Q869C3 (ACES_ANOGA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetylcholinesterase
Short name=AChE
EC=3.1.1.7

Gene names

Name:	Ace
Synonyms:	ACE1, ACHE1
ORF Names:	AGAP001356

Organism

Anopheles gambiae (African malaria mosquito) [Reference proteome]

Taxonomic identifier

7165 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicimorpha › Culicoidea › Culicidae › Anophelinae › Anopheles › Cellia › Pyretophorus › gambiae species complex

Protein attributes

Sequence length	737 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.
Catalytic activity	Acetylcholine + H2O = choline + acetate. UniProtKB P22303
Subcellular location	Cell junction › synapse.
Polymorphism	Strains Kisumu and Kisumu2 are susceptible to insecticides while strain YAO is resistant. Insensitivity to insecticides results from a loss of sensitivity of acetylcholinesterase to organophosphates and carbamates and is due to a variant at position 280. Ref.1
Sequence similarities	Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
Biological process	Neurotransmitter degradation
Cellular component	Cell junction Synapse
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Hydrolase Serine esterase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	choline metabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome neurotransmitter catabolic process Inferred from electronic annotation. Source: UniProtKB-KW synaptic transmission, cholinergic Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW synapse Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acetylcholinesterase activity Inferred from Biological aspect of Ancestor. Source: RefGenome carboxylesterase activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 38	38	Potential
	Chain	39 – 737	699	Acetylcholinesterase		PRO_0000008599
Sites
	Active site	360	1	Acyl-ester intermediate By similarity UniProtKB P22303
	Active site	486	1	Charge relay system By similarity UniProtKB P22303
	Active site	600	1	Charge relay system By similarity UniProtKB P22303
Amino acid modifications
	Glycosylation	220	1	N-linked (GlcNAc...) Potential
	Glycosylation	670	1	N-linked (GlcNAc...) Potential
	Disulfide bond	228 ↔ 255		By similarity UniProtKB P22303
	Disulfide bond	414 ↔ 427		By similarity UniProtKB P22303
	Disulfide bond	562 ↔ 683		By similarity UniProtKB P22303
Natural variations
	Natural variant	127	1	V → A in strain: Kisumu2 and YAO. Ref.1
	Natural variant	280	1	G → S in strain: YAO; confers resistance to insecticides. Ref.1
Experimental info
	Sequence conflict	35	1	F → S in CAD56157. Ref.1
	Sequence conflict	65	1	A → S in CAD56157. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q869C3 [UniParc]. Last modified April 4, 2006. Version 3. Checksum: FDE9CCAE34DF2421	FASTA	737	80,902
	10 20 30 40 50 60 MEIRGLLMGR LRLGRRMVPL GLLGVTALLL ILPPFALVQG RHHELNNGAA IGSHQLSAAA 70 80 90 100 110 120 GVGLASQSAQ SGSLASGVMS SVPAAGASSS SSSSLLSSSA EDDVARITLS KDADAFFTPY 130 140 150 160 170 180 IGHGESVRII DAELGTLEHV HSGATPRRRG LTRRESNSDA NDNDPLVVNT DKGRIRGITV 190 200 210 220 230 240 DAPSGKKVDV WLGIPYAQPP VGPLRFRHPR PAEKWTGVLN TTTPPNSCVQ IVDTVFGDFP 250 260 270 280 290 300 GATMWNPNTP LSEDCLYINV VAPRPRPKNA AVMLWIFGGG FYSGTATLDV YDHRALASEE 310 320 330 340 350 360 NVIVVSLQYR VASLGFLFLG TPEAPGNAGL FDQNLALRWV RDNIHRFGGD PSRVTLFGES 370 380 390 400 410 420 AGAVSVSLHL LSALSRDLFQ RAILQSGSPT APWALVSREE ATLRALRLAE AVGCPHEPSK 430 440 450 460 470 480 LSDAVECLRG KDPHVLVNNE WGTLGICEFP FVPVVDGAFL DETPQRSLAS GRFKKTEILT 490 500 510 520 530 540 GSNTEEGYYF IIYYLTELLR KEEGVTVTRE EFLQAVRELN PYVNGAARQA IVFEYTDWTE 550 560 570 580 590 600 PDNPNSNRDA LDKMVGDYHF TCNVNEFAQR YAEEGNNVYM YLYTHRSKGN PWPRWTGVMH 610 620 630 640 650 660 GDEINYVFGE PLNPTLGYTE DEKDFSRKIM RYWSNFAKTG NPNPNTASSE FPEWPKHTAH 670 680 690 700 710 720 GRHYLELGLN TSFVGRGPRL RQCAFWKKYL PQLVAATSNL PGPAPPSEPC ESSAFFYRPD 730 LIVLLVSLLT ATVRFIQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Insecticide resistance in mosquito vectors." Weill M., Lutfalla G., Mogensen K., Chandre F., Berthomieu A., Berticat C., Pasteur N., Philips A., Fort P., Raymond M. Nature 423:136-137(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Kisumu, Kisumu2 and YAO.
[2]	"The genome sequence of the malaria mosquito Anopheles gambiae." Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F. , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L. Science 298:129-149(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PEST.
[3]	"A novel acetylcholinesterase gene in mosquitoes codes for the insecticide target and is non-homologous to the ace gene in Drosophila." Weill M., Fort P., Berthomi eu A., Dubois M.P., Pasteur N., Raymond M. Proc. R. Soc. B 269:2007-2016(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL GENE STRUCTURE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ488492 Genomic DNA. Translation: CAD32684.2.
AJ515149, AJ515148 Genomic DNA. Translation: CAD56156.1.
AJ515150, AJ488492 Genomic DNA. Translation: CAD56157.2.
AAAB01008987 Genomic DNA. Translation: EAA01151.3.
BN000066 Genomic DNA. Translation: CAD29865.2.

RefSeq

XP_321792.2. XM_321792.4.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AZG	model	-	A	115-737	[»]

ProteinModelPortal

Q869C3.

ModBase

Search...

Protein family/group databases

MEROPS

S09.979.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

AGAP001356-RA; AGAP001356-PA; AGAP001356.

GeneID

1281827.

KEGG

aga:AgaP_AGAP001356.

VectorBase

AGAP001357. Anopheles gambiae.

Organism-specific databases

CTD

1281827.

Phylogenomic databases

eggNOG

COG2272.

HOGENOM

HOG000091866.

InParanoid

Q869C3.

KO

K01049.

OMA

AVGCPHE.

OrthoDB

EOG4X69QJ.

PhylomeDB

Q869C3.

Family and domain databases

InterPro

IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]

Pfam

PF00135. COesterase. 1 hit.
[Graphical view]

PRINTS

PR00878. CHOLNESTRASE.

PROSITE

PS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ACES_ANOGA

Accession

Primary (citable) accession number: Q869C3
Secondary accession number(s): Q7PUR2 , Q7RTM0, Q86GC7, Q8ISM4, Q8ISM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 22, 2003
Last sequence update:	April 4, 2006
Last modified:	April 3, 2013
This is version 83 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)