3L21A_BUNMU
ID 3L21A_BUNMU Reviewed; 95 AA.
AC P60615; P01378; Q9PRI6; Q9YGD1; Q9YI06; Q9YI07; Q9YI09; Q9YI10; Q9YI11;
AC Q9YI12; Q9YI13;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Alpha-bungarotoxin {ECO:0000303|PubMed:5027709};
DE Short=Alpha-Bgtx {ECO:0000303|PubMed:3507686};
DE Short=Alpha-Btx {ECO:0000303|PubMed:16549768};
DE AltName: Full=Alpha-bungarotoxin, isoform A31 {ECO:0000305};
DE Short=Alpha-BTX A31;
DE Short=Alpha-BgTx(A31);
DE Short=Alpha-bungarotoxin (A31);
DE Short=BGTX A31;
DE AltName: Full=Alpha-elapitoxin-Bm2a {ECO:0000305};
DE Short=Alpha-EPTX-Bm2a {ECO:0000305};
DE AltName: Full=Long neurotoxin 1;
DE Flags: Precursor;
OS Bungarus multicinctus (Many-banded krait).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Bungarinae; Bungarus.
OX NCBI_TaxID=8616;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Venom, and Venom gland;
RX PubMed=9837992; DOI=10.1093/nar/26.24.5624;
RA Liu L.-F., Chang C.-C., Liau M.-Y., Kuo K.-W.;
RT "Genetic characterization of the mRNAs encoding alpha-bungarotoxin:
RT isoforms and RNA editing in Bungarus multicinctus gland cells.";
RL Nucleic Acids Res. 26:5624-5629(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Liver, and Venom gland;
RX PubMed=10497260; DOI=10.1093/nar/27.20.3970;
RA Chang L.-S., Lin S.-K., Huang H.-B., Hsiao M.;
RT "Genetic organization of alpha-bungarotoxins from Bungarus multicinctus
RT (Taiwan banded krait): evidence showing that the production of alpha-
RT bungarotoxin isotoxins is not derived from edited mRNAs.";
RL Nucleic Acids Res. 27:3970-3975(1999).
RN [3]
RP PROTEIN SEQUENCE OF 22-95, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom;
RX PubMed=5027709; DOI=10.1515/bchm2.1972.353.1.243;
RA Mebs D., Narita K., Iwanaga S., Samejima Y., Lee C.Y.;
RT "Purification, properties and amino acid sequence of alpha-bungarotoxin
RT from the venom of Bungarus multicinctus.";
RL Hoppe-Seyler's Z. Physiol. Chem. 353:243-262(1972).
RN [4]
RP SEQUENCE REVISION TO 30-32; 88-89 AND 92-93.
RC TISSUE=Venom;
RX PubMed=3653402; DOI=10.1016/0014-5793(87)80195-3;
RA Ohta M., Ohta K., Nishitani H., Hayashi K.;
RT "Primary structure of alpha-bungarotoxin. Six amino acid residues differ
RT from the previously reported sequence.";
RL FEBS Lett. 222:79-82(1987).
RN [5]
RP PROTEIN SEQUENCE OF 22-95.
RC TISSUE=Venom;
RX PubMed=2458724; DOI=10.1016/s0006-291x(88)80576-x;
RA Chuang L.Y., Chang C.-C.;
RT "Isolation of antigenically reactive peptide fragments and localization of
RT antigenic regions of alpha-bungarotoxin.";
RL Biochem. Biophys. Res. Commun. 155:870-876(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-95.
RC TISSUE=Venom gland;
RX PubMed=7488184; DOI=10.1006/bbrc.1995.2732;
RA Kuo K.-W., Chen Y.C., Chang C.-C.;
RT "cDNA sequence analysis and expression of alpha-bungarotoxin from Taiwan
RT banded krait (Bungarus multicinctus).";
RL Biochem. Biophys. Res. Commun. 216:1088-1094(1995).
RN [7]
RP SEQUENCE REVISION TO 30-32 AND 88-89.
