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Q7LZG1

- ACES_NAJOX

UniProt

Q7LZG1 - ACES_NAJOX

Protein

Acetylcholinesterase

Gene

ACHE

Organism
Naja oxiana (Central Asian cobra) (Oxus cobra)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 41 (01 Oct 2014)
      Sequence version 2 (31 May 2011)
      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.

    Catalytic activityi

    Acetylcholine + H2O = choline + acetate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei76 – 761Acyl-ester intermediatePROSITE-ProRule annotation
    Active sitei132 – 1321Charge relay systemBy similarity

    GO - Molecular functioni

    1. acetylcholinesterase activity Source: UniProtKB-EC

    GO - Biological processi

    1. neurotransmitter catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Serine esterase, Toxin

    Keywords - Biological processi

    Neurotransmitter degradation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetylcholinesterase (EC:3.1.1.7)
    Short name:
    AChE
    Gene namesi
    Name:ACHE
    OrganismiNaja oxiana (Central Asian cobra) (Oxus cobra)
    Taxonomic identifieri8657 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeNaja

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›181›181AcetylcholinesterasePRO_0000408518Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.By similarity

    Expressioni

    Tissue specificityi

    Expressed by the venom gland. Is also probably expressed by liver and muscle.

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.40.50.1820. 2 hits.
    InterProiIPR029058. AB_hydrolase.
    IPR002018. CarbesteraseB.
    [Graphical view]
    PfamiPF00135. COesterase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequencei

    Sequence statusi: Fragments.

    Q7LZG1-1 [UniParc]FASTAAdd to Basket

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    SELKVATQTG FVRGLSLPVL AGHVSAHLGV PFAEPFLRPE PVKPGAEMWN    50
    PNLNIWVPSG RVGAFXFLTV TLFGESAGAA SVGMXLLSTQ RAILQSGAPN 100
    APWAQVQPAE SRFPFVPVID GEFFPLGVNK DEGSFGVPGF SKXXESLINQ 150
    AVPHANDIYT DWQDQDNGGL PLTGNPTXPH N 181
    Length:181
    Mass (Da):19,255
    Last modified:May 31, 2011 - v2
    Checksum:i19AB68C1423C4BD2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-adjacent residuesi35 – 362Curated
    Non-adjacent residuesi44 – 452Curated
    Non-adjacent residuesi52 – 532Curated
    Non-adjacent residuesi61 – 622Curated
    Non-adjacent residuesi68 – 692Curated
    Non-adjacent residuesi91 – 922Curated
    Non-adjacent residuesi125 – 1262Curated
    Non-adjacent residuesi135 – 1362Curated
    Non-adjacent residuesi151 – 1522Curated
    Non-adjacent residuesi158 – 1592Curated
    Non-adjacent residuesi168 – 1692Curated
    Non-adjacent residuesi172 – 1732Curated
    Non-terminal residuei181 – 1811

    Sequence databases

    PIRiA39022.
    A41117.

    Cross-referencesi

    Sequence databases

    PIRi A39022.
    A41117.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.50.1820. 2 hits.
    InterProi IPR029058. AB_hydrolase.
    IPR002018. CarbesteraseB.
    [Graphical view ]
    Pfami PF00135. COesterase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The active site and partial sequence of cobra venom acetylcholinesterase."
      Weise C., Kreienkamp H.J., Raba R., Aaviksaar A., Hucho F.
      J. Protein Chem. 9:53-57(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-44 AND 53-181.
      Tissue: Venom.
    2. "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 45-52.
      Tissue: Venom.

    Entry informationi

    Entry nameiACES_NAJOX
    AccessioniPrimary (citable) accession number: Q7LZG1
    Secondary accession number(s): Q7LZ27
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 31, 2011
    Last sequence update: May 31, 2011
    Last modified: October 1, 2014
    This is version 41 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

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3