ID MET3_YEAST Reviewed; 511 AA. AC P08536; D6VWI5; Q66R66; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2006, sequence version 2. DT 27-MAR-2024, entry version 207. DE RecName: Full=Sulfate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_03106}; DE EC=2.7.7.4 {ECO:0000255|HAMAP-Rule:MF_03106}; DE AltName: Full=ATP-sulfurylase {ECO:0000255|HAMAP-Rule:MF_03106}; DE AltName: Full=Methionine-requiring protein 3 {ECO:0000255|HAMAP-Rule:MF_03106}; DE AltName: Full=Sulfate adenylate transferase {ECO:0000255|HAMAP-Rule:MF_03106}; DE Short=SAT {ECO:0000255|HAMAP-Rule:MF_03106}; GN Name=MET3 {ECO:0000255|HAMAP-Rule:MF_03106}; GN OrderedLocusNames=YJR010W; ORFNames=J1436; 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]. RC STRAIN=FL100A; RX PubMed=3325778; DOI=10.1007/bf00325699; RA Cherest H., Kerjan P., Surdin-Kerjan Y.; RT "The Saccharomyces cerevisiae MET3 gene: nucleotide sequence and RT relationship of the 5' non-coding region to that of MET25."; RL Mol. Gen. Genet. 210:307-313(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=1789010; DOI=10.1002/yea.320070814; RA Mountain H.A., Korch C.; RT "TDH2 is linked to MET3 on chromosome X of Saccharomyces cerevisiae."; RL Yeast 7:873-880(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x; RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.; RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."; RL EMBO J. 15:2031-2049(1996). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [6] RP INDUCTION. RX PubMed=9799240; DOI=10.1093/emboj/17.21.6327; RA Blaiseau P.L., Thomas D.; RT "Multiple transcriptional activation complexes tether the yeast activator RT Met4 to DNA."; RL EMBO J. 17:6327-6336(1998). RN [7] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [8] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, RP SUBUNIT, DOMAIN, AND ACTIVE SITE. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=11157739; DOI=10.1093/emboj/20.3.316; RA Ullrich T.C., Blaesse M., Huber R.; RT "Crystal structure of ATP sulfurylase from Saccharomyces cerevisiae, a key RT enzyme in sulfate activation."; RL EMBO J. 20:316-329(2001). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 2-393 IN COMPLEX WITH SUBSTRATE RP ANALOGS, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DOMAIN, AND ACTIVE SITE. RX PubMed=14983089; DOI=10.1093/protein/gzg133; RA Lalor D.J., Schnyder T., Saridakis V., Pilloff D.E., Dong A., Tang H., RA Leyh T.S., Pai E.F.; RT "Structural and functional analysis of a truncated form of Saccharomyces RT cerevisiae ATP sulfurylase: C-terminal domain essential for oligomer RT formation but not for activity."; RL Protein Eng. 16:1071-1079(2003). CC -!- FUNCTION: Catalyzes the first intracellular reaction of sulfate CC assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic CC sulfate and ATP. Plays an important role in sulfate activation as a CC component of the biosynthesis pathway of sulfur-containing amino acids. CC {ECO:0000255|HAMAP-Rule:MF_03106}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + CC diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03106}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.65 mM for Sulfate {ECO:0000269|PubMed:14983089}; CC KM=0.082 mM for ATP {ECO:0000269|PubMed:14983089}; CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from CC sulfate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_03106}. CC -!