RC TISSUE=Venom;
RX PubMed=3401449; DOI=10.1021/bi00408a018;
RA Kosen P.A., Finer-Moore J., McCarthy M.P., Basus V.J.;
RT "Structural studies of alpha-bungarotoxin. 3. Corrections in the primary
RT sequence and X-ray structure and characterization of an isotoxic alpha-
RT bungarotoxin.";
RL Biochemistry 27:2775-2781(1988).
RN [8]
RP EPITOPE MAPPING.
RX PubMed=2476330; DOI=10.1016/0014-5793(89)81018-x;
RA Kase R., Kitagawa H., Hayashi K., Tanoue K., Inagaki F.;
RT "Neutralizing monoclonal antibody specific for alpha-bungarotoxin:
RT preparation and characterization of the antibody, and localization of
RT antigenic region of alpha-bungarotoxin.";
RL FEBS Lett. 254:106-110(1989).
RN [9]
RP FUNCTION.
RC TISSUE=Venom;
RX PubMed=9305882; DOI=10.1074/jbc.272.39.24279;
RA Servent D., Winckler-Dietrich V., Hu H.-Y., Kessler P., Drevet P.,
RA Bertrand D., Menez A.;
RT "Only snake curaremimetic toxins with a fifth disulfide bond have high
RT affinity for the neuronal alpha7 nicotinic receptor.";
RL J. Biol. Chem. 272:24279-24286(1997).
RN [10]
RP FUNCTION.
RX PubMed=9840221; DOI=10.1016/s0197-0186(98)00033-3;
RA Dajas-Bailador F., Costa G., Dajas F., Emmett S.;
RT "Effects of alpha-erabutoxin, alpha-bungarotoxin, alpha-cobratoxin and
RT fasciculin on the nicotine-evoked release of dopamine in the rat striatum
RT in vivo.";
RL Neurochem. Int. 33:307-312(1998).
RN [11]
RP FUNCTION.
RX PubMed=16549768; DOI=10.1073/pnas.0600847103;
RA McCann C.M., Bracamontes J., Steinbach J.H., Sanes J.R.;
RT "The cholinergic antagonist alpha-bungarotoxin also binds and blocks a
RT subset of GABA receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5149-5154(2006).
RN [12]
RP FUNCTION.
RX PubMed=26221036; DOI=10.1074/jbc.m115.648824;
RA Kudryavtsev D.S., Shelukhina I.V., Son L.V., Ojomoko L.O., Kryukova E.V.,
RA Lyukmanova E.N., Zhmak M.N., Dolgikh D.A., Ivanov I.A., Kasheverov I.E.,
RA Starkov V.G., Ramerstorfer J., Sieghart W., Tsetlin V.I., Utkin Y.N.;
RT "Neurotoxins from snake venoms and alpha-conotoxin ImI inhibit functionally
RT active ionotropic gamma-aminobutyric acid (GABA) receptors.";
RL J. Biol. Chem. 290:22747-22758(2015).
RN [13]
RP FUNCTION.
RX PubMed=25634239; DOI=10.1016/j.neuropharm.2015.01.001;
RA Hannan S., Mortensen M., Smart T.G.;
RT "Snake neurotoxin alpha-bungarotoxin is an antagonist at native GABA(A)
RT receptors.";
RL Neuropharmacology 93:28-40(2015).
RN [14] {ECO:0007744|PDB:2ABX}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-95, AND DISULFIDE BOND.
RX PubMed=3507686; DOI=10.1093/protein/1.1.37;
RA Love R.A., Stroud R.M.;
RT "The crystal structure of alpha-bungarotoxin at 2.5-A resolution: relation
RT to solution structure and binding to acetylcholine receptor.";
RL Protein Eng. 1:37-46(1986).
RN [15]
RP STRUCTURE BY NMR OF 22-95.
