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BXC_CBCP
ID   BXC_CBCP                Reviewed;        1291 AA.
AC   P18640;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   18-JUL-2018, sequence version 3.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=Botulinum neurotoxin type C;
DE            Short=BoNT/C;
DE   AltName: Full=Bontoxilysin-C1;
DE            Short=BoNT/C1 {ECO:0000303|PubMed:2204031};
DE   AltName: Full=Botulinum neurotoxin type C1;
DE   Contains:
DE     RecName: Full=Botulinum neurotoxin C light chain;
DE              Short=LC;
DE              EC=3.4.24.69 {ECO:0000269|PubMed:7737992};
DE   Contains:
DE     RecName: Full=Botulinum neurotoxin C heavy chain;
DE              Short=HC;
DE   Flags: Precursor;
OS   Clostridium botulinum C phage (Clostridium botulinum C bacteriophage).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae.
OX   NCBI_TaxID=12336;
OH   NCBI_TaxID=36828; Clostridium botulinum C.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=468C / phage c-st / Type C1;
RX   PubMed=2204031; DOI=10.1093/nar/18.16.4924;
RA   Hauser D., Eklund M.W., Kurazona H., Binz T., Niemann H., Gill D.M.,
RA   Boquet P., Popoff M.R.;
RT   "Nucleotide sequence of Clostridium botulinum C1 neurotoxin.";
RL   Nucleic Acids Res. 18:4924-4924(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Stockholm / Type C / phage C-ST;
RX   PubMed=2222445; DOI=10.1016/0006-291x(90)90828-b;
RA   Kimura K., Fujii N., Tsuzuki K., Murakami T., Indoh T., Yokosawa N.,
RA   Takeshi K., Syuto B., Oguma K.;
RT   "The complete nucleotide sequence of the gene coding for botulinum type C1
RT   toxin in the C-ST phage genome.";
RL   Biochem. Biophys. Res. Commun. 171:1304-1311(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION (BOTULINUM NEUROTOXIN TYPE C),
RP   EUKARYOTIC HOST RANGE, SUBUNIT, AND SUBCELLULAR LOCATION (BOTULINUM
RP   NEUROTOXIN C LIGHT CHAIN AND BOTULINUM NEUROTOXIN C HEAVY CHAIN).
RC   STRAIN=CB-19 / Type C;
RX   PubMed=16252491; DOI=10.1637/7347-022305r1.1;
RA   Takeda M., Tsukamoto K., Kohda T., Matsui M., Mukamoto M., Kozaki S.;
RT   "Characterization of the neurotoxin produced by isolates associated with
RT   avian botulism.";
RL   Avian Dis. 49:376-381(2005).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-26.
RC   STRAIN=Stockholm / Type C;
RX   PubMed=2450068; DOI=10.1128/iai.56.4.898-902.1988;
RA   Tsuzuki K., Yokosawa N., Syuto B., Ohishi I., Fujii N., Kimura K.,
RA   Oguma K.;
RT   "Establishment of a monoclonal antibody recognizing an antigenic site
RT   common to Clostridium botulinum type B, C1, D, and E toxins and tetanus
RT   toxin.";
RL   Infect. Immun. 56:898-902(1988).
RN   [5]
RP   FUNCTION (BOTULINUM NEUROTOXIN TYPE C).
RC   STRAIN=Type C;
RX   PubMed=2424493; DOI=10.1021/bi00358a020;
RA   Donovan J.J., Middlebrook J.L.;
RT   "Ion-conducting channels produced by botulinum toxin in planar lipid
RT   membranes.";
RL   Biochemistry 25:2872-2876(1986).
RN   [6]
RP   EUKARYOTIC HOST RANGE.
RC   STRAIN=Type C;
RX   PubMed=1978909; DOI=10.1016/0140-6736(90)93157-k;
RA   Oguma K., Yokota K., Hayashi S., Takeshi K., Kumagai M., Itoh N., Tachi N.,
RA   Chiba S.;
RT   "Infant botulism due to Clostridium botulinum type C toxin.";
RL   Lancet 336:1449-1450(1990).
RN   [7]
RP   FUNCTION (BOTULINUM NEUROTOXIN TYPE C), IDENTIFICATION OF SUBSTRATE,
RP   ACTIVITY REGULATION, AND SUBCELLULAR LOCATION (BOTULINUM NEUROTOXIN C LIGHT
RP   CHAIN).
RX   PubMed=7901002; DOI=10.1002/j.1460-2075.1993.tb06171.x;
RA   Blasi J., Chapman E.R., Yamasaki S., Binz T., Niemann H., Jahn R.;
RT   "Botulinum neurotoxin C1 blocks neurotransmitter release by means of
RT   cleaving HPC-1/syntaxin.";
RL   EMBO J. 12:4821-4828(1993).
RN   [8]
RP   SUBUNIT, AND SUBCELLULAR LOCATION (BOTULINUM NEUROTOXIN C LIGHT CHAIN AND
RP   BOTULINUM NEUROTOXIN C HEAVY CHAIN).