- SUBUNIT: Homohexamer. Dimer of trimers. {ECO:0000255|HAMAP- CC Rule:MF_03106, ECO:0000269|PubMed:11157739, CC ECO:0000269|PubMed:14983089}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03106, CC ECO:0000269|PubMed:14562095}. CC -!- INDUCTION: Expression depends on the formation of the MET4-MET28-MET31 CC and MET4-MET28-MET32 complexes on its 5' upstream region. CC {ECO:0000269|PubMed:9799240}. CC -!- DOMAIN: The oligomerization domain is distantly related to APS kinases, CC but it is not functional and does not bind APS. It is required for CC oligomerization of the enzyme, although the oligomerization state has CC no effect on the catalytic activity of the enzyme. {ECO:0000255|HAMAP- CC Rule:MF_03106, ECO:0000269|PubMed:11157739, CC ECO:0000269|PubMed:14983089}. CC -!- MISCELLANEOUS: Present with 1510 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the sulfate adenylyltransferase family. CC {ECO:0000255|HAMAP-Rule:MF_03106}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA29702.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAA42726.1; Type=Frameshift; Evidence={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; X06413; CAA29702.1; ALT_FRAME; Genomic_DNA. DR EMBL; X60157; CAA42726.1; ALT_FRAME; Genomic_DNA. DR EMBL; X87611; CAA60932.1; -; Genomic_DNA. DR EMBL; Z49510; CAA89532.1; -; Genomic_DNA. DR EMBL; AY723835; AAU09752.1; -; Genomic_DNA. DR EMBL; BK006943; DAA08801.1; -; Genomic_DNA. DR PIR; S55198; S55198. DR RefSeq; NP_012543.3; NM_001181668.3. DR PDB; 1G8F; X-ray; 1.95 A; A=1-511. DR PDB; 1G8G; X-ray; 2.60 A; A/B=1-511. DR PDB; 1G8H; X-ray; 2.80 A; A/B=1-511. DR PDB; 1J70; X-ray; 2.30 A; A/B/C=1-511. DR PDB; 1JEC; X-ray; 2.50 A; A=2-511. DR PDB; 1JED; X-ray; 2.95 A; A/B=2-511. DR PDB; 1JEE; X-ray; 2.80 A; A/B=2-511. DR PDB; 1R6X; X-ray; 1.40 A; A=2-393. DR PDBsum; 1G8F; -. DR PDBsum; 1G8G; -. DR PDBsum; 1G8H; -. DR PDBsum; 1J70; -. DR PDBsum; 1JEC; -. DR PDBsum; 1JED; -. DR PDBsum; 1JEE; -. DR PDBsum; 1R6X; -. DR AlphaFoldDB; P08536; -. DR SMR; P08536; -. DR BioGRID; 33766; 52. DR DIP; DIP-4303N; -. DR IntAct; P08536; 5. DR MINT; P08536; -. DR STRING; 4932.YJR010W; -. DR GlyGen; P08536; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; P08536; -. DR MaxQB; P08536; -. DR PaxDb; 4932-YJR010W; -. DR PeptideAtlas; P08536; -. DR TopDownProteomics; P08536; -. DR EnsemblFungi; YJR010W_mRNA; YJR010W; YJR010W. DR GeneID; 853466; -. DR KEGG; sce:YJR010W; -. DR AGR; SGD:S000003771; -. DR SGD; S000003771; MET3. DR VEuPathDB; FungiDB:YJR010W; -. DR eggNOG; KOG0636; Eukaryota. DR GeneTree; ENSGT00390000009613; -. DR HOGENOM; CLU_022950_1_0_1; -. DR InParanoid; P08536; -. DR OMA; EWFSFPE; -. DR OrthoDB; 159at2759; -. DR BioCyc; MetaCyc:YJR010W-MONOMER; -. DR BioCyc; YEAST:YJR010W-MONOMER; -. DR BRENDA; 2.7.7.4; 984. DR SABIO-RK; P08536; -. DR UniPathway; UPA00140; UER00204. DR BioGRID-ORCS; 853466; 3 hits in 10 CRISPR screens. DR EvolutionaryTrace; P08536; -. DR PRO; PR:P08536; -. DR Proteomes; UP000002311; Chromosome X. DR