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Protein

Botulinum neurotoxin type C1

Gene
N/A
Organism
Clostridium botulinum
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 cleaves syntaxin.

Catalytic activityi

Limited hydrolysis of proteins of the neuroexocytosis apparatus, synaptobrevins, SNAP25 or syntaxin. No detected action on small molecule substrates.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi229 – 2291Zinc; catalyticPROSITE-ProRule annotation
Active sitei230 – 2301PROSITE-ProRule annotation
Metal bindingi233 – 2331Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • inhibition of neurotransmitter uptake Source: InterPro
  • membrane protein proteolysis Source: CACAO
  • negative regulation of calcium ion-dependent exocytosis Source: CACAO
  • pathogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Neurotoxin, Protease, Toxin

Keywords - Biological processi

Virulence

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.69. 1462.
ReactomeiR-HSA-5250971. Toxicity of botulinum toxin type C (BoNT/C).

Names & Taxonomyi

Protein namesi
Recommended name:
Botulinum neurotoxin type C1 (EC:3.4.24.69)
Short name:
BoNT/C1
Alternative name(s):
Bontoxilysin-C1
Cleaved into the following 2 chains:
OrganismiClostridium botulinum
Taxonomic identifieri1491 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell junction, Host cell membrane, Host cytoplasm, Host membrane, Host synapse, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 449448Botulinum neurotoxin C1 light chainPRO_0000029217Add
BLAST
Chaini450 – 1291842Botulinum neurotoxin C1 heavy chainPRO_0000029218Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi437 ↔ 453Interchain (between light and heavy chains)Curated

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

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.

Structurei

Secondary structure

1
1291
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 238Combined sources
Beta strandi34 – 407Combined sources
Beta strandi43 – 464Combined sources
Beta strandi53 – 553Combined sources
Turni74 – 774Combined sources
Helixi80 – 9718Combined sources
Helixi101 – 11212Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi134 – 1418Combined sources
Beta strandi143 – 15210Combined sources
Beta strandi155 – 1595Combined sources
Beta strandi169 – 1713Combined sources
Helixi181 – 1833Combined sources
Beta strandi184 – 1863Combined sources
Beta strandi190 – 1934Combined sources
Beta strandi201 – 2077Combined sources
Helixi223 – 23816Combined sources
Beta strandi248 – 2536Combined sources
Beta strandi256 – 2583Combined sources
Beta strandi260 – 2667Combined sources
Helixi267 – 2737Combined sources
Helixi275 – 2806Combined sources
Helixi283 – 30422Combined sources
Beta strandi309 – 3124Combined sources
Helixi313 – 3186Combined sources
Helixi319 – 33012Combined sources
Helixi344 – 35613Combined sources
Helixi360 – 3667Combined sources
Beta strandi372 – 3743Combined sources
Turni390 – 3923Combined sources
Turni395 – 3973Combined sources
Helixi402 – 4043Combined sources
Helixi411 – 4133Combined sources
Turni415 – 4173Combined sources
Helixi426 – 4283Combined sources
Helixi867 – 8704Combined sources
Beta strandi872 – 8787Combined sources
Beta strandi880 – 8856Combined sources
Beta strandi887 – 8893Combined sources
Beta strandi892 – 8987Combined sources
Beta strandi909 – 9157Combined sources
Beta strandi916 – 9183Combined sources
Beta strandi920 – 9245Combined sources
Helixi927 – 9337Combined sources
Turni934 – 9363Combined sources
Beta strandi937 – 94711Combined sources
Beta strandi956 – 9638Combined sources
Beta strandi966 – 9738Combined sources
Beta strandi976 – 9849Combined sources
Beta strandi987 – 9948Combined sources
Helixi997 – 9993Combined sources
Beta strandi1008 – 10158Combined sources
Beta strandi1018 – 10247Combined sources
Beta strandi1027 – 10337Combined sources
Beta strandi1044 – 10529Combined sources
Beta strandi1067 – 107812Combined sources
Helixi1082 – 109110Combined sources
Beta strandi1103 – 11053Combined sources
Beta strandi1107 – 11093Combined sources
Beta strandi1111 – 11166Combined sources
Helixi1117 – 11193Combined sources
Beta strandi1122 – 11276Combined sources
Beta strandi1130 – 11356Combined sources
Beta strandi1148 – 11558Combined sources
Beta strandi1159 – 11613Combined sources
Beta strandi1167 – 11748Combined sources
Beta strandi1177 – 11837Combined sources
Beta strandi1191 – 11933Combined sources
Beta strandi1198 – 12058Combined sources
Helixi1212 – 12143Combined sources
Beta strandi1216 – 12227Combined sources
Beta strandi1227 – 12348Combined sources
Beta strandi1241 – 125212Combined sources
Beta strandi1261 – 12699Combined sources
Helixi1273 – 12764Combined sources
Helixi1280 – 12823Combined sources
Beta strandi1284 – 12885Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QN0X-ray1.75A1-427[»]
3DEBX-ray1.95A1-430[»]
3N7KX-ray2.50A/B866-1291[»]
3R4SX-ray2.15A/B867-1291[»]
3R4UX-ray2.20A/B867-1291[»]
ProteinModelPortaliP18640.
SMRiP18640. Positions 2-430.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18640.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M27 family.Curated

