ID ACY1_HUMAN Reviewed; 408 AA. AC Q03154; C9J6I6; C9J9D8; C9JWD4; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1994, sequence version 1. DT 11-NOV-2015, entry version 159. DE RecName: Full=Aminoacylase-1; DE Short=ACY-1; DE EC=3.5.1.14; DE AltName: Full=N-acyl-L-amino-acid amidohydrolase; GN Name=ACY1; 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). RX PubMed=8357837; DOI=10.1016/0167-4781(93)90116-U; RA Mitta M., Kato I., Tsunasawa S.; RT "The nucleotide sequence of human aminoacylase-1."; RL Biochim. Biophys. Acta 1174:201-203(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=8394326; RA Cook R.M., Burke B.J., Buchhagen D.L., Minna J.D., Miller Y.E.; RT "Human aminoacylase-1. Cloning, sequence, and expression analysis of a RT chromosome 3p21 gene inactivated in small cell lung cancer."; RL J. Biol. Chem. 268:17010-17017(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Iwaki K., Tanaka Y., Ohta T., Fukuda S., Kurimoto M.; RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., RA Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, Lung, and Skin; 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 [6] 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., RA Buerckstuemmer T., 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., RA Fischer-Posovszky P., Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion RT profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [8] 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 [9] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH ZINC IONS, RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVE SITE, AND RP MUTAGENESIS OF HIS-80; ASP-113; GLU-147; GLU-148; GLU-175; HIS-206 AND RP HIS-373. RX PubMed=12933810; DOI=10.1074/jbc.M304233200; RA Lindner H.A., Lunin V.V., Alary A., Hecker R., Cygler M., Menard R.; RT "Essential roles of zinc ligation and enzyme dimerization for RT catalysis in the aminoacylase-1/M20 family."; RL J. Biol. Chem. 278:44496-44504(2003). RN [10] RP VARIANT ACY1D CYS-353. RX PubMed=16274666; DOI=10.1016/j.bbrc.2005.10.126; RA Van Coster R.N., Gerlo E.A., Giardina T.G., Engelke U.F., Smet J.E., RA De Praeter C.M., Meersschaut V.A., De Meirleir L.J., Seneca S.H., RA Devreese B., Leroy J.G., Herga S., Perrier J.P., Wevers R.A., RA Lissens W.; RT "Aminoacylase I deficiency: a novel inborn error of metabolism."; RL Biochem. Biophys. Res. Commun. 338:1322-1326(2005). RN [11] RP VARIANTS ACY1D ASP-233 AND CYS-353, AND TISSUE SPECIFICITY. RX PubMed=16465618; DOI=10.1086/500563; RA Sass J.O., Mohr V., Olbrich H., Engelke U., Horvath J., Fliegauf M., RA Loges N.T., Schweitzer-Krantz S., Moebus R., Weiler P., Kispert A., RA Superti-Furga A., Wevers R.A., Omran H.; RT "Mutations in ACY1, the gene encoding aminoacylase 1, cause a novel RT inborn error of metabolism."; RL Am. J. Hum. Genet. 78:401-409(2006). RN [12] RP VARIANT [LARGE SCALE ANALYSIS] ASP-381. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). RN [13] RP VARIANTS ACY1D TRP-197; CYS-353 AND HIS-393. RX PubMed=17562838; DOI=10.1212/01.wnl.0000264933.56204.e8; RA Sass J.O., Olbrich H., Mohr V., Hart C., Woldseth B., Krywawych S., RA Bjurulf B., Lakhani P.K., Buchdahl R.M., Omran H.; RT "Neurological findings in aminoacylase 1 deficiency."; RL Neurology 68:2151-2153(2007). RN [14] RP VARIANTS ACY1D GLN-378; TRP-378 AND CYS-386, AND CHARACTERIZATION OF RP VARIANTS ACY1D TRP-197; ASP-233; CYS-353; TRP-378 AND CYS-386. RX PubMed=21414403; DOI=10.1016/j.bbadis.2011.03.005; RA Sommer A., Christensen E., Schwenger S., Seul R., Haas D., Olbrich H., RA Omran H., Sass J.O.; RT "The molecular basis of aminoacylase 1 deficiency."; RL Biochim. Biophys. Acta 1812:685-690(2011). CC -!- FUNCTION: Involved in the hydrolysis of N-acylated or N-acetylated CC amino acids (except L-aspartate). {ECO:0000269|PubMed:12933810}. CC -!- CATALYTIC ACTIVITY: An N-acyl-aliphatic-L-amino acid + H(2)O = an CC aliphatic L-amino acid + a carboxylate. CC {ECO:0000269|PubMed:12933810}. CC -!- CATALYTIC ACTIVITY: An N-acetyl-L-cysteine-S-conjugate + H(2)O = CC an L-cysteine-S-conjugate + acetate. CC {ECO:0000269|PubMed:12933810}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:12933810}; CC Note=Binds 2 Zn(2+) ions per subunit. CC {ECO:0000269|PubMed:12933810}; CC -!- SUBUNIT: Homodimer. Interacts with SPHK1 (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q03154-1; Sequence=Displayed; CC Name=2; CC IsoId=Q03154-2; Sequence=VSP_046877; CC Note=Gene prediction based on EST data.; CC Name=3; CC IsoId=Q03154-3; Sequence=VSP_046878; CC Note=Gene prediction based on EST data.; CC Name=4; CC IsoId=Q03154-4; Sequence=VSP_046876; CC Note=Gene prediction based on EST data.; CC -!- TISSUE SPECIFICITY: Expression is highest in kidney, strong in CC brain and weaker in placenta and spleen. CC {ECO:0000269|PubMed:16465618}. CC -!- DISEASE: Aminoacylase-1 deficiency (ACY1D) [MIM:609924]: An CC enzymatic deficiency resulting in encephalopathy, unspecific CC psychomotor delay, psychomotor delay with atrophy of the vermis CC and syringomyelia, marked muscular hypotonia or normal clinical CC features. Epileptic seizures are a frequent feature. All affected CC individuals exhibit markedly increased urinary excretion of CC several N-acetylated amino acids. {ECO:0000269|PubMed:16274666, CC ECO:0000269|PubMed:16465618, ECO:0000269|PubMed:17562838, CC ECO:0000269|PubMed:21414403}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the peptidase M20A 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; L07548; AAA02852.1; -; mRNA. DR EMBL; D14524; BAA03397.1; -; mRNA. DR EMBL; D16307; BAA03814.1; -; mRNA. DR EMBL; AC115284; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000545; AAH00545.1; -; mRNA. DR EMBL; BC003023; AAH03023.1; -; mRNA. DR EMBL; BC014112; AAH14112.1; -; mRNA. DR CCDS; CCDS2844.1; -. [Q03154-1] DR CCDS; CCDS56261.1; -. [Q03154-2] DR CCDS; CCDS56262.1; -. [Q03154-3] DR CCDS; CCDS56263.1; -. [Q03154-4] DR PIR; A47488; A47488. DR RefSeq; NP_000657.1; NM_000666.2. [Q03154-1] DR RefSeq; NP_001185824.1; NM_001198895.1. [Q03154-1] DR RefSeq; NP_001185825.1; NM_001198896.1. [Q03154-2] DR RefSeq; NP_001185826.1; NM_001198897.1. [Q03154-3] DR RefSeq; NP_001185827.1; NM_001198898.1. [Q03154-4] DR UniGene; Hs.334707; -. DR PDB; 1Q7L; X-ray; 1.40 A; A/C=1-198, B/D=321-408. DR PDBsum; 1Q7L; -. DR ProteinModelPortal; Q03154; -. DR SMR; Q03154; 7-408. DR BioGrid; 106610; 16. DR IntAct; Q03154; 6. DR MINT; MINT-4999851; -. DR STRING; 9606.ENSP00000384296; -. DR