Reviewed, UniProtKB/Swiss-Prot Q92035 (ACES_BUNFA)

Names and origin

Protein names

Recommended name:
    Acetylcholinesterase
      Short name=AChE
    EC=3.1.1.7

Gene names

Name:

ACHE

Organism

Bungarus fasciatus (Banded krait)

Taxonomic identifier

8613 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Scleroglossa › Serpentes › Colubroidea › Elapidae › Bungarinae › Bungarus

Protein attributes

Sequence length	606 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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 structure	Isoform S is monomeric. Isoform T can form oligomers, including collagen-tailed forms. Ref.2
Subcellular location	Cell junction › synapse. Secreted. Cell membrane; Peripheral membrane protein By similarity.
Tissue specificity	Liver and muscle contain both isoform T and isoform S. Venom gland predominantly contains isoform S. Ref.2
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the type-B carboxylesterase/lipase family.
Caution	It is uncertain whether Met-1 or Met-9 is the initiator.

Ontologies

Keywords
Biological process	Neurotransmitter degradation
Cellular component	Cell junction Cell membrane Membrane Secreted Synapse
Coding sequence diversity	Alternative splicing
Domain	Signal
Molecular function	Hydrolase Serine esterase
PTM	Disulfide bond Glycoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	acetylcholine catabolic process in synaptic cleft Inferred from electronic annotation. Source: InterPro
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetylcholinesterase activity Inferred from electronic annotation. Source: EC cholinesterase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform T (identifier: Q92035-2)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform S (identifier: Q92035-1)

The sequence of this isoform differs from the canonical sequence as follows:
     567-606: DNIEEAERQWKLEFHLWSAYMMHWKSQFDHYNKQDRCSEL → VDPPRADRRRRSARA

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 28	28	Potential
	Chain	29 – 606	578	Acetylcholinesterase		PRO_0000008592
Sites
	Active site	231	1	Acyl-ester intermediate By similarity
	Active site	358	1	Charge relay system By similarity
	Active site	471	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	289	1	N-linked (GlcNAc...) Potential
	Glycosylation	374	1	N-linked (GlcNAc...) Potential
	Glycosylation	484	1	N-linked (GlcNAc...) Potential
	Glycosylation	564	1	N-linked (GlcNAc...) Potential
	Disulfide bond	98 ↔ 125		By similarity
	Disulfide bond	285 ↔ 296		By similarity
	Disulfide bond	433 ↔ 552		By similarity
	Disulfide bond	603		Interchain; in isoform T By similarity
Natural variations
	Alternative sequence	567 – 606	40	DNIEE…RCSEL → VDPPRADRRRRSARA in isoform S.		VSP_008215
Experimental info
	Mutagenesis	101	1	M → Y: Increases peripheral site ligand binding.
	Mutagenesis	316	1	K → D: Increases peripheral site ligand binding.
	Sequence conflict	268	1	T → S AA sequence Ref.3
	Sequence conflict	350	1	V → L AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform T [UniParc]. Last modified September 19, 2003. Version 2. Checksum: B95998AEEA0E5709	FASTA	606	68,074
	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
	Isoform S. Checksum: 436C3CBE457E399F	FASTA	581	64,723
	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 LATQPSLRAQ ICAFWNHFLP KLLNATVDPP RADRRRRSAR A

References

[1]	"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." Cousin X., Bon S., Duval N., Massoulie J., Bon C. J. Biol. Chem. 271:15099-15108(1996) [PubMed: 8662867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM S). Tissue: Venom gland.
[2]	"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." Cousin X., Bon S., Massoulie J., Bon C. J. Biol. Chem. 273:9812-9820(1998) [PubMed: 9545320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 512-606 (ISOFORMS S AND T), SUBUNIT, TISSUE SPECIFICITY. Tissue: Liver and Muscle.
[3]	"Acetylcholinesterase from Bungarus venom: a monomeric species." Cousin X., Creminon C., Grassi J., Meflah K., Cornu G., Saliou B., Bon S., Massoulie J., Bon C. FEBS Lett. 387:196-200(1996) [PubMed: 8674549] [Abstract] Cited for: PROTEIN SEQUENCE OF 206-220; 253-272; 321-340; 347-372 AND 503-511. Tissue: Venom.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U54591 mRNA. Translation: AAC59905.1. AF045238 Genomic DNA. Translation: AAC16420.1. AF045238 Genomic DNA. Translation: AAC16421.1.
3D structure databases
SMR	Q92035. Positions 36-566, 567-600.
ModBase	Search...
Protein family/group databases
MEROPS	S09.979.
Phylogenomic databases
HOVERGEN	Q92035.
Enzyme and pathway databases
BRENDA	3.1.1.7. 97947.
Family and domain databases
InterPro	IPR014788. AChE_tetra. IPR000908. Acylcholinesterase_fish/snake. IPR002018. CarbesteraseB. IPR019826. Carboxylesterase_B_AS. IPR019819. Carboxylesterase_B_CS. IPR000997. Cholinesterase. [Graphical view]
PANTHER	PTHR11559. CarbesteraseB. 1 hit.
Pfam	PF08674. AChE_tetra. 1 hit. PF00135. COesterase. 1 hit. [Graphical view]
PRINTS	PR00879. ACHEFISH. PR00878. CHOLNESTRASE.
ProDom	PD415333. AChE_tetra. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00122. CARBOXYLESTERASE_B_1. 1 hit. PS00941. CARBOXYLESTERASE_B_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACES_BUNFA

Accession

Primary (citable) accession number: Q92035
Secondary accession number(s): O73748, Q10720

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	September 19, 2003
Last modified:	January 19, 2010
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)