UniProtKB - P04058 (ACES_TETCF)
Protein
Acetylcholinesterase
Gene
ache
Organism
Tetronarce californica (Pacific electric ray) (Torpedo californica)
Status
Functioni
Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.
Catalytic activityi
- EC:3.1.1.7
Activity regulationi
Inhibited by substrate concentrations above 0.5 mM.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 221 | Acyl-ester intermediate | 1 | |
Active sitei | 348 | Charge relay system | 1 | |
Active sitei | 461 | Charge relay system | 1 |
GO - Molecular functioni
- acetylcholinesterase activity Source: UniProtKB-EC
GO - Biological processi
- acetylcholine catabolic process in synaptic cleft Source: InterPro
Keywordsi
Molecular function | Hydrolase, Serine esterase |
Biological process | Neurotransmitter degradation |
Enzyme and pathway databases
BioCyci | MetaCyc:MONOMER-16823 |
BRENDAi | 3.1.1.7, 6395 |
Protein family/group databases
ESTHERi | torca-ACHE, AChE |
MEROPSi | S09.980 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:ache |
Organismi | Tetronarce californica (Pacific electric ray) (Torpedo californica) |
Taxonomic identifieri | 7787 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Batoidea › Torpediniformes › Torpedinidae › Tetronarce |
Subcellular locationi
Plasma membrane
Other locations
Plasma membrane
Other locations
Note: Attached to the membrane through disulfide linkage with the collagenic subunit, itself bound to the membrane.
Extracellular region or secreted
- synaptic cleft Source: GOC
Plasma Membrane
- plasma membrane Source: UniProtKB-SubCell
Other locations
- anchored component of membrane Source: UniProtKB-KW
Keywords - Cellular componenti
Cell junction, Cell membrane, Membrane, SynapsePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 220 | E → H: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 220 | E → Q or D: Decrease in activity. 1 Publication | 1 | |
Mutagenesisi | 221 | S → C: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 221 | S → V: Loss of activity. 1 Publication | 1 | |
Mutagenesisi | 446 | H → Q: Almost no loss of activity. 1 Publication | 1 | |
Mutagenesisi | 461 | H → Q: Loss of activity. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL4780 |
DrugCentrali | P04058 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 21 | 1 PublicationAdd BLAST | 21 | |
ChainiPRO_0000008595 | 22 – 564 | AcetylcholinesteraseAdd BLAST | 543 | |
PropeptideiPRO_0000008596 | 565 – 586 | Removed in mature formAdd BLAST | 22 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 80 | N-linked (GlcNAc...) asparagine2 Publications | 1 | |
Disulfide bondi | 88 ↔ 115 | |||
Disulfide bondi | 275 ↔ 286 | |||
Disulfide bondi | 423 ↔ 542 | |||
Glycosylationi | 437 | N-linked (GlcNAc...) asparagine3 Publications | 1 | |
Glycosylationi | 478 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 554 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 558 | Interchain | ||
Lipidationi | 564 | GPI-anchor amidated serine1 Publication | 1 |
Post-translational modificationi
An interchain disulfide bond is present in what becomes position 593 of the T isoform.
Keywords - PTMi
Disulfide bond, Glycoprotein, GPI-anchor, LipoproteinPTM databases
iPTMneti | P04058 |
Expressioni
Tissue specificityi
Found in the synapses and to a lower extent in extrajunctional areas of muscle and nerve, and on erythrocyte membranes.
Interactioni
Subunit structurei
Isoform H form is a homodimer; the asymmetric form is a disulfide-bonded oligomer composed of a collagenic subunit (Q) and a variable number of T catalytic subunits.
11 PublicationsProtein-protein interaction databases
MINTi | P04058 |
Chemistry databases
BindingDBi | P04058 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P04058 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P04058 |
Family & Domainsi
Sequence similaritiesi
Belongs to the type-B carboxylesterase/lipase family.Curated
Keywords - Domaini
SignalFamily and domain databases
Gene3Di | 3.40.50.1820, 1 hit |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR000908, Acylcholinesterase_fish/snake IPR002018, CarbesteraseB IPR019826, Carboxylesterase_B_AS IPR019819, Carboxylesterase_B_CS IPR000997, Cholinesterase |
Pfami | View protein in Pfam PF00135, COesterase, 1 hit |
PRINTSi | PR00879, ACHEFISH PR00878, CHOLNESTRASE |
SUPFAMi | SSF53474, SSF53474, 1 hit |
PROSITEi | View protein in PROSITE PS00122, CARBOXYLESTERASE_B_1, 1 hit PS00941, CARBOXYLESTERASE_B_2, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketNote: Additional isoforms seem to exist.
