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UniProtKB - P04058 (ACES_TETCF)

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Protein

Acetylcholinesterase

Gene

ache

Organism
Tetronarce californica (Pacific electric ray) (Torpedo californica)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.

Enzyme regulationi

Inhibited by substrate concentrations above 0.5 mM.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei221Acyl-ester intermediate1
Active sitei348Charge relay system1
Active sitei461Charge relay system1

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionHydrolase, Serine esterase
Biological processNeurotransmitter degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16823
BRENDAi3.1.1.7 6395

Protein family/group databases

ESTHERitorca-ACHE AChE
MEROPSiS09.980

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylcholinesterase (EC:3.1.1.7)
Short name:
AChE
Gene namesi
Name:ache
OrganismiTetronarce californica (Pacific electric ray) (Torpedo californica)
Taxonomic identifieri7787 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Batoidea › Torpediniformes › Torpedinidae › Tetronarce

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi220E → H: Loss of activity. 1 Publication1
Mutagenesisi220E → Q or D: Decrease in activity. 1 Publication1
Mutagenesisi221S → C: Loss of activity. 1 Publication1
Mutagenesisi221S → V: Loss of activity. 1 Publication1
Mutagenesisi446H → Q: Almost no loss of activity. 1 Publication1
Mutagenesisi461H → Q: Loss of activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4780

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 211 PublicationAdd BLAST21
ChainiPRO_000000859522 – 564AcetylcholinesteraseAdd BLAST543
PropeptideiPRO_0000008596565 – 586Removed in mature formAdd BLAST22

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi80N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi88 ↔ 115
Disulfide bondi275 ↔ 286
Disulfide bondi423 ↔ 542
Glycosylationi437N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi478N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi554N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi558Interchain
Lipidationi564GPI-anchor amidated serine1 Publication1

Post-translational modificationi

An interchain disulfide bond is present in what becomes position 593 of the T isoform.

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

PTM databases

iPTMnetiP04058

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.11 Publications

Protein-protein interaction databases

IntActiP04058, 1 interactor
MINTiP04058

Chemistry databases

BindingDBiP04058

Structurei

Secondary structure

1586
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi27 – 31Combined sources5
Beta strandi34 – 37Combined sources4
Beta strandi39 – 43Combined sources5
Beta strandi46 – 55Combined sources10
Helixi62 – 64Combined sources3
Beta strandi76 – 80Combined sources5
Beta strandi87 – 89Combined sources3
Beta strandi95 – 98Combined sources4
Helixi100 – 103Combined sources4
Beta strandi111 – 113Combined sources3
Beta strandi117 – 122Combined sources6
Beta strandi128 – 136Combined sources9
Turni140 – 142Combined sources3
Helixi149 – 151Combined sources3
Helixi154 – 160Combined sources7
Beta strandi163 – 166Combined sources4
Helixi172 – 176Combined sources5
Beta strandi183 – 187Combined sources5
Helixi189 – 204Combined sources16
Helixi205 – 208Combined sources4
Beta strandi210 – 220Combined sources11
Helixi222 – 232Combined sources11
Turni234 – 236Combined sources3
Helixi237 – 239Combined sources3
Beta strandi241 – 247Combined sources7
Turni253 – 255Combined sources3
Helixi259 – 272Combined sources14
Helixi280 – 289Combined sources10
Helixi292 – 298Combined sources7
Helixi299 – 302Combined sources4
Beta strandi304 – 306Combined sources3
Beta strandi307 – 309Combined sources3
Beta strandi319 – 324Combined sources6
Helixi326 – 332Combined sources7
Beta strandi340 – 345Combined sources6
Beta strandi347 – 349Combined sources3
Helixi350 – 356Combined sources7
Beta strandi362 – 364Combined sources3
Helixi370 – 380Combined sources11
Helixi386 – 396Combined sources11
Beta strandi401 – 403Combined sources3
Helixi405 – 420Combined sources16
Helixi422 – 435Combined sources14
Beta strandi439 – 444Combined sources6
Helixi455 – 457Combined sources3
Turni461 – 464Combined sources4
Helixi465 – 468Combined sources4
Helixi471 – 473Combined sources3
Helixi475 – 477Combined sources3
Helixi481 – 500Combined sources20
Beta strandi501 – 504Combined sources4
Turni518 – 520Combined sources3
Beta strandi522 – 529Combined sources8
Beta strandi533 – 536Combined sources4
Helixi539 – 546Combined sources8
Helixi548 – 555Combined sources8

