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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)DescriptionActionsGraphical viewLength
Active sitei221Acyl-ester intermediate1
Active sitei348Charge relay system1
Active sitei461Charge relay system1

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)DescriptionActionsGraphical viewLength
Mutagenesisi220E → H: Loss of activity. 1 Publication1
Mutagenesisi220E → Q or D: Decrease in activity. 1 Publication1
Mutagenesisi221S → C: Loss of activity. 1 Publication1
Mutagenesisi221S → V: Loss of activity. 1 Publication1
Mutagenesisi446H → Q: Almost no loss of activity. 1 Publication1
Mutagenesisi461H → Q: Loss of activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4780.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 211 PublicationAdd BLAST21
ChainiPRO_000000859522 – 564AcetylcholinesteraseAdd BLAST543
PropeptideiPRO_0000008596565 – 586Removed in mature formAdd BLAST22

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi80N-linked (GlcNAc...)2 Publications1
Disulfide bondi88 ↔ 115
Disulfide bondi275 ↔ 286
Disulfide bondi423 ↔ 542
Glycosylationi437N-linked (GlcNAc...)3 Publications1
Glycosylationi478N-linked (GlcNAc...)1 Publication1
Glycosylationi554N-linked (GlcNAc...)1 Publication1
Disulfide bondi558Interchain
Lipidationi564GPI-anchor amidated serine1 Publication1

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 databases

BindingDBiP04058.

Structurei

Secondary structure

1586
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 31Combined sources4
Beta strandi34 – 37Combined sources4
Beta strandi39 – 43Combined sources5
Beta strandi46 – 55Combined sources10
Helixi62 – 64Combined sources3
Beta strandi76 – 80Combined sources5
Beta strandi87 – 89Combined sources3
Beta strandi95 – 98Combined sources4
Helixi100 – 103Combined sources4
Beta strandi111 – 113Combined sources3
Beta strandi117 – 122Combined sources6
Beta strandi128 – 136Combined sources9
Turni140 – 142Combined sources3
Helixi149 – 151Combined sources3
Helixi154 – 160Combined sources7
Beta strandi163 – 166Combined sources4
Helixi172 – 176Combined sources5
Beta strandi183 – 185Combined sources3
Helixi189 – 204Combined sources16
Helixi205 – 208Combined sources4
Beta strandi210 – 220Combined sources11
Helixi222 – 232Combined sources11
Helixi234 – 237Combined sources4
Beta strandi241 – 247Combined sources7
Turni253 – 255Combined sources3
Helixi259 – 272Combined sources14
Helixi280 – 289Combined sources10
Helixi292 – 298Combined sources7
Helixi299 – 302Combined sources4
Beta strandi304 – 306Combined sources3
Beta strandi307 – 309Combined sources3
Beta strandi319 – 324Combined sources6
Helixi326 – 332Combined sources7
Beta strandi340 – 345Combined sources6
Beta strandi347 – 349Combined sources3
Helixi350 – 356Combined sources7
Beta strandi362 – 364Combined sources3
Helixi370 – 380Combined sources11
Helixi386 – 395Combined sources10
Turni399 – 401Combined sources3
Helixi405 – 420Combined sources16
Helixi422 – 433Combined sources12
Beta strandi435 – 437Combined sources3
Beta strandi439 – 444Combined sources6
Helixi455 – 457Combined sources3
Turni461 – 464Combined sources4
Helixi465 – 468Combined sources4
Helixi471 – 473Combined sources3
Helixi475 – 477Combined sources3
Helixi481 – 500Combined sources20
Beta strandi501 – 504Combined sources4
Turni518 – 520Combined sources3
Beta strandi522 – 529Combined sources8
Beta strandi533 – 536Combined sources4
Helixi539 – 546Combined sources8
Helixi548 – 555Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001460557 – 586ACDGE…LYLIF → ETIDEAERQWKTEFHRWSSY MMHWKNQFDHYSRHESCAEL in isoform T. CuratedAdd BLAST30

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-1518870.

Chemistry databases

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: November 2, 2016
This is version 149 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.