ID AADAT_HUMAN Reviewed; 425 AA. AC Q8N5Z0; B3KP84; Q9UL02; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 13-APR-2004, sequence version 2. DT 11-NOV-2015, entry version 124. DE RecName: Full=Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial; DE Short=KAT/AadAT; DE AltName: Full=2-aminoadipate aminotransferase; DE AltName: Full=2-aminoadipate transaminase; DE EC=2.6.1.39; DE AltName: Full=Alpha-aminoadipate aminotransferase; DE Short=AadAT; DE AltName: Full=Kynurenine aminotransferase II; DE AltName: Full=Kynurenine--oxoglutarate aminotransferase II; DE AltName: Full=Kynurenine--oxoglutarate transaminase 2; DE EC=2.6.1.7; DE AltName: Full=Kynurenine--oxoglutarate transaminase II; DE Flags: Precursor; GN Name=AADAT; Synonyms=KAT2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Gatti S., Breton J., Mostardini M., Mosca M., Tarroni P., Schwarcz R., RA Speciale C., Okuno E., Toma S., Benatti L.; RT "Cloning of human L-kynurenine/alpha-aminoadipate aminotransferase RT cDNA from brain tissue."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, AND RP COFACTOR. RX PubMed=12126930; DOI=10.1016/S1096-7192(02)00037-9; RA Goh D.L.M., Patel A., Thomas G.H., Salomons G.S., Schor D.S.M., RA Jakobs C., Geraghty M.T.; RT "Characterization of the human gene encoding alpha-aminoadipate RT aminotransferase (AADAT)."; RL Mol. Genet. Metab. 76:172-180(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH 2-OXOGLUTARATE, RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, RP SUBUNIT, AND FUNCTION. RX PubMed=18620547; DOI=10.1042/BSR20080085; RA Han Q., Cai T., Tagle D.A., Robinson H., Li J.; RT "Substrate specificity and structure of human aminoadipate RT aminotransferase/kynurenine aminotransferase II."; RL Biosci. Rep. 28:205-215(2008). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL RP PHOSPHATE AND KYRUNENINE, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT. RX PubMed=18056995; DOI=10.1074/jbc.M708358200; RA Han Q., Robinson H., Li J.; RT "Crystal structure of human kynurenine aminotransferase II."; RL J. Biol. Chem. 283:3567-3573(2008). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL RP PHOSPHATE, SUBUNIT, AND COFACTOR. RX PubMed=18056996; DOI=10.1074/jbc.M707925200; RA Rossi F., Garavaglia S., Montalbano V., Walsh M.A., Rizzi M.; RT "Crystal structure of human kynurenine aminotransferase II, a drug RT target for the treatment of schizophrenia."; RL J. Biol. Chem. 283:3559-3566(2008). CC -!- FUNCTION: Transaminase with broad substrate specificity. Has CC transaminase activity towards aminoadipate, kynurenine, methionine CC and glutamate. Shows activity also towards tryptophan, aspartate CC and hydroxykynurenine. Accepts a variety of oxo-acids as amino- CC group acceptors, with a preference for 2-oxoglutarate, 2- CC oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol CC butyric acid. Can also use glyoxylate as amino-group acceptor (in CC vitro). {ECO:0000269|PubMed:18620547}. CC -!- CATALYTIC ACTIVITY: L-kynurenine + 2-oxoglutarate = 4-(2- CC aminophenyl)-2,4-dioxobutanoate + L-glutamate. CC -!