RC   STRAIN=Stockholm / Type C / phage C-ST;
RX   PubMed=7802661; DOI=10.1006/bbrc.1994.2805;
RA   Fujinaga Y., Inoue K., Shimazaki S., Tomochika K., Tsuzuki K., Fujii N.,
RA   Watanabe T., Ohyama T., Takeshi K., Inoue K., Oguma K.;
RT   "Molecular construction of Clostridium botulinum type C progenitor toxin
RT   and its gene organization.";
RL   Biochem. Biophys. Res. Commun. 205:1291-1298(1994).
RN   [9]
RP   FUNCTION (BOTULINUM NEUROTOXIN C LIGHT CHAIN), IDENTIFICATION OF SUBSTRATE,
RP   CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION
RP   (BOTULINUM NEUROTOXIN C LIGHT CHAIN).
RC   STRAIN=NCTC 8264 / Type C;
RX   PubMed=7737992; DOI=10.1074/jbc.270.18.10566;
RA   Schiavo G., Shone C.C., Bennett M.K., Scheller R.H., Montecucco C.;
RT   "Botulinum neurotoxin type C cleaves a single Lys-Ala bond within the
RT   carboxyl-terminal region of syntaxins.";
RL   J. Biol. Chem. 270:10566-10570(1995).
RN   [10]
RP   FUNCTION (BOTULINUM NEUROTOXIN TYPE C), IDENTIFICATION OF SUBSTRATE,
RP   CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC   STRAIN=Type C1;
RX   PubMed=8611567; DOI=10.1021/bi9519009;
RA   Foran P., Lawrence G.W., Shone C.C., Foster K.A., Dolly J.O.;
RT   "Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and
RT   permeabilized chromaffin cells: correlation with its blockade of
RT   catecholamine release.";
RL   Biochemistry 35:2630-2636(1996).
RN   [11]
RP   PHARMACEUTICAL.
RX   PubMed=9086464; DOI=10.1016/s0304-3940(97)13448-6;
RA   Eleopra R., Tugnoli V., Rossetto O., Montecucco C., De Grandis D.;
RT   "Botulinum neurotoxin serotype C: a novel effective botulinum toxin therapy
RT   in human.";
RL   Neurosci. Lett. 224:91-94(1997).
RN   [12]
RP   FUNCTION (BOTULINUM NEUROTOXIN C LIGHT CHAIN), IDENTIFICATION OF SUBSTRATE,
RP   AND CATALYTIC ACTIVITY.
RC   STRAIN=Type C;
RX   PubMed=9886085; DOI=10.1046/j.1471-4159.1999.0720327.x;
RA   Vaidyanathan V.V., Yoshino K., Jahnz M., Doerries C., Bade S.,
RA   Nauenburg S., Niemann H., Binz T.;
RT   "Proteolysis of SNAP-25 isoforms by botulinum neurotoxin types A, C, and E:
RT   domains and amino acid residues controlling the formation of enzyme-
RT   substrate complexes and cleavage.";
RL   J. Neurochem. 72:327-337(1999).
RN   [13]
RP   FUNCTION (BOTULINUM NEUROTOXIN C HEAVY CHAIN), AND GANGLIOSIDE-BINDING.
RC   STRAIN=CB-19 / Type C;
RX   PubMed=16115873; DOI=10.1074/jbc.m507596200;
RA   Tsukamoto K., Kohda T., Mukamoto M., Takeuchi K., Ihara H., Saito M.,
RA   Kozaki S.;
RT   "Binding of Clostridium botulinum type C and D neurotoxins to ganglioside
RT   and phospholipid. Novel insights into the receptor for clostridial
RT   neurotoxins.";
RL   J. Biol. Chem. 280:35164-35171(2005).
RN   [14]
RP   FUNCTION (BOTULINUM NEUROTOXIN TYPE C), FUNCTION (BOTULINUM NEUROTOXIN C
RP   HEAVY CHAIN), GANGLIOSIDE-BINDING, AND MUTAGENESIS OF TRP-1258.
RC   STRAIN=468C / phage c-st / Type C1;
RX   PubMed=19650874; DOI=10.1111/j.1471-4159.2009.06298.x;
RA   Rummel A., Haefner K., Mahrhold S., Darashchonak N., Holt M., Jahn R.,
RA   Beermann S., Karnath T., Bigalke H., Binz T.;
RT   "Botulinum neurotoxins C, E and F bind gangliosides via a conserved binding
RT   site prior to stimulation-dependent uptake with botulinum neurotoxin F
RT   utilising the three isoforms of SV2 as second receptor.";
RL   J. Neurochem. 110:1942-1954(2009).
RN   [15]
RP   FUNCTION (BOTULINUM NEUROTOXIN TYPE C), AND POSSIBLE LACK OF PROTEINACEOUS
RP   RECEPTOR.
RC   STRAIN=Type C;
RX   PubMed=21483489; DOI=10.1371/journal.ppat.1002008;
RA   Peng L., Tepp W.H., Johnson E.A., Dong M.;
RT   "Botulinum neurotoxin D uses synaptic vesicle protein SV2 and gangliosides
RT   as receptors.";
RL   PLoS Pathog. 7:E1002008-E1002008(2011).
