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Protein

Acetylcholinesterase

Gene

Ache

Organism
Mus musculus (Mouse)
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 sitei234Acyl-ester intermediate1
Active sitei365Charge relay system1
Active sitei478Charge relay system1

GO - Molecular functioni

  • acetylcholine binding Source: MGI
  • acetylcholinesterase activity Source: MGI
  • cholinesterase activity Source: MGI
  • collagen binding Source: MGI
  • hydrolase activity Source: MGI
  • laminin binding Source: MGI
  • protein homodimerization activity Source: MGI
  • protein self-association Source: MGI
  • serine hydrolase activity Source: MGI

GO - Biological processi

  • acetylcholine catabolic process Source: MGI
  • cell adhesion Source: MGI
  • neurotransmitter receptor biosynthetic process Source: MGI
  • osteoblast development Source: Ensembl
  • protein tetramerization Source: MGI
  • receptor internalization Source: MGI
  • regulation of receptor recycling Source: MGI
  • retina development in camera-type eye Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Keywords - Biological processi

Neurotransmitter degradation

Enzyme and pathway databases

BRENDAi3.1.1.7. 3474.
ReactomeiR-MMU-112311. Neurotransmitter Clearance In The Synaptic Cleft.
R-MMU-1483191. Synthesis of PC.
SABIO-RKP21836.

Protein family/group databases

ESTHERimouse-ACHE. AChE.
MEROPSiS09.979.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylcholinesterase (EC:3.1.1.7)
Short name:
AChE
Gene namesi
Name:Ache
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:87876. Ache.

Subcellular locationi

GO - Cellular componenti

  • anchored component of membrane Source: UniProtKB-KW
  • basal lamina Source: MGI
  • cell junction Source: UniProtKB-KW
  • cell surface Source: MGI
  • extracellular region Source: MGI
  • extracellular space Source: MGI
  • Golgi apparatus Source: MGI
  • membrane Source: MGI
  • neuromuscular junction Source: MGI
  • perinuclear region of cytoplasm Source: MGI
  • plasma membrane Source: MGI
  • synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Secreted, Synapse

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3198.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Add BLAST31
ChainiPRO_000000858832 – 614AcetylcholinesteraseAdd BLAST583

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi100 ↔ 127
Disulfide bondi288 ↔ 303
Glycosylationi296N-linked (GlcNAc...)Sequence analysis1
Glycosylationi381N-linked (GlcNAc...)1
Disulfide bondi440 ↔ 560
Glycosylationi495N-linked (GlcNAc...)1
Disulfide bondi611InterchainBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiP21836.
PRIDEiP21836.

PTM databases

PhosphoSitePlusiP21836.

Expressioni

Tissue specificityi

Predominates in most expressing tissues except erythrocytes where a glycophospholipid-attached form of ACHE predominates.

Gene expression databases

BgeeiENSMUSG00000023328.
CleanExiMM_ACHE.
ExpressionAtlasiP21836. baseline and differential.
GenevisibleiP21836. MM.

Interactioni

Subunit structurei

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). Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers.By similarity2 Publications

GO - Molecular functioni

  • collagen binding Source: MGI
  • laminin binding Source: MGI
  • protein homodimerization activity Source: MGI
  • protein self-association Source: MGI

Protein-protein interaction databases

BioGridi197921. 1 interactor.
IntActiP21836. 2 interactors.
MINTiMINT-1206315.
STRINGi10090.ENSMUSP00000024099.

Chemistry databases

BindingDBiP21836.

