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Q29499

- ACES_RABIT

UniProt

Q29499 - ACES_RABIT

Protein

Acetylcholinesterase

Gene

ACHE

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 71 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      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 sitei204 – 2041Acyl-ester intermediatePROSITE-ProRule annotation
    Active sitei335 – 3351Charge relay systemBy similarity
    Active sitei448 – 4481Charge 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

    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
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    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
    Signal peptidei‹1 – 1›1Sequence Analysis
    Chaini2 – 584583AcetylcholinesterasePRO_0000008589Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi70 ↔ 97By similarity
    Disulfide bondi258 ↔ 273By similarity
    Glycosylationi266 – 2661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi351 – 3511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi410 ↔ 530By similarity
    Glycosylationi465 – 4651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi581 – 581InterchainBy similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homotetramer; composed of disulfide-linked homodimers. Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ29499.
    SMRiQ29499. Positions 6-578.
    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.
    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]
    PRINTSiPR00878. 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]

    Sequencei

    Sequence statusi: Fragment.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q29499-1 [UniParc]FASTAAdd to Basket

    « Hide

    AEGREDPELL VTVRGGRLRG LRLKAPGGPV SAFLGIPFEE PPVGPRRFLP    50
    PEPKRPWAGV LDATAFQSVC YQYVDTLYPG FEGTEMWNPN RELSEDCLYL 100
    NVWTPYPRPT SPTPVLVWIY GGGFYSGASS LDVYYGRFLV QAEGTVLVAM 150
    NYRVGAFGFT CLPGSREAPG NVGLLDQRLA LQWVQENVAA FGGDPASVTL 200
    FGESAGAASV GLHLLSPPSR GLFHRAVLQS GAPNGPWATV GVGEARRRAT 250
    LLARLVVCPP GGAGGNDTEL VACLRTRPAQ DLVDHEWRVL PQESIFRFSF 300
    VPVVDGDFLS DTPEALINAG DFQGLQVLVG VVKDEGTYFL VYGAPGFSKD 350
    NESFISRAQF LAGVRVGVPQ ASDLAAEAVV LHYTDWLHPE DPARLRDALS 400
    DVVGDHNVVC PVAQLAGRLA AQGARVYAYV FEHRASTLSW PLWMGVPHGY 450
    EIEFIFGLPL EPSLNYTEEE RIFAQRLMRY WANFARTGDP NEPRDAKAPQ 500
    WPPYTAGAQQ YVSLNLRPLE VRRGLRAQAC AFWNRFLPKL LSATDTLDEA 550
    ERQWKAEFHR WSSYMVHWKN QFDHYSKQDR CSDL 584
    Length:584
    Mass (Da):64,630
    Last modified:November 1, 1997 - v1
    Checksum:i2AE157F3063649FE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05036 mRNA. Translation: AAA53235.1.
    PIRiS48724.
    UniGeneiOcu.2012.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05036 mRNA. Translation: AAA53235.1 .
    PIRi S48724.
    UniGenei Ocu.2012.

    3D structure databases

    ProteinModelPortali Q29499.
    SMRi Q29499. Positions 6-578.
    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.
    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 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. "Acetylcholinesterase and butyrylcholinesterase expression in adult rabbit tissues and during development."
      Jbilo O., L'Hermite Y., Talesa V., Toutant J.-P., Chatonnet A.
      Eur. J. Biochem. 225:115-124(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Muscle.

    Entry informationi

    Entry nameiACES_RABIT
    AccessioniPrimary (citable) accession number: Q29499
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 71 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Synapses usually contain asymmetric molecules of cholinesterase, with a collagen-like part disulfide-bonded to the catalytic part. A different, globular type of cholinesterase occurs on the outer surfaces of cell membranes, including those of erythrocytes.
    This is the catalytic subunit of an asymmetric or soluble form of ACHE.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3