- CATALYTIC ACTIVITY: L-2-aminoadipate + 2-oxoglutarate = 2- CC oxoadipate + L-glutamate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|PubMed:12126930, CC ECO:0000269|PubMed:18056995, ECO:0000269|PubMed:18056996}; CC -!- ENZYME REGULATION: Kynurenine transaminase activity is CC competitively inhibited by aminoadipate, asparagine, glutamate, CC histidine, cysteine, lysine, 3-hydroxy-kynurenine and CC phenylalanine. {ECO:0000269|PubMed:18620547}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.9 mM for aminoadipate {ECO:0000269|PubMed:18620547}; CC KM=4.7 mM for kynurenine {ECO:0000269|PubMed:18620547}; CC KM=1.7 mM for methionine {ECO:0000269|PubMed:18620547}; CC KM=1.6 mM for glutamate {ECO:0000269|PubMed:18620547}; CC KM=1.8 mM for tyrosine {ECO:0000269|PubMed:18620547}; CC KM=1.2 mM for 2-oxoglutarate {ECO:0000269|PubMed:18620547}; CC KM=1.5 mM for 2-oxocaproic acid {ECO:0000269|PubMed:18620547}; CC KM=1.8 mM for phenylpyruvate {ECO:0000269|PubMed:18620547}; CC KM=1.4 mM for ino-3-pyruvate {ECO:0000269|PubMed:18620547}; CC pH dependence: CC Optimum pH is 7-9. {ECO:0000269|PubMed:18620547}; CC Temperature dependence: CC Optimum temperature is 50 degrees Celsius. CC {ECO:0000269|PubMed:18620547}; CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via CC saccharopine pathway; glutaryl-CoA from L-lysine: step 4/6. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18056995, CC ECO:0000269|PubMed:18056996, ECO:0000269|PubMed:18620547}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8N5Z0-1; Sequence=Displayed; CC Note=May be due to a competing donor splice site.; CC Name=2; CC IsoId=Q8N5Z0-2; Sequence=VSP_009874; CC -!- TISSUE SPECIFICITY: Higher expression in the liver. Also found in CC heart, brain, kidney, pancreas, prostate, testis and ovary. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase 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; AF097994; AAF04623.1; -; mRNA. DR EMBL; AF481738; AAM09683.1; -; mRNA. DR EMBL; AK055952; BAG51596.1; -; mRNA. DR EMBL; BC031068; AAH31068.1; -; mRNA. DR CCDS; CCDS3814.1; -. [Q8N5Z0-1] DR CCDS; CCDS75209.1; -. [Q8N5Z0-2] DR RefSeq; NP_001273611.1; NM_001286682.1. [Q8N5Z0-2] DR RefSeq; NP_001273612.1; NM_001286683.1. [Q8N5Z0-1] DR RefSeq; NP_057312.1; NM_016228.3. [Q8N5Z0-1] DR RefSeq; NP_872603.1; NM_182662.1. [Q8N5Z0-1] DR UniGene; Hs.529735; -. DR PDB; 2QLR; X-ray; 2.30 A; A/B/C/D=1-425. DR PDB; 2R2N; X-ray; 1.95 A; A/B/C/D=1-425. DR PDB; 2VGZ; X-ray; 2.30 A; A/B=2-425. DR PDB; 2XH1; X-ray; 2.10 A; A/B=1-425. DR PDB; 3DC1; X-ray; 2.50 A; A/B/C/D=1-425. DR PDB; 3UE8; X-ray; 3.22 A; A/B=1-425. DR PDB; 4GDY; X-ray; 2.89 A; A/B=1-425. DR PDB; 4GE4; X-ray; 2.41 A; A/B=1-425. DR PDB; 4GE7; X-ray; 2.10 A; A/B=1-425. DR PDB; 4GE9; X-ray; 2.43 A; A/B/C/D=1-425. DR PDB; 4GEB; X-ray; 2.15 A; A/B=1-425. DR PDBsum; 2QLR; -. DR PDBsum; 2R2N; -. DR PDBsum; 2VGZ; -. DR PDBsum; 2XH1; -. DR PDBsum; 3DC1; -. DR PDBsum; 3UE8; -. DR PDBsum; 4GDY; -. DR PDBsum; 4GE4; -. DR PDBsum; 4GE7; -. DR PDBsum; 4GE9; -. DR PDBsum; 4GEB; -. DR ProteinModelPortal; Q8N5Z0; -. DR SMR; Q8N5Z0; 1-425. DR BioGrid; 119346; 1. DR STRING; 9606.ENSP00000226840; -. DR BindingDB; Q8N5Z0; -. DR ChEMBL; CHEMBL2046259; -. DR PhosphoSite; Q8N5Z0; -. DR BioMuta; AADAT; -. DR