ID TGL4_YEAST Reviewed; 910 AA. AC P36165; D6VXE9; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 04-NOV-2026, entry version 187. DE RecName: Full=Triacylglycerol lipase 4; DE EC=3.1.1.3 {ECO:0000269|PubMed:16135509}; DE AltName: Full=Lipase 4; GN Name=TGL4; Synonyms=STC1; OrderedLocusNames=YKR089C; ORFNames=YKR409; 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]. RX PubMed=8203164; DOI=10.1002/yea.320100210; RA Garcia-Cantalejo J.M., Baladron V., Esteban P.F., Santos M.A., Bou G., RA Remacha M.A., Revuelta J.L., Ballesta J.P.G., Jimenez A., del Rey F.; RT "The complete sequence of an 18,002 bp segment of Saccharomyces cerevisiae RT chromosome XI contains the HBS1, MRP-L20 and PRP16 genes, and six new open RT reading frames."; RL Yeast 10:231-245(1994). 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 [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 [5] 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 [6] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=16135509; DOI=10.1074/jbc.m507261200; RA Athenstaedt K., Daum G.; RT "Tgl4p and Tgl5p, two triacylglycerol lipases of the yeast Saccharomyces RT cerevisiae are localized to lipid particles."; RL J. Biol. Chem. 280:37301-37309(2005). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-751, 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 [8] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION RP PHENOTYPE. RX PubMed=16267052; DOI=10.1074/jbc.m508414200; RA Kurat C.F., Natter K., Petschnigg J., Wolinski H., Scheuringer K., RA Scholz H., Zimmermann R., Leber R., Zechner R., Kohlwein S.D.; RT "Obese yeast: triglyceride lipolysis is functionally conserved from mammals RT to yeast."; RL J. Biol. Chem. 281:491-500(2006). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737, 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 [11] RP FUNCTION, SUBCELLULAR LOCATION, ACTIVITY REGULATION, PHOSPHORYLATION AT RP THR-675 AND SER-890, AND MUTAGENESIS OF THR-675. RX PubMed=19150427; DOI=10.1016/j.molcel.2008.12.019; RA Kurat C.F., Wolinski H., Petschnigg J., Kaluarachchi S., Andrews B., RA Natter K., Kohlwein S.D.; RT "Cdk1/Cdc28-dependent activation of the major triacylglycerol lipase Tgl4 RT in yeast links lipolysis to cell-cycle progression."; RL Mol. Cell 33:53-63(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-749; SER-751 AND RP SER-836, AND IDENTIFICATION 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 FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=20332534; DOI=10.1074/jbc.m109.076331; RA Rajakumari S., Daum G.; RT "Multiple functions as lipase, steryl ester hydrolase, phospholipase, and RT acyltransferase of Tgl4p from the yeast Saccharomyces cerevisiae."; RL J. Biol. Chem. 285:15769-15776(2010). RN [14] RP SUBCELLULAR LOCATION. RX PubMed=21820081; DOI=10.1016/j.bbalip.2011.07.015; RA Grillitsch K., Connerth M., Kofeler H., Arrey T.N., Rietschel B., RA Wagner B., Karas M., Daum G.; RT "Lipid particles/droplets of the yeast Saccharomyces cerevisiae revisited: RT lipidome meets proteome."; RL Biochim. Biophys. Acta 1811:1165-1176(2011). RN [15] 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). RN [16] RP ACTIVITY REGULATION. RX PubMed=27170177; DOI=10.1091/mbc.e15-09-0633; RA Klein I., Klug L., Schmidt C., Zandl M., Korber M., Daum G., RA Athenstaedt K.; RT "Regulation of the yeast triacylglycerol lipases Tgl4p and Tgl5p by the RT presence/absence of nonpolar lipids."; RL Mol. Biol. Cell 27:2014-2024(2016). CC -!- FUNCTION: Lipid particle-localized triacylglycerol (TAG) lipase. The CC lipid droplet/particle is a lipid storage compartment which serves as a CC depot of energy and building blocks for membrane lipid biosynthesis. CC Involved in the mobilization of the non-polar storage lipids CC triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, CC releasing and supplying specific fatty acids to the appropriate CC metabolic pathways (PubMed:16135509, PubMed:16267052). Also has steryl CC ester (SE) hydrolase and phospholipase A(2) (PLA(2)) activities, and CC catalyzes the acylation of lysophosphatidic acid (LPA) CC (PubMed:20332534). Contributes to early bud formation in late G1 phase CC of the cell cycle upon phosphorylation and activation by cyclin- CC dependent kinase 1 (Cdk1/CDC28) (PubMed:19150427). CC {ECO:0000269|PubMed:16135509, ECO:0000269|PubMed:16267052, CC