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UniProtKB/Swiss-Prot entry P23795


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACES_BOVIN
Primary accession number P23795
Secondary accession numbers O97579 Q08D79
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on July 11, 2001 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 65)
Name and origin of the protein
Protein name Acetylcholinesterase [Precursor]
Synonyms AChE
EC 3.1.1.7
Gene name
Name: ACHE
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
TISSUE=Kidney;
PubMed=9693127 [NCBI, ExPASy, EBI, Israel, Japan]
Mendelson I., Kronman C., Ariel N., Shafferman A., Velan B.;
"Bovine acetylcholinesterase: cloning, expression and characterization.";
Biochem. J. 334:251-259(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM T).
STRAIN=Hereford;
TISSUE=Basal ganglia;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 31-613 (ISOFORM H).
TISSUE=Fetal serum;
DOI=10.1016/0014-5793(90)81522-P; PubMed=2365060 [NCBI, ExPASy, EBI, Israel, Japan]
Doctor B.P., Chapman T.C., Christner C.E., Deal C.D., de la Hoz D.M., Gentry M.K., Ogert R.A., Rush R.S., Smyth K.K., Wolfe A.D.;
"Complete amino acid sequence of fetal bovine serum acetylcholinesterase and its comparison in various regions with other cholinesterases.";
FEBS Lett. 266:123-127(1990).
Comments
  • FUNCTION: Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.
  • CATALYTIC ACTIVITY: Acetylcholine + H2O = choline + acetate.
  • SUBUNIT: Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers (By similarity). Isoform H generates GPI-anchored dimers; disulfide linked. Isoform T generates multiple structures, ranging from monomers and dimers to collagen-tailed and hydrophobic-tailed forms, in which catalytic tetramers are associated with anchoring proteins that attach them to the basal lamina or to cell membranes. In the collagen-tailed forms, isoform T subunits are associated with a specific collagen, COLQ, which triggers the formation of isoform T tetramers, from monomers and dimers.
  • SUBCELLULAR LOCATION: Cell junction, synapse. Secreted. Cell membrane; Peripheral membrane protein (By similarity).
  • SUBCELLULAR LOCATION: Isoform H: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    NameT
    Isoform IDP23795-1
    This is the isoform sequence displayed in this entry.
    NameH
    Isoform IDP23795-2
    Features which should be applied to build the isoform sequence: VSP_001455.
  • SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF061815; AAC64270.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF061813; AAC64270.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF061814; AAC64270.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC123898; AAI23899.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001069688.1; -.
UniGene Bt.1299
3D structure databases
HSSP P22303; 1F8U. [HSSP ENTRY / PDB]
ModBase P23795.
Protein family/group databases
MEROPS S09.979; -.
PTM databases
GlycoSuiteDB P23795; -.
Ontologies
GO
GO:0031225; Cellular component: anchored to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0030054; Cellular component: cell junction (inferred from electronic annotation from UniProtKB-KW).
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0045202; Cellular component: synapse (inferred from electronic annotation from UniProtKB-KW).
GO:0003990; Molecular function: acetylcholinesterase activity (inferred from electronic annotation from EC).
GO:0001540; Molecular function: beta-amyloid binding (inferred from direct assay from HGNC).
GO:0004104; Molecular function: cholinesterase activity (inferred from electronic annotation from InterPro).
GO:0042135; Biological process: neurotransmitter catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR014788; AChE_tetra.
IPR002018; CarbesteraseB.
IPR000997; Cholinesterase.
Graphical view of domain structure.
PANTHER PTHR11559; CarbesteraseB; 1.
Pfam PF08674; AChE_tetra; 1.
PF00135; COesterase; 1.
Pfam graphical view of domain structure.
PRINTS PR00878; CHOLNESTRASE.
PROSITE PS00122; CARBOXYLESTERASE_B_1; 1.
PS00941; CARBOXYLESTERASE_B_2; 1.
ProtoNet P23795.
Genome annotation databases
Ensembl ENSBTAG00000001139; Bos taurus. [Contig view]
GeneID 540446; -.
KEGG bta:540446; -.
Phylogenomic databases
HOVERGEN P23795; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Cell junction; Cell membrane; Direct protein sequencing; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane; Neurotransmitter degradation; Secreted; Serine esterase; Signal; Synapse.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    30  30      
CHAIN   31   613  583     Acetylcholinesterase. PRO_0000008585
ACT_SITE   233   233        Acyl-ester intermediate (By similarity). 
ACT_SITE   364   364        Charge relay system (By similarity). 
ACT_SITE   477   477        Charge relay system (By similarity). 
CARBOHYD   91    91        N-linked (GlcNAc...) (Probable). 
CARBOHYD   295   295        N-linked (GlcNAc...) (Probable). 
CARBOHYD   380   380        N-linked (GlcNAc...) (Probable). 
CARBOHYD   494   494        N-linked (GlcNAc...) (Probable). 
DISULFID   99   126        By similarity. 
DISULFID   287   302        By similarity. 
DISULFID   439   559        By similarity. 
DISULFID   610   610        Interchain (By similarity). 
VAR_SEQ   574   613        DTLDEAERQWKAEFHRWSSYMVHWKNQFDHYSKQDRCSDL -> ASEAPCTCSGPAHGEAAPRPRPGLPLPLLLLLFLLS RLLRL (in isoform H). VSP_001455
CONFLICT   24    24        I -> L (in Ref. 2; AAI23899). 
CONFLICT   46    46        R -> E (in Ref. 3; AA sequence). 
CONFLICT   169   169        T -> V (in Ref. 3; AA sequence). 
CONFLICT   212   212        W -> S (in Ref. 3; AA sequence). 
CONFLICT   323   323        S -> H (in Ref. 3; AA sequence). 
CONFLICT   352   352        H -> V (in Ref. 3; AA sequence). 
CONFLICT   424   424        L -> W (in Ref. 3; AA sequence). 
CONFLICT   524   524        D -> A (in Ref. 3; AA sequence). 
CONFLICT   549   554        EVRRGL -> GVPQAS (in Ref. 3; AA sequence). 
CONFLICT   571   571        S -> N (in Ref. 3; AA sequence). 
Sequence information
Length: 613 AA [This is the length of the unprocessed precursor] Molecular weight: 67664 Da [This is the MW of the unprocessed precursor] CRC64: 698D4F0DF8624B12 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRPPWCPLHT PSLTPPLLLL LFLIGGGAEA EGPEDPELLV MVRGGRLRGL RLMAPRGPVS 

