MGLL_YEAST
ID MGLL_YEAST Reviewed; 313 AA.
AC P28321; D6VXJ4;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Monoglyceride lipase {ECO:0000305};
DE Short=MGL;
DE EC=3.1.1.23 {ECO:0000269|PubMed:20554061};
DE AltName: Full=Fatty acid ethyl ester hydrolase {ECO:0000303|PubMed:27036938};
DE Short=FAEE hydrolase;
DE AltName: Full=Monoacylglycerol hydrolase;
DE Short=MAG hydrolase;
DE Short=MGH;
DE AltName: Full=Monoacylglycerol lipase;
DE Short=MAG lipase;
DE Short=MAGL;
DE AltName: Full=Serine hydrolase YJU3;
GN Name=YJU3; OrderedLocusNames=YKL094W; ORFNames=YKL441;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1626433; DOI=10.1002/yea.320080509;
RA Forrova H., Kolarov J., Ghislain M., Goffeau A.;
RT "Sequence of the novel essential gene YJU2 and two flanking reading frames
RT located within a 3.2 kb EcoRI fragment from chromosome X of Saccharomyces
RT cerevisiae.";
RL Yeast 8:419-422(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8256524; DOI=10.1002/yea.320091016;
RA Pallier C., Valens M., Puzos V., Fukuhara H., Cheret G., Sor F.,
RA Bolotin-Fukuhara M.;
RT "DNA sequence analysis of a 17 kb fragment of yeast chromosome XI
RT physically localizes the MRB1 gene and reveals eight new open reading
RT frames, including a homologue of the KIN1/KIN2 and SNF1 protein kinases.";
RL Yeast 9:1149-1155(1993).
RN [3]
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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=10515935; DOI=10.1128/jb.181.20.6441-6448.1999;
RA Athenstaedt K., Zweytick D., Jandrositz A., Kohlwein S.D., Daum G.;
RT "Identification and characterization of major lipid particle proteins of
RT the yeast Saccharomyces cerevisiae.";
RL J. Bacteriol. 181:6441-6448(1999).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11914276; DOI=10.1101/gad.970902;
RA Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S.,
RA Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P.,
RA Gerstein M., Roeder G.S., Snyder M.;
RT "Subcellular localization of the yeast proteome.";
RL Genes Dev. 16:707-719(2002).
RN [7]
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 [8]
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 [9]
RP IDENTIFICATION AS A SERINE HYDROLASE BY MASS SPECTROMETRY.
RX PubMed=14645503; DOI=10.1074/mcp.m300082-mcp200;
RA Baxter S.M., Rosenblum J.S., Knutson S., Nelson M.R., Montimurro J.S.,
RA Di Gennaro J.A., Speir J.A., Burbaum J.J., Fetrow J.S.;
RT "Synergistic computational and experimental proteomics approaches for more
RT accurate detection of active serine hydrolases in yeast.";
RL Mol. Cell. Proteomics 3:209-225(2004).
RN [10]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16407407; DOI=10.1091/mbc.e05-08-0740;
RA Zahedi R.P., Sickmann A., Boehm A.M., Winkler C., Zufall N.,
RA Schoenfisch B., Guiard B., Pfanner N., Meisinger C.;
RT "Proteomic analysis of the yeast mitochondrial outer membrane reveals
RT accumulation of a subclass of preproteins.";
RL Mol. Biol. Cell 17:1436-1450(2006).
RN [11]
RP FUNCTION.
RX PubMed=19529773; DOI=10.1371/journal.pone.0005942;
RA Muccioli G.G., Sia A., Muchowski P.J., Stella N.;
RT "Genetic manipulation of palmitoylethanolamide production and inactivation
RT in Saccharomyces cerevisiae.";
RL PLoS ONE 4:E5942-E5942(2009).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20554061; DOI=10.1016/j.bbalip.2010.06.001;
RA Heier C., Taschler U., Rengachari S., Oberer M., Wolinski H., Natter K.,
RA Kohlwein S.D., Leber R., Zimmermann R.;
RT "Identification of Yju3p as functional orthologue of mammalian
RT monoglyceride lipase in the yeast Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1801:1063-1071(2010).
RN [13]
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 [14]
RP LIPASE MOTIF.
RX DOI=10.1007/s11515-011-1142-6;
RA Grillitsch K., Daum G.;
RT "Triacylglycerol lipases of the yeast.";
RL Front. Biol. 6:219-230(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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27036938; DOI=10.1074/jbc.m115.705541;
RA Heier C., Taschler U., Radulovic M., Aschauer P., Eichmann T.O., Grond S.,
RA Wolinski H., Oberer M., Zechner R., Kohlwein S.D., Zimmermann R.;
RT "Monoacylglycerol lipases act as evolutionarily conserved regulators of
RT non-oxidative ethanol metabolism.";
RL J. Biol. Chem. 291:11865-11875(2016).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP AND FUNCTION.
