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Q27677

- ACES_LEPDE

UniProt

Q27677 - ACES_LEPDE

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Protein

Acetylcholinesterase

Gene
N/A
Organism
Leptinotarsa decemlineata (Colorado potato beetle) (Doryphora decemlineata)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

Rapidly hydrolyzes choline released into the synapse.

Catalytic activityi

Acetylcholine + H2O = choline + acetate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei253 – 2531Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei382 – 3821Charge relay systemBy similarity
Active sitei496 – 4961Charge 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
OrganismiLeptinotarsa decemlineata (Colorado potato beetle) (Doryphora decemlineata)
Taxonomic identifieri7539 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaColeopteraPolyphagaCucujiformiaChrysomeloideaChrysomelidaeChrysomelinaeDoryphoriniLeptinotarsa

Subcellular locationi

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

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 – 3838Sequence AnalysisAdd
BLAST
Chaini39 – 605567AcetylcholinesterasePRO_0000008607Add
BLAST
Propeptidei606 – 62924Removed in mature formSequence AnalysisPRO_0000008608Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi103 ↔ 130By similarity
Glycosylationi125 – 1251N-linked (GlcNAc...)By similarity
Disulfide bondi307 ↔ 322By similarity
Glycosylationi308 – 3081N-linked (GlcNAc...)By similarity
Glycosylationi418 – 4181N-linked (GlcNAc...)By similarity
Disulfide bondi458 ↔ 574By similarity
Glycosylationi509 – 5091N-linked (GlcNAc...)By similarity
Lipidationi605 – 6051GPI-anchor amidated serineSequence Analysis

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Interactioni

Subunit structurei

Homodimer; disulfide-linked.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ27677.
SMRiQ27677. Positions 40-585.
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.

Q27677-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGQLSILCLF VTVCASVCGY SWPSDETTTK PSQFKDFHTD PLVVETTSGL
60 70 80 90 100
VRGYSKTVLG REVHVFTGIP FAKPPIEQLR FKKPVPIDPW HGILDATKQP
110 120 130 140 150
NSCFQERYEY FPGFEGEEMW NPNTNISEDC LYLNIWVPQR LRIRHHADKP
160 170 180 190 200
TIDRPKVPVL IWIYGGGYMS GTATLDVYDA DIIAATSDVI VASMQYRLGS
210 220 230 240 250
FGFLYLNRYF PRGSDETPGN MGLWDQILAI RWIKDNAAAF GGDPDLITLF
260 270 280 290 300
GESAGGGSIS IHLISPVTKG LVRRGIMQSG TMNAPWSYMS GERAEQIGKI
310 320 330 340 350
LIQDCGCNVS LLENSPRKVM DCMRAVDAKT ISLQQWNSYS GILGFPSTPT
360 370 380 390 400
IEGVLLPKHP MDMLAEGDYE DMEILLGSNH DEGTYFLLYD FIDFFEKDGP
410 420 430 440 450
SFLQREKYHD IIDTIFKNMS RLERDAIVFQ YTNWEHVHDG YLNQKMIGDV
460 470 480 490 500
VGDYFFVCPT NNFAEVAADR GMKVFYYYFT HRTSTSLWGE WMGVIHGDEV
510 520 530 540 550
EYVFGHPLNM SLQFNSRERE LSLKIMQAFA RFATTGKPVT DDVNWPLYTK
560 570 580 590 600
DQPQYFIFNA DKNGIGKGPR ATACAFWNDF LPKLRDNSGS EEAPCVNTYL
610 620
SKIRSSSNEL LPPSTSLVLI WIMTLLNAL
Length:629
Mass (Da):71,142
Last modified:November 1, 1996 - v1
Checksum:i06556F833EB16C72
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L41180 mRNA. Translation: AAB00466.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L41180 mRNA. Translation: AAB00466.1 .

3D structure databases

ProteinModelPortali Q27677.
SMRi Q27677. Positions 40-585.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL2366490.

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. "Cloning and sequencing of a cDNA encoding acetylcholinesterase in Colorado potato beetle, Leptinotarsa decemlineata (Say)."
    Zhu K.Y., Clark J.M.
    Insect Biochem. Mol. Biol. 25:1129-1138(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: SS.
    Tissue: Larva and Pupae.

Entry informationi

Entry nameiACES_LEPDE
AccessioniPrimary (citable) accession number: Q27677
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 81 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