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Protein

Acetylcholinesterase

Gene

ACHE

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
Active sitei233Acyl-ester intermediatePROSITE-ProRule annotation1
Active sitei364Charge relay systemBy similarity1
Active sitei477Charge relay systemBy similarity1

GO - Molecular functioni

  • acetylcholinesterase activity Source: GO_Central
  • beta-amyloid binding Source: HGNC

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Neurotransmitter degradation

Enzyme and pathway databases

BRENDAi3.1.1.7. 908.

Protein family/group databases

ESTHERibovin-ACHE. AChE.
MEROPSiS09.979.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylcholinesterase (EC:3.1.1.7)
Short name:
AChE
Gene namesi
Name:ACHE
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Secreted, Synapse

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4768.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Add BLAST30
ChainiPRO_000000858531 – 613AcetylcholinesteraseAdd BLAST583

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi91N-linked (GlcNAc...)Curated1
Disulfide bondi99 ↔ 126By similarity
Disulfide bondi287 ↔ 302By similarity
Glycosylationi295N-linked (GlcNAc...)Curated1
Glycosylationi380N-linked (GlcNAc...)Curated1
Disulfide bondi439 ↔ 559By similarity
Glycosylationi494N-linked (GlcNAc...)Curated1
Disulfide bondi610InterchainBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP23795.
PRIDEiP23795.

PTM databases

UniCarbKBiP23795.

Expressioni

Gene expression databases

BgeeiENSBTAG00000001139.

Interactioni

Subunit structurei

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.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001517.

Chemistry databases

BindingDBiP23795.

Structurei

3D structure databases

ProteinModelPortaliP23795.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4389. Eukaryota.
COG2272. LUCA.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiP23795.
KOiK01049.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform T (identifier: P23795-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MRPPWCPLHT PSLTPPLLLL LFLIGGGAEA EGPEDPELLV MVRGGRLRGL
60 70 80 90 100
RLMAPRGPVS AFLGIPFAEP PVGPRRFLPP EPKRPWPGVL NATAFQSVCY
110 120 130 140 150
QYVDTLYPGF EGTEMWNPNR ELSEDCLYLN VWTPYPRPSS PTPVLVWIYG
160 170 180 190 200
GGFYSGASSL DVYDGRFLTQ AEGTVLVSMN YRVGAFGFLA LPGSREAPGN
210 220 230 240 250
VGLLDQRLAL QWVQENVAAF GGDPTSVTLF GESAGAASVG MHLLSPPSRG
260 270 280 290 300
LFHRAVLQSG APNGPWATVG VGEARRRATL LARLVGCPPG GAGGNDTELV
310 320 330 340 350
ACLRARPAQD LVDHEWRVLP QESVFRFSFV PVVDGDFLSD TPEALINAGD
360 370 380 390 400
FHGLQVLVGV VKDEGSYFLV YGAPGFSKDN ESLISRAQFL AGVRVGVPQA
410 420 430 440 450
SDLAAEAVVL HYTDWLHPED PARLREALSD VVGDHNVVCP VAQLAGRLAA
460 470 480 490 500
QGARVYAYIF EHRASTLSWP LWMGVPHGYE IEFIFGLPLE PSLNYTIEER
510 520 530 540 550
TFAQRLMRYW ANFARTGDPN DPRDPKAPQW PPYTAGAQQY VSLNLRPLEV
560 570 580 590 600
RRGLRAQACA FWNRFLPKLL SATDTLDEAE RQWKAEFHRW SSYMVHWKNQ
610
FDHYSKQDRC SDL
Length:613
Mass (Da):67,664
Last modified:July 11, 2001 - v2
Checksum:i698D4F0DF8624B12
GO
Isoform H (identifier: P23795-2) [UniParc]FASTAAdd to basket

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

Show »
Length:614
Mass (Da):66,908
Checksum:i444F4D6D0EDFDAE3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti24I → L in AAI23899 (Ref. 2) Curated1
Sequence conflicti46R → E AA sequence (PubMed:2365060).Curated1
Sequence conflicti169T → V AA sequence (PubMed:2365060).Curated1
Sequence conflicti212W → S AA sequence (PubMed:2365060).Curated1
Sequence conflicti323S → H AA sequence (PubMed:2365060).Curated1
Sequence conflicti352H → V AA sequence (PubMed:2365060).Curated1
Sequence conflicti424L → W AA sequence (PubMed:2365060).Curated1
Sequence conflicti524D → A AA sequence (PubMed:2365060).Curated1
Sequence conflicti549 – 554EVRRGL → GVPQAS AA sequence (PubMed:2365060).Curated6
Sequence conflicti571S → N AA sequence (PubMed:2365060).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001455574 – 613DTLDE…RCSDL → ASEAPCTCSGPAHGEAAPRP RPGLPLPLLLLLFLLSRLLR L in isoform H. CuratedAdd BLAST40

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061815, AF061813, AF061814 Genomic DNA. Translation: AAC64270.1.
BC123898 mRNA. Translation: AAI23899.1.
RefSeqiNP_001069688.1. NM_001076220.1.
UniGeneiBt.1299.

Genome annotation databases

GeneIDi540446.
KEGGibta:540446.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061815, AF061813, AF061814 Genomic DNA. Translation: AAC64270.1.
BC123898 mRNA. Translation: AAI23899.1.
RefSeqiNP_001069688.1. NM_001076220.1.
UniGeneiBt.1299.

3D structure databases

ProteinModelPortaliP23795.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000001517.

Chemistry databases

BindingDBiP23795.
ChEMBLiCHEMBL4768.

Protein family/group databases

ESTHERibovin-ACHE. AChE.
MEROPSiS09.979.

PTM databases

UniCarbKBiP23795.

Proteomic databases

PaxDbiP23795.
PRIDEiP23795.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi540446.
KEGGibta:540446.

Organism-specific databases

CTDi43.

Phylogenomic databases

eggNOGiKOG4389. Eukaryota.
COG2272. LUCA.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiP23795.
KOiK01049.

Enzyme and pathway databases

BRENDAi3.1.1.7. 908.

Gene expression databases

BgeeiENSBTAG00000001139.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiACES_BOVIN
AccessioniPrimary (citable) accession number: P23795
Secondary accession number(s): O97579, Q08D79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: July 11, 2001
Last modified: October 5, 2016
This is version 123 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.