DMDM; 46395904; -. DR MaxQB; Q8N5Z0; -. DR PaxDb; Q8N5Z0; -. DR PRIDE; Q8N5Z0; -. DR DNASU; 51166; -. DR Ensembl; ENST00000337664; ENSP00000336808; ENSG00000109576. [Q8N5Z0-1] DR Ensembl; ENST00000353187; ENSP00000226840; ENSG00000109576. [Q8N5Z0-1] DR Ensembl; ENST00000509167; ENSP00000423190; ENSG00000109576. [Q8N5Z0-2] DR Ensembl; ENST00000515480; ENSP00000423341; ENSG00000109576. [Q8N5Z0-1] DR GeneID; 51166; -. DR KEGG; hsa:51166; -. DR UCSC; uc003isr.3; human. [Q8N5Z0-1] DR UCSC; uc003ist.3; human. [Q8N5Z0-2] DR CTD; 51166; -. DR GeneCards; AADAT; -. DR HGNC; HGNC:17929; AADAT. DR HPA; HPA037502; -. DR MIM; 611754; gene. DR neXtProt; NX_Q8N5Z0; -. DR PharmGKB; PA24364; -. DR eggNOG; KOG0634; Eukaryota. DR eggNOG; COG1167; LUCA. DR GeneTree; ENSGT00390000004594; -. DR HOGENOM; HOG000223057; -. DR HOVERGEN; HBG050429; -. DR InParanoid; Q8N5Z0; -. DR KO; K00825; -. DR OMA; QQWGEKG; -. DR OrthoDB; EOG7ZKSBF; -. DR PhylomeDB; Q8N5Z0; -. DR TreeFam; TF328598; -. DR BioCyc; MetaCyc:HS03239-MONOMER; -. DR BRENDA; 2.6.1.39; 2681. DR BRENDA; 2.6.1.7; 2681. DR Reactome; R-HSA-71064; Lysine catabolism. DR Reactome; R-HSA-71240; Tryptophan catabolism. DR UniPathway; UPA00868; UER00838. DR ChiTaRS; AADAT; human. DR EvolutionaryTrace; Q8N5Z0; -. DR GenomeRNAi; 51166; -. DR NextBio; 54097; -. DR PRO; PR:Q8N5Z0; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; Q8N5Z0; -. DR CleanEx; HS_AADAT; -. DR ExpressionAtlas; Q8N5Z0; baseline and differential. DR Genevisible; Q8N5Z0; HS. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0047536; F:2-aminoadipate transaminase activity; IDA:UniProtKB. DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:Ensembl. DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IDA:UniProtKB. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome. DR GO; GO:0006536; P:glutamate metabolic process; IDA:UniProtKB. DR GO; GO:0070189; P:kynurenine metabolic process; IDA:UniProtKB. DR GO; GO:0097052; P:L-kynurenine metabolic process; IDA:GOC. 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 GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0006569; P:tryptophan catabolic process; TAS:Reactome. DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IEA:Ensembl. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Aminotransferase; KW Complete proteome; Mitochondrion; Polymorphism; Pyridoxal phosphate; KW Reference proteome; Transferase; Transit peptide. FT TRANSIT 1 29 Mitochondrion. {ECO:0000255}. FT CHAIN 30 425 Kynurenine/alpha-aminoadipate FT aminotransferase, mitochondrial. FT /FTId=PRO_0000020602. FT BINDING 20 20 Substrate. FT BINDING 74 74 Substrate. FT BINDING 142 142 Substrate. FT BINDING 202 202 Substrate. FT BINDING 399 399 Substrate. FT MOD_RES 69 69 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q9WVM8}. FT MOD_RES 179 179 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q9WVM8}. FT MOD_RES 263 263 N6-(pyridoxal phosphate)lysine; FT alternate. FT MOD_RES 263 263 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:Q9WVM8}. FT MOD_RES 263 263 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:Q9WVM8}. FT MOD_RES 339 339 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:Q9WVM8}. FT