Isoform H (identifier: P04058-1) [UniParc]FASTAAdd to basket
Also known as: Globular
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MNLLVTSSLG VLLHLVVLCQ ADDHSELLVN TKSGKVMGTR VPVLSSHISA
60 70 80 90 100
FLGIPFAEPP VGNMRFRRPE PKKPWSGVWN ASTYPNNCQQ YVDEQFPGFS
110 120 130 140 150
GSEMWNPNRE MSEDCLYLNI WVPSPRPKST TVMVWIYGGG FYSGSSTLDV
160 170 180 190 200
YNGKYLAYTE EVVLVSLSYR VGAFGFLALH GSQEAPGNVG LLDQRMALQW
210 220 230 240 250
VHDNIQFFGG DPKTVTIFGE SAGGASVGMH ILSPGSRDLF RRAILQSGSP
260 270 280 290 300
NCPWASVSVA EGRRRAVELG RNLNCNLNSD EELIHCLREK KPQELIDVEW
310 320 330 340 350
NVLPFDSIFR FSFVPVIDGE FFPTSLESML NSGNFKKTQI LLGVNKDEGS
360 370 380 390 400
FFLLYGAPGF SKDSESKISR EDFMSGVKLS VPHANDLGLD AVTLQYTDWM
410 420 430 440 450
DDNNGIKNRD GLDDIVGDHN VICPLMHFVN KYTKFGNGTY LYFFNHRASN
460 470 480 490 500
LVWPEWMGVI HGYEIEFVFG LPLVKELNYT AEEEALSRRI MHYWATFAKT
510 520 530 540 550
GNPNEPHSQE SKWPLFTTKE QKFIDLNTEP MKVHQRLRVQ MCVFWNQFLP
560 570 580
KLLNATACDG ELSSSGTSSS KGIIFYVLFS ILYLIF
Note: GPI-anchored form.
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_001460 | 557 – 586 | ACDGE…LYLIF → ETIDEAERQWKTEFHRWSSY MMHWKNQFDHYSRHESCAEL in isoform T. CuratedAdd BLAST | 30 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X03439 mRNA Translation: CAA27169.1 X56516 Genomic DNA No translation available. X56517 Genomic DNA No translation available. |
PIRi | A00773, ACRYE |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X03439 mRNA Translation: CAA27169.1 X56516 Genomic DNA No translation available. X56517 Genomic DNA No translation available. |
PIRi | A00773, ACRYE |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1ACJ | X-ray | 2.80 | A | 22-556 | [»] | |
1ACL | X-ray | 2.80 | A | 22-556 | [»] | |
1AMN | X-ray | 2.80 | A | 22-558 | [»] | |
1AX9 | X-ray | 2.80 | A | 22-558 | [»] | |
1CFJ | X-ray | 2.60 | A | 22-558 | [»] | |
1DX6 | X-ray | 2.30 | A | 22-564 | [»] | |
1E3Q | X-ray | 2.85 | A | 22-564 | [»] | |
1E66 | X-ray | 2.10 | A | 22-564 | [»] | |
1EA5 | X-ray | 1.80 | A | 22-558 | [»] | |
1EEA | X-ray | 4.50 | A | 22-555 | [»] | |
1EVE | X-ray | 2.50 | A | 22-564 | [»] | |
1FSS | X-ray | 3.00 | A | 22-558 | [»] | |
1GPK | X-ray | 2.10 | A | 22-558 | [»] | |
1GPN | X-ray | 2.35 | A | 22-558 | [»] | |
1GQR | X-ray | 2.20 | A | 25-556 | [»] | |
1GQS | X-ray | 3.00 | A | 25-556 | [»] | |
1H22 | X-ray | 2.15 | A | 22-564 | [»] | |
1H23 | X-ray | 2.15 | A | 22-564 | [»] | |
1HBJ | X-ray | 2.50 | A | 22-564 | [»] | |
1JGA | model | - | A | 1-586 | [»] | |
1JGB | model | - | A | 1-586 | [»] | |
1JJB | X-ray | 2.30 | A | 25-556 | [»] | |
1OCE | X-ray | 2.70 | A | 22-558 | [»] | |
1ODC | X-ray | 2.20 | A | 22-564 | [»] | |
1QID | X-ray | 2.05 | A | 22-558 | [»] | |
