ACTPC_ACTFR
ID ACTPC_ACTFR Reviewed; 179 AA.
AC B9W5G6; P86212;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=DELTA-actitoxin-Afr1a {ECO:0000303|PubMed:22683676};
DE Short=DELTA-AITX-Afr1a {ECO:0000303|PubMed:22683676};
DE AltName: Full=Alpha-helical pore-forming toxin {ECO:0000303|PubMed:21300287, ECO:0000303|PubMed:22728830, ECO:0000303|PubMed:25716479};
DE Short=PFT {ECO:0000303|PubMed:21300287, ECO:0000303|PubMed:22728830, ECO:0000303|PubMed:25716479};
DE AltName: Full=Cytolysin {ECO:0000303|PubMed:25759390};
DE AltName: Full=Fragaceatoxin C {ECO:0000303|PubMed:19563820, ECO:0000303|PubMed:21300287, ECO:0000303|PubMed:22728830, ECO:0000303|PubMed:25759390};
DE Short=fraC {ECO:0000303|PubMed:19563820, ECO:0000303|PubMed:21300287, ECO:0000303|PubMed:22728830, ECO:0000303|PubMed:25759390};
OS Actinia fragacea (Strawberry anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Actinia.
OX NCBI_TaxID=396334;
RN [1]
RP PROTEIN SEQUENCE OF 1-15, NUCLEOTIDE SEQUENCE [MRNA] OF 13-179, FUNCTION,
RP SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=19563820; DOI=10.1016/j.toxicon.2009.06.022;
RA Bellomio A., Morante K., Barlic A., Gutierrez-Aguirre I., Viguera A.R.,
RA Gonzalez-Manas J.M.;
RT "Purification, cloning and characterization of fragaceatoxin C, a novel
RT actinoporin from the sea anemone Actinia fragacea.";
RL Toxicon 54:869-880(2009).
RN [2]
RP REVIEW.
RX PubMed=19268680; DOI=10.1016/j.toxicon.2009.02.026;
RA Kristan K.C., Viero G., Dalla Serra M., Macek P., Anderluh G.;
RT "Molecular mechanism of pore formation by actinoporins.";
RL Toxicon 54:1125-1134(2009).
RN [3]
RP NOMENCLATURE.
RX PubMed=22683676; DOI=10.1016/j.toxicon.2012.05.020;
RA Oliveira J.S., Fuentes-Silva D., King G.F.;
RT "Development of a rational nomenclature for naming peptide and protein
RT toxins from sea anemones.";
RL Toxicon 60:539-550(2012).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=27608188; DOI=10.1002/anie.201606742;
RA Wloka C., Mutter N.L., Soskine M., Maglia G.;
RT "Alpha-Helical Fragaceatoxin C Nanopore Engineered for Double-Stranded and
RT Single-Stranded Nucleic Acid Analysis.";
RL Angew. Chem. Int. Ed. 55:12494-12498(2016).
RN [5]
RP MASS SPECTROMETRY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=31295915; DOI=10.3390/toxins11070401;
RA Morante K., Bellomio A., Viguera A.R., Gonzalez-Manas J.M., Tsumoto K.,
RA Caaveiro J.M.M.;
RT "The isolation of new pore-forming toxins from the sea anemone Actinia
RT fragacea provides insights into the mechanisms of actinoporin evolution.";
RL Toxins 11:0-0(2019).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-179, AND SUBUNIT.
RX PubMed=21300287; DOI=10.1016/j.str.2010.11.013;
RA Mechaly A.E., Bellomio A., Gil-Carton D., Morante K., Valle M.,
RA Gonzalez-Manas J.M., Guerin D.M.;
RT "Structural insights into the oligomerization and architecture of
RT eukaryotic membrane pore-forming toxins.";
RL Structure 19:181-191(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS), AND SUBUNIT.
RX PubMed=22728830; DOI=10.1016/j.jsb.2012.06.003;
RA Mechaly A.E., Bellomio A., Morante K., Agirre J., Gil-Carton D., Valle M.,
RA Gonzalez-Manas J.M., Guerin D.M.;
RT "Pores of the toxin FraC assemble into 2D hexagonal clusters in both
RT crystal structures and model membranes.";
RL J. Struct. Biol. 180:312-317(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.29 ANGSTROMS) OF 3-179 OF MUTANT PRO-16, AND
RP MUTAGENESIS OF PHE-16.
