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Q92035

- ACES_BUNFA

UniProt

Q92035 - ACES_BUNFA

Protein

Acetylcholinesterase

Gene

ACHE

Organism
Bungarus fasciatus (Banded krait)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 2 (19 Sep 2003)
      Previous versions | rss
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    Functioni

    In muscle, it terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. In liver, its function is unclear: it could serve as a safeguard against any diffusion of acetylcholine from synapses into the circulation. In venom, its toxic role is unclear: It could result in less musculatory control by rapidly hydrolyzing acetylcholine, or that it works synergistically with alkaline phosphatase (ALP) in paralyzing prey through hypotension.

    Catalytic activityi

    Acetylcholine + H2O = choline + acetate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei231 – 2311Acyl-ester intermediatePROSITE-ProRule annotation
    Active sitei358 – 3581Charge relay systemBy similarity
    Active sitei471 – 4711Charge relay systemBy similarity

    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, Toxin

    Keywords - Biological processi

    Neurotransmitter degradation

    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
    OrganismiBungarus fasciatus (Banded krait)
    Taxonomic identifieri8613 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeBungarinaeBungarus

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. extracellular region Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB-SubCell
    4. synapse Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Secreted, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi101 – 1011M → Y: Increases peripheral site ligand binding.
    Mutagenesisi316 – 3161K → D: Increases peripheral site ligand binding.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 606578AcetylcholinesterasePRO_0000008592Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi98 ↔ 125By similarity
    Disulfide bondi285 ↔ 296By similarity
    Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi433 ↔ 552By similarity
    Glycosylationi484 – 4841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi564 – 5641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi603 – 603Interchain; in isoform TBy similarity

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Expressioni

    Tissue specificityi

    Liver and muscle contain both isoform T and isoform S. Venom gland predominantly contains isoform S.1 Publication

    Interactioni

    Subunit structurei

    Isoform S is monomeric. Isoform T can form oligomers, including collagen-tailed forms.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ92035.
    SMRiQ92035. Positions 36-600.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG008839.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR014788. AChE_tetra.
    IPR000908. Acylcholinesterase_fish/snake.
    IPR002018. CarbesteraseB.
    IPR019826. Carboxylesterase_B_AS.
    IPR019819. Carboxylesterase_B_CS.
    IPR000997. Cholinesterase.
    [Graphical view]
    PfamiPF08674. AChE_tetra. 1 hit.
    PF00135. COesterase. 1 hit.
    [Graphical view]
    PRINTSiPR00879. ACHEFISH.
    PR00878. CHOLNESTRASE.
    ProDomiPD415333. AChE_tetra. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    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

    Isoform T (identifier: Q92035-2) [UniParc]FASTAAdd to Basket

    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

    MPSCQPGKMP APWPWWLQLL LCIPSCVAVL PGRAGELKVS TQTGSVRGLS    50
    LPVLDGHVSA FLGIPFAEPP LGRMRFLRPE PVKPWQHVLD ATSYKPACYQ 100
    MVDTSYPGFQ GTEMWNPNRG MSEDCLYLNI WVPSPRPKDA PVLVWIYGGG 150
    FYSGAASLDV YDGRFLTYTQ NVILVSLSYR VGAFGFLGLP GSPEAPGNMG 200
    LLDQRLALQW IQNNIHPFGG NPRAVTVFGE SAGAASVGMH LLSTQSRTLF 250
    QRAILQSGGP NAPWATVTPA ESRGRAALLG KQLGCHFNND SELVSCLRSK 300
    NPQELIDEEW SVLPYKSIFR FPFVPVIDGD FFPDTPEAML SSGNFKETQV 350
    LLGVVKDEGS YFLIYGLPGF SKDNESLISR ADFLEGVRMS VPHANDIATD 400
    AVVLQYTDWQ DQDNREKNRE ALDDIVGDHN VICPVVQFAN DYAKRNSKVY 450
    AYLFDHRASN LLWPPWMGVP HGYEIEFVFG LPLNDSLNYT PQEKELSRRM 500
    MRYWANFART GNPTDPADKS GAWPTYTASQ PQYVQLNTQP LATQPSLRAQ 550
    ICAFWNHFLP KLLNATDNIE EAERQWKLEF HLWSAYMMHW KSQFDHYNKQ 600
    DRCSEL 606
    Length:606
    Mass (Da):68,074
    Last modified:September 19, 2003 - v2
    Checksum:iB95998AEEA0E5709
    GO
    Isoform S (identifier: Q92035-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         567-606: DNIEEAERQWKLEFHLWSAYMMHWKSQFDHYNKQDRCSEL → VDPPRADRRRRSARA

