[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 43181, and ATCC 43755; DOI=10.1016/0006-291X(92)91615-W; PubMed=1543481 [NCBI, ExPASy, EBI, Israel, Japan] Poulet S., Hauser D., Quanz M., Niemann H., Popoff M.R.; "Sequences of the botulinal neurotoxin E derived from Clostridium botulinum type E (strain Beluga) and Clostridium butyricum (strains ATCC 43181 and ATCC 43755)."; Biochem. Biophys. Res. Commun. 183:107-113(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-252. STRAIN=BL6340; PubMed=2033376 [NCBI, ExPASy, EBI, Israel, Japan] Fujii N., Kimura K., Murakami T., Indoh T., Tsuzuki K., Yokosawa N., Yashiki T., Oguma K.; "Cloning of a DNA fragment encoding the 5'-terminus of the botulinum type E toxin gene from Clostridium butyricum strain BL6340."; J. Gen. Microbiol. 137:519-525(1991).
[3]	PROTEIN SEQUENCE OF 2-49. STRAIN=5262; Gimenez J., Foley J., Dasgupta B.R.; "Neurotoxin type E from Clostridium botulinum and C. butyricum; partial sequence and comparison."; FASEB J. 2:A1750-A1750(1988).

Comments

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.
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/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X62088; CAA43998.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X53180; CAA37321.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JH0256; JH0256.

3D structure databases

HSSP

Q45894; 1E1H. [HSSP ENTRY / PDB]

SMR

P30995; 2-412.

ModBase

P30995.

Protein family/group databases

MEROPS

M27.002; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from InterPro).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0004222;	Molecular function: metalloendopeptidase activity (inferred from electronic annotation from InterPro).
GO:0050827;	Molecular function: toxin receptor binding (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0051609;	Biological process: inhibition of neurotransmitter uptake (inferred from electronic annotation from InterPro).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR013320; ConA_like_subgrp.
IPR006025; Pept_M_Zn_BS.
IPR000395; Peptidase_M27.
IPR013104; Toxin_rcpt_bd_C.
IPR012928; Toxin_rcpt_bd_N.
IPR012500; Toxin_trans.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.120.200; ConA_like_subgrp; 1.
G3DSA:3.90.1240.10; Peptidase_M27; 1.

Pfam

PF01742; Peptidase_M27; 1.
PF07951; Toxin_R_bind_C; 1.
PF07953; Toxin_R_bind_N; 1.
PF07952; Toxin_trans; 1.
Pfam graphical view of domain structure.

PRINTS

PR00760; BONTOXILYSIN.

ProDom

PD001963; Botulinum; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00142; ZINC_PROTEASE; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Direct protein sequencing; Hydrolase; Membrane; Metal-binding; Metalloprotease; Neurotoxin; Protease; Secreted; Toxin; Transmembrane; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 422`	`421`	`Botulinum neurotoxin E light chain.`	`PRO_0000029223`
`CHAIN`	`423 1251`	`829`	`Botulinum neurotoxin E heavy chain.`	`PRO_0000029224`
`ACT_SITE`	`213 213`		`By similarity.`
`METAL`	`212 212`		`Zinc; catalytic (By similarity).`
`METAL`	`216 216`		`Zinc; catalytic (By similarity).`
`DISULFID`	`412 426`		`Interchain (between light and heavy chains) (Probable).`
`CONFLICT`	`230 230`		`K -> M (in Ref. 2; CAA37321).`

Sequence information

Length: 1251 AA [This is the length of the unprocessed precursor]

Molecular weight: 143397 Da [This is the MW of the unprocessed precursor]

CRC64: E8D7F180E9863581 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPTINSFNYN DPVNNRTILY IKPGGCQQFY KSFNIMKNIW IIPERNVIGT IPQDFLPPTS 

        70         80         90        100        110        120 
LKNGDSSYYD PNYLQSDQEK DKFLKIVTKI FNRINDNLSG RILLEELSKA NPYLGNDNTP 

       130        140        150        160        170        180 
DGDFIINDAS AVPIQFSNGS QSILLPNVII MGAEPDLFET NSSNISLRNN YMPSNHGFGS 

       190        200        210        220        230        240 
IAIVTFSPEY SFRFKDNSMN EFIQDPALTL MHELIHSLHG LYGAKGITTK YTITQKQNPL 

       250        260        270        280        290        300 
ITNIRGTNIE EFLTFGGTDL NIITSAQSND IYTNLLADYK KIASKLSKVQ VSNPLLNPYK 

       310        320        330        340        350        360 
DVFEAKYGLD KDASGIYSVN INKFNDIFKK LYSFTEFDLA TKFQVKCRQT YIGQYKYFKL 

       370        380        390        400        410        420 
SNLLNDSIYN ISEGYNINNL KVNFRGQNAN LNPRIITPIT GRGLVKKIIR FCKNIVSVKG 

       430        440        450        460        470        480 
IRKSICIEIN NGELFFVASE NSYNDDNINT PKEIDDTVTS NNNYENDLDQ VILNFNSESA 

       490        500        510        520        530        540 
PGLSDEKLNL TIQNDAYIPK YDSNGTSDIE QHDVNELNVF FYLDAQKVPE GENNVNLTSS 

       550        560        570        580        590        600 
IDTALLEQPK IYTFFSSEFI NNVNKPVQAA LFVGWIQQVL VDFTTEANQK STVDKIADIS 

       610        620        630        640        650        660 
IVVPYIGLAL NIGNEAQKGN FKDALELLGA GILLEFEPEL LIPTILVFTI KSFLGSSDNK 

       670        680        690        700        710        720 
NKVIKAINNA LKERDEKWKE VYSFIVSNWM TKINTQFNKR KEQMYQALQN QVNALKAIIE 

       730        740        750        760        770        780 
SKYNSYTLEE KNELTNKYDI EQIENELNQK VSIAMNNIDR FLTESSISYL MKLINEVKIN 

       790        800        810        820        830        840 
KLREYDENVK TYLLDYIIKH GSILGESQQE LNSMVIDTLN NSIPFKLSSY TDDKILISYF 

       850        860        870        880        890        900 
NKFFKRIKSS SVLNMRYKND KYVDTSGYDS NININGDVYK YPTNKNQFGI YNDKLSEVNI 

       910        920        930        940        950        960 
SQNDYIIYDN KYKNFSISFW VRIPNYDNKI VNVNNEYTII NCMRDNNSGW KVSLNHNEII 

       970        980        990       1000       1010       1020 
WTLQDNSGIN QKLAFNYGNA NGISDYINKW IFVTITNDRL GDSKLYINGN LIDKKSILNL 

      1030       1040       1050       1060       1070       1080 
GNIHVSDNIL FKIVNCSYTR YIGIRYFNIF DKELDETEIQ TLYNNEPNAN ILKDFWGNYL 

      1090       1100       1110       1120       1130       1140 
LYDKEYYLLN VLKPNNFINR RTDSTLSINN IRSTILLANR LYSGIKVKIQ RVNNSSTNDN 

      1150       1160       1170       1180       1190       1200 
LVRKNDQVYI NFVASKTHLL PLYADTATTN KEKTIKISSS GNRFNQVVVM NSVGNCTMNF 

      1210       1220       1230       1240       1250 
KNNNGNNIGL LGFKADTVVA STWYYTHMRD NTNSNGFFWN FISEEHGWQE K

P30995 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools