BXF_CLOBO
ID BXF_CLOBO Reviewed; 1274 AA.
AC P30996;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Botulinum neurotoxin type F;
DE Short=BoNT/F {ECO:0000303|PubMed:7764998};
DE AltName: Full=Bontoxilysin-F;
DE Contains:
DE RecName: Full=Botulinum neurotoxin F light chain;
DE Short=LC;
DE EC=3.4.24.69 {ECO:0000269|PubMed:8505288};
DE Contains:
DE RecName: Full=Botulinum neurotoxin F heavy chain;
DE Short=HC;
DE Flags: Precursor;
GN Name=botF;
OS Clostridium botulinum.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1491;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23387 / Type F;
RX PubMed=1398040; DOI=10.1016/0378-1097(92)90408-g;
RA East A.K., Richardson P.T., Allaway D., Collins M.D., Roberts T.A.,
RA Thompson D.E.;
RT "Sequence of the gene encoding type F neurotoxin of Clostridium
RT botulinum.";
RL FEMS Microbiol. Lett. 75:225-230(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
RC STRAIN=Hobbs FT10 / Type F;
RX PubMed=7764998; DOI=10.1007/bf01575751;
RA East A.K., Collins M.D.;
RT "Conserved structure of genes encoding components of botulinum neurotoxin
RT complex M and the sequence of the gene coding for the nontoxic component in
RT nonproteolytic Clostridium botulinum type F.";
RL Curr. Microbiol. 29:69-77(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 634-1002.
RC STRAIN=Craig 610 / Type F, and Hobbs FT10 / Type F;
RX PubMed=8408542; DOI=10.1128/jcm.31.9.2255-2262.1993;
RA Campbell K.D., Collins M.D., East A.K.;
RT "Gene probes for identification of the botulinal neurotoxin gene and
RT specific identification of neurotoxin types B, E, and F.";
RL J. Clin. Microbiol. 31:2255-2262(1993).
RN [4]
RP FUNCTION (BOTULINUM NEUROTOXIN F LIGHT CHAIN), IDENTIFICATION OF SUBSTRATE,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, COFACTOR, AND SUBCELLULAR LOCATION
RP (BOTULINUM NEUROTOXIN F LIGHT CHAIN).
RC STRAIN=Type F;
RX PubMed=8505288; DOI=10.1016/s0021-9258(19)50230-7;
RA Schiavo G., Shone C.C., Rossetto O., Alexander F.C., Montecucco C.;
RT "Botulinum neurotoxin serotype F is a zinc endopeptidase specific for
RT VAMP/synaptobrevin.";
RL J. Biol. Chem. 268:11516-11519(1993).
RN [5]
RP IDENTIFICATION OF SUBSTRATE, AND SUBCELLULAR LOCATION (BOTULINUM NEUROTOXIN
RP F LIGHT CHAIN).
RC STRAIN=Type F;
RX PubMed=8175689; DOI=10.1016/s0021-9258(18)99941-2;
RA Yamasaki S., Baumeister A., Binz T., Blasi J., Link E., Cornille F.,
RA Roques B., Fykse E.M., Suedhof T.C., Jahn R., Niemann H.;
RT "Cleavage of members of the synaptobrevin/VAMP family by types D and F
RT botulinal neurotoxins and tetanus toxin.";
RL J. Biol. Chem. 269:12764-12772(1994).
RN [6]
RP FUNCTION (BOTULINUM NEUROTOXIN F LIGHT CHAIN), AND CATALYTIC ACTIVITY.
RC STRAIN=Type F;
RX PubMed=8197120; DOI=10.1073/pnas.91.11.4688;
RA Yamasaki S., Hu Y., Binz T., Kalkuhl A., Kurazono H., Tamura T., Jahn R.,
RA Kandel E., Niemann H.;
RT "Synaptobrevin/vesicle-associated membrane protein (VAMP) of Aplysia
RT californica: structure and proteolysis by tetanus toxin and botulinal
RT neurotoxins type D and F.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4688-4692(1994).
RN [7]
RP REVIEW.
RX PubMed=28356439; DOI=10.1124/pr.116.012658;
RA Pirazzini M., Rossetto O., Eleopra R., Montecucco C.;
RT "Botulinum neurotoxins: Biology, pharmacology, and toxicology.";
RL Pharmacol. Rev. 69:200-235(2017).