RNAct; P08536; Protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IDA:SGD. DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0010134; P:sulfate assimilation via adenylyl sulfate reduction; IBA:GO_Central. DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IMP:SGD. DR GO; GO:0000096; P:sulfur amino acid metabolic process; IMP:SGD. DR CDD; cd00517; ATPS; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 3.10.400.10; Sulfate adenylyltransferase; 1. DR HAMAP; MF_03106; Sulf_adenylyltr_euk; 1. DR InterPro; IPR025980; ATP-Sase_PUA-like_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR015947; PUA-like_sf. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR027535; Sulf_adenylyltr_euk. DR InterPro; IPR024951; Sulfurylase_cat_dom. DR InterPro; IPR002650; Sulphate_adenylyltransferase. DR NCBIfam; TIGR00339; sopT; 1. DR PANTHER; PTHR42700; SULFATE ADENYLYLTRANSFERASE; 1. DR PANTHER; PTHR42700:SF1; SULFATE ADENYLYLTRANSFERASE; 1. DR Pfam; PF01747; ATP-sulfurylase; 1. DR Pfam; PF14306; PUA_2; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF88697; PUA domain-like; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cytoplasm; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1..511 FT /note="Sulfate adenylyltransferase" FT /id="PRO_0000105954" FT REGION 1..167 FT /note="N-terminal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106, FT ECO:0000305|PubMed:11157739" FT REGION 168..393 FT /note="Catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106, FT ECO:0000305|PubMed:11157739" FT REGION 394..511 FT /note="Required for oligomerization; adenylyl-sulfate FT kinase-like" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106, FT ECO:0000305|PubMed:14983089" FT ACT_SITE 196 FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106, FT ECO:0000305|PubMed:11157739" FT ACT_SITE 197 FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106, FT ECO:0000305|PubMed:11157739" FT ACT_SITE 198 FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106, FT ECO:0000305|PubMed:11157739" FT BINDING 195..198 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106, FT ECO:0000269|PubMed:11157739" FT BINDING 195 FT /ligand="sulfate" FT /ligand_id="ChEBI:CHEBI:16189" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106, FT ECO:0000269|PubMed:11157739" FT BINDING 197 FT /ligand="sulfate" FT /ligand_id="ChEBI:CHEBI:16189" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106, FT ECO:0000269|PubMed:11157739" FT BINDING 289..292 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106, FT ECO:0000269|PubMed:11157739" FT BINDING 293 FT /ligand="sulfate" FT /ligand_id="ChEBI:CHEBI:16189" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106, FT ECO:0000269|PubMed:11157739" FT BINDING 331 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106, FT ECO:0000269|PubMed:11157739" FT SITE 201 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106, FT ECO:0000305|PubMed:11157739" FT SITE 204 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106, FT ECO:0000305|PubMed:11157739" FT SITE 328 FT /note="Induces change in substrate recognition on ATP FT binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03106, FT ECO:0000305|PubMed:11157739" FT CONFLICT 221 FT /note="I -> T (in Ref. 5; AAU09752)" FT /evidence="ECO:0000305" FT