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P56161

- ACES_ANOST

UniProt

P56161 - ACES_ANOST

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Protein

Acetylcholinesterase

Gene
N/A
Organism
Anopheles stephensi (Indo-Pakistan malaria mosquito)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei261 – 2611Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei390 – 3901Charge relay systemBy similarity
Active sitei504 – 5041Charge relay systemBy similarity

GO - Molecular functioni

  1. acetylcholinesterase activity Source: UniProtKB-EC

GO - Biological processi

  1. acetylcholine catabolic process in synaptic cleft Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Neurotransmitter degradation

Protein family/group databases

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

Subcellular locationi

Cell junctionsynapse. Cell membrane; Lipid-anchorGPI-anchor
Note: Attached to the membrane of the neuronal cholinergic synapses by a GPI-anchor.

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. cell junction Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-KW
  4. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Chaini30 – 647618AcetylcholinesterasePRO_0000008600Add
BLAST
Propeptidei648 – 66417Removed in mature formSequence AnalysisPRO_0000008601Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi95 ↔ 122By similarity
Glycosylationi117 – 1171N-linked (GlcNAc...)By similarity
Disulfide bondi315 ↔ 330By similarity
Glycosylationi316 – 3161N-linked (GlcNAc...)By similarity
Disulfide bondi466 ↔ 588By similarity
Glycosylationi517 – 5171N-linked (GlcNAc...)By similarity
Lipidationi647 – 6471GPI-anchor amidated asparagineSequence Analysis

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

ProteinModelPortali P56161.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S09.980.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR001445. Acylcholinesterase_insect.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view ]
Pfami PF00135. COesterase. 1 hit.
[Graphical view ]
PRINTSi PR00880. ACHEINSECT.
PR00878. CHOLNESTRASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

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

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 29, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3