Reviewed, UniProtKB/Swiss-Prot P56161 (ACES_ANOST)

Names and origin

Protein names	Recommended name:     Acetylcholinesterase       Short name=AChE     EC=3.1.1.7
Organism	Anopheles stephensi (Indo-Pakistan malaria mosquito)
Taxonomic identifier	30069 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Anophelinae › Anopheles › stephensi species complex

Protein attributes

Sequence length	664 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Rapidly hydrolyzes choline released into the synapse. It can hydrolyze butyrylthiocholine.
Catalytic activity	Acetylcholine + H2O = choline + acetate.
Subunit structure	Homodimer; disulfide-linked By similarity.
Subcellular location	Cell junction › synapse. Cell membrane; Lipid-anchor › GPI-anchor. Note: Attached to the membrane of the neuronal cholinergic synapses by a GPI-anchor.
Sequence similarities	Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
Biological process	Neurotransmitter degradation
Cellular component	Cell junction Cell membrane Membrane Synapse
Domain	Signal
Molecular function	Hydrolase Serine esterase
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Gene Ontology (GO)
Biological process	acetylcholine catabolic process in synaptic cleft Inferred from electronic annotation. Source: InterPro
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell junction Inferred from electronic annotation. Source: UniProtKB-KW 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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 29	29	Potential
	Chain	30 – 647	618	Acetylcholinesterase		PRO_0000008600
	Propeptide	648 – 664	17	Removed in mature form Potential		PRO_0000008601
Sites
	Active site	261	1	Acyl-ester intermediate By similarity
	Active site	390	1	Charge relay system By similarity
	Active site	504	1	Charge relay system By similarity
Amino acid modifications
	Lipidation	647	1	GPI-anchor amidated asparagine Potential
	Glycosylation	117	1	N-linked (GlcNAc...) By similarity
	Glycosylation	316	1	N-linked (GlcNAc...) By similarity
	Glycosylation	517	1	N-linked (GlcNAc...) By similarity
	Disulfide bond	95 ↔ 122		By similarity
	Disulfide bond	315 ↔ 330		By similarity
	Disulfide bond	466 ↔ 588		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P56161-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 0BFBF9414F8020C7	FASTA	664	74,629
	10 20 30 40 50 60 MFVNQRTRRP YMSVFVLVLG AAVICPAYGI IDRLVVQTSS GPIRGRSTMV QGREVHVFNG 70 80 90 100 110 120 VPFAKPPVDS LRFKKPVPAE PWHGVLDATR LPPSCIQERY EYFPGFAGEE MWNPNTNVSE 130 140 150 160 170 180 DCLYLNIWVP TKTRLRHGRG LNFGSNDYFQ DDDDFQRQHQ SKGGLAMLVW IYGGGFMSGT 190 200 210 220 230 240 STLDIYNAEI LAAVGNVIVA SMQYRVGAFG FLYLAPYING YEEDAPGNMG MWDQALAIRW 250 260 270 280 290 300 LKENAKAFGG DPDLITLFGE SAGGSSVSLH LLSPVTRGLS KRGILQSGTL NAPWSHMTAE 310 320 330 340 350 360 KALQIAEGLI DDCNCNLTML KESPSTVMQC MRNVDAKTIS VQQWNSYSGI LGFPSAPTID 370 380 390 400 410 420 GVFMTADPMT MLREANLEGI DILVGSNRDE GTYFLLYDFI DYFEKDAATS LPRDKFLEIM 430 440 450 460 470 480 NTIFNKASEP EREAIIFQYT GWESGNDGYQ NQHQVGRAVG DHFFICPTNE FALGLTERGA 490 500 510 520 530 540 SVHYYYFTHR TSTSLWGEWM GVLHGDEVEY IFGQPMNASL QYRQRERDLS RRMVLSVSEF 550 560 570 580 590 600 ARTGNPALEG EHWPLYTREN PIFFIFNAEG EDDLRGEKYG RGPMATSCAF WNDFLPRLRA 610 620 630 640 650 660 WSVPSKSPCN LLEQMSIASV SSTMPIVVMV VLVLIPLCAW WWAIKKNKTP PHPQVILETR AFMH

References

[1]	"The acetylcholinesterase gene of Anopheles stephensi." Hall L.M.C., Malcolm C.A. Cell. Mol. Neurobiol. 11:131-141(1991) [PubMed: 1901515] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

3D structure databases
HSSP	HSSP built from PDB template 1DX4 based on UniProtKB P07140.
SMR	P56161. Positions 32-601.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.1.1.7. 165156.
Family and domain databases
InterPro	IPR001445. Acylcholinesterase_insect. IPR002018. CarbesteraseB. IPR019826. Carboxylesterase_B_AS. IPR019819. Carboxylesterase_B_CS. IPR000997. Cholinesterase. [Graphical view]
PANTHER	PTHR11559. CarbesteraseB. 1 hit.
Pfam	PF00135. COesterase. 1 hit. [Graphical view]
PRINTS	PR00880. ACHEINSECT. PR00878. CHOLNESTRASE.
PROSITE	PS00122. CARBOXYLESTERASE_B_1. 1 hit. PS00941. CARBOXYLESTERASE_B_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACES_ANOST

Accession

Primary (citable) accession number: P56161

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	October 13, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)