1QIE | X-ray | 2.10 | A | 22-558 | [»] | |
1QIF | X-ray | 2.10 | A | 22-558 | [»] | |
1QIG | X-ray | 2.30 | A | 22-558 | [»] | |
1QIH | X-ray | 2.50 | A | 22-558 | [»] | |
1QII | X-ray | 2.65 | A | 22-558 | [»] | |
1QIJ | X-ray | 2.80 | A | 22-558 | [»] | |
1QIK | X-ray | 2.90 | A | 22-558 | [»] | |
1QIM | X-ray | 3.00 | A | 22-558 | [»] | |
1QTI | X-ray | 2.50 | A | 22-558 | [»] | |
1SOM | X-ray | 2.20 | A | 22-564 | [»] | |
1U65 | X-ray | 2.61 | A | 22-564 | [»] | |
1UT6 | X-ray | 2.40 | A | 22-556 | [»] | |
1VOT | X-ray | 2.50 | A | 22-558 | [»] | |
1VXO | X-ray | 2.40 | A | 22-558 | [»] | |
1VXR | X-ray | 2.20 | A | 22-558 | [»] | |
1W4L | X-ray | 2.16 | A | 22-564 | [»] | |
1W6R | X-ray | 2.05 | A | 22-564 | [»] | |
1W75 | X-ray | 2.40 | A/B | 22-564 | [»] | |
1W76 | X-ray | 2.30 | A/B | 22-564 | [»] | |
1ZGB | X-ray | 2.30 | A | 22-564 | [»] | |
1ZGC | X-ray | 2.10 | A/B | 22-564 | [»] | |
2ACE | X-ray | 2.50 | A | 22-558 | [»] | |
2ACK | X-ray | 2.40 | A | 22-558 | [»] | |
2BAG | X-ray | 2.40 | A | 22-564 | [»] | |
2C4H | X-ray | 2.15 | A | 22-558 | [»] | |
2C58 | X-ray | 2.30 | A | 22-558 | [»] | |
2C5F | X-ray | 2.60 | A | 22-558 | [»] | |
2C5G | X-ray | 1.95 | A | 22-558 | [»] | |
2CEK | X-ray | 2.20 | A | 22-556 | [»] | |
2CKM | X-ray | 2.15 | A | 22-564 | [»] | |
2CMF | X-ray | 2.50 | A | 22-564 | [»] | |
2DFP | X-ray | 2.30 | A | 23-556 | [»] | |
2J3D | X-ray | 2.60 | A | 22-564 | [»] | |
2J3Q | X-ray | 2.80 | A | 22-564 | [»] | |
2J4F | X-ray | 2.80 | A | 22-564 | [»] | |
2V96 | X-ray | 2.40 | A/B | 22-558 | [»] | |
2V97 | X-ray | 2.40 | A/B | 22-558 | [»] | |
2V98 | X-ray | 3.00 | A/B | 22-558 | [»] | |
2VA9 | X-ray | 2.40 | A/B | 22-558 | [»] | |
2VJA | X-ray | 2.30 | A/B | 22-558 | [»] | |
2VJB | X-ray | 2.39 | A/B | 22-558 | [»] | |
2VJC | X-ray | 2.20 | A/B | 22-558 | [»] | |
2VJD | X-ray | 2.30 | A/B | 22-558 | [»] | |
2VQ6 | X-ray | 2.71 | A | 22-564 | [»] | |
2VT6 | X-ray | 2.40 | A/B | 22-558 | [»] | |
2VT7 | X-ray | 2.20 | A/B | 22-558 | [»] | |
2W6C | X-ray | 2.69 | X | 1-586 | [»] | |
2WFZ | X-ray | 1.95 | A | 22-558 | [»] | |
2WG0 | X-ray | 2.20 | A | 22-558 | [»] | |
2WG1 | X-ray | 2.20 | A | 22-558 | [»] | |
2WG2 | X-ray | 1.95 | A | 22-558 | [»] | |
2XI4 | X-ray | 2.30 | A/B | 22-558 | [»] | |
3ACE | model | - | A | 22-558 | [»] | |
3GEL | X-ray | 2.39 | A | 25-556 | [»] | |
3I6M | X-ray | 2.26 | A | 23-556 | [»] | |
3I6Z | X-ray | 2.19 | A | 23-556 | [»] | |
3M3D | X-ray | 2.34 | A | 22-564 | [»] | |
3ZV7 | X-ray | 2.26 | A | 22-564 | [»] | |
4ACE | model | - | A | 22-558 | [»] | |
4TVK | X-ray | 2.30 | A | 23-556 | [»] | |
4W63 | X-ray | 2.80 | A | 23-556 | [»] | |
4X3C | X-ray | 2.60 | A | 23-556 | [»] | |
