PA2B8_DABRR
ID PA2B8_DABRR Reviewed; 121 AA.
AC P59071; D0VX11;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Basic phospholipase A2 VRV-PL-VIIIa;
DE Short=svPLA2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:16596639};
DE AltName: Full=DPLA2;
DE AltName: Full=P1;
DE AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE AltName: Full=Phospholipase A2 4;
DE Short=PLA24;
OS Daboia russelii (Russel's viper) (Vipera russelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Viperinae; Daboia.
OX NCBI_TaxID=8707;
RN [1]
RP PROTEIN SEQUENCE, SUBUNIT, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=7940574; DOI=10.1016/0041-0101(94)90336-0;
RA Gowda T.V., Schmidt J., Middlebrook J.L.;
RT "Primary sequence determination of the most basic myonecrotic phospholipase
RT A2 from the venom of Vipera russelli.";
RL Toxicon 32:665-673(1994).
RN [2]
RP PROTEIN SEQUENCE OF 1-50, FUNCTION, TOXIC DOSE, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=8835338; DOI=10.1016/0041-0101(95)00114-x;
RA Tsai I.-H., Lu P.-J., Su J.-C.;
RT "Two types of Russell's viper revealed by variation in phospholipases A2
RT from venom of the subspecies.";
RL Toxicon 34:99-109(1996).
RN [3]
RP PROTEIN SEQUENCE OF 1-21, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=20203422; DOI=10.2220/biomedres.31.71;
RA Suzuki M., Itoh T., Bandaranayake B.M.A.I.K., Ranasinghe J.G.,
RA Athauda S.B., Moriyama A.;
RT "Molecular diversity in venom proteins of the Russell's viper (Daboia
RT russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka.";
RL Biomed. Res. 31:71-81(2010).
RN [4]
RP CHARACTERIZATION, AND TOXIC DOSE.
RC TISSUE=Venom;
RX PubMed=2718191; DOI=10.1016/0041-0101(89)90136-0;
RA Kasturi S., Gowda T.V.;
RT "Purification and characterization of a major phospholipase A2 from
RT Russell's viper (Vipera russelli) venom.";
RL Toxicon 27:229-237(1989).
RN [5]
RP FUNCTION.
RX PubMed=2115497;
RA Kasturi S., Rudrammaji L.M., Gowda T.V.;
RT "Antibodies to a phospholipase A2 from Vipera russelli selectively
RT neutralize venom neurotoxicity.";
RL Immunology 70:175-180(1990).
RN [6]
RP FUNCTION AS AN ANTICOAGULANT.
RX PubMed=18062812; DOI=10.1186/1472-6807-7-82;
RA Faure G., Gowda V.T., Maroun R.C.;
RT "Characterization of a human coagulation factor Xa-binding site on
RT Viperidae snake venom phospholipases A2 by affinity binding studies and
RT molecular bioinformatics.";
RL BMC Struct. Biol. 7:82-82(2007).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1-38.
RX PubMed=10686108; DOI=10.1006/jmbi.2000.3537;
RA Chandra V., Kaur P., Srinivasan A., Singh T.P.;
RT "Three-dimensional structure of a presynaptic neurotoxic phospholipase A2
RT from Daboia russelli pulchella at 2.4 A resolution.";
RL J. Mol. Biol. 296:1117-1126(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-49.
RX PubMed=11717491; DOI=10.1107/s0907444901014524;
RA Chandra V., Kaur P., Jasti J., Betzel C., Singh T.P.;
RT "Regulation of catalytic function by molecular association: structure of
RT phospholipase A2 from Daboia russelli pulchella (DPLA2) at 1.9 A
RT resolution.";
RL Acta Crystallogr. D 57:1793-1798(2001).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=12351825; DOI=10.1107/s0907444902013720;
RA Chandra V., Jasti J., Kaur P., Dey S., Srinivasan A., Betzel C.,
RA Singh T.P.;
RT "Design of specific peptide inhibitors of phospholipase A2: structure of a
RT complex formed between Russell's viper phospholipase A2 and a designed
RT peptide Leu-Ala-Ile-Tyr-Ser (LAIYS).";
RL Acta Crystallogr. D 58:1813-1819(2002).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-49.
RX PubMed=12206661; DOI=10.1021/bi0258593;
RA Chandra V., Jasti J., Kaur P., Srinivasan A., Betzel C., Singh T.P.;
RT "Structural basis of phospholipase A2 inhibition for the synthesis of
RT prostaglandins by the plant alkaloid aristolochic acid from a 1.7 A crystal
RT structure.";
RL Biochemistry 41:10914-10919(2002).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=12186870; DOI=10.1074/jbc.m206130200;
RA Chandra V., Jasti J., Kaur P., Dey S., Perbandt M., Srinivasan A.,
RA Betzel C., Singh T.P.;
RT "Crystal structure of a complex formed between a snake venom phospholipase
RT A(2) and a potent peptide inhibitor Phe-Leu-Ser-Tyr-Lys at 1.8 A
RT resolution.";
RL J. Biol. Chem. 277:41079-41085(2002).
RN [12] {ECO:0000312|PDB:1TGM}
RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH ASPIRIN AND CALCIUM
RP ION, COFACTOR, AND DISULFIDE BONDS.
RA Singh N., Jabeen T., Sharma S., Bhushan A., Singh T.P.;
RT "Crystal structure of a complex formed between group II phospholipase A2
RT and aspirin at 1.86 A resolution.";
RL Submitted (MAY-2004) to the PDB data bank.
RN [13] {ECO:0000312|PDB:1Q7A}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH THE
RP ANTI-INFLAMMATORY COMPOUND OXYPHENBUTAZONE, DISULFIDE BONDS, AND ACTIVITY
RP REGULATION.
RC TISSUE=Venom;
RX PubMed=15544328; DOI=10.1021/bi0483561;
RA Singh N., Jabeen T., Somvanshi R.K., Sharma S., Dey S., Singh T.P.;
RT "Phospholipase A2 as a target protein for nonsteroidal anti-inflammatory
RT drugs (NSAIDS): crystal structure of the complex formed between
RT phospholipase A2 and oxyphenbutazone at 1.6 A resolution.";
RL Biochemistry 43:14577-14583(2004).
RN [14] {ECO:0000312|PDB:1SV3, ECO:0000312|PDB:2ARM}
RP X-RAY CRYSTALLOGRAPHY (1.23 ANGSTROMS) IN COMPLEX WITH THE NATURAL
RP ANTI-INFLAMMATORY COMPOUNDS ANISIC ACID AND ATROPINE, CATALYTIC ACTIVITY,
RP DISULFIDE BONDS, ACTIVITY REGULATION, AND SUBUNIT.
RC TISSUE=Venom;
RX PubMed=16596639; DOI=10.1002/prot.20970;
RA Singh N., Jabeen T., Pal A., Sharma S., Perbandt M., Betzel C., Singh T.P.;
RT "Crystal structures of the complexes of a group IIA phospholipase A2 with
RT two natural anti-inflammatory agents, anisic acid, and atropine reveal a
RT similar mode of binding.";
RL Proteins 64:89-100(2006).
RN [15] {ECO:0000312|PDB:4QEM, ECO:0000312|PDB:4QER, ECO:0000312|PDB:4QF7, ECO:0000312|PDB:4QF8, ECO:0000312|PDB:4QGD}
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) IN COMPLEX WITH P-COUMARIC ACID,
RP RESVERATROL, SPERMIDINE, CORTICOSTERONE AND GRAMINE DERIVATIVE, DISULFIDE
RP BONDS, AND ACTIVITY REGULATION.
