[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM S). TISSUE=Venom gland; DOI=10.1074/jbc.271.25.15099; PubMed=8662867 [NCBI, ExPASy, EBI, Israel, Japan] Cousin X., Bon S., Duval N., Massoulie J., Bon C.; "Cloning and expression of acetylcholinesterase from Bungarus fasciatus venom. A new type of COOH-terminal domain; involvement of a positively charged residue in the peripheral site."; J. Biol. Chem. 271:15099-15108(1996).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 512-606 (ISOFORMS S AND T), SUBUNIT, AND TISSUE SPECIFICITY. TISSUE=Liver, and Muscle; DOI=10.1074/jbc.273.16.9812; PubMed=9545320 [NCBI, ExPASy, EBI, Israel, Japan] Cousin X., Bon S., Massoulie J., Bon C.; "Identification of a novel type of alternatively spliced exon from the acetylcholinesterase gene of Bungarus fasciatus. Molecular forms of acetylcholinesterase in the snake liver and muscle."; J. Biol. Chem. 273:9812-9820(1998).
[3]	PROTEIN SEQUENCE OF 206-220; 253-272; 321-340; 347-372 AND 503-511. TISSUE=Venom; DOI=10.1016/0014-5793(96)00447-4; PubMed=8674549 [NCBI, ExPASy, EBI, Israel, Japan] Cousin X., Creminon C., Grassi J., Meflah K., Cornu G., Saliou B., Bon S., Massoulie J., Bon C.; "Acetylcholinesterase from Bungarus venom: a monomeric species."; FEBS Lett. 387:196-200(1996).

Comments

FUNCTION: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.
CATALYTIC ACTIVITY: Acetylcholine + H₂O = choline + acetate.
SUBUNIT: Isoform S is monomeric. Isoform T can form oligomers, including collagen-tailed forms.
SUBCELLULAR LOCATION: Cell junction, synapse. Secreted. Cell membrane; Peripheral membrane protein (By similarity).
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name T

Isoform ID Q92035-2

This is the isoform sequence displayed in this entry.

Name S

Isoform ID Q92035-1

Features which should be applied to build the isoform sequence: VSP_008215.
TISSUE SPECIFICITY: Liver and muscle contain both isoform T and isoform S. Venom gland predominantly contains isoform S.
PTM: The N-terminus is blocked.
SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.

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

U54591; AAC59905.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF045238; AAC16420.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF045238; AAC16421.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P04058; 1H23. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

Q92035.

Protein family/group databases

MEROPS

S09.979; -.

Ontologies

GO:0030054;	Cellular component: cell junction (inferred from electronic annotation from UniProtKB-KW).
GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0045202;	Cellular component: synapse (inferred from electronic annotation from UniProtKB-KW).
GO:0003990;	Molecular function: acetylcholinesterase activity (inferred from electronic annotation from InterPro).
GO:0004104;	Molecular function: cholinesterase activity (inferred from electronic annotation from InterPro).
GO:0001507;	Biological process: acetylcholine catabolic process in synaptic cleft (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR014788; AChE_tetra.
IPR000908; Acylcholinesterase_fish/snake.
IPR002018; CarbesteraseB.
IPR000997; Cholinesterase.
Graphical view of domain structure.

PANTHER

PTHR11559; CarbesteraseB; 1.

Pfam

PF08674; AChE_tetra; 1.
PF00135; COesterase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00879; ACHEFISH.
PR00878; CHOLNESTRASE.

PROSITE

PS00122; CARBOXYLESTERASE_B_1; 1.
PS00941; CARBOXYLESTERASE_B_2; 1.

ProtoNet

Q92035.

Phylogenomic databases

HOVERGEN

Q92035; -.

Other

UniRef

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

Keywords

Alternative splicing; Cell junction; Cell membrane; Direct protein sequencing; Glycoprotein; Hydrolase; Membrane; Neurotransmitter degradation; Secreted; Serine esterase; Signal; Synapse.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 28`	`28`	`Potential.`
`CHAIN`	`29 606`	`578`	`Acetylcholinesterase.`	`PRO_0000008592`
`ACT_SITE`	`231 231`		`Acyl-ester intermediate (By similarity).`
`ACT_SITE`	`358 358`		`Charge relay system (By similarity).`
`ACT_SITE`	`471 471`		`Charge relay system (By similarity).`
`CARBOHYD`	`289 289`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`374 374`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`484 484`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`564 564`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`98 125`		`By similarity.`
`DISULFID`	`285 296`		`By similarity.`
`DISULFID`	`433 552`		`By similarity.`
`DISULFID`	`603 603`		`Interchain; in isoform T (By similarity).`
`VAR_SEQ`	`567 606`		`DNIEEAERQWKLEFHLWSAYMMHWKSQFDHYNKQDRCSEL -> VDPPRADRRRRSARA (in isoform S).`	`VSP_008215`
`MUTAGEN`	`101 101`		`M->Y: Increases peripheral site ligand binding.`
`MUTAGEN`	`316 316`		`K->D: Increases peripheral site ligand binding.`
`CONFLICT`	`268 268`		`T -> S (in Ref. 3; AA sequence).`
`CONFLICT`	`350 350`		`V -> L (in Ref. 3; AA sequence).`

Sequence information

Length: 606 AA [This is the length of the unprocessed precursor]

Molecular weight: 68074 Da [This is the MW of the unprocessed precursor]

CRC64: B95998AEEA0E5709 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPSCQPGKMP APWPWWLQLL LCIPSCVAVL PGRAGELKVS TQTGSVRGLS LPVLDGHVSA 

        70         80         90        100        110        120 
FLGIPFAEPP LGRMRFLRPE PVKPWQHVLD ATSYKPACYQ MVDTSYPGFQ GTEMWNPNRG 

       130        140        150        160        170        180 
MSEDCLYLNI WVPSPRPKDA PVLVWIYGGG FYSGAASLDV YDGRFLTYTQ NVILVSLSYR 

       190        200        210        220        230        240 
VGAFGFLGLP GSPEAPGNMG LLDQRLALQW IQNNIHPFGG NPRAVTVFGE SAGAASVGMH 

       250        260        270        280        290        300 
LLSTQSRTLF QRAILQSGGP NAPWATVTPA ESRGRAALLG KQLGCHFNND SELVSCLRSK 

       310        320        330        340        350        360 
NPQELIDEEW SVLPYKSIFR FPFVPVIDGD FFPDTPEAML SSGNFKETQV LLGVVKDEGS 

       370        380        390        400        410        420 
YFLIYGLPGF SKDNESLISR ADFLEGVRMS VPHANDIATD AVVLQYTDWQ DQDNREKNRE 

       430        440        450        460        470        480 
ALDDIVGDHN VICPVVQFAN DYAKRNSKVY AYLFDHRASN LLWPPWMGVP HGYEIEFVFG 

       490        500        510        520        530        540 
LPLNDSLNYT PQEKELSRRM MRYWANFART GNPTDPADKS GAWPTYTASQ PQYVQLNTQP 

       550        560        570        580        590        600 
LATQPSLRAQ ICAFWNHFLP KLLNATDNIE EAERQWKLEF HLWSAYMMHW KSQFDHYNKQ 


DRCSEL

Q92035 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