ECO:0000269|PubMed:19150427, ECO:0000269|PubMed:20332534}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; CC Evidence={ECO:0000269|PubMed:16135509}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045; CC Evidence={ECO:0000305|PubMed:16135509}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = di-(9Z)- CC octadecenoylglycerol + (9Z)-octadecenoate + H(+); CC Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945; CC Evidence={ECO:0000269|PubMed:16267052, ECO:0000269|PubMed:20332534}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576; CC Evidence={ECO:0000305|PubMed:16267052, ECO:0000305|PubMed:20332534}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1- CC hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoate + H(+); CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; CC Evidence={ECO:0000269|PubMed:20332534}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; CC Evidence={ECO:0000305|PubMed:20332534}; CC -!- CATALYTIC ACTIVITY: CC Reaction=cholesteryl (9Z-octadecenoate) + H2O = cholesterol + (9Z)- CC octadecenoate + H(+); Xref=Rhea:RHEA:33875, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30823, CC ChEBI:CHEBI:46898; Evidence={ECO:0000269|PubMed:20332534}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33876; CC Evidence={ECO:0000305|PubMed:20332534}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + (9Z)- CC octadecenoyl-CoA = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CC CoA; Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, CC ChEBI:CHEBI:74544, ChEBI:CHEBI:74546; CC Evidence={ECO:0000269|PubMed:20332534}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132; CC Evidence={ECO:0000305|PubMed:20332534}; CC -!- ACTIVITY REGULATION: Phosphorylated and activated by cyclin-dependent CC kinase 1 (Cdk1/CDC28) (PubMed:19150427). Loses its lipolytic activity CC in cells lacking nonpolar lipids, but retains its side activity as CC lysophospholipid acyltransferase (PubMed:27170177). CC {ECO:0000269|PubMed:19150427, ECO:0000269|PubMed:27170177}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=14.3 uM for 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate CC {ECO:0000269|PubMed:20332534}; CC KM=15.1 uM for (9Z)-octadecenoyl-CoA {ECO:0000269|PubMed:20332534}; CC Vmax=11.4 nmol/min/mg enzyme towards CC 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate CC {ECO:0000269|PubMed:20332534}; CC Vmax=11.98 nmol/min/mg enzyme towards (9Z)-octadecenoyl-CoA CC {ECO:0000269|PubMed:20332534}; CC pH dependence: CC Optimum pH is 7-9 for the lysophosphatidic acid acyltransferase CC (LPAAT) reaction. {ECO:0000269|PubMed:20332534}; CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:16135509, CC ECO:0000269|PubMed:16267052, ECO:0000269|PubMed:19150427, CC ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:24868093, CC ECO:0000269|PubMed:27170177}. Note=Partially retained in the CC endoplasmic reticulum in cells lacking triacylglycerols. CC {ECO:0000269|PubMed:27170177}. CC -!- PTM: Phosphorylation at Thr-675 and Ser-890 by Cdk1/CDC28 stimulates CC enzyme activity in vivo. {ECO:0000269|PubMed:19150427}. CC -!- DISRUPTION PHENOTYPE: A double deletion of TGL3 and TGL4, the 2 major CC TGA lipases, leads to fat yeast, rendering growing cells unable to CC degrade triglycerides. {ECO:0000269|PubMed:16267052}. CC -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; Z27116; CAA81640.1; -; Genomic_DNA. DR EMBL; Z28314; CAA82168.1; -; Genomic_DNA. DR EMBL; BK006944; DAA09239.1; -; Genomic_DNA. DR PIR; S38167; S38167. DR RefSeq; NP_013015.1; NM_001179879.1. DR AlphaFoldDB; P36165; -. DR BioGRID; 34220; 84. DR DIP; DIP-5588N; -. DR FunCoup; P36165; 137. DR IntAct; P36165; 10. DR STRING; 4932.YKR089C; -. DR SwissLipids; SLP:000000053; -. DR SwissLipids; SLP:000000672; -. DR iPTMnet; P36165; -. DR PaxDb; 4932-YKR089C; -. DR PeptideAtlas; P36165; -. DR EnsemblFungi; YKR089C_mRNA; YKR089C; YKR089C. DR GeneID; 853964; -. DR KEGG; sce:YKR089C; -. DR AGR; SGD:S000001797; -. DR SGD; S000001797; TGL4. DR VEuPathDB; FungiDB:YKR089C; -. DR eggNOG; KOG2214; Eukaryota. DR HOGENOM; CLU_009031_4_0_1; -. DR InParanoid; P36165; -. DR OMA; AQKHHQF; -. DR OrthoDB; 10049244at2759; -. DR BioCyc; MetaCyc:G3O-32052-MONOMER; -. DR BioCyc; YEAST:G3O-32052-MONOMER; -. DR BioGRID-ORCS; 853964; 4 hits in 10 CRISPR