RN   [16]
RP   FUNCTION (BOTULINUM NEUROTOXIN C HEAVY CHAIN), DOMAIN, AND
RP   PHOSPHOINOSITIDE-BINDING.
RX   PubMed=22120109; DOI=10.1016/j.biochi.2011.11.004;
RA   Zhang Y., Varnum S.M.;
RT   "The receptor binding domain of botulinum neurotoxin serotype C binds
RT   phosphoinositides.";
RL   Biochimie 94:920-923(2012).
RN   [17]
RP   FUNCTION (BOTULINUM NEUROTOXIN C HEAVY CHAIN), SUBCELLULAR LOCATION
RP   (BOTULINUM NEUROTOXIN C HEAVY CHAIN), GANGLIOSIDE-BINDING, AND MUTAGENESIS
RP   OF TYR-1119; ALA-1126 AND HIS-1193.
RC   STRAIN=Stockholm / Type C;
RX   PubMed=23027864; DOI=10.1074/jbc.m112.404244;
RA   Karalewitz A.P., Fu Z., Baldwin M.R., Kim J.J., Barbieri J.T.;
RT   "Botulinum neurotoxin serotype C associates with dual ganglioside receptors
RT   to facilitate cell entry.";
RL   J. Biol. Chem. 287:40806-40816(2012).
RN   [18]
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   [19] {ECO:0007744|PDB:2QN0}
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-427 IN COMPLEX WITH ZINC,
RP   FUNCTION (BOTULINUM NEUROTOXIN C LIGHT CHAIN), COFACTOR, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=Type C;
RX   PubMed=17718519; DOI=10.1021/bi701162d;
RA   Jin R., Sikorra S., Stegmann C.M., Pich A., Binz T., Brunger A.T.;
RT   "Structural and biochemical studies of botulinum neurotoxin serotype C1
RT   light chain protease: implications for dual substrate specificity.";
RL   Biochemistry 46:10685-10693(2007).
RN   [20] {ECO:0007744|PDB:3DEB}
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-430 IN APO-FORM.
RC   STRAIN=Type C;
RA   Rawat R., Kumaran D., Swaminathan S.;
RT   "Crystal structure of apo form (zinc removed) of the botulinum neurotoxin
RT   type C light chain.";
RL   Submitted (JUN-2008) to the PDB data bank.
RN   [21] {ECO:0007744|PDB:3N7K}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 866-1291, FUNCTION (BOTULINUM
RP   NEUROTOXIN C HEAVY CHAIN), DOMAIN, GANGLIOSIDE-BINDING, AND MUTAGENESIS OF
RP   TRP-1258.
RC   STRAIN=Type C / Stockholm / phage C-ST;
RX   PubMed=20731382; DOI=10.1021/bi100865f;
RA   Karalewitz A.P., Kroken A.R., Fu Z., Baldwin M.R., Kim J.J., Barbieri J.T.;
RT   "Identification of a unique ganglioside binding loop within botulinum
RT   neurotoxins C and D-SA.";
RL   Biochemistry 49:8117-8126(2010).
RN   [22] {ECO:0007744|PDB:3R4S, ECO:0007744|PDB:3R4U}
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 867-1291 WITH AND WITHOUT SIALIC
RP   ACID, FUNCTION (BOTULINUM NEUROTOXIN C HEAVY CHAIN), AND MUTAGENESIS OF
RP   TYR-1146; TYR-1179; LEU-1203; 1258-TRP-TYR-1259; TRP-1258 AND SER-1281.
RX   PubMed=21542861; DOI=10.1111/j.1365-2958.2011.07682.x;
RA   Strotmeier J., Gu S., Jutzi S., Mahrhold S., Zhou J., Pich A., Eichner T.,
RA   Bigalke H., Rummel A., Jin R., Binz T.;
RT   "The biological activity of botulinum neurotoxin type C is dependent upon
RT   novel types of ganglioside binding sites.";
RL   Mol. Microbiol. 81:143-156(2011).
CC   -!- FUNCTION: [Botulinum neurotoxin type C]: 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 (PubMed:16252491, PubMed:7901002, PubMed:8611567).
CC       Is unique among characterized BoNTs in having 2 substrates, syntaxin
CC       (STX) and SNAP25 (PubMed:7901002, PubMed:7737992, PubMed:8611567,
CC       PubMed:9886085, PubMed:17718519). Precursor of botulinum neurotoxin C
CC       which unlike most BoNTs seems not to have a proteinaceous coreceptor,
CC       and instead recognizes 2 different complex polysialylated gangliosides
CC       found on neural tissue probably found in synaptic vesicles
CC       (PubMed:21483489, PubMed:23027864). Upon synaptic vesicle recycling the
CC       toxin is taken up via the endocytic pathway. When the pH of the toxin-
CC       containing endosome drops a structural rearrangement occurs so that the
CC       N-terminus of the heavy chain (HC) forms pores that allows the light
CC       chain (LC) to translocate into the cytosol (By similarity). Once in the
CC       cytosol the disulfide bond linking the 2 subunits is reduced and LC
CC       cleaves its target protein on synaptic vesicles, preventing their
CC       fusion with the cytoplasmic membrane and thus neurotransmitter release
CC       (By similarity). In vitro the whole toxin only has protease activity
CC       after reduction (PubMed:8611567). Electrical stimulation increases
CC       uptake of toxin, presumably by transiently exposing a receptor usually
CC       found in eukaryotic target synaptic vesicles (PubMed:19650874). Forms
CC       ion-conducting channels at around pH 6.1 (PubMed:2424493). Requires
CC       complex eukaryotic host polysialogangliosides for full neurotoxicity
CC       (PubMed:19650874, PubMed:21483489). Synaptic vesicle glycoproteins
CC       (SV2) do not seem to act as its receptor (PubMed:21483489).
