TGL4_YEAST
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 03-AUG-2022, entry version 170.
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 = (9Z)-
CC octadecenoate + di-(9Z)-octadecenoylglycerol + 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 + H(+) + hexadecanoate;
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 = (9Z)-octadecenoate +
CC cholesterol + 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=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC 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 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphate {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}.
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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; 59.
DR DIP; DIP-5588N; -.
DR IntAct; P36165; 4.
DR MINT; P36165; -.
DR STRING; 4932.YKR089C; -.
DR SwissLipids; SLP:000000053; -.
DR SwissLipids; SLP:000000672; -.
DR iPTMnet; P36165; -.
DR MaxQB; P36165; -.
DR PaxDb; P36165; -.
DR PRIDE; P36165; -.
DR EnsemblFungi; YKR089C_mRNA; YKR089C; YKR089C.
DR GeneID; 853964; -.
DR KEGG; sce:YKR089C; -.
DR SGD; S000001797; TGL4.
DR VEuPathDB; FungiDB:YKR089C; -.
DR eggNOG; KOG2214; Eukaryota.
DR GeneTree; ENSGT00940000176365; -.
DR HOGENOM; CLU_009031_4_0_1; -.
DR InParanoid; P36165; -.
DR OMA; NFMANEA; -.
DR BioCyc; MetaCyc:G3O-32052-MON; -.
DR BioCyc; YEAST:G3O-32052-MON; -.
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:0047499; F:calcium-independent phospholipase A2 activity; IDA:SGD.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IDA:SGD.
DR GO; GO:0004771; F:sterol esterase activity; IDA:SGD.
DR GO; GO:0004806; F:triglyceride 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:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR GO; GO:0019433; P:triglyceride catabolic process; IMP:SGD.
DR GO; GO:0006642; P:triglyceride mobilization; IDA:SGD.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002641; PNPLA_dom.
DR InterPro; IPR021771; Triacylglycerol_lipase_N.
DR Pfam; PF11815; DUF3336; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 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..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..114
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..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