RX PubMed=25541253; DOI=10.1016/j.bbapap.2014.12.017;
RA Shukla P.K., Gautam L., Sinha M., Kaur P., Sharma S., Singh T.P.;
RT "Structures and binding studies of the complexes of phospholipase A2 with
RT five inhibitors.";
RL Biochim. Biophys. Acta 1854:269-277(2015).
CC -!- FUNCTION: Snake venom phospholipase A2 (PLA2) that shows weak
CC neurotoxicity and medium anticoagulant effects by binding to factor Xa
CC (F10) and inhibiting the prothrombinase activity (IC(50) is 130 nM)
CC (PubMed:18062812). It also damages vital organs such as lung, liver and
CC kidney, displays edema-inducing activities when injected into the foot
CC pads of mice and induces necrosis of muscle cells when injected into
CC the thigh muscle. Has a low enzymatic activity. PLA2 catalyzes the
CC calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-
CC phosphoglycerides. {ECO:0000269|PubMed:18062812,
CC ECO:0000269|PubMed:2115497, ECO:0000269|PubMed:8835338}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000269|PubMed:16596639};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305|Ref.12};
CC Note=Binds 1 Ca(2+) ion. {ECO:0000305|Ref.12};
CC -!- ACTIVITY REGULATION: Oxyphenbutazone (OPB), anisic acid and atropine
CC inhibit the enzymatic activity by binding at the substrate-binding site
CC (PubMed:15544328, PubMed:16596639). P-coumaric acid, resveratrol,
CC spermidine, corticosterone and gramine derivative inhibit the enzymatic
CC activity by binding at the substrate-binding site (PubMed:25541253).
CC {ECO:0000269|PubMed:15544328, ECO:0000269|PubMed:16596639,
CC ECO:0000269|PubMed:25541253}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16596639,
CC ECO:0000269|PubMed:7940574}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20203422,
CC ECO:0000269|PubMed:7940574, ECO:0000269|PubMed:8835338}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:20203422, ECO:0000305|PubMed:7940574,
CC ECO:0000305|PubMed:8835338}.
CC -!- TOXIC DOSE: LD(50) is between 5.3 and 5.5 mg/kg by intravenous
CC injection into mice. {ECO:0000269|PubMed:2718191,
CC ECO:0000269|PubMed:8835338}.
CC -!- MISCELLANEOUS: D.russelli pulchella is synonymous with D.russelii.
CC {ECO:0000305|PubMed:15544328, ECO:0000305|PubMed:16596639}.
CC -!- SIMILARITY: Belongs to the phospholipase A2 family. Group II subfamily.
CC D49 sub-subfamily. {ECO:0000305}.
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 PDB; 1CL5; X-ray; 2.45 A; A/B=1-121.
DR PDB; 1FB2; X-ray; 1.95 A; A/B=1-121.
DR PDB; 1FV0; X-ray; 1.70 A; A/B=1-121.
DR PDB; 1JQ8; X-ray; 2.00 A; A/B=1-121.
DR PDB; 1JQ9; X-ray; 1.80 A; A/B=1-121.
DR PDB; 1KPM; X-ray; 1.80 A; A/B=1-121.
DR PDB; 1OXL; X-ray; 1.80 A; A/B=1-121.
DR PDB; 1OYF; X-ray; 2.45 A; A=1-121.
DR PDB; 1Q6V; X-ray; 1.86 A; A=1-121.
DR PDB; 1Q7A; X-ray; 1.60 A; A=1-121.
DR PDB; 1SKG; X-ray; 1.21 A; A=1-121.
DR PDB; 1SQZ; X-ray; 1.20 A; A=1-121.
DR PDB; 1SV3; X-ray; 1.35 A; A=1-121.
DR PDB; 1SV9; X-ray; 2.71 A; A=1-121.
DR PDB; 1SXK; X-ray; 1.21 A; A=1-121.
DR PDB; 1TDV; X-ray; 1.70 A; A=1-121.