CC       {ECO:0000250|UniProtKB:P0DPI0, ECO:0000269|PubMed:17718519,
CC       ECO:0000269|PubMed:19650874, ECO:0000269|PubMed:21483489,
CC       ECO:0000269|PubMed:2424493, ECO:0000269|PubMed:7737992,
CC       ECO:0000269|PubMed:7901002, ECO:0000269|PubMed:8611567,
CC       ECO:0000269|PubMed:9886085, ECO:0000305|PubMed:16252491,
CC       ECO:0000305|PubMed:23027864}.
CC   -!- FUNCTION: [Botulinum neurotoxin C light chain]: Has proteolytic
CC       activity. After translocation into the eukaryotic host cytosol,
CC       inhibits neurotransmitter release by acting as a zinc endopeptidase
CC       that cleaves syntaxin-1A/STX1A and syntaxin-1B/STX1B (PubMed:7901002,
CC       PubMed:7737992, PubMed:8611567). Cleaves the '253-Arg-|-Ala-254' bond
CC       of STX1 and the '252-Arg-|-Ala-253' bond of STX2; also acts on syntaxin
CC       3 (STX3) but not 4 (STX4) (PubMed:7737992). Cleaves the '198-Arg-|-Ala-
CC       199' bond of SNAP25 (PubMed:8611567, PubMed:9886085, PubMed:17718519).
CC       Recognizes the '93-Asn--Met-202' region of SNAP25 (PubMed:9886085).
CC       {ECO:0000269|PubMed:17718519, ECO:0000269|PubMed:7737992,
CC       ECO:0000269|PubMed:7901002, ECO:0000269|PubMed:8611567,
CC       ECO:0000269|PubMed:9886085}.
CC   -!- FUNCTION: [Botulinum neurotoxin C heavy chain]: Responsible for host
CC       epithelial cell transcytosis, host nerve cell targeting and
CC       translocation of light chain (LC) into eukaryotic host cytosol.
CC       Composed of 3 subdomains; the translocation domain (TD), and N-terminus
CC       and C-terminus of the receptor-binding domain (RBD). The RBD is
CC       responsible for the adherence of the toxin to the eukaryotic target
CC       cell surface. It simultaneously recognizes 2 polysialated gangliosides
CC       coreceptors in close proximity on host synaptic vesicles
CC       (PubMed:23027864, PubMed:21542861). The N-terminus of the TD wraps an
CC       extended belt around the perimeter of the LC, protecting Zn(2+) in the
CC       active site; it may also prevent premature LC dissociation from the
CC       translocation channel and protect toxin prior to translocation (By
CC       similarity). The TD inserts into synaptic vesicle membrane to allow
CC       translocation into the host cytosol (Probable). The C-terminal half of
CC       the HC (residues 864-1291) binds neurons in a dose-dependent manner
CC       (PubMed:20731382). The C-terminal half of the HC (residues 863-1291)
CC       binds eukaryotic host gangliosides in the order GD1b > GT1b > GD1a >
CC       GM1a (PubMed:16115873, PubMed:20731382, PubMed:23027864,
CC       PubMed:19650874). Has 2 ganglioside binding sites; Sia-1 prefers a sia7
CC       sialic acid and sugars within the ganglioside (GD1b > GT1b), whereas
CC       GBP2 recognizes a sia5 sialic acid (GT1b and GD1a) (PubMed:23027864,
CC       PubMed:21542861). Both sites are required for HC to enter neurons,
CC       acting via different gangliosides (PubMed:23027864). This suggests that
CC       2 gangliosides serve as toxin receptors (PubMed:16115873,
CC       PubMed:20731382, PubMed:21542861, PubMed:23027864). Synaptic activity
CC       (depolarization with K(+)) increases uptake by neurons
CC       (PubMed:23027864). Treatment of synaptosomes with proteinase K does not
CC       reduce HC binding, suggesting there is no protein receptor or it is
CC       protected from extracellular proteases (PubMed:16115873). Decreases
CC       uptake and toxicity of whole BoNT/A, but also interferes with uptake of
CC       BoNT/E and BoNT/F (PubMed:19650874). HC also binds phosphoinositides,
CC       which might play a role in membrane-binding (PubMed:22120109).
CC       {ECO:0000250|UniProtKB:P0DPI0, ECO:0000269|PubMed:16115873,
CC       ECO:0000269|PubMed:19650874, ECO:0000269|PubMed:20731382,
CC       ECO:0000269|PubMed:21542861, ECO:0000269|PubMed:22120109,
CC       ECO:0000269|PubMed:23027864, ECO:0000305|PubMed:2424493}.