RN [8] {ECO:0007744|PDB:2A8A, ECO:0007744|PDB:2A97}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-439 IN COMPLEX WITH ZINC,
RP FUNCTION (BOTULINUM NEUROTOXIN F LIGHT CHAIN), AND COFACTOR.
RX PubMed=16128577; DOI=10.1021/bi0510072;
RA Agarwal R., Binz T., Swaminathan S.;
RT "Structural analysis of botulinum neurotoxin serotype F light chain:
RT implications on substrate binding and inhibitor design.";
RL Biochemistry 44:11758-11765(2005).
CC -!- FUNCTION: [Botulinum neurotoxin type F]: Botulinum toxin causes flaccid
CC paralysis by inhibiting neurotransmitter (acetylcholine) release from
CC the presynaptic membranes of nerve terminals of the eukaryotic host
CC skeletal and autonomic nervous system, with frequent heart or
CC respiratory failure. Precursor of botulinum neurotoxin F which may have
CC 2 coreceptors; complex polysialylated gangliosides found on neural
CC tissue and specific membrane-anchored proteins found in synaptic
CC vesicles. Receptor proteins are exposed on host presynaptic cell
CC membrane during neurotransmitter release, when the toxin heavy chain
CC (HC) binds to them. Upon synaptic vesicle recycling the toxin is taken
CC up via the endocytic pathway. When the pH of the toxin-containing
CC endosome drops a structural rearrangement occurs so that the N-terminus
CC of the HC forms pores that allows the light chain (LC) to translocate
CC into the cytosol. Once in the cytosol the disulfide bond linking the 2
CC subunits is reduced and LC cleaves its target protein on synaptic
CC vesicles, preventing their fusion with the cytoplasmic membrane and
CC thus neurotransmitter release (By similarity). Whole toxin only has
CC protease activity after reduction, which releases LC (PubMed:8505288).
CC Requires complex eukaryotic host polysialogangliosides for full
CC neurotoxicity (By similarity). It is not clear whether a synaptic
CC vesicle protein acts as its receptor; there is evidence for and against
CC SV2 fulfilling this function (By similarity).
CC {ECO:0000250|UniProtKB:A7GBG3, ECO:0000269|PubMed:8505288}.
CC -!- FUNCTION: [Botulinum neurotoxin F light chain]: Has proteolytic
CC activity (PubMed:8505288, PubMed:8175689, PubMed:8197120). After
CC translocation into the eukaryotic host cytosol, inhibits
CC neurotransmitter release by acting as a zinc endopeptidase that
CC catalyzes the hydrolysis of the '60-Gln-|-Lys-61' bond of
CC synaptobrevin-1/VAMP1 and the equivalent 'Gln-|-Lys' sites in VAMP2 and
CC VAMP3 (PubMed:8505288, PubMed:8175689). Cleaves the '48-Gln-|-Lys-49'
CC bond of A.californica synaptobrevin (AC P35589) (PubMed:8197120).
CC {ECO:0000269|PubMed:8175689, ECO:0000269|PubMed:8197120,
CC ECO:0000269|PubMed:8505288, ECO:0000305|PubMed:16128577}.
CC -!- FUNCTION: [Botulinum neurotoxin F heavy chain]: Responsible for host
CC epithelial cell transcytosis, host nerve cell targeting and
CC translocation of light chain (LC) into host cytosol. Composed of 3
CC subdomains; the translocation domain (TD), and N-terminus and C-
CC terminus of the receptor-binding domain (RBD). The RBD is responsible
CC for the adherence of the toxin to the cell surface. It simultaneously
CC recognizes 2 coreceptors; polysialated gangliosides and the receptor
CC protein SV2A, SV2B and SV2C in close proximity on host synaptic
CC vesicles; although not all evidence indicates these are the receptors
CC (By similarity). The N-terminus of the TD wraps an extended belt around
CC the perimeter of the LC, protecting Zn(2+) in the active site; it may
CC also prevent premature LC dissociation from the translocation channel
CC and protect toxin prior to translocation (By similarity). The TD
CC inserts into synaptic vesicle membrane to allow translocation into the
CC host cytosol (By similarity). {ECO:0000250|UniProtKB:A7GBG3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Limited hydrolysis of proteins of the neuroexocytosis
CC apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on
CC small molecule substrates.; EC=3.4.24.69;
CC Evidence={ECO:0000269|PubMed:8197120, ECO:0000269|PubMed:8505288};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16128577, ECO:0000305|PubMed:8505288};
CC Note=Binds 1 zinc ion per subunit (PubMed:8505288, PubMed:16128577).