RX PubMed=25759390; DOI=10.1074/jbc.m114.615211;
RA Morante K., Caaveiro J.M., Tanaka K., Gonzalez-Manas J.M., Tsumoto K.;
RT "A pore-forming toxin requires a specific residue for its activity in
RT membranes with particular physicochemical properties.";
RL J. Biol. Chem. 290:10850-10861(2015).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) IN WATER-SOLUBLE STATE; IN MONOMERIC
RP LIPID-BOUND FORM; IN PREPORE FORM AND IN FULLY ASSEMBLED TRANSMEMBRANE
RP PORE, AND MUTAGENESIS OF VAL-8; VAL-60; LYS-69; TRP-112; TRP-116 AND
RP TRP-149.
RX PubMed=25716479; DOI=10.1038/ncomms7337;
RA Tanaka K., Caaveiro J.M., Morante K., Gonzalez-Manas J.M., Tsumoto K.;
RT "Structural basis for self-assembly of a cytolytic pore lined by protein
RT and lipid.";
RL Nat. Commun. 6:6337-6337(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 3-179 IN COMPLEX WITH
RP CARBOHYDRATES VIA THE LIPID-BINDING MODULE.
RX PubMed=28630155; DOI=10.1098/rstb.2016.0216;
RA Tanaka K., Caaveiro J.M.M., Morante K., Tsumoto K.;
RT "Haemolytic actinoporins interact with carbohydrates using their lipid-
RT binding module.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 372:0-0(2017).
CC -!- FUNCTION: Pore-forming toxin (PFT) that consists of a crown-shaped
CC octamer or nonamer that forms cation-selective hydrophilic pores of
CC about 1.5 nm (inside) and 13 nm (outside) (PubMed:21300287,
CC PubMed:25716479). It causes cardiac stimulation and hemolysis
CC (HC(50)=1.6 nM) (PubMed:19563820, PubMed:31295915, PubMed:25759390).
CC Interestingly, the Phe-16 is crucial for hemolysis (PubMed:25759390).
CC Pore formation is a multi-step process that involves specific
CC recognition of membrane sphingomyelin (but neither cholesterol nor
CC phosphatidylcholine) using aromatic rich region and adjacent
CC phosphocholine (POC) binding site, firm binding to the membrane (mainly
CC driven by hydrophobic interactions) accompanied by the transfer of the
CC N-terminal region to the lipid-water interface and finally pore
CC formation after oligomerization of monomers (PubMed:19563820,
CC PubMed:25716479). It is probable that a dimeric form is an assembly
CC intermediate before the complete oligomerization (PubMed:25716479). The
CC formation of stable pores occurs only in vesicles composed of DOPC/SM
CC (there is no oligomerization when the PFT is treated with vesicles of
CC DOPC or SM alone) (PubMed:25716479). The transmembrane pore displays 8
CC lateral perforations, one at each subunit-subunit interface, partially
CC occupied by the acyl-chain region of a bridging lipid
CC (PubMed:25716479). Each pore contains 24 lipid molecules, firmly bound
CC to each subunit, that is, 3 lipids (L1, L2, L3, L4 and/or L5) are
CC associated to each subunit (PubMed:25716479). Lipid L1 bridges 2
CC subunits, whereas lipids L2 and L3 bind to sites at single subunit
CC (PubMed:25716479). {ECO:0000269|PubMed:19563820,
CC ECO:0000269|PubMed:21300287, ECO:0000269|PubMed:25716479,
CC ECO:0000269|PubMed:25759390}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Stable up to about 53 degrees Celsius. {ECO:0000269|PubMed:31295915};
CC -!- SUBUNIT: Octamer or nonamer in membranes (PubMed:21300287,
CC PubMed:22728830, PubMed:25716479). Monomer in the soluble state
CC (PubMed:21300287, PubMed:22728830, PubMed:25716479).
CC {ECO:0000269|PubMed:21300287, ECO:0000269|PubMed:22728830,
CC ECO:0000269|PubMed:25716479}.
CC -!- INTERACTION:
CC B9W5G6; B9W5G6: -; NbExp=2; IntAct=EBI-15910829, EBI-15910829;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19563820}.
CC Nematocyst {ECO:0000250|UniProtKB:P61914}. Target cell membrane
CC {ECO:0000269|PubMed:19563820, ECO:0000269|PubMed:21300287,
CC ECO:0000269|PubMed:25716479}. Note=Forms an alpha-helical membrane
CC channel in the prey (PubMed:19563820,PubMed:21300287,PubMed:25716479).
CC -!- DOMAIN: The N-terminal region, before the pore is formed, is bound to
CC the lipid membrane. It partitions into the lipid-water interface and
CC stabilizes the monomeric molecule on the membrane. Finally, it
CC traverses the bilayer, thus forming the transmembrane pore.