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:7737992, ECO:0000269|PubMed:8611567,
CC         ECO:0000269|PubMed:9886085};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:17718519, ECO:0000269|PubMed:7737992};
CC       Note=Binds 2 zinc ions per subunit (PubMed:7737992). The catalytic
CC       Zn(2+) is bound by LC, the other Zn(2+) must bind to another region
CC       (PubMed:17718519). {ECO:0000269|PubMed:17718519,
CC       ECO:0000269|PubMed:7737992};
CC   -!- ACTIVITY REGULATION: 1,10-phenanthroline, EDTA and partially captopril
CC       block cleavage of syntaxin in brain synaptosomes (PubMed:7901002,
CC       PubMed:7737992). Treatment of synaptosomes with a mild detergent also
CC       inhibits cleavage (PubMed:7737992). 1,10-phenanthroline partially
CC       antagonizes inhibitions of neurotransmitter release (PubMed:8611567).
CC       {ECO:0000269|PubMed:7737992, ECO:0000269|PubMed:7901002,
CC       ECO:0000269|PubMed:8611567}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=18.6 uM for purified SNAP25 with isolated botulinum neurotoxin C
CC         light chain {ECO:0000269|PubMed:17718519};
CC         Note=kcat is 0.391 min(-1), for isolated botulinum neurotoxin C light
CC         chain. {ECO:0000269|PubMed:17718519};
CC   -!- SUBUNIT: Heterodimer; disulfide-linked heterodimer of a light chain
CC       (LC) and a heavy chain (HC) (PubMed:16252491). The LC has the
CC       proteolytic/pharmacological activity (PubMed:7901002, PubMed:7737992,
CC       PubMed:8611567). The N- and C-terminal of the HC mediate channel
CC       formation and toxin binding, respectively. Can also be purified in
CC       complex with a non-toxic component that is larger than the HC
CC       (PubMed:16252491, PubMed:7802661). The stoichiometry of the whole
CC       complex has been modeled as one BoNT/C, one NTNHA, three HA-70, six HA-
CC       33 and three HA-17 (By similarity). {ECO:0000250|UniProtKB:P19321,
CC       ECO:0000269|PubMed:16252491, ECO:0000269|PubMed:7737992,
CC       ECO:0000269|PubMed:7802661, ECO:0000269|PubMed:7901002,
CC       ECO:0000269|PubMed:8611567}.
CC   -!- SUBCELLULAR LOCATION: [Botulinum neurotoxin type C]: Secreted
CC       {ECO:0000269|PubMed:16252491}.
CC   -!- SUBCELLULAR LOCATION: [Botulinum neurotoxin C light chain]: Secreted
CC       {ECO:0000269|PubMed:16252491, ECO:0000269|PubMed:7802661}. Note=In
CC       animals that have ingested BoNT/C the LC acts in the eukaryotic host
CC       cytosol (PubMed:7901002, PubMed:7737992, PubMed:8611567,
CC       PubMed:9886085, PubMed:17718519). {ECO:0000305|PubMed:17718519,
CC       ECO:0000305|PubMed:7737992, ECO:0000305|PubMed:7901002,
CC       ECO:0000305|PubMed:8611567, ECO:0000305|PubMed:9886085}.
CC   -!- SUBCELLULAR LOCATION: [Botulinum neurotoxin C heavy chain]: Secreted
CC       {ECO:0000269|PubMed:16252491, ECO:0000269|PubMed:7802661}. Note=Upon
CC       incubation with cultured neurons the HC is detected in a synaptophysin-
CC       positive intracellular compartment (probably host synaptic vesicles)
CC       (PubMed:23027864). It probably integrates into the eukaryotic host
CC       synaptic vesicle membrane (PubMed:2424493).
CC       {ECO:0000269|PubMed:23027864, ECO:0000305|PubMed:2424493}.
CC   -!- DOMAIN: [Botulinum neurotoxin C light chain]: Has proteolytic activity
CC       (PubMed:7901002, PubMed:7737992, PubMed:8611567, PubMed:9886085,
CC       PubMed:17718519). {ECO:0000269|PubMed:17718519,
CC       ECO:0000269|PubMed:7737992, ECO:0000269|PubMed:7901002,
CC       ECO:0000269|PubMed:8611567, ECO:0000269|PubMed:9886085}.
CC   -!- DOMAIN: [Botulinum neurotoxin C 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). The N-terminus of the TD wraps an extended belt around the
CC       perimeter of the LC, protecting Zn(2+) in the active site and may be a
CC       pseudosubstrate inhibitor which serves as an intramolecular chaperone
CC       for the LC prior to its translocation into the host cytosol. The RBD
CC       binds transiently exposed coreceptors on the host presynaptic cell
CC       membrane (By similarity). Binds phosphoinositides, which might play a
CC       role in membrane-binding (PubMed:22120109).
CC       {ECO:0000250|UniProtKB:P0DPI0, ECO:0000269|PubMed:22120109}.
CC   -!- PHARMACEUTICAL: Has been used to treat human idiopathic facial
CC       hemispasm and blepharospasm; improvement is seen in 2-3 days and the
CC       effects last up to 12-13 weeks, making it a viable option in BoNT/A
CC       non-responders (PubMed:9086464). {ECO:0000269|PubMed:9086464}.
