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P23795 (ACES_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetylcholinesterase

Short name=AChE
EC=3.1.1.7
Gene names
Name:ACHE
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length613 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 structure

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 junctionsynapse. Secreted. Cell membrane; Peripheral membrane protein By similarity.

Isoform H: Cell membrane; Lipid-anchorGPI-anchor; Extracellular side.

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
   Biological processNeurotransmitter degradation
   Cellular componentCell junction
Cell membrane
Membrane
Secreted
Synapse
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionHydrolase
Serine esterase
   PTMDisulfide bond
Glycoprotein
GPI-anchor
Lipoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcholine metabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

neurotransmitter catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of axonogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of dendrite morphogenesis

Inferred from Biological aspect of Ancestor. Source: RefGenome

synapse assembly

Inferred from Biological aspect of Ancestor. Source: RefGenome

synaptic transmission, cholinergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

axon

Inferred from Biological aspect of Ancestor. Source: RefGenome

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface

Inferred from Biological aspect of Ancestor. Source: RefGenome

dendrite

Inferred from Biological aspect of Ancestor. Source: RefGenome

endoplasmic reticulum lumen

Inferred from Biological aspect of Ancestor. Source: RefGenome

extracellular space

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuromuscular junction

Inferred from Biological aspect of Ancestor. Source: RefGenome

postsynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

presynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionacetylcholinesterase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

beta-amyloid binding

Inferred from direct assay PubMed 9547230. Source: HGNC

cholinesterase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform T (identifier: P23795-1)

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.
Isoform H (identifier: P23795-2)

The sequence of this isoform differs from the canonical sequence as follows:
     574-613: DTLDEAERQW...YSKQDRCSDL → ASEAPCTCSG...LFLLSRLLRL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Ref.3
Chain31 – 613583Acetylcholinesterase
PRO_0000008585

Sites

Active site2331Acyl-ester intermediate By similarity
Active site3641Charge relay system By similarity
Active site4771Charge relay system By similarity

Amino acid modifications

Glycosylation911N-linked (GlcNAc...) Probable
Glycosylation2951N-linked (GlcNAc...) Probable
Glycosylation3801N-linked (GlcNAc...) Probable
Glycosylation4941N-linked (GlcNAc...) Probable
Disulfide bond99 ↔ 126 By similarity
Disulfide bond287 ↔ 302 By similarity
Disulfide bond439 ↔ 559 By similarity
Disulfide bond610Interchain By similarity

Natural variations

Alternative sequence574 – 61340DTLDE…RCSDL → ASEAPCTCSGPAHGEAAPRP RPGLPLPLLLLLFLLSRLLR L in isoform H.
VSP_001455

Experimental info

Sequence conflict241I → L in AAI23899. Ref.2
Sequence conflict461R → E AA sequence Ref.3
Sequence conflict1691T → V AA sequence Ref.3
Sequence conflict2121W → S AA sequence Ref.3
Sequence conflict3231S → H AA sequence Ref.3
Sequence conflict3521H → V AA sequence Ref.3
Sequence conflict4241L → W AA sequence Ref.3
Sequence conflict5241D → A AA sequence Ref.3
Sequence conflict549 – 5546EVRRGL → GVPQAS AA sequence Ref.3
Sequence conflict5711S → N AA sequence Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform T [UniParc].

Last modified July 11, 2001. Version 2.
Checksum: 698D4F0DF8624B12

FASTA61367,664
        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 

« Hide

Isoform H [UniParc].

Checksum: 444F4D6D0EDFDAE3
Show »

FASTA61466,908

References

« Hide 'large scale' references
[1]"Bovine acetylcholinesterase: cloning, expression and characterization."
Mendelson I., Kronman C., Ariel N., Shafferman A., Velan B.
Biochem. J. 334:251-259(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Tissue: Kidney.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM T).
Strain: Hereford.
Tissue: Basal ganglia.
[3]"Complete amino acid sequence of fetal bovine serum acetylcholinesterase and its comparison in various regions with other cholinesterases."
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.
FEBS Lett. 266:123-127(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 31-613 (ISOFORM H).
Tissue: Fetal serum.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF061815, AF061813, AF061814 Genomic DNA. Translation: AAC64270.1.
BC123898 mRNA. Translation: AAI23899.1.
RefSeqNP_001069688.1. NM_001076220.1.
UniGeneBt.1299.

3D structure databases

ProteinModelPortalP23795.
SMRP23795. Positions 35-607.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP23795.
ChEMBLCHEMBL4768.

Protein family/group databases

MEROPSS09.979.

PTM databases

UniCarbKBP23795.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000001512; ENSBTAP00000001512; ENSBTAG00000001139.
GeneID540446.
KEGGbta:540446.

Organism-specific databases

CTD43.

Phylogenomic databases

eggNOGCOG2272.
GeneTreeENSGT00740000115241.
HOGENOMHOG000091866.
HOVERGENHBG008839.
InParanoidP23795.
KOK01049.
OrthoDBEOG789C9R.

Family and domain databases

InterProIPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]
PfamPF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view]
PRINTSPR00878. CHOLNESTRASE.
ProDomPD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20878642.

Entry information

Entry nameACES_BOVIN
AccessionPrimary (citable) accession number: P23795
Secondary accession number(s): O97579, Q08D79
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: July 11, 2001
Last modified: April 16, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families