A1HA_LOXIN
ID A1HA_LOXIN Reviewed; 306 AA.
AC P0CE80; B2KKV9; P83045; Q3HL91; Q6W8Q5; Q7YW73;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Dermonecrotic toxin LiSicTox-alphaIA1a;
DE EC=4.6.1.- {ECO:0000250|UniProtKB:Q4ZFU2};
DE AltName: Full=Dermonecrotic toxin 1 {ECO:0000303|PubMed:21590705};
DE Short=DT1 {ECO:0000303|PubMed:21590705};
DE Short=LiRecDT1 {ECO:0000303|PubMed:17900646, ECO:0000303|PubMed:21590705};
DE AltName: Full=P1 {ECO:0000303|PubMed:9790962};
DE AltName: Full=Phospholipase D;
DE Short=PLD;
DE AltName: Full=Sphingomyelin phosphodiesterase D 1;
DE Short=SMD 1;
DE Short=SMase D 1;
DE Short=Sphingomyelinase D 1;
DE Flags: Precursor;
OS Loxosceles intermedia (Brown spider).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Araneomorphae; Haplogynae; Scytodoidea; Sicariidae; Loxosceles.
OX NCBI_TaxID=58218;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND FUNCTION.
RC TISSUE=Venom gland;
RX PubMed=16581177; DOI=10.1016/j.biochi.2006.02.008;
RA da Silveira R.B., Pigozzo R.B., Chaim O.M., Appel M.H., Dreyfuss J.L.,
RA Toma L., Mangili O.C., Gremski W., Dietrich C.P., Nader H.B., Veiga S.S.;
RT "Molecular cloning and functional characterization of two isoforms of
RT dermonecrotic toxin from Loxosceles intermedia (Brown spider) venom
RT gland.";
RL Biochimie 88:1241-1253(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Venom gland;
RX PubMed=16005484; DOI=10.1016/j.taap.2005.05.015;
RA Chaim O.M., Sade Y.B., da Silveira R.B., Toma L., Kalapothakis E.,
RA Chavez-Olortegui C., Mangili O.C., Gremski W., Dietrich C.P., Nader H.B.,
RA Veiga S.S.;
RT "Brown spider dermonecrotic toxin directly induces nephrotoxicity.";
RL Toxicol. Appl. Pharmacol. 211:64-77(2006).
RN [3]
RP PROTEIN SEQUENCE OF 27-64, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Venom;
RX PubMed=9790962; DOI=10.1006/bbrc.1998.9474;
RA Tambourgi D.V., Magnoli F.C., van den Berg C.W., Morgan B.P.,
RA de Araujo P.S., Alves E.W., Da Silva W.D.;
RT "Sphingomyelinases in the venom of the spider Loxosceles intermedia are
RT responsible for both dermonecrosis and complement-dependent hemolysis.";
RL Biochem. Biophys. Res. Commun. 251:366-373(1998).
RN [4]
RP FUNCTION, AND BIOASSAY.
RX PubMed=17900646; DOI=10.1016/j.toxicon.2007.08.001;
RA Ribeiro R.O., Chaim O.M., da Silveira R.B., Gremski L.H., Sade Y.B.,
RA Paludo K.S., Senff-Ribeiro A., de Moura J., Chavez-Olortegui C.,
RA Gremski W., Nader H.B., Veiga S.S.;
RT "Biological and structural comparison of recombinant phospholipase D toxins
RT from Loxosceles intermedia (brown spider) venom.";
RL Toxicon 50:1162-1174(2007).
RN [5]
RP FUNCTION, BIOASSAY, MUTAGENESIS OF HIS-38, AND ACTIVE SITE.
RX PubMed=18760322; DOI=10.1016/j.biochi.2008.07.011;
RA Kusma J., Chaim O.M., Wille A.C., Ferrer V.P., Sade Y.B., Donatti L.,
RA Gremski W., Mangili O.C., Veiga S.S.;
RT "Nephrotoxicity caused by brown spider venom phospholipase-D (dermonecrotic
RT toxin) depends on catalytic activity.";
RL Biochimie 90:1722-1736(2008).
RN [6]
RP FUNCTION ON RAT LIVER.