CC {ECO:0000269|PubMed:16128577, ECO:0000305|PubMed:8505288};
CC -!- ACTIVITY REGULATION: Proteolysis inhibited by 1,10-phenanthroline,
CC captopril and EDTA (PubMed:8505288). {ECO:0000269|PubMed:8505288}.
CC -!- SUBUNIT: Heterodimer; disulfide-linked heterodimer of a light chain
CC (LC) and a heavy chain (HC). The LC has the proteolytic/pharmacological
CC activity, while the N- and C-terminal of the HC mediate channel
CC formation and toxin binding, respectively. Interacts with host synaptic
CC vesicle glycoproteins SV2A, SV2B and SV2C (By similarity).
CC {ECO:0000250|UniProtKB:A7GBG3}.
CC -!- SUBCELLULAR LOCATION: [Botulinum neurotoxin type F]: Secreted
CC {ECO:0000250|UniProtKB:P0DPI0}.
CC -!- SUBCELLULAR LOCATION: [Botulinum neurotoxin F light chain]: Secreted
CC {ECO:0000250|UniProtKB:P0DPI0}. Host cytoplasm, host cytosol
CC {ECO:0000305|PubMed:8175689, ECO:0000305|PubMed:8505288}.
CC -!- SUBCELLULAR LOCATION: [Botulinum neurotoxin F heavy chain]: Secreted
CC {ECO:0000250|UniProtKB:P0DPI0}. Host synapse, host presynaptic cell
CC membrane {ECO:0000305}. Host cytoplasmic vesicle, host secretory
CC vesicle, host synaptic vesicle membrane {ECO:0000250|UniProtKB:P0DPI0};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- DOMAIN: [Botulinum neurotoxin F light chain]: Has protease activity
CC (PubMed:8505288, PubMed:8175689, PubMed:8197120).
CC {ECO:0000269|PubMed:8175689, ECO:0000269|PubMed:8197120,
CC ECO:0000269|PubMed:8505288}.
CC -!- DOMAIN: [Botulinum neurotoxin F heavy chain]: Has 3 functional domains;
CC the translocation domain (TD) and the receptor-binding domain (RBD)
CC which is further subdivided into N- and C-terminal domains (N-RBD and
CC C-RBD) (By similarity). The N-terminus of the TD wraps an extended belt
CC around the perimeter of the LC, protecting Zn(2+) in the active site
CC and may be a pseudosubstrate inhibitor which serves as an
CC intramolecular chaperone for the LC prior to its translocation into the
CC host cytosol (By similarity). The RBD binds transiently exposed
CC coreceptors on the host presynaptic cell membrane (By similarity).
CC {ECO:0000250|UniProtKB:A7GBG3}.
CC -!- MISCELLANEOUS: There are seven antigenically distinct forms of
CC botulinum neurotoxin: Types A, B, C, D, E, F, and G; new subtypes are
CC quite frequent.
CC -!- MISCELLANEOUS: Botulism poisoning is usually food-borne, either by
CC ingesting toxin or bacterial-contaminated food, or less frequently by
CC inhalation poisoning. In both cases the neurotoxin binds to the apical
CC surface of epithelial cells in the gut or airway. Toxin undergoes
CC receptor-mediated endocytosis (using a different receptor than on
CC target nerve cells), transcytosis across the epithelial cells and
CC release into the general circulation. Once in the general circulation
CC it binds to its target cells. {ECO:0000250|UniProtKB:P0DPI0}.
CC -!- SIMILARITY: Belongs to the peptidase M27 family. {ECO:0000305}.
CC -!- CAUTION: It is not clear whether a synaptic vesicle protein acts as its
CC receptor; there is evidence for and against SV2 fulfilling this
CC function. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=BotDB - A Database Resource for Clostridial
CC Neurotoxins;
CC URL="https://botdb.abcc.ncifcrf.gov/";
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DR EMBL; M92906; AAA23263.1; -; Genomic_DNA.