DR PDB; 1TG1; X-ray; 1.25 A; A=1-121.
DR PDB; 1TG4; X-ray; 1.70 A; A=1-121.
DR PDB; 1TGM; X-ray; 1.86 A; A=1-121.
DR PDB; 1TH6; X-ray; 1.23 A; A=1-121.
DR PDB; 1TJ9; X-ray; 1.10 A; A=1-121.
DR PDB; 1TJK; X-ray; 1.25 A; A=1-121.
DR PDB; 1TK4; X-ray; 1.10 A; A=1-121.
DR PDB; 1TP2; X-ray; 2.40 A; A/B=1-121.
DR PDB; 1Y38; X-ray; 2.44 A; A/B=1-121.
DR PDB; 1ZR8; X-ray; 2.03 A; A=1-121.
DR PDB; 1ZWP; X-ray; 1.10 A; A=1-121.
DR PDB; 1ZYX; X-ray; 1.95 A; A=1-121.
DR PDB; 2ARM; X-ray; 1.23 A; A=1-121.
DR PDB; 2B17; X-ray; 2.71 A; A=1-121.
DR PDB; 2DO2; X-ray; 2.60 A; A=1-121.
DR PDB; 2DPZ; X-ray; 2.10 A; A=1-121.
DR PDB; 2FNX; X-ray; 2.70 A; A=1-121.
DR PDB; 2G58; X-ray; 0.98 A; A=1-121.
DR PDB; 2GNS; X-ray; 2.30 A; A=1-121.
DR PDB; 2O1N; X-ray; 2.80 A; A=1-121.
DR PDB; 2OLI; X-ray; 2.21 A; A=1-121.
DR PDB; 2OTF; X-ray; 1.95 A; A=1-121.
DR PDB; 2OTH; X-ray; 2.90 A; A=1-121.
DR PDB; 2OUB; X-ray; 2.75 A; A=1-121.
DR PDB; 2OYF; X-ray; 1.20 A; A=1-121.
DR PDB; 2PB8; X-ray; 2.00 A; A=1-121.
DR PDB; 2PMJ; X-ray; 2.40 A; A=1-121.
DR PDB; 2PVT; X-ray; 2.10 A; A=1-121.
DR PDB; 2PWS; X-ray; 2.21 A; A=1-121.
DR PDB; 2PYC; X-ray; 1.50 A; A=1-121.
DR PDB; 2Q1P; X-ray; 1.50 A; A=1-121.
DR PDB; 2QHW; X-ray; 2.21 A; A=1-121.
DR PDB; 2QU9; X-ray; 2.08 A; A=1-121.
DR PDB; 2QUE; X-ray; 2.25 A; A=1-121.
DR PDB; 2QVD; X-ray; 1.93 A; A=1-121.
DR PDB; 2ZBH; X-ray; 2.60 A; A=1-121.
DR PDB; 3CBI; X-ray; 3.15 A; A/B/C/D=1-121.
DR PDB; 3FO7; X-ray; 1.40 A; A=1-121.
DR PDB; 3G8F; X-ray; 1.25 A; A=1-121.
DR PDB; 3H1X; X-ray; 1.40 A; A=1-121.
DR PDB; 4EIX; X-ray; 2.90 A; A=1-121.
DR PDB; 4FGA; X-ray; 2.30 A; A=1-121.
DR PDB; 4GFY; X-ray; 2.70 A; A=1-121.
DR PDB; 4GLD; X-ray; 1.69 A; A=1-121.
DR PDB; 4HMB; X-ray; 2.21 A; A=1-121.
DR PDB; 4QEM; X-ray; 1.20 A; A=1-121.
DR PDB; 4QER; X-ray; 1.20 A; A=1-121.
DR PDB; 4QF7; X-ray; 1.48 A; A=1-121.
DR PDB; 4QF8; X-ray; 1.65 A; A=1-121.
