GPT2_YEAST
ID GPT2_YEAST Reviewed; 743 AA.
AC P36148; D6VXC8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Glycerol-3-phosphate O-acyltransferase 2;
DE Short=G-3-P acyltransferase 2;
DE Short=GPAT 2;
DE EC=2.3.1.15 {ECO:0000269|PubMed:11544256};
DE AltName: Full=Dihydroxyacetone phosphate acyltransferase 2;
DE Short=DHAP-AT 2;
DE EC=2.3.1.42 {ECO:0000269|PubMed:11544256};
DE AltName: Full=Glycerol-3-phosphate / dihydroxyacetone phosphate acyltransferase 2;
GN Name=GPT2; Synonyms=GAT1 {ECO:0000303|PubMed:11544256};
GN OrderedLocusNames=YKR067W;
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF GLY-262.
RC STRAIN=ATCC 204660 / DBY746;
RX PubMed=11544256; DOI=10.1074/jbc.m104749200;
RA Zheng Z., Zou J.;
RT "The initial step of the glycerolipid pathway: identification of glycerol-
RT 3-phosphate / dihydroxyacetone phosphate dual substrate acyltransferases in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 276:41710-41716(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=9401016; DOI=10.1128/jb.179.24.7611-7616.1997;
RA Athenstaedt K., Daum G.;
RT "Biosynthesis of phosphatidic acid in lipid particles and endoplasmic
RT reticulum of Saccharomyces cerevisiae.";
RL J. Bacteriol. 179:7611-7616(1997).
RN [5]
RP FUNCTION.
RX PubMed=10049376; DOI=10.1128/jb.181.5.1458-1463.1999;
RA Athenstaedt K., Weys S., Paltauf F., Daum G.;
RT "Redundant systems of phosphatidic acid biosynthesis via acylation of
RT glycerol-3-phosphate or dihydroxyacetone phosphate in the yeast
RT Saccharomyces cerevisiae.";
RL J. Bacteriol. 181:1458-1463(1999).
RN [6]
RP FUNCTION.
RX PubMed=12167660; DOI=10.1074/jbc.m207753200;
RA Zaremberg V., McMaster C.R.;
RT "Differential partitioning of lipids metabolized by separate yeast
RT glycerol-3-phosphate acyltransferases reveals that phospholipase D
RT generation of phosphatidic acid mediates sensitivity to choline-containing
RT lysolipids and drugs.";
RL J. Biol. Chem. 277:39035-39044(2002).
RN [7]
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 [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-654; SER-668 AND SER-671, AND
RP IDENTIFICATION BY 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 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 SUBCELLULAR LOCATION.
RX PubMed=19525420; DOI=10.1128/ec.00085-09;
RA Bratschi M.W., Burrowes D.P., Kulaga A., Cheung J.F., Alvarez A.L.,
RA Kearley J., Zaremberg V.;
RT "Glycerol-3-phosphate acyltransferases gat1p and gat2p are microsomal
RT phosphoproteins with differential contributions to polarized cell growth.";
RL Eukaryot. Cell 8:1184-1196(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632; SER-637; SER-647;
RP SER-651; SER-654; SER-657; SER-664; SER-668; SER-671; THR-673; SER-688;
RP THR-692 AND SER-693, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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=22267742; DOI=10.1074/jbc.m111.314112;
RA Marr N., Foglia J., Terebiznik M., Athenstaedt K., Zaremberg V.;
RT "Controlling lipid fluxes at glycerol-3-phosphate acyltransferase step in
RT yeast: unique contribution of Gat1p to oleic acid-induced lipid particle
RT formation.";
RL J. Biol. Chem. 287:10251-10264(2012).
RN [14]
RP TOPOLOGY.
RX PubMed=29073188; DOI=10.1371/journal.pone.0186840;
RA Debelyy M.O., Waridel P., Quadroni M., Schneiter R., Conzelmann A.;
RT "Chemical crosslinking and mass spectrometry to elucidate the topology of
RT integral membrane proteins.";
RL PLoS ONE 12:e0186840-e0186840(2017).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-664; SER-668 AND
RP SER-671, AND PHOSPHORYLATION AT SER-664; SER-668 AND SER-671.