DR EMBL; S73676; AAC60475.1; -; Genomic_DNA.
DR EMBL; X70820; CAA50151.1; -; Genomic_DNA.
DR EMBL; X70816; CAA50147.1; -; Genomic_DNA.
DR PIR; I40813; I40813.
DR PIR; S48109; S48109.
DR PDB; 2A8A; X-ray; 2.00 A; A=1-439.
DR PDB; 2A97; X-ray; 1.80 A; A/B=1-439.
DR PDBsum; 2A8A; -.
DR PDBsum; 2A97; -.
DR AlphaFoldDB; P30996; -.
DR SMR; P30996; -.
DR IntAct; P30996; 2.
DR MINT; P30996; -.
DR BindingDB; P30996; -.
DR ChEMBL; CHEMBL2007627; -.
DR DrugBank; DB13901; Equine Botulinum Neurotoxin F Immune FAB2.
DR ABCD; P30996; 10 sequenced antibodies.
DR BRENDA; 3.4.24.69; 1462.
DR Reactome; R-HSA-5250981; Toxicity of botulinum toxin type F (botF).
DR EvolutionaryTrace; P30996; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044161; C:host cell cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0044164; C:host cell cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0044156; C:host cell junction; IEA:UniProtKB-KW.
DR GO; GO:0044231; C:host cell presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008320; F:protein transmembrane transporter activity; TAS:Reactome.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR DisProt; DP03019; -.
DR Gene3D; 1.20.1120.10; -; 1.
DR InterPro; IPR000395; Bot/tetX_LC.
DR InterPro; IPR036248; Clostridium_toxin_transloc.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR InterPro; IPR013104; Toxin_rcpt-bd_C.
DR InterPro; IPR012928; Toxin_rcpt-bd_N.
DR InterPro; IPR012500; Toxin_trans.
DR Pfam; PF01742; Peptidase_M27; 1.
DR Pfam; PF07951; Toxin_R_bind_C; 1.
DR Pfam; PF07953; Toxin_R_bind_N; 1.
DR Pfam; PF07952; Toxin_trans; 1.
DR PRINTS; PR00760; BONTOXILYSIN.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
DR SUPFAM; SSF58091; SSF58091; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Host cell membrane; Host cytoplasm;
KW Host cytoplasmic vesicle; Host membrane; Host synapse; Hydrolase;
KW Lipid-binding; Membrane; Metal-binding; Metalloprotease; Neurotoxin;
KW Protease; Secreted; Toxin; Transmembrane; Virulence; Zinc.
FT CHAIN 1..1274
FT /note="Botulinum neurotoxin type F"
FT /id="PRO_0000444921"
FT CHAIN 1..436
FT /note="Botulinum neurotoxin F light chain"
FT /id="PRO_0000029225"
FT CHAIN 437..1274
FT /note="Botulinum neurotoxin F heavy chain"
FT /id="PRO_0000029226"
FT REGION 440..862
FT /note="Translocation domain (TD)"
FT /evidence="ECO:0000250|UniProtKB:P0DPI0"
FT REGION 485..534
FT /note="Belt"
FT /evidence="ECO:0000250|UniProtKB:P0DPI0"
FT REGION 863..1087
FT /note="N-terminus of receptor binding domain (N-RBD)"
FT /evidence="ECO:0000250|UniProtKB:P0DPI0"
FT REGION 1088..1274
FT /note="C-terminus of receptor binding domain (C-RBD)"
FT /evidence="ECO:0000250|UniProtKB:P0DPI0"
FT MOTIF 1245..1248
FT /note="Host ganglioside-binding motif"
FT /evidence="ECO:0000250|UniProtKB:P0DPI0"
FT ACT_SITE 228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:16128577, ECO:0007744|PDB:2A8A,
FT ECO:0007744|PDB:2A97"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:16128577, ECO:0007744|PDB:2A8A,
FT ECO:0007744|PDB:2A97"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16128577,
FT ECO:0007744|PDB:2A8A, ECO:0007744|PDB:2A97"
FT DISULFID 429..445
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000250|UniProtKB:P0DPI0, ECO:0000305"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:2A97"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:2A97"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:2A97"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:2A97"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:2A97"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2A97"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:2A97"