DR PDB; 4QGD; X-ray; 1.80 A; A=1-121.
DR PDB; 4QMC; X-ray; 1.09 A; A=1-121.
DR PDB; 5VET; X-ray; 2.00 A; A/B=1-121.
DR PDBsum; 1CL5; -.
DR PDBsum; 1FB2; -.
DR PDBsum; 1FV0; -.
DR PDBsum; 1JQ8; -.
DR PDBsum; 1JQ9; -.
DR PDBsum; 1KPM; -.
DR PDBsum; 1OXL; -.
DR PDBsum; 1OYF; -.
DR PDBsum; 1Q6V; -.
DR PDBsum; 1Q7A; -.
DR PDBsum; 1SKG; -.
DR PDBsum; 1SQZ; -.
DR PDBsum; 1SV3; -.
DR PDBsum; 1SV9; -.
DR PDBsum; 1SXK; -.
DR PDBsum; 1TDV; -.
DR PDBsum; 1TG1; -.
DR PDBsum; 1TG4; -.
DR PDBsum; 1TGM; -.
DR PDBsum; 1TH6; -.
DR PDBsum; 1TJ9; -.
DR PDBsum; 1TJK; -.
DR PDBsum; 1TK4; -.
DR PDBsum; 1TP2; -.
DR PDBsum; 1Y38; -.
DR PDBsum; 1ZR8; -.
DR PDBsum; 1ZWP; -.
DR PDBsum; 1ZYX; -.
DR PDBsum; 2ARM; -.
DR PDBsum; 2B17; -.
DR PDBsum; 2DO2; -.
DR PDBsum; 2DPZ; -.
DR PDBsum; 2FNX; -.
DR PDBsum; 2G58; -.
DR PDBsum; 2GNS; -.
DR PDBsum; 2O1N; -.
DR PDBsum; 2OLI; -.
DR PDBsum; 2OTF; -.
DR PDBsum; 2OTH; -.
DR PDBsum; 2OUB; -.
DR PDBsum; 2OYF; -.
DR PDBsum; 2PB8; -.
DR PDBsum; 2PMJ; -.
DR PDBsum; 2PVT; -.
DR PDBsum; 2PWS; -.
DR PDBsum; 2PYC; -.
DR PDBsum; 2Q1P; -.
DR PDBsum; 2QHW; -.
DR PDBsum; 2QU9; -.
DR PDBsum; 2QUE; -.
DR PDBsum; 2QVD; -.
DR PDBsum; 2ZBH; -.
DR PDBsum; 3CBI; -.
DR PDBsum; 3FO7; -.
DR PDBsum; 3G8F; -.
DR PDBsum; 3H1X; -.
DR PDBsum; 4EIX; -.
DR PDBsum; 4FGA; -.
DR PDBsum; 4GFY; -.
DR PDBsum; 4GLD; -.
DR PDBsum; 4HMB; -.
DR PDBsum; 4QEM; -.
DR PDBsum; 4QER; -.
DR PDBsum; 4QF7; -.
DR PDBsum; 4QF8; -.
DR PDBsum; 4QGD; -.
DR PDBsum; 4QMC; -.
DR PDBsum; 5VET; -.
DR AlphaFoldDB; P59071; -.
DR SMR; P59071; -.
DR BindingDB; P59071; -.
DR ChEMBL; CHEMBL3784910; -.
DR BRENDA; 3.1.1.4; 5485.
DR EvolutionaryTrace; P59071; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004623; F:phospholipase A2 activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0050482; P:arachidonic acid secretion; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
DR CDD; cd00125; PLA2c; 1.
DR Gene3D; 1.20.90.10; -; 1.
DR InterPro; IPR001211; PLipase_A2.
DR InterPro; IPR033112; PLipase_A2_Asp_AS.
DR InterPro; IPR016090; PLipase_A2_dom.
DR InterPro; IPR036444; PLipase_A2_dom_sf.
