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Protein

Acetylcholinesterase

Gene

ache

Organism
Tetronarce californica (Pacific electric ray) (Torpedo californica)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Acetylcholine + H2O = choline + acetate.

Enzyme regulationi

Inhibited by substrate concentrations above 0.5 mM.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei221 – 2211Acyl-ester intermediate
Active sitei348 – 3481Charge relay system
Active sitei461 – 4611Charge relay system

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Neurotransmitter degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16823.
BRENDAi3.1.1.7. 6395.

Protein family/group databases

ESTHERitorca-ACHE. AChE.
MEROPSiS09.980.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylcholinesterase (EC:3.1.1.7)
Short name:
AChE
Gene namesi
Name:ache
OrganismiTetronarce californica (Pacific electric ray) (Torpedo californica)
Taxonomic identifieri7787 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataChondrichthyesElasmobranchiiBatoideaTorpediniformesTorpedinidaeTetronarce

Subcellular locationi

Isoform T :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi220 – 2201E → H: Loss of activity. 1 Publication
Mutagenesisi220 – 2201E → Q or D: Decrease in activity. 1 Publication
Mutagenesisi221 – 2211S → C: Loss of activity. 1 Publication
Mutagenesisi221 – 2211S → V: Loss of activity. 1 Publication
Mutagenesisi446 – 4461H → Q: Almost no loss of activity. 1 Publication
Mutagenesisi461 – 4611H → Q: Loss of activity. 1 Publication

Chemistry

ChEMBLiCHEMBL4780.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 564543AcetylcholinesterasePRO_0000008595Add
BLAST
Propeptidei565 – 58622Removed in mature formPRO_0000008596Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi80 – 801N-linked (GlcNAc...)2 Publications
Disulfide bondi88 ↔ 115
Disulfide bondi275 ↔ 286
Disulfide bondi423 ↔ 542
Glycosylationi437 – 4371N-linked (GlcNAc...)3 Publications
Glycosylationi478 – 4781N-linked (GlcNAc...)1 Publication
Glycosylationi554 – 5541N-linked (GlcNAc...)1 Publication
Disulfide bondi558 – 558Interchain
Lipidationi564 – 5641GPI-anchor amidated serine1 Publication

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, Lipoprotein

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 Publications

Protein-protein interaction databases

MINTiMINT-1518870.

Chemistry

BindingDBiP04058.