RX PubMed=18765244; DOI=10.1016/j.toxicon.2008.08.001;
RA de Oliveira Christoff A., de Oliveira A., Chaim O.M., Lugarini D.,
RA Bastos Pereira A.L., Paludo K.S., Queiroz Telles J.E., Bracht A.,
RA Veiga S.S., Acco A.;
RT "Effects of the venom and the dermonecrotic toxin LiRecDT1 of Loxosceles
RT intermedia in the rat liver.";
RL Toxicon 52:695-704(2008).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, MUTAGENESIS OF HIS-38, AND ACTIVE SITE.
RX PubMed=19455508; DOI=10.1002/jcb.22148;
RA Chaves-Moreira D., Chaim O.M., Sade Y.B., Paludo K.S., Gremski L.H.,
RA Donatti L., de Moura J., Mangili O.C., Gremski W., da Silveira R.B.,
RA Senff-Ribeiro A., Veiga S.S.;
RT "Identification of a direct hemolytic effect dependent on the catalytic
RT activity induced by phospholipase-D (dermonecrotic toxin) from brown spider
RT venom.";
RL J. Cell. Biochem. 107:655-666(2009).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-38, SUBSTRATE SPECIFICITY,
RP AND ACTIVE SITE.
RX PubMed=21590705; DOI=10.1002/jcb.23177;
RA Chaves-Moreira D., Souza F.N., Fogaca R.T., Mangili O.C., Gremski W.,
RA Senff-Ribeiro A., Chaim O.M., Veiga S.S.;
RT "The relationship between calcium and the metabolism of plasma membrane
RT phospholipids in hemolysis induced by brown spider venom phospholipase-D
RT toxin.";
RL J. Cell. Biochem. 112:2529-2540(2011).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-38; GLU-58; ASP-60;
RP HIS-74; CYS-80; LYS-120; GLY-122; CYS-223; TYR-249 AND TRP-251, SUBSTRATE
RP SPECIFICITY, AND ACTIVE SITES.
RX PubMed=27233517; DOI=10.1016/j.bbalip.2016.05.009;
RA Vuitika L., Chaves-Moreira D., Caruso I., Lima M.A., Matsubara F.H.,
RA Murakami M.T., Takahashi H.K., Toledo M.S., Coronado M.A., Nader H.B.,
RA Senff-Ribeiro A., Chaim O.M., Arni R.K., Veiga S.S.;
RT "Active site mapping of Loxosceles phospholipases D: biochemical and
RT biological features.";
RL Biochim. Biophys. Acta 1861:970-979(2016).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 28-306 IN COMPLEX WITH MAGNESIUM,
RP DISULFIDE BONDS, MUTAGENESIS OF HIS-38, ACTIVE SITE, AND COFACTOR.
RX PubMed=21301094; DOI=10.1107/s1744309110050931;
RA Ullah A., de Giuseppe P.O., Murakami M.T., Trevisan-Silva D., Wille A.C.,
RA Chaves-Moreira D., Gremski L.H., da Silveira R.B., Sennf-Ribeiro A.,
RA Chaim O.M., Veiga S.S., Arni R.K.;
RT "Crystallization and preliminary X-ray diffraction analysis of a class II
RT phospholipase D from Loxosceles intermedia venom.";
RL Acta Crystallogr. F 67:234-236(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.
RX PubMed=21616057; DOI=10.1016/j.bbrc.2011.05.053;
RA de Giuseppe P.O., Ullah A., Silva D.T., Gremski L.H., Wille A.C.,
RA Chaves Moreira D., Ribeiro A.S., Chaim O.M., Murakami M.T., Veiga S.S.,
RA Arni R.K.;
RT "Structure of a novel class II phospholipase D: catalytic cleft is modified
RT by a disulphide bridge.";
RL Biochem. Biophys. Res. Commun. 409:622-627(2011).