MOD_RES 339 339 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:Q9WVM8}. FT MOD_RES 367 367 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:Q9WVM8}. FT MOD_RES 367 367 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:Q9WVM8}. FT MOD_RES 422 422 N6-acetyllysine. FT {ECO:0000250|UniProtKB:Q9WVM8}. FT VAR_SEQ 23 23 T -> SEKRA (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_009874. FT VARIANT 243 243 V -> I (in dbSNP:rs56350236). FT /FTId=VAR_061005. FT CONFLICT 103 103 P -> Q (in Ref. 4; AAH31068). FT {ECO:0000305}. FT CONFLICT 380 380 L -> S (in Ref. 3; BAG51596). FT {ECO:0000305}. FT HELIX 3 6 {ECO:0000244|PDB:2R2N}. FT HELIX 9 12 {ECO:0000244|PDB:2R2N}. FT HELIX 19 21 {ECO:0000244|PDB:2R2N}. FT HELIX 22 28 {ECO:0000244|PDB:2R2N}. FT HELIX 43 45 {ECO:0000244|PDB:2R2N}. FT STRAND 47 55 {ECO:0000244|PDB:2R2N}. FT TURN 56 58 {ECO:0000244|PDB:4GEB}. FT STRAND 61 63 {ECO:0000244|PDB:2R2N}. FT HELIX 65 71 {ECO:0000244|PDB:2R2N}. FT HELIX 81 95 {ECO:0000244|PDB:2R2N}. FT TURN 98 101 {ECO:0000244|PDB:2R2N}. FT HELIX 104 106 {ECO:0000244|PDB:2R2N}. FT STRAND 109 116 {ECO:0000244|PDB:2R2N}. FT HELIX 117 128 {ECO:0000244|PDB:2R2N}. FT STRAND 134 140 {ECO:0000244|PDB:2R2N}. FT HELIX 143 149 {ECO:0000244|PDB:2R2N}. FT HELIX 150 152 {ECO:0000244|PDB:2R2N}. FT STRAND 155 159 {ECO:0000244|PDB:2R2N}. FT HELIX 168 175 {ECO:0000244|PDB:2R2N}. FT HELIX 180 182 {ECO:0000244|PDB:2XH1}. FT STRAND 183 185 {ECO:0000244|PDB:2R2N}. FT HELIX 186 188 {ECO:0000244|PDB:2QLR}. FT STRAND 192 196 {ECO:0000244|PDB:2R2N}. FT TURN 202 204 {ECO:0000244|PDB:2R2N}. FT HELIX 210 222 {ECO:0000244|PDB:2R2N}. FT STRAND 226 230 {ECO:0000244|PDB:2R2N}. FT HELIX 234 236 {ECO:0000244|PDB:2R2N}. FT STRAND 237 241 {ECO:0000244|PDB:2R2N}. FT HELIX 247 249 {ECO:0000244|PDB:2R2N}. FT STRAND 251 253 {ECO:0000244|PDB:4GE4}. FT STRAND 255 261 {ECO:0000244|PDB:2R2N}. FT TURN 262 265 {ECO:0000244|PDB:2R2N}. FT TURN 267 270 {ECO:0000244|PDB:4GE9}. FT STRAND 272 277 {ECO:0000244|PDB:2R2N}. FT HELIX 278 289 {ECO:0000244|PDB:2R2N}. FT TURN 290 292 {ECO:0000244|PDB:2R2N}. FT STRAND 293 295 {ECO:0000244|PDB:4GE7}. FT HELIX 297 340 {ECO:0000244|PDB:2R2N}. FT STRAND 342 347 {ECO:0000244|PDB:2R2N}. FT STRAND 351 360 {ECO:0000244|PDB:2R2N}. FT HELIX 367 371 {ECO:0000244|PDB:2R2N}. FT HELIX 373 376 {ECO:0000244|PDB:2R2N}. FT STRAND 381 383 {ECO:0000244|PDB:4GDY}. FT HELIX 384 387 {ECO:0000244|PDB:2R2N}. FT STRAND 388 390 {ECO:0000244|PDB:2R2N}. FT STRAND 391 393 {ECO:0000244|PDB:3UE8}. FT STRAND 397 401 {ECO:0000244|PDB:2R2N}. FT TURN 402 404 {ECO:0000244|PDB:3UE8}. FT HELIX 407 424 {ECO:0000244|PDB:2R2N}. SQ SEQUENCE 425 AA; 47352 MW; 448CCAAB2173A7BA CRC64; MNYARFITAA SAARNPSPIR TMTDILSRGP KSMISLAGGL PNPNMFPFKT AVITVENGKT IQFGEEMMKR ALQYSPSAGI PELLSWLKQL QIKLHNPPTI HYPPSQGQMD LCVTSGSQQG LCKVFEMIIN PGDNVLLDEP AYSGTLQSLH PLGCNIINVA SDESGIVPDS LRDILSRWKP EDAKNPQKNT PKFLYTVPNG NNPTGNSLTS ERKKEIYELA RKYDFLIIED DPYYFLQFNK FRVPTFLSMD VDGRVIRADS FSKIISSGLR IGFLTGPKPL IERVILHIQV STLHPSTFNQ LMISQLLHEW GEEGFMAHVD RVIDFYSNQK DAILAAADKW LTGLAEWHVP AAGMFLWIKV KGINDVKELI EEKAVKMGVL MLPGNAFYVD SSAPSPYLRA SFSSASPEQM DVAFQVLAQL IKESL //