RX PubMed=31421179; DOI=10.1016/j.bbalip.2019.08.005;
RA Kiegerl B., Tavassoli M., Smart H., Shabits B.N., Zaremberg V.,
RA Athenstaedt K.;
RT "Phosphorylation of the lipid droplet localized glycerol-3-phosphate
RT acyltransferase Gpt2 prevents a futile triacylglycerol cycle in yeast.";
RL Biochim. Biophys. Acta 1864:158509-158509(2019).
CC -!- FUNCTION: Dual substrate-specific glycerol-3-phosphate/dihydroxyacetone
CC phosphate sn-1 acyltransferase, catalyzing the first and committed
CC reaction in the de novo synthesis of glycerophospholipids and
CC triacylglycerols (TAGs). Can use both Gly-3-P and dihydroxyacetone
CC phosphate with similar efficiencies and has a broad fatty acyl-CoA
CC specificity profile. Transfers a fatty acid from fatty acyl-CoA to the
CC sn-1 position of glycerol-3-phosphate to produce lysophosphatidic acid
CC (LysoPA). These lipids not only are precursors of glycerolipids, but
CC also are dynamic components of signal transduction systems that control
CC cell physiology. {ECO:0000269|PubMed:10049376,
CC ECO:0000269|PubMed:11544256, ECO:0000269|PubMed:12167660,
CC ECO:0000269|PubMed:31421179}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC Evidence={ECO:0000269|PubMed:11544256};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + dihydroxyacetone phosphate = a 1-acylglycerone
CC 3-phosphate + CoA; Xref=Rhea:RHEA:17657, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57534, ChEBI:CHEBI:57642, ChEBI:CHEBI:58342; EC=2.3.1.42;
CC Evidence={ECO:0000269|PubMed:11544256};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + sn-glycerol 3-phosphate = 1-hexadecanoyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35723,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57518,
CC ChEBI:CHEBI:57597; Evidence={ECO:0000269|PubMed:11544256};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35724;
CC Evidence={ECO:0000305|PubMed:11544256};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z-
CC hexadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:44188,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57597, ChEBI:CHEBI:61540,
CC ChEBI:CHEBI:74694; Evidence={ECO:0000269|PubMed:11544256};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44189;
CC Evidence={ECO:0000305|PubMed:11544256};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=octadecanoyl-CoA + sn-glycerol 3-phosphate = 1-octadecanoyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37195,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:74565; Evidence={ECO:0000269|PubMed:11544256};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37196;
CC Evidence={ECO:0000305|PubMed:11544256};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37199,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:74544; Evidence={ECO:0000269|PubMed:11544256};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37200;
CC Evidence={ECO:0000305|PubMed:11544256};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:22267742,
CC ECO:0000269|PubMed:31421179, ECO:0000269|PubMed:9401016}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:19525420,
CC ECO:0000269|PubMed:31421179}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to both perinuclear and cortical
CC endoplasmic reticulum. {ECO:0000269|PubMed:19525420}.
CC -!- PTM: Phosphorylatied at a conserved motif involving Ser-664, Ser-668
CC and Ser-671. This phosphorylation plays a critical role for efficient
CC TAG mobilization. Phosphorylation deficiency at this motif increases
CC the enzyme activity and consequently induces de novo formation of
CC phosphatidic acid. {ECO:0000269|PubMed:31421179}.
CC -!- MISCELLANEOUS: Present with 3100 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family. {ECO:0000305}.
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DR EMBL; AJ311354; CAC85303.1; -; Genomic_DNA.
DR EMBL; Z28292; CAA82146.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09218.1; -; Genomic_DNA.
DR PIR; S38143; S38143.
DR RefSeq; NP_012993.3; NM_001179857.3.
DR AlphaFoldDB; P36148; -.
DR SMR; P36148; -.
DR BioGRID; 34198; 169.
DR DIP; DIP-6620N; -.
DR IntAct; P36148; 40.
DR MINT; P36148; -.
DR STRING; 4932.YKR067W; -.
DR SwissLipids; SLP:000000047; -.
DR iPTMnet; P36148; -.
DR MaxQB; P36148; -.
DR PaxDb; P36148; -.
DR PRIDE; P36148; -.
DR EnsemblFungi; YKR067W_mRNA; YKR067W; YKR067W.
DR GeneID; 853941; -.
DR KEGG; sce:YKR067W; -.
DR SGD; S000001775; GPT2.
DR VEuPathDB; FungiDB:YKR067W; -.