CC -!- FUNCTION: Dermonecrotic toxins cleave the phosphodiester linkage
CC between the phosphate and headgroup of certain phospholipids
CC (sphingolipid and lysolipid substrates), forming an alcohol (often
CC choline) and a cyclic phosphate (By similarity). This toxin acts on
CC sphingomyelin (SM) with high activity (PubMed:16581177, PubMed:9790962,
CC PubMed:21590705, PubMed:27233517). It also acts on
CC lysophosphatidylcholine (LPC), and lyso-platelet activating factor
CC (LPAF, an alkyl-LPC) but not on phosphatidylcholine (PC)
CC (PubMed:21590705, PubMed:27233517). It may also act on ceramide
CC phosphoethanolamine (CPE), lysophosphatidylcholine (LPC) and
CC lysophosphatidylethanolamine (LPE), but not on lysophosphatidylserine
CC (LPS), and lysophosphatidylglycerol (LPG) (By similarity). It acts by
CC transphosphatidylation, releasing exclusively cyclic phosphate products
CC as second products (By similarity). In vivo, it induces dermonecrosis,
CC vascular permeability, platelet aggregation, inflammatory response,
CC edema and cytotoxicity against renal epithelial cells (PubMed:16581177,
CC PubMed:9790962, PubMed:17900646, PubMed:27233517). It causes direct
CC nephrotoxicity (PubMed:16005484) and is directly toxic to liver
CC (PubMed:18765244). It also induces hemolysis in a complement-dependent
CC manner as well as in a complement-independent manner (PubMed:9790962,
CC PubMed:17900646, PubMed:21590705, PubMed:27233517). The hemolysis
CC provoked in a complement-independent manner is composed of several
CC steps (PubMed:21590705). The toxin binds to erythrocyte membranes,
CC hydrolyzes membrane phospholipids (SM and LPC) thus generating
CC metabolism products that cause hemolysis, probably by provoking an
CC increase of calcium inside cells (PubMed:21590705). The calcium influx
CC is due to the opening of L-type calcium channels, since L-type calcium
CC channel blockers inhibit calcium influx (PubMed:21590705). In vivo, is
CC lethal to mice when intraperitoneally injected (PubMed:17900646).
CC {ECO:0000250|UniProtKB:A0A0D4WTV1, ECO:0000269|PubMed:16005484,
CC ECO:0000269|PubMed:16581177, ECO:0000269|PubMed:17900646,
CC ECO:0000269|PubMed:18765244, ECO:0000269|PubMed:21590705,
CC ECO:0000269|PubMed:27233517, ECO:0000269|PubMed:9790962}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-(acyl)-sphingosylphosphocholine = an N-(acyl)-sphingosyl-
CC 1,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60652,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:64583, ChEBI:CHEBI:143892;
CC Evidence={ECO:0000305|PubMed:16581177, ECO:0000305|PubMed:21590705,
CC ECO:0000305|PubMed:27233517, ECO:0000305|PubMed:9790962};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-(acyl)-sphingosylphosphoethanolamine = an N-(acyl)-
CC sphingosyl-1,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60648,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:143891, ChEBI:CHEBI:143892;
CC Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine = a 1-acyl-sn-glycero-
CC 2,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60700,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:58168, ChEBI:CHEBI:143947;
CC Evidence={ECO:0000305|PubMed:21590705, ECO:0000305|PubMed:27233517};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine = a 1-acyl-sn-
CC glycero-2,3-cyclic phosphate + ethanolamine; Xref=Rhea:RHEA:60704,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:64381, ChEBI:CHEBI:143947;
CC Evidence={ECO:0000250|UniProtKB:A0A0D4WTV1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-
CC sn-glycero-2,3-cyclic phosphate + choline; Xref=Rhea:RHEA:60656,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:72998, ChEBI:CHEBI:143893;
CC Evidence={ECO:0000305|PubMed:21590705};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21301094, ECO:0000269|PubMed:21616057,
CC ECO:0000312|PDB:3RLG, ECO:0000312|PDB:3RLH};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:21301094,
CC ECO:0000269|PubMed:21616057, ECO:0000312|PDB:3RLG,
CC ECO:0000312|PDB:3RLH};
CC -!- ACTIVITY REGULATION: Catalytic activity and hemolysis are inhibited by
CC divalent ion chelators (1,10-phenanthroline, EDTA, and EGTA).
CC {ECO:0000269|PubMed:19455508}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9790962}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:9790962}.
CC -!- SIMILARITY: Belongs to the arthropod phospholipase D family. Class II
CC subfamily. Class IIa sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: The most common activity assay for dermonecrotic toxins
CC detects enzymatic activity by monitoring choline release from
CC substrate. Liberation of choline from sphingomyelin (SM) or
CC lysophosphatidylcholine (LPC) is commonly assumed to result from
CC substrate hydrolysis, giving either ceramide-1-phosphate (C1P) or
CC lysophosphatidic acid (LPA), respectively, as a second product.