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. Types C and D can undergo domain swapping to create
CC       hybrid types.
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   -!- MISCELLANEOUS: Botulinum neurotoxin type C is synthesized by C strains
CC       of C.botulinum which carry the appropriate bacteriophage.
CC       {ECO:0000305|PubMed:20731382, ECO:0000305|PubMed:2204031,
CC       ECO:0000305|PubMed:2222445, ECO:0000305|PubMed:9886085}.
CC   -!- MISCELLANEOUS: Strain CB-19 was isolated from mink (PubMed:16252491).
CC       BoNT/C usually causes animal and avian botulism; it is less toxic to
CC       chicken than is BoNT/CD (PubMed:16115873). One case of human infant
CC       botulism caused by this serotype is known (PubMed:1978909).
CC       {ECO:0000269|PubMed:16252491, ECO:0000269|PubMed:1978909,
CC       ECO:0000305|PubMed:16115873}.
CC   -!- MISCELLANEOUS: This protein can also be encoded on a prophage.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M27 family. {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; X66433; CAA47060.1; -; Genomic_DNA.
DR   EMBL; X72793; CAA51313.1; -; Genomic_DNA.
DR   EMBL; X53751; CAA37780.1; -; Genomic_DNA.
DR   EMBL; D90210; BAA14235.1; -; Genomic_DNA.
DR   EMBL; X62389; CAA44263.1; -; Genomic_DNA.
DR   EMBL; AB200358; BAD90566.1; -; Genomic_DNA.
DR   RefSeq; YP_398516.1; NC_007581.1.
DR   PDB; 2QN0; X-ray; 1.75 A; A=1-427.
DR   PDB; 3DEB; X-ray; 1.95 A; A=1-430.
DR   PDB; 3N7K; X-ray; 2.50 A; A/B=866-1291.
DR   PDB; 3R4S; X-ray; 2.15 A; A/B=867-1291.
DR   PDB; 3R4U; X-ray; 2.20 A; A/B=867-1291.
DR   PDBsum; 2QN0; -.
DR   PDBsum; 3DEB; -.
DR   PDBsum; 3N7K; -.
DR   PDBsum; 3R4S; -.
DR   PDBsum; 3R4U; -.
DR   SMR; P18640; -.
DR   DrugBank; DB13898; Equine Botulinum Neurotoxin C Immune FAB2.
DR   UniLectin; P18640; -.
DR   GeneID; 3772941; -.
DR   KEGG; vg:3772941; -.
DR   BRENDA; 3.4.24.69; 1462.
DR   Reactome; R-HSA-5250971; Toxicity of botulinum toxin type C (botC).
DR   EvolutionaryTrace; P18640; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0035594; F:ganglioside binding; IDA:UniProtKB.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008320; F:protein transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0033619; P:membrane protein proteolysis; IDA:CACAO.
DR   GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IDA:CACAO.
DR   GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IDA:UniProtKB.
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; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Lipid-binding; Metal-binding; Metalloprotease; Neurotoxin; Pharmaceutical;
KW   Protease; Secreted; Toxin; Virulence; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2450068"
FT   CHAIN           2..1291
FT                   /note="Botulinum neurotoxin type C"
FT                   /id="PRO_0000444905"
FT   CHAIN           2..449
FT                   /note="Botulinum neurotoxin C light chain"
FT                   /id="PRO_0000029217"
FT   CHAIN           450..1291
FT                   /note="Botulinum neurotoxin C heavy chain"
FT                   /id="PRO_0000029218"
FT   REGION          450..865
FT                   /note="Translocation domain (TD)"
FT                   /evidence="ECO:0000250|UniProtKB:P0DPI0"
FT   REGION          490..541
FT                   /note="Belt"
FT                   /evidence="ECO:0000250|UniProtKB:P10844"
FT   REGION          866..1093
FT                   /note="N-terminus of receptor binding domain (N-RBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P0DPI0"
FT   REGION          1094..1291
FT                   /note="C-terminus of receptor binding domain (C-RBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P0DPI0"
FT   REGION          1269..1283
FT                   /note="Ganglioside-binding loop"
FT                   /evidence="ECO:0000305|PubMed:20731382,
FT                   ECO:0000305|PubMed:21542861"
FT   MOTIF           1256..1258
FT                   /note="Host ganglioside-binding motif"
FT                   /evidence="ECO:0000250|UniProtKB:P10844,
FT                   ECO:0000305|PubMed:19650874"
FT   ACT_SITE        230
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         229
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:17718519, ECO:0007744|PDB:2QN0"
FT   BINDING         233
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:17718519, ECO:0007744|PDB:2QN0"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:17718519,
FT                   ECO:0007744|PDB:2QN0"
FT   BINDING         1119
FT                   /ligand="ganglioside GD1a (d18:1(4E))"
FT                   /ligand_id="ChEBI:CHEBI:78445"
FT                   /note="GBP2 binding site"
FT                   /evidence="ECO:0000305|PubMed:23027864"