DR eggNOG; ENOG502QQ2N; Eukaryota.
DR GeneTree; ENSGT00940000176524; -.
DR HOGENOM; CLU_007860_1_0_1; -.
DR InParanoid; P36148; -.
DR OMA; IDHSEMY; -.
DR BioCyc; MetaCyc:MON3O-4095; -.
DR BioCyc; YEAST:MON3O-4095; -.
DR BRENDA; 2.3.1.15; 984.
DR SABIO-RK; P36148; -.
DR UniPathway; UPA00557; UER00612.
DR PRO; PR:P36148; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36148; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IDA:SGD.
DR GO; GO:0016287; F:glycerone-phosphate O-acyltransferase activity; IDA:SGD.
DR GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IDA:SGD.
DR GO; GO:0090207; P:regulation of triglyceride metabolic process; IMP:SGD.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis; Lipid droplet;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..743
FT /note="Glycerol-3-phosphate O-acyltransferase 2"
FT /id="PRO_0000195258"
FT TOPO_DOM 1..34
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258,
FT ECO:0000305|PubMed:29073188"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:29073188"
FT TOPO_DOM 56..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258,
FT ECO:0000305|PubMed:29073188"
FT TRANSMEM 443..457
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:29073188"
FT TOPO_DOM 458
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258,
FT ECO:0000305|PubMed:29073188"
FT TRANSMEM 459..473
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:29073188"
FT TOPO_DOM 474..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258,
FT ECO:0000305|PubMed:29073188"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:29073188"
FT TOPO_DOM 523..531
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:16847258,
FT ECO:0000305|PubMed:29073188"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:29073188"
FT TOPO_DOM 553..743
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258,
FT ECO:0000305|PubMed:29073188"
FT REGION 682..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:31421179,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:31421179,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:31421179,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 673
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 692
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 262
FT /note="G->D: In GAT1-TTA1; abolishes both GAT and DHAPAT
FT activities."
FT /evidence="ECO:0000269|PubMed:11544256"
FT MUTAGEN 664
FT /note="S->A: In GPT2-3A; increases the enzyme activity of
FT GPT2; when associated with A-668 and A-671."
FT MUTAGEN 668
FT /note="S->A: In GPT2-3A; increases the enzyme activity of
FT GPT2; when associated with A-664 and A-671."
FT MUTAGEN 671
FT /note="S->A: In GPT2-3A; increases the enzyme activity of
FT GPT2; when associated with A-664 and A-668."
SQ SEQUENCE 743 AA; 83645 MW; 84B9946E56B82F15 CRC64;
MSAPAADHNA AKPIPHVPQA SRRYKNSYNG FVYNIHTWLY DVSVFLFNIL FTIFFREIKV
RGAYNVPEVG VPTILVCAPH ANQFIDPALV MSQTRLLKTS AGKSRSRMPC FVTAESSFKK
RFISFFGHAM GGIPVPRIQD NLKPVDENLE IYAPDLKNHP EIIKGRSKNP QTTPVNFTKR
FSAKSLLGLP DYLSNAQIKE IPDDETIILS SPFRTSKSKV VELLTNGTNF KYAEKIDNTE
TFQSVFDHLH TKGCVGIFPE GGSHDRPSLL PIKAGVAIMA LGAVAADPTM KVAVVPCGLH
YFHRNKFRSR AVLEYGEPIV VDGKYGEMYK DSPRETVSKL LKKITNSLFS VTENAPDYDT
LMVIQAARRL YQPVKVRLPL PAIVEINRRL LFGYSKFKDD PRIIHLKKLV YDYNRKLDSV
GLKDHQVMQL KTTKLEALRC FVTLIVRLIK FSVFAILSLP GSILFTPIFI ICRVYSEKKA
KEGLKKSLVK IKGTDLLATW KLIVALILAP ILYVTYSILL IILARKQHYC RIWVPSNNAF
IQFVYFYALL VFTTYSSLKT GEIGVDLFKS LRPLFVSIVY PGKKIEEIQT TRKNLSLELT
AVCNDLGPLV FPDYDKLATE IFSKRDGYDV SSDAESSISR MSVQSRSRSS SIHSIGSLAS
NALSRVNSRG SLTDIPIFSD AKQGQWKSEG ETSEDEDEFD EKNPAIVQTA RSSDLNKENS
RNTNISSKIA SLVRQKREHE KKE
