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Q92035

- ACES_BUNFA

UniProt

Q92035 - ACES_BUNFA

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Protein

Acetylcholinesterase

Gene

ACHE

Organism
Bungarus fasciatus (Banded krait)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

In muscle, it terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. In liver, its function is unclear: it could serve as a safeguard against any diffusion of acetylcholine from synapses into the circulation. In venom, its toxic role is unclear: It could result in less musculatory control by rapidly hydrolyzing acetylcholine, or that it works synergistically with alkaline phosphatase (ALP) in paralyzing prey through hypotension.

Catalytic activityi

Acetylcholine + H2O = choline + acetate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei231 – 2311Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei358 – 3581Charge relay systemBy similarity
Active sitei471 – 4711Charge relay systemBy similarity

GO - Molecular functioni

  1. acetylcholinesterase activity Source: UniProtKB-EC

GO - Biological processi

  1. acetylcholine catabolic process in synaptic cleft Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase, Toxin

Keywords - Biological processi

Neurotransmitter degradation

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
OrganismiBungarus fasciatus (Banded krait)
Taxonomic identifieri8613 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeBungarinaeBungarus

Subcellular locationi

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. extracellular region Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-KW
  4. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Secreted, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi101 – 1011M → Y: Increases peripheral site ligand binding.
Mutagenesisi316 – 3161K → D: Increases peripheral site ligand binding.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Chaini29 – 606578AcetylcholinesterasePRO_0000008592Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi98 ↔ 125By similarity
Disulfide bondi285 ↔ 296By similarity
Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi433 ↔ 552By similarity
Glycosylationi484 – 4841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi564 – 5641N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi603 – 603Interchain; in isoform TBy similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Liver and muscle contain both isoform T and isoform S. Venom gland predominantly contains isoform S.1 Publication

Interactioni

Subunit structurei

Isoform S is monomeric. Isoform T can form oligomers, including collagen-tailed forms.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ92035.
SMRiQ92035. Positions 36-600.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG008839.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR014788. AChE_tetra.
IPR000908. Acylcholinesterase_fish/snake.
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]
PRINTSiPR00879. ACHEFISH.
PR00878. 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: Q92035-2) [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
MPSCQPGKMP APWPWWLQLL LCIPSCVAVL PGRAGELKVS TQTGSVRGLS
60 70 80 90 100
LPVLDGHVSA FLGIPFAEPP LGRMRFLRPE PVKPWQHVLD ATSYKPACYQ
110 120 130 140 150
MVDTSYPGFQ GTEMWNPNRG MSEDCLYLNI WVPSPRPKDA PVLVWIYGGG
160 170 180 190 200
FYSGAASLDV YDGRFLTYTQ NVILVSLSYR VGAFGFLGLP GSPEAPGNMG
210 220 230 240 250
LLDQRLALQW IQNNIHPFGG NPRAVTVFGE SAGAASVGMH LLSTQSRTLF
260 270 280 290 300
QRAILQSGGP NAPWATVTPA ESRGRAALLG KQLGCHFNND SELVSCLRSK
310 320 330 340 350
NPQELIDEEW SVLPYKSIFR FPFVPVIDGD FFPDTPEAML SSGNFKETQV
360 370 380 390 400
LLGVVKDEGS YFLIYGLPGF SKDNESLISR ADFLEGVRMS VPHANDIATD
410 420 430 440 450
AVVLQYTDWQ DQDNREKNRE ALDDIVGDHN VICPVVQFAN DYAKRNSKVY
460 470 480 490 500
AYLFDHRASN LLWPPWMGVP HGYEIEFVFG LPLNDSLNYT PQEKELSRRM
510 520 530 540 550
MRYWANFART GNPTDPADKS GAWPTYTASQ PQYVQLNTQP LATQPSLRAQ
560 570 580 590 600
ICAFWNHFLP KLLNATDNIE EAERQWKLEF HLWSAYMMHW KSQFDHYNKQ

DRCSEL
Length:606
Mass (Da):68,074
Last modified:September 19, 2003 - v2
Checksum:iB95998AEEA0E5709
GO
Isoform S (identifier: Q92035-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     567-606: DNIEEAERQWKLEFHLWSAYMMHWKSQFDHYNKQDRCSEL → VDPPRADRRRRSARA

Show »
Length:581
Mass (Da):64,723
Checksum:i436C3CBE457E399F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti268 – 2681T → S AA sequence (PubMed:8674549)Curated
Sequence conflicti350 – 3501V → L AA sequence (PubMed:8674549)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei567 – 60640DNIEE…RCSEL → VDPPRADRRRRSARA in isoform S. 1 PublicationVSP_008215Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54591 mRNA. Translation: AAC59905.1.
AF045238 Genomic DNA. Translation: AAC16420.1.
AF045238 Genomic DNA. Translation: AAC16421.1.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54591 mRNA. Translation: AAC59905.1 .
AF045238 Genomic DNA. Translation: AAC16420.1 .
AF045238 Genomic DNA. Translation: AAC16421.1 .

3D structure databases

ProteinModelPortali Q92035.
SMRi Q92035. Positions 36-600.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S09.979.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG008839.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR014788. AChE_tetra.
IPR000908. Acylcholinesterase_fish/snake.
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 PR00879. ACHEFISH.
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

  1. "Cloning and expression of acetylcholinesterase from Bungarus fasciatus venom. A new type of COOH-terminal domain; involvement of a positively charged residue in the peripheral site."
    Cousin X., Bon S., Duval N., Massoulie J., Bon C.
    J. Biol. Chem. 271:15099-15108(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM S).
    Tissue: Venom gland.
  2. "Identification of a novel type of alternatively spliced exon from the acetylcholinesterase gene of Bungarus fasciatus. Molecular forms of acetylcholinesterase in the snake liver and muscle."
    Cousin X., Bon S., Massoulie J., Bon C.
    J. Biol. Chem. 273:9812-9820(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 512-606 (ISOFORMS S AND T), SUBUNIT, TISSUE SPECIFICITY.
    Tissue: Liver and Muscle.
  3. "Acetylcholinesterase from Bungarus venom: a monomeric species."
    Cousin X., Creminon C., Grassi J., Meflah K., Cornu G., Saliou B., Bon S., Massoulie J., Bon C.
    FEBS Lett. 387:196-200(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 206-220; 253-272; 321-340; 347-372 AND 503-511.
    Tissue: Venom.

Entry informationi

Entry nameiACES_BUNFA
AccessioniPrimary (citable) accession number: Q92035
Secondary accession number(s): O73748, Q10720
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 19, 2003
Last modified: October 29, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-9 is the initiator.Curated

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3