Keywords - Domaini

Transmembrane

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProiIPR000395. Bot/tetX.
IPR013320. ConA-like_dom.
IPR011065. Kunitz_inhibitor_ST1-like.
IPR013104. Toxin_rcpt-bd_C.
IPR012928. Toxin_rcpt-bd_N.
IPR012500. Toxin_trans.
[Graphical view]
PfamiPF01742. Peptidase_M27. 1 hit.
PF07951. Toxin_R_bind_C. 1 hit.
PF07953. Toxin_R_bind_N. 1 hit.
PF07952. Toxin_trans. 1 hit.
[Graphical view]
PRINTSiPR00760. BONTOXILYSIN.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF50386. SSF50386. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18640-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPITINNFNY SDPVDNKNIL YLDTHLNTLA NEPEKAFRIT GNIWVIPDRF
60 70 80 90 100
SRNSNPNLNK PPRVTSPKSG YYDPNYLSTD SDKDPFLKEI IKLFKRINSR
110 120 130 140 150
EIGEELIYRL STDIPFPGNN NTPINTFDFD VDFNSVDVKT RQGNNWVKTG
160 170 180 190 200
SINPSVIITG PRENIIDPET STFKLTNNTF AAQEGFGALS IISISPRFML
210 220 230 240 250
TYSNATNDVG EGRFSKSEFC MDPILILMHE LNHAMHNLYG IAIPNDQTIS
260 270 280 290 300
SVTSNIFYSQ YNVKLEYAEI YAFGGPTIDL IPKSARKYFE EKALDYYRSI
310 320 330 340 350
AKRLNSITTA NPSSFNKYIG EYKQKLIRKY RFVVESSGEV TVNRNKFVEL
360 370 380 390 400
YNELTQIFTE FNYAKIYNVQ NRKIYLSNVY TPVTANILDD NVYDIQNGFN
410 420 430 440 450
IPKSNLNVLF MGQNLSRNPA LRKVNPENML YLFTKFCHKA IDGRSLYNKT
460 470 480 490 500
LDCRELLVKN TDLPFIGDIS DVKTDIFLRK DINEETEVIY YPDNVSVDQV
510 520 530 540 550
ILSKNTSEHG QLDLLYPSID SESEILPGEN QVFYDNRTQN VDYLNSYYYL
560 570 580 590 600
ESQKLSDNVE DFTFTRSIEE ALDNSAKVYT YFPTLANKVN AGVQGGLFLM
610 620 630 640 650
WANDVVEDFT TNILRKDTLD KISDVSAIIP YIGPALNISN SVRRGNFTEA
660 670 680 690 700
FAVTGVTILL EAFPEFTIPA LGAFVIYSKV QERNEIIKTI DNCLEQRIKR
710 720 730 740 750
WKDSYEWMMG TWLSRIITQF NNISYQMYDS LNYQAGAIKA KIDLEYKKYS
760 770 780 790 800
GSDKENIKSQ VENLKNSLDV KISEAMNNIN KFIRECSVTY LFKNMLPKVI
810 820 830 840 850
DELNEFDRNT KAKLINLIDS HNIILVGEVD KLKAKVNNSF QNTIPFNIFS
860 870 880 890 900
YTNNSLLKDI INEYFNNIND SKILSLQNRK NTLVDTSGYN AEVSEEGDVQ
910 920 930 940 950
LNPIFPFDFK LGSSGEDRGK VIVTQNENIV YNSMYESFSI SFWIRINKWV
960 970 980 990 1000
SNLPGYTIID SVKNNSGWSI GIISNFLVFT LKQNEDSEQS INFSYDISNN
1010 1020 1030 1040 1050
APGYNKWFFV TVTNNMMGNM KIYINGKLID TIKVKELTGI NFSKTITFEI
1060 1070 1080 1090 1100
NKIPDTGLIT SDSDNINMWI RDFYIFAKEL DGKDINILFN SLQYTNVVKD
1110 1120 1130 1140 1150
YWGNDLRYNK EYYMVNIDYL NRYMYANSRQ IVFNTRRNNN DFNEGYKIII
1160 1170 1180 1190 1200
KRIRGNTNDT RVRGGDILYF DMTINNKAYN LFMKNETMYA DNHSTEDIYA
1210 1220 1230 1240 1250
IGLREQTKDI NDNIIFQIQP MNNTYYYASQ IFKSNFNGEN ISGICSIGTY
1260 1270 1280 1290
RFRLGGDWYR HNYLVPTVKQ GNYASLLEST STHWGFVPVS E
Length:1,291
Mass (Da):148,866
Last modified:January 23, 2007 - v2
Checksum:i31F1405E2141FB16
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851P → T in CAA47060 (PubMed:2222445).Curated
Sequence conflicti85 – 851P → T in CAA51313 (PubMed:2222445).Curated
Sequence conflicti85 – 851P → T in BAA14235 (PubMed:2222445).Curated
Sequence conflicti85 – 851P → T in CAA44263 (PubMed:2222445).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66433 Genomic DNA. Translation: CAA47060.1.
X72793 Genomic DNA. Translation: CAA51313.1.
X53751 Genomic DNA. Translation: CAA37780.1.
D90210 Genomic DNA. Translation: BAA14235.1.
X62389 Genomic DNA. Translation: CAA44263.1.