RX PubMed=3401447; DOI=10.1021/bi00408a016;
RA Basus V.J., Billeter M., Love R.A., Stroud R.M., Kuntz I.D.;
RT "Structural studies of alpha-bungarotoxin. 1. Sequence-specific 1H NMR
RT resonance assignments.";
RL Biochemistry 27:2763-2771(1988).
RN [16]
RP STRUCTURE BY NMR OF 22-95.
RX PubMed=3401448; DOI=10.1021/bi00408a017;
RA Basus V.J., Scheek R.M.;
RT "Structural studies of alpha-bungarotoxin. 2. 1H NMR assignments via an
RT improved relayed coherence transfer nuclear overhauser enhancement
RT experiment.";
RL Biochemistry 27:2772-2775(1988).
RN [17] {ECO:0007744|PDB:1ABT}
RP STRUCTURE BY NMR OF 22-95.
RX PubMed=8241115; DOI=10.1021/bi00097a004;
RA Basus V.J., Song G., Hawrot E.;
RT "NMR solution structure of an alpha-bungarotoxin/nicotinic receptor peptide
RT complex.";
RL Biochemistry 32:12290-12298(1993).
RN [18] {ECO:0007744|PDB:1BXP, ECO:0007744|PDB:2BTX}
RP STRUCTURE BY NMR OF 22-95.
RX PubMed=9177168; DOI=10.1073/pnas.94.12.6059;
RA Scherf T., Balass M., Fuchs S., Katchalski-Katzir E., Anglister J.;
RT "Three-dimensional solution structure of the complex of alpha-bungarotoxin
RT with a library-derived peptide.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6059-6064(1997).
RN [19] {ECO:0007744|PDB:1IDG, ECO:0007744|PDB:1IDH, ECO:0007744|PDB:1IDI, ECO:0007744|PDB:1IDL}
RP STRUCTURE BY NMR OF 22-95 IN COMPLEX WITH A 18-RESIDUE PEPTIDE HOMOLOGOUS
RP TO THE BINDING REGION OF THE ALPHA-1 SUBUNIT OF ACETYLCHOLINE RECEPTOR.
RX PubMed=11312275; DOI=10.1074/jbc.m102300200;
RA Zeng H., Moise L., Grant M.A., Hawrot E.;
RT "The solution structure of the complex formed between alpha-bungarotoxin
RT and an 18-mer cognate peptide derived from the alpha 1 subunit of the
RT nicotinic acetylcholine receptor from Torpedo californica.";
RL J. Biol. Chem. 276:22930-22940(2001).
RN [20] {ECO:0007744|PDB:1HAA, ECO:0007744|PDB:1HAJ}
RP STRUCTURE BY NMR OF 22-95 IN COMPLEX WITH A 13-RESIDUE PEPTIDE HOMOLOGOUS
RP TO THE BINDING REGION OF THE ALPHA SUBUNIT OF ACETYLCHOLINE RECEPTOR.
RX PubMed=11381118; DOI=10.1073/pnas.111164298;
RA Scherf T., Kasher R., Balass M., Fridkin M., Fuchs S.,
RA Katchalski-Katzir E.;
RT "A beta -hairpin structure in a 13-mer peptide that binds alpha
RT -bungarotoxin with high affinity and neutralizes its toxicity.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6629-6634(2001).
RN [21] {ECO:0007744|PDB:1HOY, ECO:0007744|PDB:1IK8, ECO:0007744|PDB:1IKC, ECO:0007744|PDB:1JBD}
RP STRUCTURE BY NMR OF 22-95 IN COMPLEX WITH A 13-RESIDUE PEPTIDE INHIBITING
RP BINDING WITH ACETYLCHOLINE RECEPTOR.
RX PubMed=11814338; DOI=10.1021/bi011012f;
RA Scarselli M., Spiga O., Ciutti A., Bernini A., Bracci L., Lelli B.,
RA Lozzi L., Calamandrei D., Di Maro D., Klein S., Niccolai N.;
RT "NMR structure of alpha-bungarotoxin free and bound to a mimotope of the
RT nicotinic acetylcholine receptor.";
RL Biochemistry 41:1457-1463(2002).