Structurei

Secondary structure

1
586
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 314Combined sources
Beta strandi34 – 374Combined sources
Beta strandi39 – 435Combined sources
Beta strandi46 – 5510Combined sources
Helixi62 – 643Combined sources
Beta strandi76 – 805Combined sources
Beta strandi87 – 893Combined sources
Beta strandi95 – 984Combined sources
Helixi100 – 1034Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi117 – 1226Combined sources
Beta strandi128 – 1369Combined sources
Turni140 – 1423Combined sources
Helixi149 – 1513Combined sources
Helixi154 – 1607Combined sources
Beta strandi163 – 1664Combined sources
Helixi172 – 1765Combined sources
Beta strandi183 – 1853Combined sources
Helixi189 – 20416Combined sources
Helixi205 – 2084Combined sources
Beta strandi210 – 22011Combined sources
Helixi222 – 23211Combined sources
Helixi234 – 2374Combined sources
Beta strandi241 – 2477Combined sources
Turni253 – 2553Combined sources
Helixi259 – 27214Combined sources
Helixi280 – 28910Combined sources
Helixi292 – 2987Combined sources
Helixi299 – 3024Combined sources
Beta strandi304 – 3063Combined sources
Beta strandi307 – 3093Combined sources
Beta strandi319 – 3246Combined sources
Helixi326 – 3327Combined sources
Beta strandi340 – 3456Combined sources
Beta strandi347 – 3493Combined sources
Helixi350 – 3567Combined sources
Beta strandi362 – 3643Combined sources
Helixi370 – 38011Combined sources
Helixi386 – 39510Combined sources
Turni399 – 4013Combined sources
Helixi405 – 42016Combined sources
Helixi422 – 43312Combined sources
Beta strandi435 – 4373Combined sources
Beta strandi439 – 4446Combined sources
Helixi455 – 4573Combined sources
Turni461 – 4644Combined sources
Helixi465 – 4684Combined sources
Helixi471 – 4733Combined sources
Helixi475 – 4773Combined sources
Helixi481 – 50020Combined sources
Beta strandi501 – 5044Combined sources
Turni518 – 5203Combined sources
Beta strandi522 – 5298Combined sources
Beta strandi533 – 5364Combined sources
Helixi539 – 5468Combined sources
Helixi548 – 5558Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ACJX-ray2.80A22-556[»]
1ACLX-ray2.80A22-556[»]
1AMNX-ray2.80A22-558[»]
1AX9X-ray2.80A22-558[»]
1CFJX-ray2.60A22-558[»]
1DX6X-ray2.30A22-564[»]
1E3QX-ray2.85A22-564[»]
1E66X-ray2.10A22-564[»]
1EA5X-ray1.80A22-558[»]
1EEAX-ray4.50A22-555[»]
1EVEX-ray2.50A22-564[»]
1FSSX-ray3.00A22-558[»]
1GPKX-ray2.10A22-558[»]
1GPNX-ray2.35A22-558[»]
1GQRX-ray2.20A25-556[»]
1GQSX-ray3.00A25-556[»]
1H22X-ray2.15A22-564[»]
1H23X-ray2.15A22-564[»]
1HBJX-ray2.50A22-564[»]
1JGAmodel-A1-586[»]
1JGBmodel-A1-586[»]
1JJBX-ray2.30A25-556[»]
1OCEX-ray2.70A22-558[»]
1ODCX-ray2.20A22-564[»]
1QIDX-ray2.05A22-558[»]
1QIEX-ray2.10A22-558[»]
1QIFX-ray2.10A22-558[»]
1QIGX-ray2.30A22-558[»]
1QIHX-ray2.50A22-558[»]
1QIIX-ray2.65A22-558[»]
1QIJX-ray2.80A22-558[»]
1QIKX-ray2.90A22-558[»]
1QIMX-ray3.00A22-558[»]
1QTIX-ray2.50A22-558[»]
1SOMX-ray2.20A22-564[»]
1U65X-ray2.61A22-564[»]
1UT6X-ray2.40A22-556[»]
1VOTX-ray2.50A22-558[»]
1VXOX-ray2.40A22-558[»]
1VXRX-ray2.20A22-558[»]
1W4LX-ray2.16A22-564[»]
1W6RX-ray2.05A22-564[»]
1W75X-ray2.40A/B22-564[»]
1W76X-ray2.30A/B22-564[»]
1ZGBX-ray2.30A22-564[»]
1ZGCX-ray2.10A/B22-564[»]
2ACEX-ray2.50A22-558[»]
2ACKX-ray2.40A22-558[»]
2BAGX-ray2.40A22-564[»]
2C4HX-ray2.15A22-558[»]
2C58X-ray2.30A22-558[»]
2C5FX-ray2.60A22-558[»]
2C5GX-ray1.95A22-558[»]
2CEKX-ray2.20A22-556[»]
2CKMX-ray2.15A22-564[»]
2CMFX-ray2.50A22-564[»]
2DFPX-ray2.30A23-556[»]
2J3DX-ray2.60A22-564[»]
2J3QX-ray2.80A22-564[»]
2J4FX-ray2.80A22-564[»]
2V96X-ray2.40A/B22-558[»]
2V97X-ray2.40A/B22-558[»]
2V98X-ray3.00A/B22-558[»]
2VA9X-ray2.40A/B22-558[»]
2VJAX-ray2.30A/B22-558[»]
2VJBX-ray2.39A/B22-558[»]
2VJCX-ray2.20A/B22-558[»]
2VJDX-ray2.30A/B22-558[»]
2VQ6X-ray2.71A22-564[»]
2VT6X-ray2.40A/B22-558[»]
2VT7X-ray2.20A/B22-558[»]
2W6CX-ray2.69X1-586[»]
2WFZX-ray1.95A22-558[»]
2WG0X-ray2.20A22-558[»]
2WG1X-ray2.20A22-558[»]
2WG2X-ray1.95A22-558[»]
2XI4X-ray2.30A/B22-558[»]
3ACEmodel-A22-558[»]
3GELX-ray2.39A25-556[»]
3I6MX-ray2.26A23-556[»]
3I6ZX-ray2.19A23-556[»]
3M3DX-ray2.34A22-564[»]
3ZV7X-ray2.26A22-564[»]
4ACEmodel-A22-558[»]
4TVKX-ray2.30A23-556[»]
4W63X-ray2.80A23-556[»]
4X3CX-ray2.60A23-556[»]
5BWBX-ray2.57A22-558[»]
5BWCX-ray2.45A22-558[»]
5DLPX-ray2.70A22-564[»]
5E2IX-ray2.65A25-556[»]
5E4JX-ray2.54A25-556[»]
5E4TX-ray2.43A22-564[»]
ProteinModelPortaliP04058.
SMRiP04058. Positions 23-556.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04058.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG008839.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000908. Acylcholinesterase_fish/snake.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00879. ACHEFISH.
PR00878. CHOLNESTRASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Note: 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 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        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.
Length:586
Mass (Da):65,906
Last modified:June 1, 1994 - v2
Checksum:i731D5F0F3ABA62A8
GO
Isoform T (identifier: P04058-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     557-586: ACDGELSSSGTSSSKGIIFYVLFSILYLIF → ETIDEAERQWKTEFHRWSSYMMHWKNQFDHYSRHESCAEL

Show »
Length:596
Mass (Da):67,818
Checksum:i36D5E9A30F9E6065
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei557 – 58630ACDGE…LYLIF → ETIDEAERQWKTEFHRWSSY MMHWKNQFDHYSRHESCAEL in isoform T. CuratedVSP_001460Add
BLAST

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.
PIRiA00773. ACRYE.

