DPP1_YEAST
ID DPP1_YEAST Reviewed; 289 AA.
AC Q05521; D6VSR4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Diacylglycerol pyrophosphate phosphatase 1 {ECO:0000303|PubMed:8567632, ECO:0000303|PubMed:9452443};
DE Short=DGPP phosphatase;
DE EC=3.1.3.81;
DE AltName: Full=Lysophosphatidate phosphatase;
DE EC=3.1.3.106;
DE AltName: Full=Phosphatidate phosphatase;
DE EC=3.1.3.4;
GN Name=DPP1; Synonyms=ZRG1; OrderedLocusNames=YDR284C;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 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 [4]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=8567632; DOI=10.1074/jbc.271.4.1868;
RA Wu W.-I., Liu Y., Riedel B., Wissing J.B., Fischl A.S., Carman G.M.;
RT "Purification and characterization of diacylglycerol pyrophosphate
RT phosphatase from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 271:1868-1876(1996).
RN [5]
RP SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8940025; DOI=10.1074/jbc.271.48.30548;
RA Dillon D.A., Wu W.I., Riedel B., Wissing J.B., Dowhan W., Carman G.M.;
RT "The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate
RT phosphatase activity.";
RL J. Biol. Chem. 271:30548-30553(1996).
RN [6]
RP FUNCTION.
RX PubMed=9452443; DOI=10.1074/jbc.273.6.3278;
RA Toke D.A., Bennett W.L., Dillon D.A., Wu W.I., Chen X., Ostrander D.B.,
RA Oshiro J., Cremesti A., Voelker D.R., Fischl A.S., Carman G.M.;
RT "Isolation and characterization of the Saccharomyces cerevisiae DPP1 gene
RT encoding diacylglycerol pyrophosphate phosphatase.";
RL J. Biol. Chem. 273:3278-3284(1998).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10329682; DOI=10.1074/jbc.274.21.14831;
RA Faulkner A., Chen X., Rush J., Horazdovsky B., Waechter C.J., Carman G.M.,
RA Sternweis P.C.;
RT "The LPP1 and DPP1 gene products account for most of the isoprenoid
RT phosphate phosphatase activities in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 274:14831-14837(1999).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=11139591; DOI=10.1074/jbc.m011421200;
RA Han G.-S., Johnston C.N., Chen X., Athenstaedt K., Daum G., Carman G.M.;
RT "Regulation of the Saccharomyces cerevisiae DPP1-encoded diacylglycerol
RT pyrophosphate phosphatase by zinc.";
RL J. Biol. Chem. 276:10126-10133(2001).
RN [9]
RP INDUCTION.
RX PubMed=12799368; DOI=10.1074/jbc.m305452200;
RA Oshiro J., Han G.-S., Iwanyshyn W.M., Conover K., Carman G.M.;
RT "Regulation of the yeast DPP1-encoded diacylglycerol pyrophosphate
RT phosphatase by transcription factor Gis1p.";
RL J. Biol. Chem. 278:31495-31503(2003).
RN [10]
RP TOPOLOGY, AND PHOSPHATASE SEQUENCE MOTIF.
RX PubMed=14630917; DOI=10.1074/jbc.m311779200;
RA Han G.-S., Johnston C.N., Carman G.M.;
RT "Vacuole membrane topography of the DPP1-encoded diacylglycerol
RT pyrophosphate phosphatase catalytic site from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 279:5338-5345(2004).
RN [11]
RP MUTAGENESIS OF ARG-125; HIS-169 AND HIS-223.
RX PubMed=10545184; DOI=10.1021/bi991472x;
RA Toke D.A., McClintick M.L., Carman G.M.;
RT "Mutagenesis of the phosphatase sequence motif in diacylglycerol
RT pyrophosphate phosphatase from Saccharomyces cerevisiae.";
RL Biochemistry 38:14606-14613(1999).
RN [12]
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 [13]
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 [14]
RP REVIEW, AND INDUCTION.
RX PubMed=14642771; DOI=10.1016/j.bbalip.2003.10.002;
RA Oshiro J., Han G.-S., Carman G.M.;
RT "Diacylglycerol pyrophosphate phosphatase in Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1635:1-9(2003).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION BY
RP 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Catalyzes the dephosphorylation of diacylglycerol diphosphate
CC (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA
CC to diacylglycerol (DAG). Together with LPP1, regulates intracellular
CC DGPP and PA levels, which are phospholipid molecules believed to play a
CC signaling role in stress response. Can also use lysophosphatidic acid
CC (LPA) and phosphatidylglycerophosphate as substrates. Substrate
CC preference is DGPP > LPA > PA. Activity is independent of a divalent
CC cation ion and insensitive to inhibition by N-ethylmaleimide.
CC {ECO:0000269|PubMed:10329682, ECO:0000269|PubMed:11139591,
CC ECO:0000269|PubMed:8567632, ECO:0000269|PubMed:8940025,
CC ECO:0000269|PubMed:9452443}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:27449,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.1.3.81;
CC Evidence={ECO:0000269|PubMed:10329682, ECO:0000269|PubMed:8567632,
CC ECO:0000269|PubMed:8940025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27450;
CC Evidence={ECO:0000305|PubMed:10329682, ECO:0000305|PubMed:8567632,
CC ECO:0000305|PubMed:8940025};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC Evidence={ECO:0000269|PubMed:8567632, ECO:0000269|PubMed:8940025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC Evidence={ECO:0000305|PubMed:8567632, ECO:0000305|PubMed:8940025};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycerol +
CC phosphate; Xref=Rhea:RHEA:33155, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57970, ChEBI:CHEBI:64683;
CC EC=3.1.3.106; Evidence={ECO:0000269|PubMed:8940025};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33156;
CC Evidence={ECO:0000305|PubMed:8940025};
CC -!- ACTIVITY REGULATION: Inhibited by sodium fluoride (NaF) and
CC pyrophosphate. Strongly inhibited by manganese ion and, to a lower
CC extent, by magnesium and calcium ions. Also inhibited by Cu(2+) ion. In
CC an indirect manner, it is also inhibited by the zinc ion which is able
CC to form a complex with DGPP and prevent the enzyme from removing the
CC phosphate from the substrate. Not inhibited by N-ethylmaleimide.
