O42275
Gene name |
ache |
Protein name |
Acetylcholinesterase |
Names |
AChE |
Species |
Electrophorus electricus (Electric eel) (Gymnotus electricus) |
KEGG Pathway |
|
EC number |
3.1.1.7: Carboxylic ester hydrolases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for O42275
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O42275-F1 | Predicted | AlphaFoldDB |
No variants for O42275
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O42275 | |||||
No associated diseases with O42275
No regional properties for O42275
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for O42275 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.1.7 | Carboxylic ester hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| anchoring junction | A cell junction that mechanically attaches a cell (and its cytoskeleton) to neighboring cells or to the extracellular matrix. |
| extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| synapse | The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| acetylcholinesterase activity | Catalysis of the reaction: acetylcholine + H2O = choline + acetate. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| neurotransmitter catabolic process | The chemical reactions and pathways resulting in the breakdown of any of a group of substances that are released on excitation from the axon terminal of a presynaptic neuron of the central or peripheral nervous system and travel across the synaptic cleft to either excite or inhibit the target cell. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKILDALLFP | VIFIMFFIHL | SIAQTDPELT | IMTRLGQVQG | TRLPVPDRSH | VIAFLGIPFA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EPPLGKMRFK | PPEPKKPWND | VFDARDYPSA | CYQYVDTSYP | GFSGTEMWNP | NRMMSEDCLY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LNVWVPATPR | PHNLTVMVWI | YGGGFYSGSS | SLDVYDGRYL | AHSEKVVVVS | MNYRVSAFGF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LALNGSAEAP | GNVGLLDQRL | ALQWVQDNIH | FFGGNPKQVT | IFGESAGAAS | VGMHLLSPDS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RPKFTRAILQ | SGVPNGPWRT | VSFDEARRRA | IKLGRLVGCP | DGNDTDLIDC | LRSKQPQDLI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DQEWLVLPFS | GLFRFSFVPV | IDGVVFPDTP | EAMLNSGNFK | DTQILLGVNQ | NEGSYFLIYG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| APGFSKDNES | LITREDFLQG | VKMSVPHANE | IGLEAVILQY | TDWMDEDNPI | KNREAMDDIV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GDHNVVCPLQ | HFAKMYAQYS | ILQGQTGTAS | QGNLGWGNSG | SASNSGNSQV | SVYLYMFDHR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ASNLVWPEWM | GVIHGYEIEF | VFGLPLEKRL | NYTLEEEKLS | RRMMKYWANF | ARTGNPNINV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DGSIDSRRRW | PVFTSTEQKH | VGLNTDSLKV | HKGLKSQFCA | LWNRFLPRLL | NVTENIDDAE |
| 610 | 620 | 630 | |||
| RQWKAEFHRW | SSYMMHWKNQ | FDHYSKQERC | TNL |