HELIX 12..15 FT /evidence="ECO:0007829|PDB:1R6X" FT HELIX 17..19 FT /evidence="ECO:0007829|PDB:1R6X" FT HELIX 20..27 FT /evidence="ECO:0007829|PDB:1R6X" FT STRAND 32..36 FT /evidence="ECO:0007829|PDB:1R6X" FT HELIX 39..49 FT /evidence="ECO:0007829|PDB:1R6X" FT TURN 51..55 FT /evidence="ECO:0007829|PDB:1R6X" FT HELIX 62..71 FT /evidence="ECO:0007829|PDB:1R6X" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:1R6X" FT HELIX 90..94 FT /evidence="ECO:0007829|PDB:1R6X" FT STRAND 101..106 FT /evidence="ECO:0007829|PDB:1R6X" FT TURN 107..109 FT /evidence="ECO:0007829|PDB:1R6X" FT STRAND 110..121 FT /evidence="ECO:0007829|PDB:1R6X" FT HELIX 125..133 FT /evidence="ECO:0007829|PDB:1R6X" FT HELIX 140..147 FT /evidence="ECO:0007829|PDB:1R6X" FT STRAND 151..161 FT /evidence="ECO:0007829|PDB:1R6X" FT TURN 170..172 FT /evidence="ECO:0007829|PDB:1G8F" FT HELIX 176..185 FT /evidence="ECO:0007829|PDB:1R6X" FT STRAND 191..194 FT /evidence="ECO:0007829|PDB:1R6X" FT HELIX 202..214 FT /evidence="ECO:0007829|PDB:1R6X" FT STRAND 218..221 FT /evidence="ECO:0007829|PDB:1R6X" FT HELIX 235..245 FT /evidence="ECO:0007829|PDB:1R6X" FT HELIX 246..248 FT /evidence="ECO:0007829|PDB:1R6X" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:1R6X" FT HELIX 267..280 FT /evidence="ECO:0007829|PDB:1R6X" FT STRAND 284..288 FT /evidence="ECO:0007829|PDB:1R6X" FT TURN 290..293 FT /evidence="ECO:0007829|PDB:1R6X" FT STRAND 303..305 FT /evidence="ECO:0007829|PDB:1R6X" FT HELIX 309..321 FT /evidence="ECO:0007829|PDB:1R6X" FT STRAND 324..327 FT /evidence="ECO:0007829|PDB:1R6X" FT STRAND 331..334 FT /evidence="ECO:0007829|PDB:1R6X" FT HELIX 335..337 FT /evidence="ECO:0007829|PDB:1R6X" FT STRAND 339..342 FT /evidence="ECO:0007829|PDB:1R6X" FT TURN 343..345 FT /evidence="ECO:0007829|PDB:1R6X" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:1R6X" FT HELIX 358..366 FT /evidence="ECO:0007829|PDB:1R6X" FT TURN 373..375 FT /evidence="ECO:0007829|PDB:1R6X" FT HELIX 378..384 FT /evidence="ECO:0007829|PDB:1R6X" FT HELIX 391..393 FT /evidence="ECO:0007829|PDB:1G8F" FT STRAND 396..400 FT /evidence="ECO:0007829|PDB:1G8F" FT HELIX 408..419 FT /evidence="ECO:0007829|PDB:1G8F" FT STRAND 428..430 FT /evidence="ECO:0007829|PDB:1G8F" FT HELIX 437..440 FT /evidence="ECO:0007829|PDB:1G8F" FT HELIX 443..448 FT /evidence="ECO:0007829|PDB:1G8F" FT STRAND 452..457 FT /evidence="ECO:0007829|PDB:1G8F" FT HELIX 461..466 FT /evidence="ECO:0007829|PDB:1G8F" FT STRAND 472..478 FT /evidence="ECO:0007829|PDB:1G8F" FT STRAND 482..484 FT /evidence="ECO:0007829|PDB:1G8F" FT HELIX 492..505 FT /evidence="ECO:0007829|PDB:1G8F" SQ SEQUENCE 511 AA; 57725 MW; A1E7B994A9C24DFD CRC64; MPAPHGGILQ DLIARDALKK NELLSEAQSS DILVWNLTPR QLCDIELILN GGFSPLTGFL NENDYSSVVT DSRLADGTLW TIPITLDVDE AFANQIKPDT RIALFQDDEI PIAILTVQDV YKPNKTIEAE KVFRGDPEHP AISYLFNVAG DYYVGGSLEA IQLPQHYDYP GLRKTPAQLR LEFQSRQWDR VVAFQTRNPM HRAHRELTVR AAREANAKVL IHPVVGLTKP GDIDHHTRVR VYQEIIKRYP NGIAFLSLLP LAMRMSGDRE AVWHAIIRKN YGASHFIVGR DHAGPGKNSK GVDFYGPYDA QELVESYKHE LDIEVVPFRM VTYLPDEDRY APIDQIDTTK TRTLNISGTE LRRRLRVGGE IPEWFSYPEV VKILRESNPP RPKQGFSIVL GNSLTVSREQ LSIALLSTFL QFGGGRYYKI FEHNNKTELL SLIQDFIGSG SGLIIPNQWE DDKDSVVGKQ NVYLLDTSSS ADIQLESADE PISHIVQKVV LFLEDNGFFV F //