CC However, two studies from Lajoie and colleagues (2013 and 2015) report
CC the observation of exclusive formation of cyclic phosphate products as
CC second products, resulting from intramolecular transphosphatidylation.
CC Cyclic phosphates have vastly different biological properties from
CC their monoester counterparts, and they may be relevant to the pathology
CC of brown spider envenomation. {ECO:0000250|UniProtKB:A0A0D4WTV1,
CC ECO:0000250|UniProtKB:A0A0D4WV12, ECO:0000250|UniProtKB:Q4ZFU2}.
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DR EMBL; DQ218155; ABA62021.1; -; mRNA.
DR PDB; 3RLG; X-ray; 1.60 A; A=28-306.
DR PDB; 3RLH; X-ray; 1.72 A; A=1-306.
DR PDBsum; 3RLG; -.
DR PDBsum; 3RLH; -.
DR AlphaFoldDB; P0CE80; -.
DR SMR; P0CE80; -.
DR EvolutionaryTrace; P0CE80; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR SUPFAM; SSF51695; SSF51695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Dermonecrotic toxin; Direct protein sequencing;
KW Disulfide bond; Hemolysis; Lipid degradation; Lipid metabolism; Lyase;
KW Magnesium; Metal-binding; Secreted; Signal; Toxin; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..26
FT /evidence="ECO:0000269|PubMed:9790962"
FT /id="PRO_0000035579"
FT CHAIN 27..306
FT /note="Dermonecrotic toxin LiSicTox-alphaIA1a"
FT /evidence="ECO:0000305|PubMed:9790962"
FT /id="PRO_0000035580"
FT ACT_SITE 38
FT /evidence="ECO:0000269|PubMed:18760322,
FT ECO:0000269|PubMed:19455508, ECO:0000269|PubMed:21301094,
FT ECO:0000269|PubMed:21590705, ECO:0000269|PubMed:27233517"
FT ACT_SITE 74
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:27233517"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21301094,
FT ECO:0000269|PubMed:21616057, ECO:0000312|PDB:3RLG,
FT ECO:0000312|PDB:3RLH"
FT BINDING 60
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21301094,
FT ECO:0000269|PubMed:21616057, ECO:0000312|PDB:3RLG,
FT ECO:0000312|PDB:3RLH"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:21301094,
FT ECO:0000269|PubMed:21616057, ECO:0000312|PDB:3RLG,
FT ECO:0000312|PDB:3RLH"
FT DISULFID 78..84
FT /evidence="ECO:0000269|PubMed:21301094,
FT ECO:0000269|PubMed:21616057, ECO:0000312|PDB:3RLG,
FT ECO:0000312|PDB:3RLH"
FT DISULFID 80..223
FT /evidence="ECO:0000269|PubMed:21301094,
FT ECO:0000269|PubMed:21616057, ECO:0000312|PDB:3RLG,
FT ECO:0000312|PDB:3RLH"
FT MUTAGEN 38
FT /note="H->A: Loss of catalytic activity on sphingomyelin
FT and lysophosphatidylcholine, and loss of hemolytic,
FT vascular permeability, nephrotoxic, and dermonecrotic
FT activities. Loss of catalytic activity on sphingomyelin and
FT lysophosphatidylcholine, and loss of hemolytic, vascular
FT permeability, and dermonecrotic activities; when associated
FT with A-74."
FT /evidence="ECO:0000269|PubMed:18760322,
FT ECO:0000269|PubMed:19455508, ECO:0000269|PubMed:21301094,
FT ECO:0000269|PubMed:21590705, ECO:0000269|PubMed:27233517"
FT MUTAGEN 58
FT /note="E->A: Loss of catalytic activity on sphingomyelin.
FT Loss of catalytic activity on sphingomyelin and
FT lysophosphatidylcholine, high decrease of hemolytic
FT activity, and loss of vascular permeability and
FT dermonecrotic activities; when associated with A-60."
FT /evidence="ECO:0000269|PubMed:27233517"
FT MUTAGEN 60
FT /note="D->A: Loss of catalytic activity on sphingomyelin.
