; -. DR Pharos; Q9UDR5; Tbio. DR PRO; PR:Q9UDR5; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9UDR5; protein. DR Bgee; ENSG00000008311; Expressed in right ovary and 199 other tissues. DR ExpressionAtlas; Q9UDR5; baseline and differential. DR Genevisible; Q9UDR5; HS. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; NAS:UniProtKB. DR GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway. DR GO; GO:0006554; P:lysine catabolic process; TAS:Reactome. DR InterPro; IPR007886; AlaDH/PNT_N. DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR032095; Sacchrp_dh_C. DR InterPro; IPR005097; Sacchrp_dh_NADP. DR Pfam; PF05222; AlaDh_PNT_N; 1. DR Pfam; PF16653; Sacchrp_dh_C; 1. DR Pfam; PF03435; Sacchrp_dh_NADP; 1. DR SMART; SM01002; AlaDh_PNT_C; 1. DR SMART; SM01003; AlaDh_PNT_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Mitochondrion; Multifunctional enzyme; NAD; KW NADP; Oxidoreductase; Reference proteome; Transit peptide. FT TRANSIT 1..32 FT /note="Mitochondrion" FT /evidence="ECO:0000250" FT CHAIN 33..926 FT /note="Alpha-aminoadipic semialdehyde synthase, FT mitochondrial" FT /id="PRO_0000001052" FT NP_BIND 488..491 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:Q9P4R4" FT NP_BIND 603..605 FT /note="NADP" FT /evidence="ECO:0000250|UniProtKB:Q9P4R4" FT REGION 33..455 FT /note="Lysine-ketoglutarate reductase" FT REGION 477..926 FT /note="Saccharopine dehydrogenase" FT REGION 577..578 FT /note="Saccharopine binding" FT /evidence="ECO:0000250|UniProtKB:Q9P4R4" FT REGION 724..726 FT /note="Saccharopine binding" FT /evidence="ECO:0000250|UniProtKB:Q9P4R4" FT BINDING 604 FT /note="Saccharopine" FT /evidence="ECO:0000250|UniProtKB:Q9P4R4" FT BINDING 653 FT /note="NADP; via amide nitrogen" FT /evidence="ECO:0000250|UniProtKB:Q9P4R4" FT BINDING 703 FT /note="Saccharopine" FT /evidence="ECO:0000250|UniProtKB:Q9P4R4" FT MOD_RES 48 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 56 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 93 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 93 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 128 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 138 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 138 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 274 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 286 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 286 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 333 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 458 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 458 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 523 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 523 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 535 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 535 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 584 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 584 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 707 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 732 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 739 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 761 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 761 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT MOD_RES 780 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99K67" FT CONFLICT 589 FT /note="S -> C (in Ref. 2; CAA07619)" FT /evidence="ECO:0000305" FT STRAND 483..486 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 492..499 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 500..503 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 507..512 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 514..523 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 527..530 FT /evidence="ECO:0000244|PDB:5O1P" FT TURN 533..535 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 537..545 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 548..552 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 556..558 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 559..569 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 572..577 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 581..584 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 587..593 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 596..598 FT /evidence="ECO:0000244|PDB:5O1P" FT TURN 603..606 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 607..620 FT /evidence="ECO:0000244|PDB:5O1P" FT TURN 621..623 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 625..637 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 639..641 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 650..652 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 655..660 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 665..669 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 672..676 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 679..685 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 687..689 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 697..701 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 703..705 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 708..712 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 718..727 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 730..740 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 760..768 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 775..785 FT /evidence="ECO:0000244|PDB:5O1P" FT TURN 787..789 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 791..800 FT /evidence="ECO:0000244|PDB:5O1P" FT TURN 801..803 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 814..825 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 834..845 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 851..861 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 864..866 FT /evidence="ECO:0000244|PDB:5L76" FT HELIX 869..886 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 894..896 FT /evidence="ECO:0000244|PDB:5O1P" FT HELIX 901..910 FT /evidence="ECO:0000244|PDB:5O1P" FT TURN 911..915 FT /evidence="ECO:0000244|PDB:5O1P" FT STRAND 917..924 FT /evidence="ECO:0000244|PDB:5O1P" SQ SEQUENCE 926 AA; 102132 MW; CB4194014351A18D CRC64; MLQVHRTGLG RLGVSLSKGL HHKAVLAVRR EDVNAWERRA PLAPKHIKGI TNLGYKVLIQ PSNRRAIHDK DYVKAGGILQ EDISEACLIL GVKRPPEEKL MSRKTYAFFS HTIKAQEANM GLLDEILKQE IRLIDYEKMV DHRGVRVVAF GQWAGVAGMI NILHGMGLRL LALGHHTPFM HIGMAHNYRN SSQAVQAVRD AGYEISLGLM PKSIGPLTFV FTGTGNVSKG AQAIFNELPC EYVEPHELKE VSQTGDLRKV YGTVLSRHHH LVRKTDAVYD PAEYDKHPER YISRFNTDIA PYTTCLINGI YWEQNTPRLL TRQDAQSLLA PGKFSPAGVE GCPALPHKLV AICDISADTG GSIEFMTECT TIEHPFCMYD ADQHIIHDSV EGSGILMCSI DNLPAQLPIE ATECFGDMLY PYVEEMILSD ATQPLESQNF SPVVRDAVIT SNGTLPDKYK YIQTLRESRE RAQSLSMGTR RKVLVLGSGY ISEPVLEYLS RDGNIEITVG SDMKNQIEQL GKKYNINPVS MDICKQEEKL GFLVAKQDLV ISLLPYVLHP LVAKACITNK VNMVTASYIT PALKELEKSV EDAGITIIGE LGLDPGLDHM LAMETIDKAK EVGATIESYI SYCGGLPAPE HSNNPLRYKF SWSPVGVLMN VMQSATYLLD GKVVNVAGGI SFLDAVTSMD FFPGLNLEGY PNRDSTKYAE IYGISSAHTL LRGTLRYKGY MKALNGFVKL GLINREALPA FRPEANPLTW KQLLCDLVGI SPSSEHDVLK EAVLKKLGGD NTQLEAAEWL GLLGDEQVPQ AESILDALSK HLVMKLSYGP EEKDMIVMRD SFGIRHPSGH LEHKTIDLVA YGDINGFSAM AKTVGLPTAM AAKMLLDGEI GAKGLMGPFS KEIYGPILER IKAEGIIYTT QSTIKP //