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P07692

- ACES_TORMA

UniProt

P07692 - ACES_TORMA

Protein

Acetylcholinesterase

Gene

ache

Organism
Torpedo marmorata (Marbled electric ray)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei224 – 2241Acyl-ester intermediatePROSITE-ProRule annotation
    Active sitei351 – 3511Charge relay systemBy similarity
    Active sitei464 – 4641Charge 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

    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
    OrganismiTorpedo marmorata (Marbled electric ray)
    Taxonomic identifieri7788 [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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24241 PublicationAdd
    BLAST
    Chaini25 – 567543AcetylcholinesterasePRO_0000008597Add
    BLAST
    Propeptidei568 – 59023Removed in mature formPRO_0000008598Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi91 ↔ 118By similarity
    Disulfide bondi278 ↔ 289By similarity
    Disulfide bondi426 ↔ 545By similarity
    Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi481 – 4811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi557 – 5571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi561 – 561Interchain
    Lipidationi567 – 5671GPI-anchor amidated serineBy similarity

    Post-translational modificationi

    An interchain disulfide bond is present in what becomes position 596 of the T isoform.By similarity

    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.2 Publications

    Structurei

    3D structure databases

    ProteinModelPortaliP07692.
    SMRiP07692. Positions 28-560.
    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.
    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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform H (identifier: P07692-1) [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

    MREMNLLVTS SLGVLLHLVV LCQADDDSEL LVNTKSGKVM RTRIPVLSSH    50
    ISAFLGIPFA EPPVGNMRFR RPEPKKPWSG VWNASTYPNN CQQYVDEQFP 100
    GFPGSEMWNP NREMSEDCLY LNIWVPSPRP KSATVMLWIY GGGFYSGSST 150
    LDVYNGKYLA YTEEVVLVSL SYRVGAFGFL ALHGSQEAPG NMGLLDQRMA 200
    LQWVHDNIQF FGGDPKTVTL FGESAGRASV GMHILSPGSR DLFRRAILQS 250
    GSPNCPWASV SVAEGRRRAV ELRRNLNCNL NSDEDLIQCL REKKPQELID 300
    VEWNVLPFDS IFRFSFVPVI DGEFFPTSLE SMLNAGNFKK TQILLGVNKD 350
    EGSFFLLYGA PGFSKDSESK ISREDFMSGV KLSVPHANDL GLDAVTLQYT 400
    DWMDDNNGIK NRDGLDDIVG DHNVICPLMH FVNKYTKFGN GTYLYFFNHR 450
    ASNLVWPEWM GVIHGYEIEF VFGLPLVKEL NYTAEEEALS RRIMHYWATF 500
    AKTGNPNEPH SQESKWPLFT TKEQKFIDLN TEPIKVHQRL RVQMCVFWNQ 550
    FLPKLLNATA CDGELSSSGT SSSKGIIFYV LFSILYLIFY 590

    Note: GPI-anchored form.

    Length:590
    Mass (Da):66,744
    Last modified:June 1, 1994 - v2
    Checksum:i73FAC284C9784F25
    GO
    Isoform T (identifier: P07692-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         560-590: ACDGELSSSGTSSSKGIIFYVLFSILYLIFY → ETIDEAERQWKTEFHRWSSYMMHWKNQFDQYSRHENCAEL

    Show »
    Length:599
    Mass (Da):68,511
    Checksum:i20C387082E8FAF9B
    GO
    Isoform 3 (identifier: P07692-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         560-590: ACDGELSSSGTSSSKGIIFYVLFSILYLIFY → GNVFAFHMQK...RCWESWGRIL

    Show »
    Length:625
    Mass (Da):70,909
    Checksum:i6A277207F667035E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti41 – 411R → G AA sequence (PubMed:3792544)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei560 – 59031ACDGE…YLIFY → GNVFAFHMQKVRTPAKTYHF GVIVAHLLLLSLPTASDVPR LASSKWWAHSDPLCSRRCWE SWGRIL in isoform 3. CuratedVSP_001462Add
    BLAST
    Alternative sequencei560 – 59031ACDGE…YLIFY → ETIDEAERQWKTEFHRWSSY MMHWKNQFDQYSRHENCAEL in isoform T. CuratedVSP_001461Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05497 mRNA. Translation: CAA29047.1.
    X13172 mRNA. Translation: CAA31570.1.
    X13174 mRNA. Translation: CAA31572.1.
    X13173 mRNA. Translation: CAA31571.1.
    PIRiA38868.
    S01293.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05497 mRNA. Translation: CAA29047.1 .
    X13172 mRNA. Translation: CAA31570.1 .
    X13174 mRNA. Translation: CAA31572.1 .
    X13173 mRNA. Translation: CAA31571.1 .
    PIRi A38868.
    S01293.

    3D structure databases

    ProteinModelPortali P07692.
    SMRi P07692. Positions 28-560.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P07692.

    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.
    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. "cDNA sequences of Torpedo marmorata acetylcholinesterase: primary structure of the precursor of a catalytic subunit; existence of multiple 5'-untranslated regions."
      Sikorav J.-L., Krejci E., Massoulie J.
      EMBO J. 6:1865-1873(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Electric organ.
    2. "Identical N-terminal peptide sequences of asymmetric forms and of low-salt-soluble and detergent-soluble amphiphilic dimers of Torpedo acetylcholinesterase. Comparison with bovine acetylcholinesterase."
      Bon S., Chang J.Y., Strosberg A.D.
      FEBS Lett. 209:206-212(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-47.
    3. "Complex alternative splicing of acetylcholinesterase transcripts in Torpedo electric organ; primary structure of the precursor of the glycolipid-anchored dimeric form."
      Sikorav J.-L., Duval N., Anselmet A., Bon S., Krejci E., Legay C., Osterlund M., Reimund B., Massoulie J.
      EMBO J. 7:2983-2993(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING.
      Tissue: Electric organ.
    4. "Molecular architecture of acetylcholinesterase collagen-tailed forms; construction of a glycolipid-tailed tetramer."
      Duval N., Krejci E., Grassi J., Coussen F., Massoulie J., Bon S.
      EMBO J. 11:3255-3261(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNITS INTERACTION.
      Tissue: Electric organ.
    5. "H and T subunits of acetylcholinesterase from Torpedo, expressed in COS cells, generate all types of globular forms."
      Duval N., Massoulie J., Bon S.
      J. Cell Biol. 118:641-653(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNITS INTERACTION, SEQUENCE REVISION TO 421.

    Entry informationi

    Entry nameiACES_TORMA
    AccessioniPrimary (citable) accession number: P07692
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 107 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

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3