screens. DR PRO; PR:P36165; -. DR Proteomes; UP000002311; Chromosome XI. DR RNAct; P36165; protein. DR GO; GO:0005811; C:lipid droplet; IDA:SGD. DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:RHEA. DR GO; GO:0004623; F:A2-type glycerophospholipase activity; IDA:SGD. DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IDA:SGD. DR GO; GO:0004771; F:sterol ester esterase activity; IDA:SGD. DR GO; GO:0004806; F:triacylglycerol lipase activity; IDA:SGD. DR GO; GO:0007114; P:cell budding; IMP:SGD. DR GO; GO:0006644; P:phospholipid metabolic process; IMP:SGD. DR GO; GO:0019433; P:triglyceride catabolic process; IMP:SGD. DR GO; GO:0006642; P:triglyceride mobilization; IDA:SGD. DR CDD; cd07230; Pat_TGL4-5_like; 1. DR FunFam; 3.40.1090.10:FF:000037; Lipase 4; 1. DR Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1. DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase. DR InterPro; IPR050301; NTE. DR InterPro; IPR002641; PNPLA_dom. DR InterPro; IPR021771; Triacylglycerol_lipase_N. DR PANTHER; PTHR14226; NEUROPATHY TARGET ESTERASE/SWISS CHEESE D.MELANOGASTER; 1. DR PANTHER; PTHR14226:SF10; TRIACYLGLYCEROL LIPASE 4-RELATED; 1. DR Pfam; PF11815; DUF3336; 1. DR Pfam; PF01734; Patatin; 1. DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1. DR PROSITE; PS51635; PNPLA; 1. PE 1: Evidence at protein level; KW Hydrolase; Lipid degradation; Lipid droplet; Lipid metabolism; KW Phosphoprotein; Reference proteome; Sporulation. FT CHAIN 1..910 FT /note="Triacylglycerol lipase 4" FT /id="PRO_0000203227" FT DOMAIN 282..483 FT /note="PNPLA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161" FT REGION 51..120 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 657..683 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 713..777 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 874..910 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 286..291 FT /note="GXGXXG" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161" FT MOTIF 313..317 FT /note="GXSXG" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161" FT COMPBIAS 51..66 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 70..85 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 90..116 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 666..683 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 739..768 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 889..899 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 900..910 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 315 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161" FT ACT_SITE 470 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161" FT MOD_RES 55 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 675 FT /note="Phosphothreonine; by Cdk1" FT /evidence="ECO:0000269|PubMed:19150427" FT MOD_RES 737 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 749 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 751 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15665377, FT ECO:0007744|PubMed:19779198" FT MOD_RES 836 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 890 FT /note="Phosphoserine; by Cdk1" FT /evidence="ECO:0000269|PubMed:19150427" FT MUTAGEN 675 FT /note="T->E: Highly stimulates TGA lipolysis." FT /evidence="ECO:0000269|PubMed:19150427" SQ SEQUENCE 910 AA; 102717 MW; 1CFC03C4A6E64B9C CRC64; MSSKISDLTS TQNKPLLVTQ QLIEKYYEQI LGTSQNIIPI LNPKNKFIRP SKDNSDVERV EEDAGKRLQT GKNKTTNKVN FNLDTGNEDK LDDDQETVTE NENNDIEMVE TDEGEDERQG SSLASKCKSF LYNVFVGNYE RDILIDKVCS QKQHAMSFEE WCSAGARLDD LTGKTEWKQK LESPLYDYKL IKDLTSRMRE ERLNRNYAQL LYIIRTNWVR NLGNMGNVNL YRHSHVGTKY LIDEYMMESR LALESLMESD LDDSYLLGIL QQTRRNIGRT ALVLSGGGTF GLFHIGVLGT LFELDLLPRV ISGSSAGAIV ASILSVHHKE EIPVLLNHIL DKEFNIFKDD KQKSESENLL IKISRFFKNG TWFDNKHLVN TMIEFLGDLT FREAYNRTGK ILNITVSPAS LFEQPRLLNN LTAPNVLIWS AVCASCSLPG IFPSSPLYEK DPKTGERKPW TGSSSVKFVD GSVDNDLPIS RLSEMFNVDH IIACQVNIHV FPFLKLSLSC VGGEIEDEFS ARLKQNLSSI YNFMANEAIH ILEIGSEMGI AKNALTKLRS VLSQQYSGDI TILPDMCMLF RIKELLSNPT KEFLLREITN GAKATWPKVS IIQNHCGQEF ALDKAISYIK GRMIVTSSLK TPFQFADSVI GLIKAPEQTS DESKNPENST LLTRTPTKGD NHISNVLDDN LLESESTNSL LLLRENASTY GRSPSGFRPR YSITSASLNP RHQRRKSDTI STSRRPAKSF SFSVASPTSR MLRQSSKING HPPPILQKKT SMGRLMFPMD AKTYDPESHE LIPHSASIET PAMVDKKLHF GRKSRYLRHM NKKWVSSSNI LYTDSDKEDH PTLRLISNFD SDAMIHSDLA GNFRRHSIDG RPPSQATKSS PFRSRPSSST QHKSTTSFTQ //