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P23795

- ACES_BOVIN

UniProt

P23795 - ACES_BOVIN

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Protein

Acetylcholinesterase

Gene

ACHE

Organism
Bos taurus (Bovine)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei233 – 2331Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei364 – 3641Charge relay systemBy similarity
Active sitei477 – 4771Charge relay systemBy similarity

GO - Molecular functioni

  1. acetylcholinesterase activity Source: RefGenome
  2. beta-amyloid binding Source: HGNC
  3. cholinesterase activity Source: RefGenome

GO - Biological processi

  1. choline metabolic process Source: RefGenome
  2. neurotransmitter catabolic process Source: UniProtKB-KW
  3. regulation of axonogenesis Source: RefGenome
  4. regulation of dendrite morphogenesis Source: RefGenome
  5. synapse assembly Source: RefGenome
  6. synaptic transmission, cholinergic Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Neurotransmitter degradation

Enzyme and pathway databases

ReactomeiREACT_223134. Neurotransmitter Clearance In The Synaptic Cleft.
REACT_223586. Synthesis of PC.

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 25

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. axon Source: RefGenome
  3. cell junction Source: UniProtKB-KW
  4. cell surface Source: RefGenome
  5. dendrite Source: RefGenome
  6. endoplasmic reticulum lumen Source: RefGenome
  7. extracellular space Source: RefGenome
  8. neuromuscular junction Source: RefGenome
  9. postsynaptic membrane Source: RefGenome
  10. presynaptic membrane Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Secreted, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Add
BLAST
Chaini31 – 613583AcetylcholinesterasePRO_0000008585Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi91 – 911N-linked (GlcNAc...)Curated
Disulfide bondi99 ↔ 126By similarity
Disulfide bondi287 ↔ 302By similarity
Glycosylationi295 – 2951N-linked (GlcNAc...)Curated
Glycosylationi380 – 3801N-linked (GlcNAc...)Curated
Disulfide bondi439 ↔ 559By similarity
Glycosylationi494 – 4941N-linked (GlcNAc...)Curated
Disulfide bondi610 – 610InterchainBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

PTM databases

UniCarbKBiP23795.

Expressioni

Gene expression databases

ExpressionAtlasiP23795. baseline.

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

Structurei

3D structure databases

ProteinModelPortaliP23795.
SMRiP23795. Positions 35-607.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2272.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiP23795.
KOiK01049.
OrthoDBiEOG789C9R.

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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241I → L in AAI23899. 1 PublicationCurated
Sequence conflicti46 – 461R → E AA sequence (PubMed:2365060)Curated
Sequence conflicti169 – 1691T → V AA sequence (PubMed:2365060)Curated
Sequence conflicti212 – 2121W → S AA sequence (PubMed:2365060)Curated
Sequence conflicti323 – 3231S → H AA sequence (PubMed:2365060)Curated
Sequence conflicti352 – 3521H → V AA sequence (PubMed:2365060)Curated
Sequence conflicti424 – 4241L → W AA sequence (PubMed:2365060)Curated
Sequence conflicti524 – 5241D → A AA sequence (PubMed:2365060)Curated
Sequence conflicti549 – 5546EVRRGL → GVPQAS AA sequence (PubMed:2365060)Curated
Sequence conflicti571 – 5711S → N AA sequence (PubMed:2365060)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei574 – 61340DTLDE…RCSDL → ASEAPCTCSGPAHGEAAPRP RPGLPLPLLLLLFLLSRLLR L in isoform H. CuratedVSP_001455Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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

EnsembliENSBTAT00000001512; ENSBTAP00000001512; ENSBTAG00000001139.
GeneIDi540446.
KEGGibta:540446.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF061815 , AF061813 , AF061814 Genomic DNA. Translation: AAC64270.1 .
BC123898 mRNA. Translation: AAI23899.1 .
RefSeqi NP_001069688.1. NM_001076220.1.
UniGenei Bt.1299.

3D structure databases

ProteinModelPortali P23795.
SMRi P23795. Positions 35-607.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P23795.
ChEMBLi CHEMBL4768.

Protein family/group databases

MEROPSi S09.979.

PTM databases

UniCarbKBi P23795.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000001512 ; ENSBTAP00000001512 ; ENSBTAG00000001139 .
GeneIDi 540446.
KEGGi bta:540446.

Organism-specific databases

CTDi 43.

Phylogenomic databases

eggNOGi COG2272.
GeneTreei ENSGT00760000118946.
HOGENOMi HOG000091866.
HOVERGENi HBG008839.
InParanoidi P23795.
KOi K01049.
OrthoDBi EOG789C9R.

Enzyme and pathway databases

Reactomei REACT_223134. Neurotransmitter Clearance In The Synaptic Cleft.
REACT_223586. Synthesis of PC.

Miscellaneous databases

NextBioi 20878642.

Gene expression databases

ExpressionAtlasi P23795. baseline.

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

« Hide 'large scale' publications
  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.

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 29, 2014
This is version 108 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

External Data

Dasty 3