3D structure databases

ProteinModelPortaliP04058
SMRiP04058
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04058

Family & Domainsi

Sequence similaritiesi

Belongs to the type-B carboxylesterase/lipase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG008839

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR000908 Acylcholinesterase_fish/snake
IPR002018 CarbesteraseB
IPR019826 Carboxylesterase_B_AS
IPR019819 Carboxylesterase_B_CS
IPR000997 Cholinesterase
PfamiView protein in Pfam
PF00135 COesterase, 1 hit
PRINTSiPR00879 ACHEFISH
PR00878 CHOLNESTRASE
SUPFAMiSSF53474 SSF53474, 1 hit
PROSITEiView protein in PROSITE
PS00122 CARBOXYLESTERASE_B_1, 1 hit
PS00941 CARBOXYLESTERASE_B_2, 1 hit

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

Note: Additional isoforms seem to exist.
Isoform H (identifier: P04058-1) [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

        10         20         30         40         50
MNLLVTSSLG VLLHLVVLCQ ADDHSELLVN TKSGKVMGTR VPVLSSHISA 
        60         70         80         90        100
FLGIPFAEPP VGNMRFRRPE PKKPWSGVWN ASTYPNNCQQ YVDEQFPGFS 
       110        120        130        140        150
GSEMWNPNRE MSEDCLYLNI WVPSPRPKST TVMVWIYGGG FYSGSSTLDV 
       160        170        180        190        200
YNGKYLAYTE EVVLVSLSYR VGAFGFLALH GSQEAPGNVG LLDQRMALQW 
       210        220        230        240        250
VHDNIQFFGG DPKTVTIFGE SAGGASVGMH ILSPGSRDLF RRAILQSGSP 
       260        270        280        290        300
NCPWASVSVA EGRRRAVELG RNLNCNLNSD EELIHCLREK KPQELIDVEW 
       310        320        330        340        350
NVLPFDSIFR FSFVPVIDGE FFPTSLESML NSGNFKKTQI LLGVNKDEGS 
       360        370        380        390        400
FFLLYGAPGF SKDSESKISR EDFMSGVKLS VPHANDLGLD AVTLQYTDWM 
       410        420        430        440        450
DDNNGIKNRD GLDDIVGDHN VICPLMHFVN KYTKFGNGTY LYFFNHRASN 
       460        470        480        490        500
LVWPEWMGVI HGYEIEFVFG LPLVKELNYT AEEEALSRRI MHYWATFAKT 
       510        520        530        540        550
GNPNEPHSQE SKWPLFTTKE QKFIDLNTEP MKVHQRLRVQ MCVFWNQFLP 
       560        570        580 
KLLNATACDG ELSSSGTSSS KGIIFYVLFS ILYLIF
Note: GPI-anchored form.
Length:586
Mass (Da):65,906
Last modified:June 1, 1994 - v2
Checksum:i731D5F0F3ABA62A8
GO
Isoform T (identifier: P04058-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     557-586: ACDGELSSSGTSSSKGIIFYVLFSILYLIF → ETIDEAERQWKTEFHRWSSYMMHWKNQFDHYSRHESCAEL

Show »
Length:596
Mass (Da):67,818
Checksum:i36D5E9A30F9E6065
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_001460557 – 586ACDGE…LYLIF → ETIDEAERQWKTEFHRWSSY MMHWKNQFDHYSRHESCAEL in isoform T. CuratedAdd BLAST30

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03439 mRNA Translation: CAA27169.1
X56516 Genomic DNA No translation available.
X56517 Genomic DNA No translation available.
PIRiA00773 ACRYE

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiACES_TETCF
AccessioniPrimary (citable) accession number: P04058
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: June 1, 1994
Last modified: July 18, 2018
This is version 160 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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