Cross-referencesi

Web resourcesi

BotDB - A Database Resource for Clostridial Neurotoxins

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66433 Genomic DNA. Translation: CAA47060.1.
X72793 Genomic DNA. Translation: CAA51313.1.
X53751 Genomic DNA. Translation: CAA37780.1.
D90210 Genomic DNA. Translation: BAA14235.1.
X62389 Genomic DNA. Translation: CAA44263.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QN0X-ray1.75A1-427[»]
3DEBX-ray1.95A1-430[»]
3N7KX-ray2.50A/B866-1291[»]
3R4SX-ray2.15A/B867-1291[»]
3R4UX-ray2.20A/B867-1291[»]
ProteinModelPortaliP18640.
SMRiP18640. Positions 2-430.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.24.69. 1462.
ReactomeiR-HSA-5250971. Toxicity of botulinum toxin type C (BoNT/C).

Miscellaneous databases

EvolutionaryTraceiP18640.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.90.1240.10. 1 hit.
InterProiIPR000395. Bot/tetX.
IPR013320. ConA-like_dom.
IPR011065. Kunitz_inhibitor_ST1-like.
IPR013104. Toxin_rcpt-bd_C.
IPR012928. Toxin_rcpt-bd_N.
IPR012500. Toxin_trans.
[Graphical view]
PfamiPF01742. Peptidase_M27. 1 hit.
PF07951. Toxin_R_bind_C. 1 hit.
PF07953. Toxin_R_bind_N. 1 hit.
PF07952. Toxin_trans. 1 hit.
[Graphical view]
PRINTSiPR00760. BONTOXILYSIN.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF50386. SSF50386. 1 hit.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete nucleotide sequence of the gene coding for botulinum type C1 toxin in the C-ST phage genome."
    Kimura K., Fujii N., Tsuzuki K., Murakami T., Indoh T., Yokosawa N., Takeshi K., Syuto B., Oguma K.
    Biochem. Biophys. Res. Commun. 171:1304-1311(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Type C / Stockholm.
  3. "Establishment of a monoclonal antibody recognizing an antigenic site common to Clostridium botulinum type B, C1, D, and E toxins and tetanus toxin."
    Tsuzuki K., Yokosawa N., Syuto B., Ohishi I., Fujii N., Kimura K., Oguma K.
    Infect. Immun. 56:898-902(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 3-26.
    Strain: Type C / Stockholm.
  4. "Botulinum neurotoxin C1 blocks neurotransmitter release by means of cleaving HPC-1/syntaxin."
    Blasi J., Chapman E.R., Yamasaki S., Binz T., Niemann H., Jahn R.
    EMBO J. 12:4821-4828(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF SUBSTRATE.

Entry informationi

Entry nameiBXC1_CLOBO
AccessioniPrimary (citable) accession number: P18640
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

There are seven antigenically distinct forms of botulinum neurotoxin: Types A, B, C1, D, E, F, and G.
Botulinum type C1 neurotoxin is synthesized by C strains of C.botulinum which carry the appropriate bacteriophage.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.