FT Loss of catalytic activity on sphingomyelin and
FT lysophosphatidylcholine, high decrease of hemolytic
FT activity, and loss of vascular permeability and
FT dermonecrotic activities; when associated with A-58."
FT /evidence="ECO:0000269|PubMed:27233517"
FT MUTAGEN 74
FT /note="H->A: Loss of catalytic activity on sphingomyelin.
FT Loss of catalytic activity on sphingomyelin and
FT lysophosphatidylcholine, and high decrease of hemolytic
FT activity; when associated with A-38."
FT /evidence="ECO:0000269|PubMed:27233517"
FT MUTAGEN 80
FT /note="C->A: Moderate decrease of catalytic activity on
FT sphingomyelin and lysophosphatidylcholine, and moderate
FT decrease of hemolytic, vascular permeability, and
FT dermonecrotic activities; when associated with A-223."
FT /evidence="ECO:0000269|PubMed:27233517"
FT MUTAGEN 120
FT /note="K->A: Important decrease of catalytic activity on
FT sphingomyelin and lysophosphatidylcholine, and moderate
FT decrease of hemolytic, vascular permeability, and
FT dermonecrotic activities."
FT /evidence="ECO:0000269|PubMed:27233517"
FT MUTAGEN 122
FT /note="G->A: No or very weak change in catalytic activity
FT on sphingomyelin and lysophosphatidylcholine, and no change
FT in hemolytic, vascular permeability, and dermonecrotic
FT activities."
FT /evidence="ECO:0000269|PubMed:27233517"
FT MUTAGEN 223
FT /note="C->A: Moderate decrease of catalytic activity on
FT sphingomyelin and lysophosphatidylcholine, and moderate
FT decrease of hemolytic, vascular permeability, and
FT dermonecrotic activities; when associated with A-80."
FT /evidence="ECO:0000269|PubMed:27233517"
FT MUTAGEN 249
FT /note="Y->A: Loss of catalytic activity on sphingomyelin
FT and lysophosphatidylcholine, high decrease of hemolytic
FT activity, and loss of vascular permeability and
FT dermonecrotic activities."
FT /evidence="ECO:0000269|PubMed:27233517"
FT MUTAGEN 251
FT /note="W->A: Moderate decrease of catalytic activity on
FT sphingomyelin and lysophosphatidylcholine, and moderate
FT decrease of hemolytic, vascular permeability, and
FT dermonecrotic activities."
FT /evidence="ECO:0000269|PubMed:27233517"
FT CONFLICT 58
FT /note="E -> EI (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="S -> F (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:3RLG"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:3RLG"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:3RLG"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:3RLG"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:3RLG"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:3RLG"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3RLG"
FT HELIX 129..143
FT /evidence="ECO:0007829|PDB:3RLG"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:3RLG"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:3RLG"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:3RLG"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:3RLG"
FT HELIX 182..187
FT /evidence="ECO:0007829|PDB:3RLG"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:3RLG"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:3RLG"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:3RLG"
FT HELIX 229..238
FT /evidence="ECO:0007829|PDB:3RLG"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:3RLG"
FT HELIX 256..264
FT /evidence="ECO:0007829|PDB:3RLG"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:3RLG"
FT HELIX 275..282
FT /evidence="ECO:0007829|PDB:3RLG"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:3RLG"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:3RLG"
SQ SEQUENCE 306 AA; 34158 MW; A62718AE5D9FADAE CRC64;
MLPYIVLVLG CWSVLSQAAQ TDDEERAGNR RPIWIMGHMV NAIGQIDEFV NLGANSIETD
VSFDDNANPE YTYHGIPCDC GRNCKKYENF NDFLKGLRSA TTPGNSKYQE KLVLVVFDLK
TGSLYDNQAN DAGKKLAKNL LQHYWNNGNN GGRAYIVLSI PDLNHYPLIK GFKDQLTKDG
HPELMDKVGH DFSGNDDIGD VGKAYKKAGI TGHIWQSDGI TNCLPRGLSR VNAAVANRDS
ANGFINKVYY WTVDKRSTTR DALDAGVDGI MTNYPDVITD VLNEAAYKKK FRVATYDENP
WVTFKK