RN [22] {ECO:0007744|PDB:1KC4, ECO:0007744|PDB:1KFH, ECO:0007744|PDB:1KL8}
RP STRUCTURE BY NMR OF 22-95 IN COMPLEX WITH A 19-RESIDUE PEPTIDE HOMOLOGOUS
RP TO THE BINDING REGION OF THE ALPHA-7 SUBUNIT OF ACETYLCHOLINE RECEPTOR.
RX PubMed=11790782; DOI=10.1074/jbc.m110320200;
RA Moise L., Piserchio A., Basus V.J., Hawrot E.;
RT "NMR structural analysis of alpha-bungarotoxin and its complex with the
RT principal alpha-neurotoxin-binding sequence on the alpha 7 subunit of a
RT neuronal nicotinic acetylcholine receptor.";
RL J. Biol. Chem. 277:12406-12417(2002).
RN [23] {ECO:0007744|PDB:1L4W, ECO:0007744|PDB:1LJZ}
RP STRUCTURE BY NMR OF 22-95 IN COMPLEX WITH A 21-RESIDUE PEPTIDE HOMOLOGOUS
RP TO THE BINDING REGION OF THE ALPHA-1 SUBUNIT OF ACETYLCHOLINE RECEPTOR.
RX PubMed=12160749; DOI=10.1016/s0896-6273(02)00773-0;
RA Samson A.O., Scherf T., Eisenstein M., Chill J.H., Anglister J.;
RT "The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins
RT and species-specific resistance to alpha-bungarotoxin revealed by NMR.";
RL Neuron 35:319-332(2002).
CC -!- FUNCTION: Binds with high affinity to muscular (tested on Torpedo
CC marmorata, Kd=0.4 nM) and neuronal (tested on chimeric alpha-7/CHRNA7,
CC Kd=0.95 nM) nicotinic acetylcholine receptor (nAChR) and inhibits
CC acetylcholine from binding to the receptor, thereby impairing
CC neuromuscular and neuronal transmission (PubMed:9305882). It also shows
CC an activity on GABA(A) receptors (PubMed:16549768, PubMed:25634239). It
CC antagonises GABA-activated currents with high potency when tested on
CC primary hippocampal neurons (PubMed:25634239). It inhibits
CC recombinantly expressed GABA(A) receptors composed of alpha-2-beta-2-
CC gamma-2 (GABRA2-GABRB2-GABRG2) subunits with high potency (62.3%
CC inhibition at 20 uM of toxin) (PubMed:25634239). It also shows a weaker
CC inhibition on GABA(A) receptors composed of alpha-1-beta-2-gamma-2
CC (GABRA1-GABRB2-GABRG2) subunits, alpha-4-beta-2-gamma-2 (GABRA4-GABRB2-
CC GABRG2) subunits, and alpha-5-beta-2-gamma-2 (GABRA5-GABRB2-GABRG2)
CC subunits (PubMed:25634239). A very weak inhibition is also observed on
CC GABA(A) receptor composed of alpha-1-beta-3-gamma-2 (GABRA1-GABRB3-
CC GABRG2) (PubMed:26221036). It has also been shown to bind and inhibit
CC recombinant GABA(A) receptor beta-3/GABRB3 subunit (Kd=about 50 nM)
CC (PubMed:16549768). In addition, it blocks the extracellular increase of
CC dopamine evoked by nicotine only at the higher dose (4.2 uM)
CC (PubMed:9840221). In vivo, when intraperitoneally injected into mice,
CC induces flaccid paralysis of the limbs and respiratory distress, and
CC causes death in a dose-dependent manner. {ECO:0000269|PubMed:16549768,
CC ECO:0000269|PubMed:25634239, ECO:0000269|PubMed:9305882,
CC ECO:0000269|PubMed:9840221}.
CC -!- SUBUNIT: Monomer in solution, homodimer in crystal state.
