ID   NTE1_YEAST              Reviewed;        1679 AA.
AC   Q04958; D6VZB4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=Lysophospholipase NTE1;
DE            EC=3.1.1.5 {ECO:0000269|PubMed:15044461};
DE   AltName: Full=Intracellular phospholipase B;
DE   AltName: Full=Neuropathy target esterase homolog;
GN   Name=NTE1; OrderedLocusNames=YML059C; ORFNames=YM9958.03C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
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   [3]
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   [4]
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   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACTIVITY REGULATION,
RP   AND MUTAGENESIS OF SER-1406.
RX   PubMed=15044461; DOI=10.1074/jbc.m400830200;
RA   Zaccheo O., Dinsdale D., Meacock P.A., Glynn P.;
RT   "Neuropathy target esterase and its yeast homologue degrade
RT   phosphatidylcholine to glycerophosphocholine in living cells.";
RL   J. Biol. Chem. 279:24024-24033(2004).
RN   [6]
RP   FUNCTION, AND ACTIVITY REGULATION.
RX   PubMed=15611060; DOI=10.1074/jbc.m413999200;
RA   Fernandez-Murray J.P., McMaster C.R.;
RT   "Nte1p-mediated deacylation of phosphatidylcholine functionally interacts
RT   with Sec14p.";
RL   J. Biol. Chem. 280:8544-8552(2005).
RN   [7]
RP   FUNCTION.
RX   PubMed=16777854; DOI=10.1074/jbc.m603548200;
RA   Gaspar M.L., Aregullin M.A., Jesch S.A., Henry S.A.;
RT   "Inositol induces a profound alteration in the pattern and rate of
RT   synthesis and turnover of membrane lipids in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 281:22773-22785(2006).
RN   [8]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634 AND THR-803, AND
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   [11]
RP   FUNCTION.
RX   PubMed=19841481; DOI=10.1074/jbc.m109.063958;
RA   Fernandez-Murray J.P., Gaspard G.J., Jesch S.A., McMaster C.R.;
RT   "NTE1-encoded phosphatidylcholine phospholipase B regulates transcription
RT   of phospholipid biosynthetic genes.";
RL   J. Biol. Chem. 284:36034-36046(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-312; SER-632;
RP   SER-634; SER-653; SER-661; SER-670; SER-680 AND SER-739, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [13]
RP   SUBCELLULAR LOCATION.
RX   PubMed=24868093; DOI=10.1194/jlr.m050229;
RA   Currie E., Guo X., Christiano R., Chitraju C., Kory N., Harrison K.,
RA   Haas J., Walther T.C., Farese R.V. Jr.;
RT   "High-confidence proteomic analysis of yeast lipid droplets identifies
RT   additional droplet proteins and reveals connections to dolichol synthesis
RT   and sterol acetylation.";
RL   J. Lipid Res. 55:1465-1477(2014).
CC   -!- FUNCTION: Intracellular phospholipase B that catalyzes the double
CC       deacylation of phosphatidylcholine (PC) to glycerophosphocholine
CC       (GroPCho). Plays an important role in membrane lipid homeostasis.
CC       Responsible for the rapid PC turnover in response to inositol, elevated
CC       temperatures, or when choline is present in the growth medium
CC       (PubMed:15044461, PubMed:15611060, PubMed:16777854). NTE1 activity
CC       impacts the repressing transcriptional activity of OPI1, the main
CC       regulator of phospholipid synthesis gene transcription
CC       (PubMed:19841481). {ECO:0000269|PubMed:15044461,
CC       ECO:0000269|PubMed:15611060, ECO:0000269|PubMed:16777854,
CC       ECO:0000269|PubMed:19841481}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC         H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC         Evidence={ECO:0000269|PubMed:15044461};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC         Evidence={ECO:0000305|PubMed:15044461};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + 2 H2O = 2 a
CC         carboxylate + 2 H(+) + sn-glycerol 3-phosphocholine;
CC         Xref=Rhea:RHEA:32907, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16870, ChEBI:CHEBI:29067, ChEBI:CHEBI:57643;
CC         Evidence={ECO:0000269|PubMed:15044461};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32908;
CC         Evidence={ECO:0000305|PubMed:15044461};
CC   -!- ACTIVITY REGULATION: Positively regulated by SEC14. Inhibited by
CC       organophosphorus esters in the order phenyl saligenin phosphate (PSP) >
CC       phenyldipentyl phosphinate (PDPP) = diisopropyl fluorophosphate (DFP) >
CC       and paraoxon (PXN). {ECO:0000269|PubMed:15044461,
CC       ECO:0000269|PubMed:15611060}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15044461}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:15044461}. Lipid droplet
CC       {ECO:0000269|PubMed:24868093}.
