MET3_YEAST
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 03-AUG-2022, entry version 200.
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}; OrderedLocusNames=YJR010W;
GN 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};
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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; 48.
DR DIP; DIP-4303N; -.
DR IntAct; P08536; 5.
DR MINT; P08536; -.
DR STRING; 4932.YJR010W; -.
DR iPTMnet; P08536; -.
DR MaxQB; P08536; -.
DR PaxDb; P08536; -.
DR PRIDE; P08536; -.
DR TopDownProteomics; P08536; -.
DR EnsemblFungi; YJR010W_mRNA; YJR010W; YJR010W.
DR GeneID; 853466; -.
DR KEGG; sce:YJR010W; -.
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; LQHMIIR; -.
DR BioCyc; MetaCyc:YJR010W-MON; -.
DR BioCyc; YEAST:YJR010W-MON; -.
DR BRENDA; 2.7.7.4; 984.
DR SABIO-RK; P08536; -.
DR UniPathway; UPA00140; UER00204.
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; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.620; -; 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 Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00339; sopT; 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
