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Q29499

- ACES_RABIT

UniProt

Q29499 - ACES_RABIT

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Protein

Acetylcholinesterase

Gene

ACHE

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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 sitei204 – 2041Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei335 – 3351Charge relay systemBy similarity
Active sitei448 – 4481Charge relay systemBy similarity

GO - Molecular functioni

  1. acetylcholinesterase activity Source: UniProtKB-EC

GO - Biological processi

  1. neurotransmitter catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei‹1 – 1›1Sequence Analysis
Chaini2 – 584583AcetylcholinesterasePRO_0000008589Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi70 ↔ 97By similarity
Disulfide bondi258 ↔ 273By similarity
Glycosylationi266 – 2661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi351 – 3511N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi410 ↔ 530By similarity
Glycosylationi465 – 4651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi581 – 581InterchainBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotetramer; composed of disulfide-linked homodimers. Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ29499.
SMRiQ29499. Positions 6-578.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG008839.
InParanoidiQ29499.

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]

Sequencei

Sequence statusi: Fragment.

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

Q29499-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
AEGREDPELL VTVRGGRLRG LRLKAPGGPV SAFLGIPFEE PPVGPRRFLP
60 70 80 90 100
PEPKRPWAGV LDATAFQSVC YQYVDTLYPG FEGTEMWNPN RELSEDCLYL
110 120 130 140 150
NVWTPYPRPT SPTPVLVWIY GGGFYSGASS LDVYYGRFLV QAEGTVLVAM
160 170 180 190 200
NYRVGAFGFT CLPGSREAPG NVGLLDQRLA LQWVQENVAA FGGDPASVTL
210 220 230 240 250
FGESAGAASV GLHLLSPPSR GLFHRAVLQS GAPNGPWATV GVGEARRRAT
260 270 280 290 300
LLARLVVCPP GGAGGNDTEL VACLRTRPAQ DLVDHEWRVL PQESIFRFSF
310 320 330 340 350
VPVVDGDFLS DTPEALINAG DFQGLQVLVG VVKDEGTYFL VYGAPGFSKD
360 370 380 390 400
NESFISRAQF LAGVRVGVPQ ASDLAAEAVV LHYTDWLHPE DPARLRDALS
410 420 430 440 450
DVVGDHNVVC PVAQLAGRLA AQGARVYAYV FEHRASTLSW PLWMGVPHGY
460 470 480 490 500
EIEFIFGLPL EPSLNYTEEE RIFAQRLMRY WANFARTGDP NEPRDAKAPQ
510 520 530 540 550
WPPYTAGAQQ YVSLNLRPLE VRRGLRAQAC AFWNRFLPKL LSATDTLDEA
560 570 580
ERQWKAEFHR WSSYMVHWKN QFDHYSKQDR CSDL
Length:584
Mass (Da):64,630
Last modified:November 1, 1997 - v1
Checksum:i2AE157F3063649FE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U05036 mRNA. Translation: AAA53235.1.
PIRiS48724.
UniGeneiOcu.2012.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U05036 mRNA. Translation: AAA53235.1 .
PIRi S48724.
UniGenei Ocu.2012.

3D structure databases

ProteinModelPortali Q29499.
SMRi Q29499. Positions 6-578.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S09.979.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG008839.
InParanoidi Q29499.

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

  1. "Acetylcholinesterase and butyrylcholinesterase expression in adult rabbit tissues and during development."
    Jbilo O., L'Hermite Y., Talesa V., Toutant J.-P., Chatonnet A.
    Eur. J. Biochem. 225:115-124(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Muscle.

Entry informationi

Entry nameiACES_RABIT
AccessioniPrimary (citable) accession number: Q29499
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Synapses usually contain asymmetric molecules of cholinesterase, with a collagen-like part disulfide-bonded to the catalytic part. A different, globular type of cholinesterase occurs on the outer surfaces of cell membranes, including those of erythrocytes.
This is the catalytic subunit of an asymmetric or soluble form of ACHE.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3