CC {ECO:0000269|PubMed:11139591, ECO:0000269|PubMed:8567632}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=167 umol/min/mg enzyme with lysophosphatidic acid as substrate
CC {ECO:0000269|PubMed:8940025};
CC pH dependence:
CC Optimum pH is 6.0-8.5 (PubMed:8940025). Optimum pH for
CC geranylgeranyl-P-P phosphatase reaction is 5.0-5.5 (PubMed:10329682).
CC {ECO:0000269|PubMed:10329682, ECO:0000269|PubMed:8940025};
CC -!- INTERACTION:
CC Q05521; Q05521: DPP1; NbExp=3; IntAct=EBI-2054360, EBI-2054360;
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:11139591,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8567632}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:11139591,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8567632}.
CC -!- INDUCTION: Induced by the transcription factor ZAP1 during zinc
CC depletion and negatively regulated by the transcription factor GIS1
CC predominantly during nutrient limitation. Induced by inositol
CC supplementation. {ECO:0000269|PubMed:11139591,
CC ECO:0000269|PubMed:12799368, ECO:0000269|PubMed:14642771}.
CC -!- DOMAIN: The phosphatase sequence motif I (including Arg-125) and II
CC (including His-169) are part of the cytoplasmic loop 2 and phosphatase
CC sequence motif III (including His-223) is part of the cytoplasmic loop
CC 3.
CC -!- MISCELLANEOUS: Present with 3038 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC family. {ECO:0000305}.
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DR EMBL; U51031; AAB64475.1; -; Genomic_DNA.
DR EMBL; AY557744; AAS56070.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12124.1; -; Genomic_DNA.
DR PIR; S70114; S70114.
DR RefSeq; NP_010570.1; NM_001180592.1.
DR AlphaFoldDB; Q05521; -.
DR BioGRID; 32337; 65.
DR DIP; DIP-8807N; -.
DR IntAct; Q05521; 11.
DR MINT; Q05521; -.
DR STRING; 4932.YDR284C; -.
DR SwissLipids; SLP:000000057; -.
DR TCDB; 9.B.105.3.2; the lead resistance fusion protein (pbrbc) family.
DR iPTMnet; Q05521; -.
DR MaxQB; Q05521; -.
DR PaxDb; Q05521; -.
DR PRIDE; Q05521; -.
DR TopDownProteomics; Q05521; -.
DR DNASU; 851878; -.
DR EnsemblFungi; YDR284C_mRNA; YDR284C; YDR284C.
DR GeneID; 851878; -.
DR KEGG; sce:YDR284C; -.
DR SGD; S000002692; DPP1.
DR VEuPathDB; FungiDB:YDR284C; -.
DR eggNOG; KOG3030; Eukaryota.
DR GeneTree; ENSGT00940000174574; -.
DR HOGENOM; CLU_021458_6_1_1; -.
DR InParanoid; Q05521; -.
DR OMA; CTPLIVI; -.
DR BioCyc; MetaCyc:YDR284C-MON; -.
DR BioCyc; YEAST:YDR284C-MON; -.
DR BRENDA; 3.1.3.81; 984.
DR Reactome; R-SCE-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-SCE-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-SCE-419408; Lysosphingolipid and LPA receptors.
DR PRO; PR:Q05521; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q05521; protein.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000810; F:diacylglycerol diphosphate phosphatase activity; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:SGD.
DR GO; GO:0006644; P:phospholipid metabolic process; IMP:SGD.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043216; PA_PP_rel.
DR PANTHER; PTHR10165; PTHR10165; 1.
DR Pfam; PF01569; PAP2; 1.
DR SMART; SM00014; acidPPc; 1.
DR SUPFAM; SSF48317; SSF48317; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Vacuole.
FT CHAIN 1..289
FT /note="Diacylglycerol pyrophosphate phosphatase 1"
FT /id="PRO_0000220918"
FT TOPO_DOM 1..21
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..92
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..289
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT REGION 118..126
FT /note="Phosphatase sequence motif I"
FT REGION 166..169
FT /note="Phosphatase sequence motif II"
FT REGION 216..227
FT /note="Phosphatase sequence motif III"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 125
FT /note="R->A: Complete loss of DGPP phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10545184"
FT MUTAGEN 169
FT /note="H->A: 91% decrease of DGPP phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10545184"
FT MUTAGEN 223
FT /note="H->A: Complete loss of DGPP phosphatase activity."
FT /evidence="ECO:0000269|PubMed:10545184"
SQ SEQUENCE 289 AA; 33514 MW; 9CBEA0D7A0F0E13A CRC64;
MNRVSFIKTP FNIGAKWRLE DVFLLIIMIL LNYPVYYQQP FERQFYINDL TISHPYATTE
RVNNNMLFVY SFVVPSLTIL IIGSILADRR HLIFILYTSL LGLSLAWFST SFFTNFIKNW
IGRLRPDFLD RCQPVEGLPL DTLFTAKDVC TTKNHERLLD GFRTTPSGHS SESFAGLGYL
YFWLCGQLLT ESPLMPLWRK MVAFLPLLGA ALIALSRTQD YRHHFVDVIL GSMLGYIMAH
FFYRRIFPPI DDPLPFKPLM DDSDVTLEEA VTHQRIPDEE LHPLSDEGM