DrugBank; DB06151; Acetylcysteine. DR DrugBank; DB00128; L-Aspartic Acid. DR MEROPS; M20.973; -. DR PhosphoSite; Q03154; -. DR BioMuta; ACY1; -. DR DMDM; 461466; -. DR REPRODUCTION-2DPAGE; IPI00009268; -. DR PaxDb; Q03154; -. DR PeptideAtlas; Q03154; -. DR PRIDE; Q03154; -. DR DNASU; 95; -. DR Ensembl; ENST00000404366; ENSP00000384296; ENSG00000243989. [Q03154-1] DR Ensembl; ENST00000476351; ENSP00000417056; ENSG00000243989. [Q03154-4] DR Ensembl; ENST00000476854; ENSP00000419262; ENSG00000243989. [Q03154-3] DR Ensembl; ENST00000494103; ENSP00000417618; ENSG00000243989. [Q03154-2] DR GeneID; 95; -. DR KEGG; hsa:95; -. DR UCSC; uc003dcp.3; human. [Q03154-1] DR CTD; 95; -. DR GeneCards; ACY1; -. DR HGNC; HGNC:177; ACY1. DR HPA; CAB003695; -. DR HPA; HPA036174; -. DR HPA; HPA036175; -. DR MIM; 104620; gene. DR MIM; 609924; phenotype. DR neXtProt; NX_Q03154; -. DR Orphanet; 137754; Neurological conditions associated with aminoacylase 1 deficiency. DR PharmGKB; PA24497; -. DR eggNOG; KOG2275; Eukaryota. DR eggNOG; COG0624; LUCA. DR GeneTree; ENSGT00730000111049; -. DR HOGENOM; HOG000021196; -. DR HOVERGEN; HBG000982; -. DR InParanoid; Q03154; -. DR KO; K14677; -. DR PhylomeDB; Q03154; -. DR TreeFam; TF313693; -. DR BioCyc; MetaCyc:HS03800-MONOMER; -. DR BRENDA; 3.5.1.14; 2681. DR Reactome; R-HSA-5423646; Aflatoxin activation and detoxification. DR Reactome; R-HSA-5579007; Defective ACY1 causes encephalopathy. DR SABIO-RK; Q03154; -. DR ChiTaRS; ACY1; human. DR EvolutionaryTrace; Q03154; -. DR GeneWiki; ACY1; -. DR GenomeRNAi; 95; -. DR NextBio; 361; -. DR PRO; PR:Q03154; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; Q03154; -. DR CleanEx; HS_ACY1; -. DR ExpressionAtlas; Q03154; baseline and differential. DR Genevisible; Q03154; HS. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0004046; F:aminoacylase activity; TAS:ProtInc. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro. DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. DR Gene3D; 3.30.70.360; -; 1. DR InterPro; IPR001261; ArgE/DapE_CS. DR InterPro; IPR010159; N-acyl_aa_amidohydrolase. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR PIRSF; PIRSF036696; ACY-1; 1. DR SUPFAM; SSF55031; SSF55031; 1. DR TIGRFAMs; TIGR01880; Ac-peptdase-euk; 1. DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1. DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; KW Disease mutation; Hydrolase; Metal-binding; Polymorphism; KW Reference proteome; Zinc. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P37111}. FT CHAIN 2 408 Aminoacylase-1. FT /FTId=PRO_0000185236. FT ACT_SITE 82 82 {ECO:0000250}. FT ACT_SITE 147 147 Proton acceptor. FT {ECO:0000269|PubMed:12933810}. FT METAL 80 80 Zinc 1. FT METAL 113 113 Zinc 1. FT METAL 113 113 Zinc 2. FT METAL 148 148 Zinc 2. FT METAL 175 175 Zinc 1. FT METAL 373 373 Zinc 2. FT VAR_SEQ 32 66 Missing (in isoform 4). {ECO:0000305}. FT /FTId=VSP_046876. FT VAR_SEQ 103 174 Missing (in isoform 2). {ECO:0000305}. FT /FTId=VSP_046877. FT VAR_SEQ 220 284 Missing (in isoform 3). {ECO:0000305}. FT /FTId=VSP_046878. FT VARIANT 179 179 N -> S (in dbSNP:rs887540). FT /FTId=VAR_051805. FT VARIANT 197 197 R -> W (in ACY1D; loss of activity). FT {ECO:0000269|PubMed:17562838, FT ECO:0000269|PubMed:21414403}. FT /FTId=VAR_043113. FT VARIANT 233 233 E -> D (in ACY1D; loss of activity). FT {ECO:0000269|PubMed:16465618, FT ECO:0000269|PubMed:21414403}. FT /FTId=VAR_026104. FT VARIANT 353 353 R -> C (in ACY1D; loss of activity; FT dbSNP:rs121912698). FT {ECO:0000269|PubMed:16274666, FT ECO:0000269|PubMed:16465618, FT ECO:0000269|PubMed:17562838, FT ECO:0000269|PubMed:21414403}. FT /FTId=VAR_026105. FT VARIANT 378 378 R -> Q (in ACY1D). FT {ECO:0000269|PubMed:21414403}. FT /FTId=VAR_065562. FT VARIANT 378 378 R -> W (in ACY1D; slightly reduced FT activity). {ECO:0000269|PubMed:21414403}. FT /FTId=VAR_065563. FT VARIANT 381 381 E -> D (in a breast cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_036076. FT VARIANT 386 386 R -> C (in ACY1D; loss of activity; FT dbSNP:rs2229152). FT {ECO:0000269|PubMed:21414403}. FT /FTId=VAR_020452. FT VARIANT 393 393 R -> H (in ACY1D; dbSNP:rs121912701). FT {ECO:0000269|PubMed:17562838}. FT /FTId=VAR_043114. FT MUTAGEN 80 80 H->A: Almost abolishes enzyme activity. FT {ECO:0000269|PubMed:12933810}. FT MUTAGEN 113 113 D->A: Almost abolishes enzyme activity. FT {ECO:0000269|PubMed:12933810}. FT MUTAGEN 147 147 E->A,Q: Almost abolishes enzyme activity. FT {ECO:0000269|PubMed:12933810}. FT MUTAGEN 147 147 E->D: Decreased protein stability. Loss FT of enzyme activity. FT {ECO:0000269|PubMed:12933810}. FT MUTAGEN 148 148 E->A: Almost abolishes enzyme activity. FT {ECO:0000269|PubMed:12933810}. FT MUTAGEN 175 175 E->A: Almost abolishes enzyme activity. FT {ECO:0000269|PubMed:12933810}. FT MUTAGEN 206 206 H->N: Almost abolishes enzyme activity. FT {ECO:0000269|PubMed:12933810}. FT MUTAGEN 373 373 H->A: Almost abolishes enzyme activity. FT {ECO:0000269|PubMed:12933810}. FT HELIX 11 20 {ECO:0000244|PDB:1Q7L}. FT HELIX 31 45 {ECO:0000244|PDB:1Q7L}. FT STRAND 48 55 {ECO:0000244|PDB:1Q7L}. FT STRAND 58 65 {ECO:0000244|PDB:1Q7L}. FT STRAND 74 80 {ECO:0000244|PDB:1Q7L}. FT HELIX 88 90 {ECO:0000244|PDB:1Q7L}. FT TURN 95 97 {ECO:0000244|PDB:1Q7L}. FT STRAND 104 107 {ECO:0000244|PDB:1Q7L}. FT TURN 109 114 {ECO:0000244|PDB:1Q7L}. FT HELIX 115 130 {ECO:0000244|PDB:1Q7L}. FT STRAND 139 145 {ECO:0000244|PDB:1Q7L}. FT HELIX 147 149 {ECO:0000244|PDB:1Q7L}. FT TURN 152 154 {ECO:0000244|PDB:1Q7L}. FT HELIX 155 158 {ECO:0000244|PDB:1Q7L}. FT HELIX 162 165 {ECO:0000244|PDB:1Q7L}. FT STRAND 169 174 {ECO:0000244|PDB:1Q7L}. FT STRAND 180 188 {ECO:0000244|PDB:1Q7L}. FT HELIX 194 196 {ECO:0000244|PDB:1Q7L}. FT HELIX 322 333 {ECO:0000244|PDB:1Q7L}. FT STRAND 338 342 {ECO:0000244|PDB:1Q7L}. FT HELIX 348 354 {ECO:0000244|PDB:1Q7L}. FT STRAND 359 362 {ECO:0000244|PDB:1Q7L}. FT STRAND 378 380 {ECO:0000244|PDB:1Q7L}. FT HELIX 381 399 {ECO:0000244|PDB:1Q7L}. FT HELIX 405 407 {ECO:0000244|PDB:1Q7L}. SQ SEQUENCE 408 AA; 45885 MW; 293350CD7759826C CRC64; MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE TARQLGLGCQ KVEVAPGYVV TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK DSEGYIYARG AQDMKCVSIQ YLEAVRRLKV EGHRFPRTIH MTFVPDEEVG GHQGMELFVQ RPEFHALRAG FALDEGIANP TDAFTVFYSE RSPWWVRVTS TGRPGHASRF MEDTAAEKLH KVVNSILAFR EKEWQRLQSN PHLKEGSVTS VNLTKLEGGV AYNVIPATMS ASFDFRVAPD VDFKAFEEQL QSWCQAAGEG VTLEFAQKWM HPQVTPTDDS NPWWAAFSRV CKDMNLTLEP EIMPAATDNR YIRAVGVPAL GFSPMNRTPV LLHDHDERLH EAVFLRGVDI YTRLLPALAS VPALPSDS //