FT   BINDING         1126..1129
FT                   /ligand="ganglioside GD1b (d18:1(4E))"
FT                   /ligand_id="ChEBI:CHEBI:87785"
FT                   /note="Sia-1 binding site"
FT                   /evidence="ECO:0000305|PubMed:21542861,
FT                   ECO:0007744|PDB:3R4S"
FT   BINDING         1146
FT                   /ligand="ganglioside GD1b (d18:1(4E))"
FT                   /ligand_id="ChEBI:CHEBI:87785"
FT                   /note="Sia-1 binding site"
FT                   /evidence="ECO:0000305|PubMed:21542861,
FT                   ECO:0007744|PDB:3R4S"
FT   BINDING         1247..1250
FT                   /ligand="ganglioside GD1a (d18:1(4E))"
FT                   /ligand_id="ChEBI:CHEBI:78445"
FT                   /note="GBP2 binding site"
FT                   /evidence="ECO:0000305|PubMed:23027864"
FT   BINDING         1281
FT                   /ligand="ganglioside GD1a (d18:1(4E))"
FT                   /ligand_id="ChEBI:CHEBI:78445"
FT                   /note="GBP2 binding site"
FT                   /evidence="ECO:0000305|PubMed:23027864"
FT   DISULFID        437..453
FT                   /note="Interchain (between light and heavy chains)"
FT                   /evidence="ECO:0000250|UniProtKB:P10844, ECO:0000305"
FT   MUTAGEN         1119
FT                   /note="Y->A: Receptor-binding domain (RBD) no longer binds
FT                   eukaryotic gangliosides GD1a or GM1a, reduced GT1b binding,
FT                   GD1b binding unaffected. RBD fragment enters neurons but
FT                   does not compartmentalize normally; uptake is not
FT                   stimulated by K(+)."
FT                   /evidence="ECO:0000269|PubMed:23027864"
FT   MUTAGEN         1126
FT                   /note="A->K: Receptor-binding domain (RBD) no longer binds
FT                   eukaryotic gangliosides GM1a, GD1b, reduced binding of GD1a
FT                   and GT1b. RBD fragment does not enter neurons; uptake is
FT                   not stimulated by K(+)."
FT                   /evidence="ECO:0000269|PubMed:23027864"
FT   MUTAGEN         1146
FT                   /note="Y->A: Whole toxin has dramatically reduced
FT                   toxicity."
FT                   /evidence="ECO:0000269|PubMed:21542861"
FT   MUTAGEN         1179
FT                   /note="Y->S: Receptor-binding domain (RBD) has decreased
FT                   binding to neurons. Greatly decreased binding to neurons;
FT                   when associated with L-1258. Whole toxin has greatly
FT                   decreased toxicity, even less toxic; when associated with
FT                   L-1258. Decreased binding to mixed gangliosides, even less
FT                   binding to mixed gangliosides; when associated with L-
FT                   1258."
FT                   /evidence="ECO:0000269|PubMed:21542861"
FT   MUTAGEN         1193
FT                   /note="H->A: No effect on receptor-binding domain (RBD)
FT                   binding to eukaryotic gangliosides."
FT                   /evidence="ECO:0000269|PubMed:23027864"
FT   MUTAGEN         1203
FT                   /note="L->F: Receptor-binding domain (RBD) has decreased
FT                   binding to neurons. Whole toxin has greatly decreased
FT                   toxicity. Decreased binding to mixed gangliosides."
FT                   /evidence="ECO:0000269|PubMed:21542861"
FT   MUTAGEN         1258..1259
FT                   /note="WY->AA: Whole toxin has greatly decreased toxicity."
FT                   /evidence="ECO:0000269|PubMed:21542861"
FT   MUTAGEN         1258
FT                   /note="W->A: Receptor-binding domain (RBD) has greatly
FT                   reduced binding of ganglioside GD1b, no longer binds
FT                   neurons."
FT                   /evidence="ECO:0000269|PubMed:20731382"
FT   MUTAGEN         1258
FT                   /note="W->L: Receptor-binding domain (RBD) has decreased
FT                   binding to neurons (Ref.16). Greatly decreased binding to
FT                   neurons; when associated with S-1179. Whole toxin has
FT                   greatly decreased toxicity, even less toxic; when
FT                   associated with S-1179. Decreased binding to mixed
FT                   gangliosides, even less binding to mixed gangliosides; when
FT                   associated with S-1179."
FT                   /evidence="ECO:0000269|PubMed:19650874,
FT                   ECO:0000269|PubMed:21542861"
FT   MUTAGEN         1281
FT                   /note="S->Y: Receptor-binding domain (RBD) has decreased
FT                   binding to neurons. Whole toxin has decreased toxicity and
FT                   decreased binding to mixed gangliosides."