CC {ECO:0000250|UniProtKB:P61914}.
CC -!- MASS SPECTROMETRY: Mass=19719; Mass_error=3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:19563820};
CC -!- MASS SPECTROMETRY: Mass=19720; Mass_error=3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:31295915};
CC -!- BIOTECHNOLOGY: Has been engineered for DNA analysis in nanopore
CC technology. {ECO:0000269|PubMed:27608188}.
CC -!- MISCELLANEOUS: This protein has been found to bind carbohydrates, since
CC it shows a substantial delay in elution profile in size-exclusion
CC chromatography. The carbohydrate pocket ovelaps with the lipid-binding
CC module of actinoporins. {ECO:0000269|PubMed:28630155}.
CC -!- SIMILARITY: Belongs to the actinoporin family. Sea anemone subfamily.
CC {ECO:0000305}.
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DR EMBL; FM958450; CAX16792.1; -; mRNA.
DR PDB; 3LIM; X-ray; 1.80 A; A/B/C/D/E/F=2-179.
DR PDB; 3VWI; X-ray; 1.70 A; A/B/C/D=1-179.
DR PDB; 3W9P; X-ray; 2.10 A; A/B=1-179.
DR PDB; 3ZWG; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O=1-179.
DR PDB; 3ZWJ; X-ray; 2.37 A; A/B/C/D/E/F/G/H/I=1-179.
DR PDB; 4TSL; X-ray; 1.60 A; A/B=1-179.
DR PDB; 4TSN; X-ray; 1.57 A; A/B/C/D=1-179.
DR PDB; 4TSO; X-ray; 2.30 A; A/B=1-179.
DR PDB; 4TSP; X-ray; 2.15 A; A/B=1-179.
DR PDB; 4TSQ; X-ray; 1.60 A; A/B/C/D/E/F=1-179.
DR PDB; 4TSY; X-ray; 3.14 A; A/B/C/D=1-179.
DR PDB; 4WDC; X-ray; 1.29 A; A=3-179.
DR PDB; 5BPG; X-ray; 2.14 A; A/B/C/D=1-179.
DR PDB; 5GWF; X-ray; 1.55 A; A/B/C/D=3-179.
DR PDBsum; 3LIM; -.
DR PDBsum; 3VWI; -.
DR PDBsum; 3W9P; -.
DR PDBsum; 3ZWG; -.
DR PDBsum; 3ZWJ; -.
DR PDBsum; 4TSL; -.
DR PDBsum; 4TSN; -.
DR PDBsum; 4TSO; -.
DR PDBsum; 4TSP; -.
DR PDBsum; 4TSQ; -.
DR PDBsum; 4TSY; -.
DR PDBsum; 4WDC; -.
DR PDBsum; 5BPG; -.
DR PDBsum; 5GWF; -.
DR AlphaFoldDB; B9W5G6; -.
DR SMR; B9W5G6; -.
DR DIP; DIP-59108N; -.
DR TCDB; 1.C.38.1.8; the pore-forming equinatoxin (equinatoxin) family.
DR EvolutionaryTrace; B9W5G6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:InterPro.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006812; P:cation transport; IEA:InterPro.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0046931; P:pore complex assembly; IEA:InterPro.
DR Gene3D; 2.60.270.20; -; 1.
DR InterPro; IPR009104; Anemon_actinoporin-like.
DR InterPro; IPR015926; Cytolysin/lectin.
DR Pfam; PF06369; Anemone_cytotox; 1.
DR SUPFAM; SSF63724; SSF63724; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Direct protein sequencing; Hemolysis;
KW Ion transport; Lipid-binding; Membrane; Nematocyst; Secreted;
KW Target cell membrane; Target membrane; Toxin; Transmembrane; Transport.