        70         80         90        100        110        120 
AFLGIPFAEP PVGPRRFLPP EPKRPWPGVL NATAFQSVCY QYVDTLYPGF EGTEMWNPNR 

       130        140        150        160        170        180 
ELSEDCLYLN VWTPYPRPSS PTPVLVWIYG GGFYSGASSL DVYDGRFLTQ AEGTVLVSMN 

       190        200        210        220        230        240 
YRVGAFGFLA LPGSREAPGN VGLLDQRLAL QWVQENVAAF GGDPTSVTLF GESAGAASVG 

       250        260        270        280        290        300 
MHLLSPPSRG LFHRAVLQSG APNGPWATVG VGEARRRATL LARLVGCPPG GAGGNDTELV 

       310        320        330        340        350        360 
ACLRARPAQD LVDHEWRVLP QESVFRFSFV PVVDGDFLSD TPEALINAGD FHGLQVLVGV 

       370        380        390        400        410        420 
VKDEGSYFLV YGAPGFSKDN ESLISRAQFL AGVRVGVPQA SDLAAEAVVL HYTDWLHPED 

       430        440        450        460        470        480 
PARLREALSD VVGDHNVVCP VAQLAGRLAA QGARVYAYIF EHRASTLSWP LWMGVPHGYE 

       490        500        510        520        530        540 
IEFIFGLPLE PSLNYTIEER TFAQRLMRYW ANFARTGDPN DPRDPKAPQW PPYTAGAQQY 

       550        560        570        580        590        600 
VSLNLRPLEV RRGLRAQACA FWNRFLPKLL SATDTLDEAE RQWKAEFHRW SSYMVHWKNQ 

       610 
FDHYSKQDRC SDL 

P23795 in FASTA format

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