FT                   /evidence="ECO:0000269|PubMed:21542861"
FT   CONFLICT        85
FT                   /note="T -> P (in Ref. 1; CAA37780)"
FT   STRAND          16..23
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   STRAND          34..40
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   STRAND          43..46
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   TURN            74..77
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   HELIX           80..97
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   HELIX           101..112
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   STRAND          126..128
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   STRAND          134..141
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   STRAND          143..152
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   STRAND          155..159
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   STRAND          169..171
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   HELIX           181..183
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   STRAND          184..186
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   STRAND          190..193
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   STRAND          201..207
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   HELIX           223..238
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   STRAND          248..253
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   STRAND          260..266
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   HELIX           267..273
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   HELIX           275..280
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   HELIX           283..304
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   STRAND          309..312
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   HELIX           313..318
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   HELIX           319..330
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   HELIX           344..356
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   HELIX           360..366
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   STRAND          372..374
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   TURN            390..392
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   TURN            395..397
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   HELIX           402..404
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   HELIX           411..413
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   TURN            415..417
FT                   /evidence="ECO:0007829|PDB:2QN0"
FT   HELIX           426..428
FT                   /evidence="ECO:0007829|PDB:3DEB"
FT   HELIX           867..870
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          872..878
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          880..885
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          887..889
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          892..898
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          909..915
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          916..918
FT                   /evidence="ECO:0007829|PDB:3N7K"
FT   STRAND          920..924
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   HELIX           927..933
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   TURN            934..936
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          937..947
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          956..963
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          966..973
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          976..984
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          987..994
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   HELIX           997..999
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1008..1015
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1018..1024
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1027..1033
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1044..1052
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1067..1078
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   HELIX           1082..1091
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1103..1105
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1107..1109
FT                   /evidence="ECO:0007829|PDB:3N7K"
FT   STRAND          1111..1116
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   HELIX           1117..1119
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1122..1127
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1130..1135
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1148..1155
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1159..1161
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1167..1174
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1177..1183
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1191..1193
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1198..1205
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   HELIX           1212..1214
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1216..1222
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1227..1234
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1241..1252
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1261..1269
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   HELIX           1273..1276
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   HELIX           1280..1282
FT                   /evidence="ECO:0007829|PDB:3R4S"
FT   STRAND          1284..1288
FT                   /evidence="ECO:0007829|PDB:3R4S"
SQ   SEQUENCE   1291 AA;  148870 MW;  4A21DB35B8743CF8 CRC64;
     MPITINNFNY SDPVDNKNIL YLDTHLNTLA NEPEKAFRIT GNIWVIPDRF SRNSNPNLNK
     PPRVTSPKSG YYDPNYLSTD SDKDTFLKEI IKLFKRINSR EIGEELIYRL STDIPFPGNN
     NTPINTFDFD VDFNSVDVKT RQGNNWVKTG SINPSVIITG PRENIIDPET STFKLTNNTF
     AAQEGFGALS IISISPRFML TYSNATNDVG EGRFSKSEFC MDPILILMHE LNHAMHNLYG
     IAIPNDQTIS SVTSNIFYSQ YNVKLEYAEI YAFGGPTIDL IPKSARKYFE EKALDYYRSI
     AKRLNSITTA NPSSFNKYIG EYKQKLIRKY RFVVESSGEV TVNRNKFVEL YNELTQIFTE
     FNYAKIYNVQ NRKIYLSNVY TPVTANILDD NVYDIQNGFN IPKSNLNVLF MGQNLSRNPA
     LRKVNPENML YLFTKFCHKA IDGRSLYNKT LDCRELLVKN TDLPFIGDIS DVKTDIFLRK
     DINEETEVIY YPDNVSVDQV ILSKNTSEHG QLDLLYPSID SESEILPGEN QVFYDNRTQN
     VDYLNSYYYL ESQKLSDNVE DFTFTRSIEE ALDNSAKVYT YFPTLANKVN AGVQGGLFLM
     WANDVVEDFT TNILRKDTLD KISDVSAIIP YIGPALNISN SVRRGNFTEA FAVTGVTILL
     EAFPEFTIPA LGAFVIYSKV QERNEIIKTI DNCLEQRIKR WKDSYEWMMG TWLSRIITQF
     NNISYQMYDS LNYQAGAIKA KIDLEYKKYS GSDKENIKSQ VENLKNSLDV KISEAMNNIN
     KFIRECSVTY LFKNMLPKVI DELNEFDRNT KAKLINLIDS HNIILVGEVD KLKAKVNNSF
     QNTIPFNIFS YTNNSLLKDI INEYFNNIND SKILSLQNRK NTLVDTSGYN AEVSEEGDVQ
     LNPIFPFDFK LGSSGEDRGK VIVTQNENIV YNSMYESFSI SFWIRINKWV SNLPGYTIID
     SVKNNSGWSI GIISNFLVFT LKQNEDSEQS INFSYDISNN APGYNKWFFV TVTNNMMGNM
     KIYINGKLID TIKVKELTGI NFSKTITFEI NKIPDTGLIT SDSDNINMWI RDFYIFAKEL
     DGKDINILFN SLQYTNVVKD YWGNDLRYNK EYYMVNIDYL NRYMYANSRQ IVFNTRRNNN
     DFNEGYKIII KRIRGNTNDT RVRGGDILYF DMTINNKAYN LFMKNETMYA DNHSTEDIYA
     IGLREQTKDI NDNIIFQIQP MNNTYYYASQ IFKSNFNGEN ISGICSIGTY RFRLGGDWYR
     HNYLVPTVKQ GNYASLLEST STHWGFVPVS E
 
 
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