FT CHAIN 1..179
FT /note="DELTA-actitoxin-Afr1a"
FT /evidence="ECO:0000305|PubMed:19563820"
FT /id="PRO_0000381730"
FT REGION 1..29
FT /note="N-terminal alpha-helix that contributes to the pore"
FT /evidence="ECO:0000305|PubMed:21300287"
FT REGION 105..120
FT /note="Trp-rich region, which is important for the binding
FT to lipid membrane"
FT /evidence="ECO:0000250|UniProtKB:P61914"
FT MOTIF 144..146
FT /note="Cell attachment site"
FT /evidence="ECO:0000250|UniProtKB:P61914, ECO:0000255"
FT BINDING 31
FT /ligand="an N-(acyl)-sphingosylphosphocholine"
FT /ligand_id="ChEBI:CHEBI:64583"
FT /ligand_label="1"
FT /ligand_note="bridging lipid L1"
FT /note="in subunit A; in oligomeric forms only"
FT /evidence="ECO:0000305|PubMed:25716479"
FT BINDING 51
FT /ligand="N-acetyl-D-glucosamine 6-sulfate"
FT /ligand_id="ChEBI:CHEBI:84775"
FT /evidence="ECO:0000269|PubMed:28630155"
FT BINDING 53
FT /ligand="an N-(acyl)-sphingosylphosphocholine"
FT /ligand_id="ChEBI:CHEBI:64583"
FT /ligand_label="2"
FT /ligand_note="lipid L2"
FT /note="in monomeric and oligomeric forms"
FT /evidence="ECO:0000305|PubMed:25716479"
FT BINDING 53
FT /ligand="N-acetyl-D-glucosamine 6-sulfate"
FT /ligand_id="ChEBI:CHEBI:84775"
FT /evidence="ECO:0000269|PubMed:28630155"
FT BINDING 54
FT /ligand="an N-(acyl)-sphingosylphosphocholine"
FT /ligand_id="ChEBI:CHEBI:64583"
FT /ligand_label="2"
FT /ligand_note="lipid L2"
FT /note="in monomeric and oligomeric forms"
FT /evidence="ECO:0000305|PubMed:25716479"
FT BINDING 79
FT /ligand="an N-(acyl)-sphingosylphosphocholine"
FT /ligand_id="ChEBI:CHEBI:64583"
FT /ligand_label="1"
FT /ligand_note="bridging lipid L1"
FT /note="in subunit B; in oligomeric forms only"
FT /evidence="ECO:0000305|PubMed:25716479"
FT BINDING 85
FT /ligand="an N-(acyl)-sphingosylphosphocholine"
FT /ligand_id="ChEBI:CHEBI:64583"
FT /ligand_label="2"
FT /ligand_note="lipid L2"
FT /note="in monomeric and oligomeric forms"
FT /evidence="ECO:0000305|PubMed:25716479"
FT BINDING 108
FT /ligand="an N-(acyl)-sphingosylphosphocholine"
FT /ligand_id="ChEBI:CHEBI:64583"
FT /ligand_label="2"
FT /ligand_note="lipid L2"
FT /note="in monomeric and oligomeric forms"
FT /evidence="ECO:0000305|PubMed:25716479"
FT BINDING 113
FT /ligand="an N-(acyl)-sphingosylphosphocholine"
FT /ligand_id="ChEBI:CHEBI:64583"
FT /ligand_label="2"
FT /ligand_note="lipid L2"
FT /note="in monomeric and oligomeric forms"
FT /evidence="ECO:0000305|PubMed:25716479"
FT BINDING 114
FT /ligand="an N-(acyl)-sphingosylphosphocholine"
FT /ligand_id="ChEBI:CHEBI:64583"
FT /ligand_label="5"
FT /ligand_note="lipid L5"
FT /note="in monomeric and oligomeric forms"
FT /evidence="ECO:0000305|PubMed:25716479"
FT BINDING 116
FT /ligand="an N-(acyl)-sphingosylphosphocholine"
FT /ligand_id="ChEBI:CHEBI:64583"
FT /ligand_label="3"
FT /ligand_note="lipid L3"
FT /note="in monomeric and oligomeric forms"
FT /evidence="ECO:0000305|PubMed:25716479"
FT BINDING 133
FT /ligand="an N-(acyl)-sphingosylphosphocholine"
FT /ligand_id="ChEBI:CHEBI:64583"
FT /ligand_label="4"
FT /ligand_note="lipid L4"
FT /note="in monomeric and oligomeric forms"
FT /evidence="ECO:0000305|PubMed:25716479"
FT BINDING 137
FT /ligand="an N-(acyl)-sphingosylphosphocholine"
FT /ligand_id="ChEBI:CHEBI:64583"
FT /ligand_label="3"
FT /ligand_note="lipid L3"
FT /note="in monomeric and oligomeric forms"
FT /evidence="ECO:0000305|PubMed:25716479"
FT BINDING 138
FT /ligand="an N-(acyl)-sphingosylphosphocholine"
FT /ligand_id="ChEBI:CHEBI:64583"
FT /ligand_label="4"
FT /ligand_note="lipid L4"
FT /note="in monomeric and oligomeric forms"
FT /evidence="ECO:0000305|PubMed:25716479"
FT BINDING 138
FT /ligand="N-acetyl-D-glucosamine 6-sulfate"
FT /ligand_id="ChEBI:CHEBI:84775"
FT /evidence="ECO:0000269|PubMed:28630155"
FT BINDING 144