5BWB | X-ray | 2.57 | A | 22-558 | [»] | |
5BWC | X-ray | 2.45 | A | 22-558 | [»] | |
5DLP | X-ray | 2.70 | A | 22-564 | [»] | |
5E2I | X-ray | 2.65 | A | 25-556 | [»] | |
5E4J | X-ray | 2.54 | A | 25-556 | [»] | |
5E4T | X-ray | 2.43 | A | 22-564 | [»] | |
5EHX | X-ray | 2.10 | A | 25-556 | [»] | |
5EI5 | X-ray | 2.10 | A | 23-556 | [»] | |
5IH7 | X-ray | 2.40 | A | 23-556 | [»] | |
5NAP | X-ray | 2.17 | A | 22-564 | [»] | |
5NAU | X-ray | 2.25 | A | 22-564 | [»] | |
5NUU | X-ray | 2.50 | A | 22-564 | [»] | |
6EUC | X-ray | 2.22 | A | 25-556 | [»] | |
6EUE | X-ray | 2.00 | A | 24-556 | [»] | |
6EWK | X-ray | 2.22 | A | 25-556 | [»] | |
6EZG | X-ray | 2.20 | A/B | 22-558 | [»] | |
6EZH | X-ray | 2.60 | A/B | 22-558 | [»] | |
6FLD | X-ray | 2.40 | A | 25-556 | [»] | |
6FQN | X-ray | 2.30 | A | 25-556 | [»] | |
6G17 | X-ray | 2.20 | A | 22-558 | [»] | |
6G1U | X-ray | 1.79 | A/B | 22-586 | [»] | |
6G1V | X-ray | 1.82 | A/B | 22-586 | [»] | |
6G1W | X-ray | 1.90 | A/B | 22-586 | [»] | |
6G4M | X-ray | 2.63 | A/B | 22-558 | [»] | |
6G4N | X-ray | 2.90 | A/B | 22-558 | [»] | |
6G4O | X-ray | 2.78 | A/B | 22-558 | [»] | |
6G4P | X-ray | 2.83 | A/B | 22-558 | [»] | |
6H12 | X-ray | 2.20 | A/B | 22-586 | [»] | |
6H13 | X-ray | 2.80 | A/B | 22-586 | [»] | |
6H14 | X-ray | 1.86 | A/B | 22-586 | [»] | |
6TT0 | X-ray | 2.80 | A | 25-556 | [»] | |
SMRi | P04058 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
MINTi | P04058 |
Chemistry databases
BindingDBi | P04058 |
ChEMBLi | CHEMBL4780 |
DrugCentrali | P04058 |
Protein family/group databases
ESTHERi | torca-ACHE, AChE |
MEROPSi | S09.980 |
PTM databases
iPTMneti | P04058 |
Enzyme and pathway databases
BioCyci | MetaCyc:MONOMER-16823 |
BRENDAi | 3.1.1.7, 6395 |
Miscellaneous databases
EvolutionaryTracei | P04058 |
PROi | PR:P04058 |
Family and domain databases
Gene3Di | 3.40.50.1820, 1 hit |
InterProi | View protein in InterPro IPR029058, AB_hydrolase IPR000908, Acylcholinesterase_fish/snake IPR002018, CarbesteraseB IPR019826, Carboxylesterase_B_AS IPR019819, Carboxylesterase_B_CS IPR000997, Cholinesterase |
Pfami | View protein in Pfam PF00135, COesterase, 1 hit |
PRINTSi | PR00879, ACHEFISH PR00878, CHOLNESTRASE |
SUPFAMi | SSF53474, SSF53474, 1 hit |
PROSITEi | View protein in PROSITE PS00122, CARBOXYLESTERASE_B_1, 1 hit PS00941, CARBOXYLESTERASE_B_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ACES_TETCF | |
Accessioni | P04058Primary (citable) accession number: P04058 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1986 |
Last sequence update: | June 1, 1994 | |
Last modified: | February 10, 2021 | |
This is version 174 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families