CC {ECO:0000269|PubMed:11312275, ECO:0000269|PubMed:11381118,
CC ECO:0000269|PubMed:11790782, ECO:0000269|PubMed:11814338,
CC ECO:0000269|PubMed:12160749}.
CC -!- INTERACTION:
CC P60615; Q05941: Chrna7; Xeno; NbExp=4; IntAct=EBI-7516391, EBI-79422;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:5027709}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC -!- TOXIC DOSE: LD(50) is 0.3 mg/kg by subcutaneous injection.
CC -!- MISCELLANEOUS: Is identical to Alpha-bungarotoxin (A31) from B.candidus
CC (AC Q7T3J2). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the snake three-finger toxin family. Long-chain
CC subfamily. Type II alpha-neurotoxin sub-subfamily. {ECO:0000305}.
CC -!- CAUTION: PubMed:9837992 indicates that a number of mRNA with sequence
CC conflict(s) are produced by RNA editing. This seems not to be the case
CC as discussed in PubMed:10497260. {ECO:0000305}.
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DR EMBL; AF056400; AAC83981.1; -; mRNA.
DR EMBL; AF056401; AAC83982.1; -; Genomic_DNA.
DR EMBL; AF056402; AAC83983.1; -; mRNA.
DR EMBL; AF056403; AAC83984.1; -; mRNA.
DR EMBL; AF056404; AAC83985.1; -; mRNA.
DR EMBL; AF056405; AAC83986.1; -; mRNA.
DR EMBL; AF056406; AAC83987.1; -; mRNA.
DR EMBL; AF056407; AAC83988.1; -; mRNA.
DR EMBL; AF056408; AAC83989.1; -; mRNA.
DR EMBL; AF056409; AAC83990.1; -; mRNA.
DR EMBL; AF056410; AAC83991.1; -; mRNA.
DR EMBL; AF056411; AAC83992.1; -; mRNA.
DR EMBL; AF056412; AAC83993.1; -; mRNA.
DR EMBL; AF056413; AAC83994.1; -; mRNA.
DR EMBL; AF056415; AAC83996.1; -; mRNA.
DR EMBL; AF056416; AAC83997.1; -; mRNA.
DR EMBL; Y17694; CAB51844.1; -; Genomic_DNA.
DR EMBL; Y17058; CAB51842.1; -; mRNA.
DR EMBL; X91990; CAA63045.1; -; mRNA.
DR PIR; A31519; N2KF1U.
DR PDB; 1ABT; NMR; -; A=22-95.
DR PDB; 1BXP; NMR; -; A=22-95.
DR PDB; 1HAA; NMR; -; A=22-95.
DR PDB; 1HAJ; NMR; -; A=22-95.
DR PDB; 1HC9; X-ray; 1.80 A; B=22-95.
DR PDB; 1HOY; NMR; -; A=22-95.
DR PDB; 1IDG; NMR; -; A=22-95.
DR PDB; 1IDH; NMR; -; A=22-95.
DR PDB; 1IDI; NMR; -; A=22-95.
DR PDB; 1IDL; NMR; -; A=22-95.
DR PDB; 1IK8; NMR; -; A=22-95.
DR PDB; 1IKC; NMR; -; A=22-95.
DR PDB; 1JBD; NMR; -; A=22-95.
DR PDB; 1KC4; NMR; -; A=22-95.
DR PDB; 1KFH; NMR; -; A=22-95.
DR PDB; 1KL8; NMR; -; A=22-95.
DR PDB; 1L4W; NMR; -; A=22-95.
DR PDB; 1LJZ; NMR; -; A=22-95.
DR PDB; 1RGJ; NMR; -; A=22-95.
DR PDB; 2ABX; X-ray; 2.50 A; A/B=22-95.
DR PDB; 2BTX; NMR; -; A=22-95.
DR PDB; 6UWZ; EM; 2.69 A; F/G=22-95.
DR PDBsum; 1ABT; -.
DR PDBsum; 1BXP; -.
