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Protein

Acetylcholinesterase

Gene
N/A
Organism
Anopheles stephensi (Indo-Pakistan malaria mosquito)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Rapidly hydrolyzes choline released into the synapse. It can hydrolyze butyrylthiocholine.

Catalytic activityi

Acetylcholine + H2O = choline + acetate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei261Acyl-ester intermediatePROSITE-ProRule annotation1
Active sitei390Charge relay systemBy similarity1
Active sitei504Charge relay systemBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Neurotransmitter degradation

Protein family/group databases

ESTHERianost-ACHE. AChE.
MEROPSiS09.980.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylcholinesterase (EC:3.1.1.7)
Short name:
AChE
OrganismiAnopheles stephensi (Indo-Pakistan malaria mosquito)
Taxonomic identifieri30069 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraNematoceraCulicoideaCulicidaeAnophelinaeAnopheles
Proteomesi
  • UP000076408 Componenti: Genome assembly

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Sequence analysisAdd BLAST29
ChainiPRO_000000860030 – 647AcetylcholinesteraseAdd BLAST618
PropeptideiPRO_0000008601648 – 664Removed in mature formSequence analysisAdd BLAST17

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi95 ↔ 122By similarity
Glycosylationi117N-linked (GlcNAc...)By similarity1
Disulfide bondi315 ↔ 330By similarity
Glycosylationi316N-linked (GlcNAc...)By similarity1
Disulfide bondi466 ↔ 588By similarity
Glycosylationi517N-linked (GlcNAc...)By similarity1
Lipidationi647GPI-anchor amidated asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

Structurei

3D structure databases

ProteinModelPortaliP56161.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001445. Acylcholinesterase_insect.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00880. ACHEINSECT.
PR00878. CHOLNESTRASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P56161-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFVNQRTRRP YMSVFVLVLG AAVICPAYGI IDRLVVQTSS GPIRGRSTMV
60 70 80 90 100
QGREVHVFNG VPFAKPPVDS LRFKKPVPAE PWHGVLDATR LPPSCIQERY
110 120 130 140 150
EYFPGFAGEE MWNPNTNVSE DCLYLNIWVP TKTRLRHGRG LNFGSNDYFQ
160 170 180 190 200
DDDDFQRQHQ SKGGLAMLVW IYGGGFMSGT STLDIYNAEI LAAVGNVIVA
210 220 230 240 250
SMQYRVGAFG FLYLAPYING YEEDAPGNMG MWDQALAIRW LKENAKAFGG
260 270 280 290 300
DPDLITLFGE SAGGSSVSLH LLSPVTRGLS KRGILQSGTL NAPWSHMTAE
310 320 330 340 350
KALQIAEGLI DDCNCNLTML KESPSTVMQC MRNVDAKTIS VQQWNSYSGI
360 370 380 390 400
LGFPSAPTID GVFMTADPMT MLREANLEGI DILVGSNRDE GTYFLLYDFI
410 420 430 440 450
DYFEKDAATS LPRDKFLEIM NTIFNKASEP EREAIIFQYT GWESGNDGYQ
460 470 480 490 500
NQHQVGRAVG DHFFICPTNE FALGLTERGA SVHYYYFTHR TSTSLWGEWM
510 520 530 540 550
GVLHGDEVEY IFGQPMNASL QYRQRERDLS RRMVLSVSEF ARTGNPALEG
560 570 580 590 600
EHWPLYTREN PIFFIFNAEG EDDLRGEKYG RGPMATSCAF WNDFLPRLRA
610 620 630 640 650
WSVPSKSPCN LLEQMSIASV SSTMPIVVMV VLVLIPLCAW WWAIKKNKTP
660
PHPQVILETR AFMH
Length:664
Mass (Da):74,629
Last modified:November 1, 1997 - v1
Checksum:i0BFBF9414F8020C7
GO

Cross-referencesi

3D structure databases

ProteinModelPortaliP56161.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERianost-ACHE. AChE.
MEROPSiS09.980.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR001445. Acylcholinesterase_insect.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00880. ACHEINSECT.
PR00878. CHOLNESTRASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACES_ANOST
AccessioniPrimary (citable) accession number: P56161
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 5, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.