CC   -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the NTE 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; Z46729; CAA86716.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09838.1; -; Genomic_DNA.
DR   PIR; S49802; S49802.
DR   RefSeq; NP_013652.1; NM_001182418.1.
DR   AlphaFoldDB; Q04958; -.
DR   SMR; Q04958; -.
DR   BioGRID; 35107; 100.
DR   DIP; DIP-5949N; -.
DR   IntAct; Q04958; 16.
DR   MINT; Q04958; -.
DR   STRING; 4932.YML059C; -.
DR   SwissLipids; SLP:000000073; -.
DR   GlyGen; Q04958; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q04958; -.
DR   MaxQB; Q04958; -.
DR   PaxDb; 4932-YML059C; -.
DR   PeptideAtlas; Q04958; -.
DR   TopDownProteomics; Q04958; -.
DR   EnsemblFungi; YML059C_mRNA; YML059C; YML059C.
DR   GeneID; 854943; -.
DR   KEGG; sce:YML059C; -.
DR   AGR; SGD:S000004524; -.
DR   SGD; S000004524; NTE1.
DR   VEuPathDB; FungiDB:YML059C; -.
DR   eggNOG; KOG2968; Eukaryota.
DR   GeneTree; ENSGT00940000168388; -.
DR   HOGENOM; CLU_000960_1_1_1; -.
DR   InParanoid; Q04958; -.
DR   OMA; SSGYVWR; -.
DR   OrthoDB; 5303733at2759; -.
DR   BioCyc; MetaCyc:G3O-32654-MONOMER; -.
DR   BioCyc; YEAST:G3O-32654-MONOMER; -.
DR   Reactome; R-SCE-6814848; Glycerophospholipid catabolism.
DR   BioGRID-ORCS; 854943; 2 hits in 10 CRISPR screens.
DR   PRO; PR:Q04958; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q04958; Protein.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR   GO; GO:0004622; F:lysophospholipase activity; IDA:SGD.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0034638; P:phosphatidylcholine catabolic process; IMP:SGD.
DR   GO; GO:0071071; P:regulation of phospholipid biosynthetic process; IMP:SGD.
DR   CDD; cd00038; CAP_ED; 2.
DR   CDD; cd07227; Pat_Fungal_NTE1; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 2.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 3.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
DR   InterPro; IPR001423; LysoPLipase_patatin_CS.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   PANTHER; PTHR14226:SF29; NEUROPATHY TARGET ESTERASE SWS; 1.
DR   PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 3.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS51635; PNPLA; 1.
DR   PROSITE; PS01237; UPF0028; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Hydrolase; Lipid degradation; Lipid droplet;
KW   Lipid metabolism; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..1679
FT                   /note="Lysophospholipase NTE1"
FT                   /id="PRO_0000172528"
FT   TOPO_DOM        1..49
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:16847258"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..103
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:16847258"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..1679
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:16847258"
FT   DOMAIN          1373..1537
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          261..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          498..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          775..800
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          855..882
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           1377..1382
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1404..1408
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           1524..1526
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        261..276
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..295
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        855..876
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1406
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        1524
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   BINDING         803..947
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="1"
FT   BINDING         943..1074
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /ligand_label="2"
FT   MOD_RES         300
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         312
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         632
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         634
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         653
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         661
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         670
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         680
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         739
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         803
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         1406
FT                   /note="S->A: Loss of esterase activity."