DR PDBsum; 1HAA; -.
DR PDBsum; 1HAJ; -.
DR PDBsum; 1HC9; -.
DR PDBsum; 1HOY; -.
DR PDBsum; 1IDG; -.
DR PDBsum; 1IDH; -.
DR PDBsum; 1IDI; -.
DR PDBsum; 1IDL; -.
DR PDBsum; 1IK8; -.
DR PDBsum; 1IKC; -.
DR PDBsum; 1JBD; -.
DR PDBsum; 1KC4; -.
DR PDBsum; 1KFH; -.
DR PDBsum; 1KL8; -.
DR PDBsum; 1L4W; -.
DR PDBsum; 1LJZ; -.
DR PDBsum; 1RGJ; -.
DR PDBsum; 2ABX; -.
DR PDBsum; 2BTX; -.
DR PDBsum; 6UWZ; -.
DR AlphaFoldDB; P60615; -.
DR BMRB; P60615; -.
DR SMR; P60615; -.
DR IntAct; P60615; 5.
DR MINT; P60615; -.
DR BindingDB; P60615; -.
DR TCDB; 1.C.74.1.2; the snake cytotoxin (sct) family.
DR EvolutionaryTrace; P60615; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd00206; snake_toxin; 1.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR003571; Snake_3FTx.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR018354; Snake_toxin_con_site.
DR InterPro; IPR035076; Toxin/TOLIP.
DR Pfam; PF00087; Toxin_TOLIP; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00272; SNAKE_TOXIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylcholine receptor inhibiting toxin;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Neurotoxin; Postsynaptic neurotoxin; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:2458724,
FT ECO:0000269|PubMed:5027709"
FT CHAIN 22..95
FT /note="Alpha-bungarotoxin"
FT /evidence="ECO:0000269|PubMed:2458724,
FT ECO:0000269|PubMed:5027709"
FT /id="PRO_0000035406"
FT DISULFID 24..44
FT /evidence="ECO:0000269|PubMed:3507686,
FT ECO:0000312|PDB:2ABX"
FT DISULFID 37..65
FT /evidence="ECO:0000269|PubMed:3507686,
FT ECO:0000312|PDB:2ABX"
FT DISULFID 50..54
FT /evidence="ECO:0000269|PubMed:3507686,
FT ECO:0000312|PDB:2ABX"
FT DISULFID 69..80
FT /evidence="ECO:0000269|PubMed:3507686,
FT ECO:0000312|PDB:2ABX"
FT DISULFID 81..86
FT /evidence="ECO:0000269|PubMed:3507686,
FT ECO:0000312|PDB:2ABX"
FT CONFLICT 48
FT /note="M -> V (in Ref. 1; AAC83985)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="F -> S (in Ref. 1; AAC83996)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="S -> N (in Ref. 1; AAC83986)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="R -> K (in Ref. 1; AAC83982/AAC83983/AAC83984/
FT AAC83985/AAC83986/AAC83987/AAC83988/AAC83989)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="T -> P (in Ref. 1; AAC83996)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="P -> S (in Ref. 1; AAC83987)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="K -> E (in Ref. 1; AAC83996/AAC83997)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="K -> R (in Ref. 1; AAC83988)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="T -> S (in Ref. 1; AAC83996/AAC83997)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="K -> Q (in Ref. 1; AAC83990)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="N -> H (in Ref. 1; AAC83990)"
FT /evidence="ECO:0000305"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1HC9"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:1HC9"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1HC9"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:2ABX"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:1HC9"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1IDH"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:1HC9"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:1HC9"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1ABT"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1HC9"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1ABT"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1IDH"
SQ SEQUENCE 95 AA; 10285 MW; 589B26743ABBA5E4 CRC64;
MKTLLLTLVV VTIVCLDLGY TIVCHTTATS PISAVTCPPG ENLCYRKMWC DAFCSSRGKV
VELGCAATCP SKKPYEEVTC CSTDKCNPHP KQRPG
