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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)DescriptionActionsGraphical viewLength
Metal bindingi229Zinc; catalyticPROSITE-ProRule annotation1
Active sitei230PROSITE-ProRule annotation1
Metal bindingi233Zinc; catalyticPROSITE-ProRule annotation1

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000292172 – 449Botulinum neurotoxin C1 light chainAdd BLAST448
ChainiPRO_0000029218450 – 1291Botulinum neurotoxin C1 heavy chainAdd BLAST842

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi437 ↔ 453Interchain (between light and heavy chains)Curated

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP18640.

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

11291
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 23Combined sources8
Beta strandi34 – 40Combined sources7
Beta strandi43 – 46Combined sources4
Beta strandi53 – 55Combined sources3
Turni74 – 77Combined sources4
Helixi80 – 97Combined sources18
Helixi101 – 112Combined sources12
Beta strandi126 – 128Combined sources3
Beta strandi134 – 141Combined sources8
Beta strandi143 – 152Combined sources10
Beta strandi155 – 159Combined sources5
Beta strandi169 – 171Combined sources3
Helixi181 – 183Combined sources3
Beta strandi184 – 186Combined sources3
Beta strandi190 – 193Combined sources4
Beta strandi201 – 207Combined sources7
Helixi223 – 238Combined sources16
Beta strandi248 – 253Combined sources6
Beta strandi256 – 258Combined sources3
Beta strandi260 – 266Combined sources7
Helixi267 – 273Combined sources7
Helixi275 – 280Combined sources6
Helixi283 – 304Combined sources22
Beta strandi309 – 312Combined sources4
Helixi313 – 318Combined sources6
Helixi319 – 330Combined sources12
Helixi344 – 356Combined sources13
Helixi360 – 366Combined sources7
Beta strandi372 – 374Combined sources3
Turni390 – 392Combined sources3
Turni395 – 397Combined sources3
Helixi402 – 404Combined sources3
Helixi411 – 413Combined sources3
Turni415 – 417Combined sources3
Helixi426 – 428Combined sources3
Helixi867 – 870Combined sources4
Beta strandi872 – 878Combined sources7
Beta strandi880 – 885Combined sources6
Beta strandi887 – 889Combined sources3
Beta strandi892 – 898Combined sources7
Beta strandi909 – 915Combined sources7
Beta strandi916 – 918Combined sources3
Beta strandi920 – 924Combined sources5
Helixi927 – 933Combined sources7
Turni934 – 936Combined sources3
Beta strandi937 – 947Combined sources11
Beta strandi956 – 963Combined sources8
Beta strandi966 – 973Combined sources8
Beta strandi976 – 984Combined sources9
Beta strandi987 – 994Combined sources8
Helixi997 – 999Combined sources3
Beta strandi1008 – 1015Combined sources8
Beta strandi1018 – 1024Combined sources7
Beta strandi1027 – 1033Combined sources7
Beta strandi1044 – 1052Combined sources9
Beta strandi1067 – 1078Combined sources12
Helixi1082 – 1091Combined sources10
Beta strandi1103 – 1105Combined sources3
Beta strandi1107 – 1109Combined sources3
Beta strandi1111 – 1116Combined sources6
Helixi1117 – 1119Combined sources3
Beta strandi1122 – 1127Combined sources6
Beta strandi1130 – 1135Combined sources6
Beta strandi1148 – 1155Combined sources8
Beta strandi1159 – 1161Combined sources3
Beta strandi1167 – 1174Combined sources8
Beta strandi1177 – 1183Combined sources7
Beta strandi1191 – 1193Combined sources3
Beta strandi1198 – 1205Combined sources8
Helixi1212 – 1214Combined sources3
Beta strandi1216 – 1222Combined sources7
Beta strandi1227 – 1234Combined sources8
Beta strandi1241 – 1252Combined sources12
Beta strandi1261 – 1269Combined sources9
Helixi1273 – 1276Combined sources4
Helixi1280 – 1282Combined sources3
Beta strandi1284 – 1288Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti85P → T in CAA47060 (PubMed:2222445).Curated1
Sequence conflicti85P → T in CAA51313 (PubMed:2222445).Curated1
Sequence conflicti85P → T in BAA14235 (PubMed:2222445).Curated1
Sequence conflicti85P → T in CAA44263 (PubMed:2222445).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP18640.

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...

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: November 2, 2016
This is version 147 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.