    Show »
    Length:581
    Mass (Da):64,723
    Checksum:i436C3CBE457E399F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti268 – 2681T → S AA sequence (PubMed:8674549)Curated
    Sequence conflicti350 – 3501V → L AA sequence (PubMed:8674549)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei567 – 60640DNIEE…RCSEL → VDPPRADRRRRSARA in isoform S. 1 PublicationVSP_008215Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U54591 mRNA. Translation: AAC59905.1.
    AF045238 Genomic DNA. Translation: AAC16420.1.
    AF045238 Genomic DNA. Translation: AAC16421.1.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U54591 mRNA. Translation: AAC59905.1 .
    AF045238 Genomic DNA. Translation: AAC16420.1 .
    AF045238 Genomic DNA. Translation: AAC16421.1 .

    3D structure databases

    ProteinModelPortali Q92035.
    SMRi Q92035. Positions 36-600.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S09.979.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG008839.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR014788. AChE_tetra.
    IPR000908. Acylcholinesterase_fish/snake.
    IPR002018. CarbesteraseB.
    IPR019826. Carboxylesterase_B_AS.
    IPR019819. Carboxylesterase_B_CS.
    IPR000997. Cholinesterase.
    [Graphical view ]
    Pfami PF08674. AChE_tetra. 1 hit.
    PF00135. COesterase. 1 hit.
    [Graphical view ]
    PRINTSi PR00879. ACHEFISH.
    PR00878. CHOLNESTRASE.
    ProDomi PD415333. AChE_tetra. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    PROSITEi PS00122. CARBOXYLESTERASE_B_1. 1 hit.
    PS00941. CARBOXYLESTERASE_B_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of acetylcholinesterase from Bungarus fasciatus venom. A new type of COOH-terminal domain; involvement of a positively charged residue in the peripheral site."
      Cousin X., Bon S., Duval N., Massoulie J., Bon C.
      J. Biol. Chem. 271:15099-15108(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM S).
      Tissue: Venom gland.
    2. "Identification of a novel type of alternatively spliced exon from the acetylcholinesterase gene of Bungarus fasciatus. Molecular forms of acetylcholinesterase in the snake liver and muscle."
      Cousin X., Bon S., Massoulie J., Bon C.
      J. Biol. Chem. 273:9812-9820(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 512-606 (ISOFORMS S AND T), SUBUNIT, TISSUE SPECIFICITY.
      Tissue: Liver and Muscle.
    3. "Acetylcholinesterase from Bungarus venom: a monomeric species."
      Cousin X., Creminon C., Grassi J., Meflah K., Cornu G., Saliou B., Bon S., Massoulie J., Bon C.
      FEBS Lett. 387:196-200(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 206-220; 253-272; 321-340; 347-372 AND 503-511.
      Tissue: Venom.

    Entry informationi

    Entry nameiACES_BUNFA
    AccessioniPrimary (citable) accession number: Q92035
    Secondary accession number(s): O73748, Q10720
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: September 19, 2003
    Last modified: October 1, 2014
    This is version 83 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    It is uncertain whether Met-1 or Met-9 is the initiator.Curated

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3