Keywords - Coding sequence diversityi

Alternative splicing

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.
PIRiA00773. ACRYE.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ACJX-ray2.80A22-556[»]
1ACLX-ray2.80A22-556[»]
1AMNX-ray2.80A22-558[»]
1AX9X-ray2.80A22-558[»]
1CFJX-ray2.60A22-558[»]
1DX6X-ray2.30A22-564[»]
1E3QX-ray2.85A22-564[»]
1E66X-ray2.10A22-564[»]
1EA5X-ray1.80A22-558[»]
1EEAX-ray4.50A22-555[»]
1EVEX-ray2.50A22-564[»]
1FSSX-ray3.00A22-558[»]
1GPKX-ray2.10A22-558[»]
1GPNX-ray2.35A22-558[»]
1GQRX-ray2.20A25-556[»]
1GQSX-ray3.00A25-556[»]
1H22X-ray2.15A22-564[»]
1H23X-ray2.15A22-564[»]
1HBJX-ray2.50A22-564[»]
1JGAmodel-A1-586[»]
1JGBmodel-A1-586[»]
1JJBX-ray2.30A25-556[»]
1OCEX-ray2.70A22-558[»]
1ODCX-ray2.20A22-564[»]
1QIDX-ray2.05A22-558[»]
1QIEX-ray2.10A22-558[»]
1QIFX-ray2.10A22-558[»]
1QIGX-ray2.30A22-558[»]
1QIHX-ray2.50A22-558[»]
1QIIX-ray2.65A22-558[»]
1QIJX-ray2.80A22-558[»]
1QIKX-ray2.90A22-558[»]
1QIMX-ray3.00A22-558[»]
1QTIX-ray2.50A22-558[»]
1SOMX-ray2.20A22-564[»]
1U65X-ray2.61A22-564[»]
1UT6X-ray2.40A22-556[»]
1VOTX-ray2.50A22-558[»]
1VXOX-ray2.40A22-558[»]
1VXRX-ray2.20A22-558[»]
1W4LX-ray2.16A22-564[»]
1W6RX-ray2.05A22-564[»]
1W75X-ray2.40A/B22-564[»]
1W76X-ray2.30A/B22-564[»]
1ZGBX-ray2.30A22-564[»]
1ZGCX-ray2.10A/B22-564[»]
2ACEX-ray2.50A22-558[»]
2ACKX-ray2.40A22-558[»]
2BAGX-ray2.40A22-564[»]
2C4HX-ray2.15A22-558[»]
2C58X-ray2.30A22-558[»]
2C5FX-ray2.60A22-558[»]
2C5GX-ray1.95A22-558[»]
2CEKX-ray2.20A22-556[»]
2CKMX-ray2.15A22-564[»]
2CMFX-ray2.50A22-564[»]
2DFPX-ray2.30A23-556[»]
2J3DX-ray2.60A22-564[»]
2J3QX-ray2.80A22-564[»]
2J4FX-ray2.80A22-564[»]
2V96X-ray2.40A/B22-558[»]
2V97X-ray2.40A/B22-558[»]
2V98X-ray3.00A/B22-558[»]
2VA9X-ray2.40A/B22-558[»]
2VJAX-ray2.30A/B22-558[»]
2VJBX-ray2.39A/B22-558[»]
2VJCX-ray2.20A/B22-558[»]
2VJDX-ray2.30A/B22-558[»]
2VQ6X-ray2.71A22-564[»]
2VT6X-ray2.40A/B22-558[»]
2VT7X-ray2.20A/B22-558[»]
2W6CX-ray2.69X1-586[»]
2WFZX-ray1.95A22-558[»]
2WG0X-ray2.20A22-558[»]
2WG1X-ray2.20A22-558[»]
2WG2X-ray1.95A22-558[»]
2XI4X-ray2.30A/B22-558[»]
3ACEmodel-A22-558[»]
3GELX-ray2.39A25-556[»]
3I6MX-ray2.26A23-556[»]
3I6ZX-ray2.19A23-556[»]
3M3DX-ray2.34A22-564[»]
3ZV7X-ray2.26A22-564[»]
4ACEmodel-A22-558[»]
4TVKX-ray2.30A23-556[»]
4W63X-ray2.80A23-556[»]
4X3CX-ray2.60A23-556[»]
5BWBX-ray2.57A22-558[»]
5BWCX-ray2.45A22-558[»]
5DLPX-ray2.70A22-564[»]
5E2IX-ray2.65A25-556[»]
5E4JX-ray2.54A25-556[»]
5E4TX-ray2.43A22-564[»]
ProteinModelPortaliP04058.
SMRiP04058. Positions 23-556.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1518870.

Chemistry

BindingDBiP04058.
ChEMBLiCHEMBL4780.

Protein family/group databases

ESTHERitorca-ACHE. AChE.
MEROPSiS09.980.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG008839.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16823.
BRENDAi3.1.1.7. 6395.

Miscellaneous databases

EvolutionaryTraceiP04058.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000908. Acylcholinesterase_fish/snake.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
PRINTSiPR00879. ACHEFISH.
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_TETCF
AccessioniPrimary (citable) accession number: P04058
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: June 1, 1994
Last modified: September 7, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.