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P04058

- ACES_TORCA

UniProt

P04058 - ACES_TORCA

Protein

Acetylcholinesterase

Gene

ache

Organism
Torpedo californica (Pacific electric ray)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Keywords - Biological processi

    Neurotransmitter degradation

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16823.

    Protein family/group databases

    MEROPSiS09.979.

    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-SubCell
    4. synapse Source: UniProtKB-SubCell

    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

    MNLLVTSSLG VLLHLVVLCQ ADDHSELLVN TKSGKVMGTR VPVLSSHISA    50
    FLGIPFAEPP VGNMRFRRPE PKKPWSGVWN ASTYPNNCQQ YVDEQFPGFS 100
    GSEMWNPNRE MSEDCLYLNI WVPSPRPKST TVMVWIYGGG FYSGSSTLDV 150
    YNGKYLAYTE EVVLVSLSYR VGAFGFLALH GSQEAPGNVG LLDQRMALQW 200
    VHDNIQFFGG DPKTVTIFGE SAGGASVGMH ILSPGSRDLF RRAILQSGSP 250
    NCPWASVSVA EGRRRAVELG RNLNCNLNSD EELIHCLREK KPQELIDVEW 300
    NVLPFDSIFR FSFVPVIDGE FFPTSLESML NSGNFKKTQI LLGVNKDEGS 350
    FFLLYGAPGF SKDSESKISR EDFMSGVKLS VPHANDLGLD AVTLQYTDWM 400
    DDNNGIKNRD GLDDIVGDHN VICPLMHFVN KYTKFGNGTY LYFFNHRASN 450
    LVWPEWMGVI HGYEIEFVFG LPLVKELNYT AEEEALSRRI MHYWATFAKT 500
    GNPNEPHSQE SKWPLFTTKE QKFIDLNTEP MKVHQRLRVQ MCVFWNQFLP 550
    KLLNATACDG ELSSSGTSSS KGIIFYVLFS ILYLIF 586

    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.
    DrugBanki DB00674. Galantamine.

    Protein family/group databases

    MEROPSi S09.979.

    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 1, 2014
    This is version 133 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