FT /ligand="an N-(acyl)-sphingosylphosphocholine"
FT /ligand_id="ChEBI:CHEBI:64583"
FT /ligand_label="5"
FT /ligand_note="lipid L5"
FT /note="in monomeric and oligomeric forms"
FT /evidence="ECO:0000305|PubMed:25716479"
FT BINDING 168
FT /ligand="an N-(acyl)-sphingosylphosphocholine"
FT /ligand_id="ChEBI:CHEBI:64583"
FT /ligand_label="1"
FT /ligand_note="bridging lipid L1"
FT /note="in subunit A; in oligomeric forms only"
FT /evidence="ECO:0000305|PubMed:25716479"
FT SITE 16
FT /note="Part of the hydrophobic cavity (in subunit A) that
FT receives Val-60 from the adjacent subunit (B); essential in
FT hemolysis, since it is critical for pore formation in
FT cholesterol-rich membrane cells (such as red blood cells)"
FT /evidence="ECO:0000305|PubMed:21300287,
FT ECO:0000305|PubMed:25716479, ECO:0000305|PubMed:25759390"
FT SITE 60
FT /note="Protrudes from one subunit (B) and inserts into the
FT hydrophobic cavity from the adjacent subunit (A)"
FT /evidence="ECO:0000305|PubMed:21300287,
FT ECO:0000305|PubMed:25716479"
FT SITE 149
FT /note="Part of the hydrophobic cavity (in subunit A) that
FT receives Val-60 from the adjacent subunit (B)"
FT /evidence="ECO:0000305|PubMed:21300287,
FT ECO:0000305|PubMed:25716479"
FT SITE 163
FT /note="Part of the hydrophobic cavity (in subunit A) that
FT receives Val-60 from the adjacent subunit (B)"
FT /evidence="ECO:0000305|PubMed:21300287"
FT MUTAGEN 8
FT /note="V->C: In V8C/K69C; loss of ability to form stable
FT pores after addition of a new disulfide bond."
FT /evidence="ECO:0000269|PubMed:25716479"
FT MUTAGEN 16
FT /note="F->A,G,P: Loss of pore formation ability in
FT cholesterol-rich membranes, but does not change effect on
FT membranes with low cholesterol content."
FT /evidence="ECO:0000269|PubMed:25759390"
FT MUTAGEN 60
FT /note="V->E: V60E/W149A; decrease in hemolytic activity,
FT suggesting that this mutant forms functional but
FT structurally weak pores."
FT /evidence="ECO:0000269|PubMed:25716479"
FT MUTAGEN 69
FT /note="K->C: In V8C/K69C; loss of ability to form stable
FT pores after addition of a new disulfide bond."
FT /evidence="ECO:0000269|PubMed:25716479"
FT MUTAGEN 112
FT /note="W->R: In W112R/W116F; loss of ability to bind
FT membranes."
FT /evidence="ECO:0000269|PubMed:25716479"
FT MUTAGEN 116
FT /note="W->F: In W112R/W116F; loss of ability to bind
FT membranes."
FT /evidence="ECO:0000269|PubMed:25716479"
FT MUTAGEN 149
FT /note="W->A: In V60E/W149A; decrease in hemolytic activity,
FT suggesting that this mutant forms functional but
FT structurally weak pores."
FT /evidence="ECO:0000269|PubMed:25716479"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:4WDC"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:4WDC"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:4WDC"
FT STRAND 30..43
FT /evidence="ECO:0007829|PDB:4WDC"
FT STRAND 45..54
FT /evidence="ECO:0007829|PDB:4WDC"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4WDC"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:4WDC"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4WDC"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:4WDC"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:4WDC"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:4WDC"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:4WDC"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:4WDC"
FT STRAND 146..155
FT /evidence="ECO:0007829|PDB:4WDC"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:4WDC"
FT STRAND 166..178
FT /evidence="ECO:0007829|PDB:4WDC"
SQ SEQUENCE 179 AA; 19719 MW; 2BEBB150A05FFBEC CRC64;
SADVAGAVID GAGLGFDVLK TVLEALGNVK RKIAVGIDNE SGKTWTAMNT YFRSGTSDIV
LPHKVAHGKA LLYNGQKNRG PVATGVVGVI AYSMSDGNTL AVLFSVPYDY NWYSNWWNVR
VYKGQKRADQ RMYEELYYHR SPFRGDNGWH SRGLGYGLKS RGFMNSSGHA ILEIHVTKA
