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P04058

- ACES_TORCA

UniProt

P04058 - ACES_TORCA

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Protein

Acetylcholinesterase

Gene

ache

Organism
Torpedo californica (Pacific electric ray)
Status
Reviewed - 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

  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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16823.

Protein family/group databases

MEROPSiS09.980.

Names & Taxonomyi

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

Subcellular locationi

Isoform T : Cell membrane; Peripheral membrane protein. Cell junctionsynapse
Note: Attached to the membrane through disulfide linkage with the collagenic subunit, itself bound to the membrane.

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

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

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.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
2W9IX-ray2.43A1-586[»]
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[»]
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. Align

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
2W9I X-ray 2.43 A 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 [» ]
ProteinModelPortali P04058.
SMRi P04058. Positions 23-556.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1518870.

Chemistry

BindingDBi P04058.
ChEMBLi CHEMBL4780.

Protein family/group databases

MEROPSi S09.980.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG008839.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-16823.

Miscellaneous databases

EvolutionaryTracei P04058.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000908. Acylcholinesterase_fish/snake.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view ]
Pfami PF00135. COesterase. 1 hit.
[Graphical view ]
PRINTSi PR00879. ACHEFISH.
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. "Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence."
    Schumacher M., Camp S., Maulet Y., Newton M., McPhee-Quigley K., Taylor S.S., Friedmann T., Taylor P.
    Nature 319:407-409(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-586.
  2. "Multiple messenger RNA species give rise to the structural diversity in acetylcholinesterase."
    Schumacher M.
    J. Biol. Chem. 263:18979-18987(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
  3. "Primary structures of the catalytic subunits from two molecular forms of acetylcholinesterase. A comparison of NH2-terminal and active center sequences."
    MacPhee-Quigley K., Taylor P., Taylor S.
    J. Biol. Chem. 260:12185-12189(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-45 AND 214-237.
  4. "Anionic subsites of the catalytic center of acetylcholinesterase from Torpedo and from cobra venom."
    Kreienkamp H.J., Weise C., Raba R., Aaviksaar A., Hucho F.
    Proc. Natl. Acad. Sci. U.S.A. 88:6117-6121(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 100-108.
  5. "Divergence in primary structure between the molecular forms of acetylcholinesterase."
    Gibney G., Macphee-Quigley K., Thompson B., Vedvick T., Low M.G., Taylor S.S., Taylor P.
    J. Biol. Chem. 263:1140-1145(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 552-558.
  6. "Single gene encodes glycophospholipid-anchored and asymmetric acetylcholinesterase forms: alternative coding exons contain inverted repeat sequences."
    Maulet Y., Camp S., Gibney G., Rachinsky T.L., Ekstroem T.J., Taylor P.
    Neuron 4:289-301(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  7. "Profile of the disulfide bonds in acetylcholinesterase."
    McPhee-Quigley K., Vedvick T.S., Taylor P., Taylor S.S.
    J. Biol. Chem. 261:13565-13570(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  8. "Structure of the glycosyl-phosphatidylinositol membrane anchor of acetylcholinesterase from the electric organ of the electric-fish, Torpedo californica."
    Mehlert A., Varon L., Silman I., Homans S.W., Ferguson M.A.
    Biochem. J. 296:473-479(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE OF THE GPI-ANCHOR.
  9. "Residues in Torpedo californica acetylcholinesterase necessary for processing to a glycosyl phosphatidylinositol-anchored form."
    Bucht G., Hjalmarsson K.
    Biochim. Biophys. Acta 1292:223-232(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: GPI-ANCHOR AT SER-564.
  10. "Mutagenesis of essential functional residues in acetylcholinesterase."
    Gibney G., Camp S., Dionne M., McPhee-Quigley K., Taylor P.
    Proc. Natl. Acad. Sci. U.S.A. 87:7546-7550(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  11. "Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein."
    Sussman J.L., Harel M., Frolow F., Oefner C., Goldman A., Toker L., Silman I.
