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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Type F / ATCC 23387;
DOI=10.1016/0378-1097(92)90408-G; PubMed=1398040 [NCBI, ExPASy, EBI, Israel, Japan]
East A.K.,
Richardson P.T.,
Allaway D.,
Collins M.D.,
Roberts T.A.,
Thompson D.E.;
"Sequence of the gene encoding type F neurotoxin of Clostridium botulinum.";
FEMS Microbiol. Lett. 75:225-230(1992).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
STRAIN=Type F / Hobbs FT10;
DOI=10.1007/BF01575751; PubMed=7764998 [NCBI, ExPASy, EBI, Israel, Japan]
East A.K.,
Collins M.D.;
"Conserved structure of genes encoding components of botulinum neurotoxin complex M and the sequence of the gene coding for the nontoxic component in nonproteolytic Clostridium botulinum type F.";
Curr. Microbiol. 29:69-77(1994).
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[3]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 634-1002.
PubMed=8408542 [NCBI, ExPASy, EBI, Israel, Japan]
Campbell K.D.,
Collins M.D.,
East A.K.;
"Gene probes for identification of the botulinal neurotoxin gene and specific identification of neurotoxin types B, E, and F.";
J. Clin. Microbiol. 31:2255-2262(1993).
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[4]
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IDENTIFICATION OF SUBSTRATE.
PubMed=8175689 [NCBI, ExPASy, EBI, Israel, Japan]
Yamasaki S.,
Baumeister A.,
Binz T.,
Blasi J.,
Link E.,
Cornille F.,
Roques B.,
Fykse E.M.,
Suedhof T.C.,
Jahn R.,
Niemann H.;
"Cleavage of members of the synaptobrevin/VAMP family by types D and F botulinal neurotoxins and tetanus toxin.";
J. Biol. Chem. 269:12764-12772(1994).
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- FUNCTION: Botulinum toxin acts by inhibiting neurotransmitter release. It binds to peripheral neuronal synapses, is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '58-Gln-|-Lys-59' bond of synaptobrevins-1 and -2.
- CATALYTIC ACTIVITY: Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.
- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
- SUBUNIT: Disulfide-linked heterodimer of a light chain (L) and a heavy chain (H). The light chain has the pharmacological activity, while the N- and C-terminal of the heavy chain mediate channel formation and toxin binding, respectively.
- SUBCELLULAR LOCATION: Secreted.
- MISCELLANEOUS: There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C1, D, E, F, and G.
- SIMILARITY: Belongs to the peptidase M27 family [view classification].
- WEB RESOURCE: Name=BotDB - A Database Resource for Clostridial Neurotoxins; URL="http://botdb.abcc.ncifcrf.gov/";.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 1274 AA [This is the length of the unprocessed precursor] |
Molecular weight: 146710 Da [This is the MW of the unprocessed precursor] |
CRC64: 5B99756A7438B921 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MPVAINSFNY NDPVNDDTIL YMQIPYEEKS KKYYKAFEIM RNVWIIPERN TIGTNPSDFD
70 80 90 100 110 120
PPASLKNGSS AYYDPNYLTT DAEKDRYLKT TIKLFKRINS NPAGKVLLQE ISYAKPYLGN
130 140 150 160 170 180
DHTPIDEFSP VTRTTSVNIK LSTNVESSML LNLLVLGAGP DIFESCCYPV RKLIDPDVVY
190 200 210 220 230 240
DPSNYGFGSI NIVTFSPEYE YTFNDISGGH NSSTESFIAD PAISLAHELI HALHGLYGAR
250 260 270 280 290 300
GVTYEETIEV KQAPLMIAEK PIRLEEFLTF GGQDLNIITS AMKEKIYNNL LANYEKIATR
310 320 330 340 350 360
LSEVNSAPPE YDINEYKDYF QWKYGLDKNA DGSYTVNENK FNEIYKKLYS FTESDLANKF
370 380 390 400 410 420
KVKCRNTYFI KYEFLKVPNL LDDDIYTVSE GFNIGNLAVN NRGQSIKLNP KIIDSIPDKG
430 440 450 460 470 480
LVEKIVKFCK SVIPRKGTKA PPRLCIRVNN SELFFVASES SYNENDINTP KEIDDTTNLN
490 500 510 520 530 540
NNYRNNLDEV ILDYNSQTIP QISNRTLNTL VQDNSYVPRY DSNGTSEIEE YDVVDFNVFF
550 560 570 580 590 600
YLHAQKVPEG ETNISLTSSI DTALLEESKD IFFSSEFIDT INKPVNAALF IDWISKVIRD
610 620 630 640 650 660
FTTEATQKST VDKIADISLI VPYVGLALNI IIEAEKGNFE EAFELLGVGI LLEFVPELTI
670 680 690 700 710 720
PVILVFTIKS YIDSYENKNK AIKAINNSLI EREAKWKEIY SWIVSNWLTR INTQFNKRKE
730 740 750 760 770 780
QMYQALQNQV DAIKTAIEYK YNNYTSDEKN RLESEYNINN IEEELNKKVS LAMKNIERFM
790 800 810 820 830 840
TESSISYLMK LINEAKVGKL KKYDNHVKSD LLNYILDHRS ILGEQTNELS DLVTSTLNSS
850 860 870 880 890 900
IPFELSSYTN DKILIIYFNR LYKKIKDSSI LDMRYENNKF IDISGYGSNI SINGNVYIYS
910 920 930 940 950 960
TNRNQFGIYN SRLSEVNIAQ NNDIIYNSRY QNFSISFWVR IPKHYKPMNH NREYTIINCM
970 980 990 1000 1010 1020
GNNNSGWKIS LRTVRDCEII WTLQDTSGNK ENLIFRYEEL NRISNYINKW IFVTITNNRL
1030 1040 1050 1060 1070 1080
GNSRIYINGN LIVEKSISNL GDIHVSDNIL FKIVGCDDET YVGIRYFKVF NTELDKTEIE
1090 1100 1110 1120 1130 1140
TLYSNEPDPS ILKNYWGNYL LYNKKYYLFN LLRKDKYITL NSGILNINQQ RGVTEGSVFL
1150 1160 1170 1180 1190 1200
NYKLYEGVEV IIRKNGPIDI SNTDNFVRKN DLAYINVVDR GVEYRLYADT KSEKEKIIRT
1210 1220 1230 1240 1250 1260
SNLNDSLGQI IVMDSIGNNC TMNFQNNNGS NIGLLGFHSN NLVASSWYYN NIRRNTSSNG
1270
CFWSSISKEN GWKE
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P30996 in FASTA format |
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