FT                   /evidence="ECO:0000269|PubMed:15044461"
SQ   SEQUENCE   1679 AA;  187133 MW;  550FFCD4ACAF8E25 CRC64;
     MRSMNCTTNN TNNTGQNTKN SLGSSFNSSN YTSYRFQTCL TDQIISEAQT WSLSSLFNFS
     WVVSYFVMGA SRMIFRYGWY LATLSLLRIP KWIFFKLHHV QFTLSFWLIL FALAVIVFVT
     YTIMKERILS QYKRLTPEFL PLENTGKSGS SANINAASTQ SANAPPAIGS STTGASSIID
     SKKHSLKDGN ENETFLSSYL DQFLSAIKIF GYLEKPVFHD LTKNMKTQKM DEGEILLLDS
     TIGFAIVVEG TLQLYHEVDH SDKDHGDETD HSDTDGLDDQ DRDEEDEEED DDIDNYDTKS
     CSSNLIDEED ESVGYIHLKN GLGNFQLLNT VKPGNPLTSL VSILNLFTHS MSSYGNSNFP
     SELSSPIDTT VSVNNMFCSS EQNFSNTDSM TNSTNSFPTF PSSMPKLVAR AATDCTIGII
     PPQSFAKLTA KYPRSASHII QMVLTKLYHV TFQTAHDYLG LTKEIMDIEV LLNKSIVYEL
     PYYLKEAVIR KFKTVDKSSG SADLEPKPKN SNASSKLKKP PKAKPSDGII QSLKIANANA
     NTSSNSLSLK PEFTHHPSSR HVVLGSRDQF NPGDLLSNVP LSRTMDILSP NPIHNNNRNK
     SNGINTSTSN QHKRSSRSSS NNASVHSKKF SSLSPELRNA QLSTSPLSLD NTSVHDHIHP
     SPVHLKGRVS PRPNLLPTTS FSAAQEETED SALRMALVEA MLTYLGVNKS NMSVSSSSIA
     NMSSLNSPQL NEMYSRRPSN ASFLMSPHCT PSDISVASSF ASPQTQPTML RILPKEYTIS
     NKRHNKSKSQ DKKKPRAYKE ELTPNLDFED VKKDFAQGIQ LKFFKKGTTI VEQNARGKGL
     FYIISGKVNV TTNSSSSVVS SMSKPEQVSA QSSHKGENPH HTQHLLYSVG SGGIVGYLSS
     LIGYKSFVNI VAKSDVYVGF LSSATLERLF DKYFLIYLRI SDSLTKLLSS RLLKLDHALE
     WVHLRASETL FSQGDSANGI YVVLNGRLRQ LQQQSLSNSN TSSEEVETQN IILGELAQGE
     SFGEVEVLTA MNRYSTIVAV RDSELARIPR TLFELLALEH PSIMIRVSRL VAKKIVGDRT
     VPALTGDPLS IKENDFTSLI PPTKASYSSS LSHKPQNITS GTITFRTITI LPITSGLPVE
     AFAMKLVQAF KQVGRTTIGL NQRTTLTHLG RHAFDRLSKL KQSGYFAELE EMYQTVVYIS
     DTPVKSNWTR TCIAQGDCIL LLADARSPSA EIGEYEKLLL NSKTTARTEL ILLHPERYVE
     PGLTHKWLRY RPWVHSHHHI QFSLTGTTLM NEGKMHVLNN GALALMDKLI QTEFSRKTQQ
     NISKLLPDSI KNTVENFSSR FMKSKRQYYT PVHRHKNDFL RLARILSGQA IGLVLGGGGA
     RGISHLGVIQ AIEEQGIPVD VIGGTSIGSF VGGLYAKDYD LVPIYGRVKK FAGRISSIWR
     MLTDLTWPVT SYTTGHEFNR GIWKTFGDTR IEDFWIQYYC NSTNITDSVQ EIHSFGYAWR
     YIRASMSLAG LLPPLEENGS MLLDGGYVDN LPVTEMRARG CQTIFAVDVG SADDRTPMEY
     GDSLNGFWII FNRWNPFSSH PNIPNMAEIQ VRLGYVASVN ALEKAKNTPG VVYVRPPIEE
     YATLDFSKFE EIYHVGVDYG RIFLQGLIDD DKMPYIPGSQ ETTLNSQVPE FLLHRRNSI
//