    Science 253:872-879(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-558, ACTIVE SITE, GLYCOSYLATION AT ASN-437, DISULFIDE BONDS, SUBUNIT.
  12. "Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase."
    Harel M., Schalk I., Ehret-Sabatier L., Bouet F., Goeldner M., Hirth C., Axelsen P.H., Silman I., Sussman J.L.
    Proc. Natl. Acad. Sci. U.S.A. 90:9031-9035(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-556 IN COMPLEX WITH SUBSTRATE ANALOGS.
  13. "Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target."
    Harel M., Kleywegt G.J., Ravelli R.B., Silman I., Sussman J.L.
    Structure 3:1355-1366(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-558 IN COMPLEX WITH FASCICULIN.
  14. "Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A."
    Raves M.L., Harel M., Pang Y.P., Silman I., Kozikowski A.P., Sussman J.L.
    Nat. Struct. Biol. 4:57-63(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-558 IN COMPLEX WITH THE INHIBITOR HUPERZINE A.
  15. "'Back door' opening implied by the crystal structure of a carbamoylated acetylcholinesterase."
    Bartolucci C., Perola E., Cellai L., Brufani M., Lamba D.
    Biochemistry 38:5714-5719(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-558.
  16. "Crystal structures of aged phosphonylated acetylcholinesterase: nerve agent reaction products at the atomic level."
    Millard C.B., Kryger G., Ordentlich A., Greenblatt H.M., Harel M., Raves M.L., Segall Y., Barak D., Shafferman A., Silman I., Sussman J.L.
    Biochemistry 38:7032-7039(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-558.
  17. "Structure of acetylcholinesterase complexed with (-)-galanthamine at 2.3-A resolution."
    Greenblatt H.M., Kryger G., Lewis T., Silman I., Sussman J.L.
    FEBS Lett. 463:321-326(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-564 IN COMPLEX WITH GALANTHAMINE.
  18. "Structure of acetylcholinesterase complexed with E2020 (Aricept(R)): implications for the design of new anti-Alzheimer drugs."
    Kryger G., Silman I., Sussman J.L.
    Structure 7:297-307(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE SYNTHETIC INHIBITOR ARICEPT, GLYCOSYLATION AT ASN-80; ASN-437; ASN-478 AND ASN-554.
  19. "3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 A resolution: kinetic and molecular dynamic correlates."
    Dvir H., Wong D.M., Harel M., Barril X., Orozco M., Luque F.J., Munoz-Torrero D., Camps P., Rosenberry T.L., Silman I., Sussman J.L.
    Biochemistry 41:2970-2981(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE SYNTHETIC INHIBITOR HUPRINE.
  20. "Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug rivastigmine."
    Bar-On P., Millard C.B., Harel M., Dvir H., Enz A., Sussman J.L., Silman I.
    Biochemistry 41:3555-3564(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-556 IN COMPLEX WITH THE SYNTHETIC INHIBITOR RIVASTIGMINE.
  21. "The crystal structure of the complex of the anticancer prodrug 7-ethyl-10-[4-(1-piperidino)-1-piperidino]-carbonyloxycamptothecin (CPT-11) with Torpedo californica acetylcholinesterase provides a molecular explanation for its cholinergic action."
    Harel M., Hyatt J.L., Brumshtein B., Morton C.L., Yoon K.J., Wadkins R.M., Silman I., Sussman J.L., Potter P.M.
    Mol. Pharmacol. 67:1874-1881(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE SYNTHETIC INHIBITOR CPT-11.
  22. "Structural insights into substrate traffic and inhibition in acetylcholinesterase."
    Colletier J.-P., Fournier D., Greenblatt H.M., Stojan J., Sussman J.L., Zaccai G., Silman I., Weik M.
    EMBO J. 25:2746-2756(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 22-558 IN COMPLEXES WITH SUBSTRATE AND SUBSTRATE ANALOGS, GLYCOSYLATION AT ASN-80 AND ASN-437, ACTIVE SITE, ENZYME REGULATION.
  23. "Crystallographic snapshots of nonaged and aged conjugates of soman with acetylcholinesterase, and of a ternary complex of the aged conjugate with pralidoxime."
    Sanson B., Nachon F., Colletier J.P., Froment M.T., Toker L., Greenblatt H.M., Sussman J.L., Ashani Y., Masson P., Silman I., Weik M.
    J. Med. Chem. 52:7593-7603(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-558 IN COMPLEX WITH SOMAN, ACTIVE SITE, DISULFIDE BONDS.
  24. "Probing Torpedo californica acetylcholinesterase catalytic gorge with two novel bis-functional galanthamine derivatives."
    Bartolucci C., Haller L.A., Jordis U., Fels G., Lamba D.
    J. Med. Chem. 53:745-751(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 23-556 IN COMPLEX WITH GALANTHAMINE DERIVATIVES.

Entry informationi

Entry nameiACES_TORCA
AccessioniPrimary (citable) accession number: P04058
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: June 1, 1994
Last modified: October 29, 2014
This is version 134 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

External Data

Dasty 3