RX PubMed=26869448; DOI=10.1016/j.bbalip.2016.02.005;
RA Aschauer P., Rengachari S., Lichtenegger J., Schittmayer M., Das K.M.,
RA Mayer N., Breinbauer R., Birner-Gruenberger R., Gruber C.C., Zimmermann R.,
RA Gruber K., Oberer M.;
RT "Crystal structure of the Saccharomyces cerevisiae monoglyceride lipase
RT Yju3p.";
RL Biochim. Biophys. Acta 1861:462-470(2016).
CC -!- FUNCTION: Converts monoacylglycerides (MAG) to free fatty acids and
CC glycerol (PubMed:20554061). Has a strong preference for monounsaturated
CC monoglycerides (PubMed:26869448). Required for efficient degradation of
CC MAG, short-lived intermediates of glycerolipid metabolism which may
CC also function as lipid signaling molecules. Controls inactivation of
CC the signaling lipid N-palmitoylethanolamine (PEA) (PubMed:19529773).
CC Involved in fatty acid ethyl ester (FAEE) catabolism. FAEEs are non-
CC oxidative metabolites of ethanol that are transiently incorporated into
CC lipid droplets (LDs). Their mobilization by LD-resident FAEE hydrolases
CC facilitates a controlled metabolism of these potentially toxic lipid
CC metabolites (PubMed:27036938). {ECO:0000269|PubMed:19529773,
CC ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:26869448,
CC ECO:0000269|PubMed:27036938}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.;
CC EC=3.1.1.23; Evidence={ECO:0000269|PubMed:20554061};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acid ethyl ester + H2O = a fatty acid + ethanol +
CC H(+); Xref=Rhea:RHEA:50148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16236, ChEBI:CHEBI:28868, ChEBI:CHEBI:78206;
CC Evidence={ECO:0000269|PubMed:27036938};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000269|PubMed:20554061,
CC ECO:0000269|PubMed:26869448};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000305|PubMed:20554061};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73990; Evidence={ECO:0000269|PubMed:20554061};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492;
CC Evidence={ECO:0000305|PubMed:20554061};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:39959, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:69081; Evidence={ECO:0000269|PubMed:20554061,
CC ECO:0000269|PubMed:27036938};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39960;
CC Evidence={ECO:0000305|PubMed:20554061, ECO:0000305|PubMed:27036938};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hexadecanoylglycerol + H2O = glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:39963, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:75455; Evidence={ECO:0000269|PubMed:20554061};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39964;
CC Evidence={ECO:0000305|PubMed:20554061};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethyl hexadecanoate + H2O = ethanol + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:50132, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16236, ChEBI:CHEBI:84932;
CC Evidence={ECO:0000269|PubMed:27036938};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50133;
CC Evidence={ECO:0000305|PubMed:27036938};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethyl (9Z)-octadecenoate + H2O = (9Z)-octadecenoate + ethanol
CC + H(+); Xref=Rhea:RHEA:50136, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16236, ChEBI:CHEBI:30823, ChEBI:CHEBI:84940;
CC Evidence={ECO:0000269|PubMed:27036938};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50137;
CC Evidence={ECO:0000305|PubMed:27036938};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethyl (9Z)-hexadecenoate + H2O = (9Z)-hexadecenoate + ethanol
CC + H(+); Xref=Rhea:RHEA:50144, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16236, ChEBI:CHEBI:32372, ChEBI:CHEBI:84934;
CC Evidence={ECO:0000269|PubMed:27036938};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50145;
CC Evidence={ECO:0000305|PubMed:27036938};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethyl octadecanoate + H2O = ethanol + H(+) + octadecanoate;
CC Xref=Rhea:RHEA:50316, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16236, ChEBI:CHEBI:25629, ChEBI:CHEBI:84936;
CC Evidence={ECO:0000269|PubMed:27036938};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50317;
CC Evidence={ECO:0000305|PubMed:27036938};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=260 uM for rac-1(3)-oleoylglycerol {ECO:0000269|PubMed:20554061};
CC Vmax=10.3 mmol/h/mg enzyme {ECO:0000269|PubMed:20554061};
CC pH dependence:
CC Active from pH 4.5 to 8. {ECO:0000269|PubMed:20554061};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
CC {ECO:0000269|PubMed:20554061}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:10515935,
CC ECO:0000269|PubMed:20554061, ECO:0000269|PubMed:21820081,
CC ECO:0000269|PubMed:24868093}. Cytoplasm {ECO:0000269|PubMed:11914276}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:14562095}. Mitochondrion
CC outer membrane {ECO:0000269|PubMed:16407407}. Note=Although the protein
CC is identified in the cytoplasm, several membrane systems and lipid
CC droplets, MGL activity is only measured in membrane fractions and lipid
CC droplets. {ECO:0000269|PubMed:20554061}.
CC -!- MISCELLANEOUS: Present with 2140 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Monoacylglycerol
CC lipase family. {ECO:0000305}.
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DR EMBL; X66245; CAA46971.1; -; Genomic_DNA.