DR InterPro; IPR033113; PLipase_A2_His_AS.
DR PANTHER; PTHR11716; PTHR11716; 1.
DR Pfam; PF00068; Phospholip_A2_1; 1.
DR PRINTS; PR00389; PHPHLIPASEA2.
DR SMART; SM00085; PA2c; 1.
DR SUPFAM; SSF48619; SSF48619; 1.
DR PROSITE; PS00119; PA2_ASP; 1.
DR PROSITE; PS00118; PA2_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation cascade inhibiting toxin; Calcium;
KW Direct protein sequencing; Disulfide bond; Hemostasis impairing toxin;
KW Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding; Myotoxin;
KW Neurotoxin; Presynaptic neurotoxin; Secreted; Toxin.
FT CHAIN 1..121
FT /note="Basic phospholipase A2 VRV-PL-VIIIa"
FT /evidence="ECO:0000269|PubMed:7940574"
FT /id="PRO_0000161717"
FT ACT_SITE 47
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT ACT_SITE 89
FT /evidence="ECO:0000250|UniProtKB:P14418"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:1TGM"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:1TGM"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:1TGM"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|Ref.12, ECO:0007744|PDB:1TGM"
FT DISULFID 26..115
FT /evidence="ECO:0000269|PubMed:12186870,
FT ECO:0000269|PubMed:12351825, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:1JQ8, ECO:0007744|PDB:1JQ9,
FT ECO:0007744|PDB:1TGM"
FT DISULFID 28..44
FT /evidence="ECO:0000269|PubMed:12186870,
FT ECO:0000269|PubMed:12351825, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:1JQ8, ECO:0007744|PDB:1JQ9,
FT ECO:0007744|PDB:1TGM"
FT DISULFID 43..95
FT /evidence="ECO:0000269|PubMed:12186870,
FT ECO:0000269|PubMed:12351825, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:1JQ8, ECO:0007744|PDB:1JQ9,
FT ECO:0007744|PDB:1TGM"
FT DISULFID 49..121
FT /evidence="ECO:0000269|PubMed:12186870,
FT ECO:0000269|PubMed:12351825, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:1JQ8, ECO:0007744|PDB:1JQ9,
FT ECO:0007744|PDB:1TGM"
FT DISULFID 50..88
FT /evidence="ECO:0000269|PubMed:12186870,
FT ECO:0000269|PubMed:12351825, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:1JQ8, ECO:0007744|PDB:1JQ9,
FT ECO:0007744|PDB:1TGM"
FT DISULFID 57..81
FT /evidence="ECO:0000269|PubMed:12186870,
FT ECO:0000269|PubMed:12351825, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:1JQ8, ECO:0007744|PDB:1JQ9,
FT ECO:0007744|PDB:1TGM"
FT DISULFID 75..86
FT /evidence="ECO:0000269|PubMed:12186870,
FT ECO:0000269|PubMed:12351825, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:1JQ8, ECO:0007744|PDB:1JQ9,
FT ECO:0007744|PDB:1TGM"
FT HELIX 2..13
FT /evidence="ECO:0007829|PDB:2G58"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:2G58"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1TJ9"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:2G58"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2G58"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:4GFY"
FT HELIX 39..52
FT /evidence="ECO:0007829|PDB:2G58"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:3CBI"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2G58"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:2G58"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2G58"
FT HELIX 80..98
FT /evidence="ECO:0007829|PDB:2G58"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:2G58"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:2G58"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:2G58"
SQ SEQUENCE 121 AA; 13611 MW; 5CDF82DDA7DA638E CRC64;
SLLEFGKMIL EETGKLAIPS YSSYGCYCGW GGKGTPKDAT DRCCFVHDCC YGNLPDCNPK
SDRYKYKRVN GAIVCEKGTS CENRICECDK AAAICFRQNL NTYSKKYMLY PDFLCKGELK
C