FT HELIX 81..98
FT /evidence="ECO:0007829|PDB:2A97"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:2A97"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:2A97"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:2A97"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:2A97"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:2A97"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:2A97"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:2A97"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2A97"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:2A97"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:2A97"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:2A8A"
FT HELIX 221..236
FT /evidence="ECO:0007829|PDB:2A97"
FT TURN 241..245
FT /evidence="ECO:0007829|PDB:2A97"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:2A8A"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:2A8A"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:2A8A"
FT HELIX 264..270
FT /evidence="ECO:0007829|PDB:2A97"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:2A97"
FT HELIX 280..303
FT /evidence="ECO:0007829|PDB:2A97"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:2A97"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:2A97"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:2A97"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:2A97"
FT HELIX 353..360
FT /evidence="ECO:0007829|PDB:2A97"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:2A97"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:2A97"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:2A97"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:2A97"
FT HELIX 395..404
FT /evidence="ECO:0007829|PDB:2A97"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:2A97"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:2A97"
SQ SEQUENCE 1274 AA; 146710 MW; 5B99756A7438B921 CRC64;
MPVAINSFNY NDPVNDDTIL YMQIPYEEKS KKYYKAFEIM RNVWIIPERN TIGTNPSDFD
PPASLKNGSS AYYDPNYLTT DAEKDRYLKT TIKLFKRINS NPAGKVLLQE ISYAKPYLGN
DHTPIDEFSP VTRTTSVNIK LSTNVESSML LNLLVLGAGP DIFESCCYPV RKLIDPDVVY
DPSNYGFGSI NIVTFSPEYE YTFNDISGGH NSSTESFIAD PAISLAHELI HALHGLYGAR
GVTYEETIEV KQAPLMIAEK PIRLEEFLTF GGQDLNIITS AMKEKIYNNL LANYEKIATR
LSEVNSAPPE YDINEYKDYF QWKYGLDKNA DGSYTVNENK FNEIYKKLYS FTESDLANKF
KVKCRNTYFI KYEFLKVPNL LDDDIYTVSE GFNIGNLAVN NRGQSIKLNP KIIDSIPDKG
LVEKIVKFCK SVIPRKGTKA PPRLCIRVNN SELFFVASES SYNENDINTP KEIDDTTNLN
NNYRNNLDEV ILDYNSQTIP QISNRTLNTL VQDNSYVPRY DSNGTSEIEE YDVVDFNVFF
YLHAQKVPEG ETNISLTSSI DTALLEESKD IFFSSEFIDT INKPVNAALF IDWISKVIRD
FTTEATQKST VDKIADISLI VPYVGLALNI IIEAEKGNFE EAFELLGVGI LLEFVPELTI
PVILVFTIKS YIDSYENKNK AIKAINNSLI EREAKWKEIY SWIVSNWLTR INTQFNKRKE
QMYQALQNQV DAIKTAIEYK YNNYTSDEKN RLESEYNINN IEEELNKKVS LAMKNIERFM
TESSISYLMK LINEAKVGKL KKYDNHVKSD LLNYILDHRS ILGEQTNELS DLVTSTLNSS
IPFELSSYTN DKILIIYFNR LYKKIKDSSI LDMRYENNKF IDISGYGSNI SINGNVYIYS
TNRNQFGIYN SRLSEVNIAQ NNDIIYNSRY QNFSISFWVR IPKHYKPMNH NREYTIINCM
GNNNSGWKIS LRTVRDCEII WTLQDTSGNK ENLIFRYEEL NRISNYINKW IFVTITNNRL
GNSRIYINGN LIVEKSISNL GDIHVSDNIL FKIVGCDDET YVGIRYFKVF NTELDKTEIE
TLYSNEPDPS ILKNYWGNYL LYNKKYYLFN LLRKDKYITL NSGILNINQQ RGVTEGSVFL
NYKLYEGVEV IIRKNGPIDI SNTDNFVRKN DLAYINVVDR GVEYRLYADT KSEKEKIIRT
SNLNDSLGQI IVMDSIGNNC TMNFQNNNGS NIGLLGFHSN NLVASSWYYN NIRRNTSSNG
CFWSSISKEN GWKE