DR EMBL; X71133; CAA50463.1; -; Genomic_DNA.
DR EMBL; Z28094; CAA81932.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09064.1; -; Genomic_DNA.
DR PIR; S37921; S37921.
DR RefSeq; NP_012829.1; NM_001179660.1.
DR PDB; 4ZWN; X-ray; 2.49 A; A/B/C/D=2-313.
DR PDB; 4ZXF; X-ray; 2.50 A; A/B/C/D=1-313.
DR PDBsum; 4ZWN; -.
DR PDBsum; 4ZXF; -.
DR AlphaFoldDB; P28321; -.
DR SMR; P28321; -.
DR BioGRID; 34039; 63.
DR IntAct; P28321; 9.
DR MINT; P28321; -.
DR STRING; 4932.YKL094W; -.
DR SwissLipids; SLP:000000055; -.
DR ESTHER; yeast-mgll; Monoglyceridelipase_lysophospholip.
DR MEROPS; S33.993; -.
DR iPTMnet; P28321; -.
DR MaxQB; P28321; -.
DR PaxDb; P28321; -.
DR PRIDE; P28321; -.
DR EnsemblFungi; YKL094W_mRNA; YKL094W; YKL094W.
DR GeneID; 853768; -.
DR KEGG; sce:YKL094W; -.
DR SGD; S000001577; YJU3.
DR VEuPathDB; FungiDB:YKL094W; -.
DR eggNOG; KOG1455; Eukaryota.
DR GeneTree; ENSGT00390000011364; -.
DR HOGENOM; CLU_026209_5_0_1; -.
DR InParanoid; P28321; -.
DR OMA; RQFNDMF; -.
DR BioCyc; MetaCyc:G3O-31885-MON; -.
DR BioCyc; YEAST:G3O-31885-MON; -.
DR Reactome; R-SCE-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-SCE-426048; Arachidonate production from DAG.
DR UniPathway; UPA00256; -.
DR PRO; PR:P28321; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P28321; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005811; C:lipid droplet; IDA:SGD.
DR GO; GO:0016020; C:membrane; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0047372; F:acylglycerol lipase activity; IMP:SGD.
DR GO; GO:0016298; F:lipase activity; IBA:GO_Central.
DR GO; GO:0017171; F:serine hydrolase activity; HDA:SGD.
DR GO; GO:0019433; P:triglyceride catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:SGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR022742; Hydrolase_4.
DR Pfam; PF12146; Hydrolase_4; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endoplasmic reticulum; Hydrolase; Lipid droplet;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Reference proteome.
FT CHAIN 1..313
FT /note="Monoglyceride lipase"
FT /id="PRO_0000203164"
FT MOTIF 121..125
FT /note="GXSXG"
FT /evidence="ECO:0000305|Ref.14"
FT ACT_SITE 123
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:26869448"
FT ACT_SITE 251
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:26869448"
FT ACT_SITE 281
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:26869448"
FT CONFLICT 244
FT /note="I -> V (in Ref. 1; CAA46971)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="K -> E (in Ref. 1; CAA46971)"
FT /evidence="ECO:0000305"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:4ZWN"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:4ZWN"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:4ZWN"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:4ZWN"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:4ZWN"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:4ZWN"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:4ZWN"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4ZWN"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:4ZWN"
FT HELIX 92..113
FT /evidence="ECO:0007829|PDB:4ZWN"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:4ZWN"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:4ZWN"
FT TURN 137..141
FT /evidence="ECO:0007829|PDB:4ZWN"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:4ZWN"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:4ZWN"
FT HELIX 156..161
FT /evidence="ECO:0007829|PDB:4ZWN"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:4ZWN"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:4ZWN"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:4ZWN"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:4ZWN"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:4ZWN"
FT HELIX 212..227
FT /evidence="ECO:0007829|PDB:4ZWN"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:4ZWN"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:4ZWN"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:4ZWN"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:4ZWN"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:4ZWN"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:4ZWN"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:4ZWN"
FT HELIX 289..305
FT /evidence="ECO:0007829|PDB:4ZWN"
SQ SEQUENCE 313 AA; 35563 MW; 5E0C3B431406DDF0 CRC64;
MAPYPYKVQT TVPELQYENF DGAKFGYMFW PVQNGTNEVR GRVLLIHGFG EYTKIQFRLM
DHLSLNGYES FTFDQRGAGV TSPGRSKGVT DEYHVFNDLE HFVEKNLSEC KAKGIPLFMW
GHSMGGGICL NYACQGKHKN EISGYIGSGP LIILHPHTMY NKPTQIIAPL LAKFLPRVRI
DTGLDLKGIT SDKAYRAFLG SDPMSVPLYG SFRQIHDFMQ RGAKLYKNEN NYIQKNFAKD
KPVIIMHGQD DTINDPKGSE KFIQDCPSAD KELKLYPGAR HSIFSLETDK VFNTVFNDMK
QWLDKHTTTE AKP