Structurei

Secondary structure

1614
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi32 – 34Combined sources3
Helixi37 – 39Combined sources3
Beta strandi40 – 43Combined sources4
Beta strandi46 – 49Combined sources4
Beta strandi51 – 55Combined sources5
Beta strandi58 – 67Combined sources10
Helixi74 – 76Combined sources3
Beta strandi88 – 92Combined sources5
Beta strandi99 – 101Combined sources3
Helixi112 – 115Combined sources4
Beta strandi123 – 125Combined sources3
Beta strandi129 – 137Combined sources9
Beta strandi143 – 149Combined sources7
Turni153 – 155Combined sources3
Helixi162 – 164Combined sources3
Helixi167 – 173Combined sources7
Beta strandi176 – 180Combined sources5
Helixi185 – 189Combined sources5
Beta strandi196 – 198Combined sources3
Helixi202 – 217Combined sources16
Helixi218 – 221Combined sources4
Beta strandi223 – 233Combined sources11
Helixi235 – 244Combined sources10
Helixi247 – 250Combined sources4
Beta strandi254 – 260Combined sources7
Beta strandi263 – 268Combined sources6
Helixi272 – 285Combined sources14
Turni286 – 290Combined sources5
Beta strandi291 – 293Combined sources3
Helixi297 – 306Combined sources10
Helixi309 – 315Combined sources7
Helixi316 – 318Combined sources3
Beta strandi321 – 323Combined sources3
Beta strandi336 – 341Combined sources6
Helixi343 – 349Combined sources7
Beta strandi356 – 362Combined sources7
Turni363 – 366Combined sources4
Helixi367 – 370Combined sources4
Turni371 – 373Combined sources3
Beta strandi379 – 381Combined sources3
Helixi387 – 397Combined sources11
Helixi403 – 413Combined sources11
Beta strandi416 – 418Combined sources3
Helixi422 – 437Combined sources16
Helixi439 – 451Combined sources13
Beta strandi455 – 461Combined sources7
Helixi472 – 474Combined sources3
Turni478 – 481Combined sources4
Helixi482 – 485Combined sources4
Helixi488 – 490Combined sources3
Helixi492 – 494Combined sources3
Helixi498 – 517Combined sources20
Turni523 – 525Combined sources3
Beta strandi526 – 528Combined sources3
Turni536 – 538Combined sources3
Beta strandi540 – 547Combined sources8
Beta strandi550 – 553Combined sources4
Helixi557 – 564Combined sources8
Helixi567 – 570Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C2BX-ray4.50A35-574[»]
1C2OX-ray4.20A/B/C/D36-574[»]
1J06X-ray2.35A/B32-574[»]
1J07X-ray2.35A/B32-574[»]
1KU6X-ray2.50A32-580[»]
1MAAX-ray2.90A/B/C/D32-578[»]
1MAHX-ray3.20A32-574[»]
1N5MX-ray2.20A/B32-572[»]
1N5RX-ray2.25A/B32-574[»]
1Q83X-ray2.65A/B1-580[»]
1Q84X-ray2.45A/B1-580[»]
2C0PX-ray2.50A/B32-574[»]
2C0QX-ray2.50A/B32-574[»]
2GYUX-ray2.20A/B32-574[»]
2GYVX-ray2.50A/B32-574[»]
2GYWX-ray2.40A/B32-574[»]
2H9YX-ray2.40A/B32-574[»]
2HA0X-ray2.20A/B32-574[»]
2HA2X-ray2.05A/B32-574[»]
2HA3X-ray2.25A/B32-574[»]
2HA4X-ray2.56A/B32-574[»]
2HA5X-ray2.15A/B32-574[»]
2HA6X-ray2.25A/B32-574[»]
2HA7X-ray2.66A/B32-574[»]
2JEYX-ray2.70A/B32-574[»]
2JEZX-ray2.60A/B32-574[»]
2JF0X-ray2.50A/B32-574[»]
2JGEX-ray2.60A/B32-574[»]
2JGFX-ray2.50A/B32-574[»]
2JGIX-ray2.90A/B32-574[»]
2JGJX-ray2.50A/B32-574[»]
2JGKX-ray2.90A/B32-574[»]
2JGLX-ray2.60A/B32-574[»]
2JGMX-ray2.90A/B32-574[»]
2WHPX-ray2.20A/B32-573[»]
2WHQX-ray2.15A/B32-574[»]
2WHRX-ray2.54A/B32-574[»]
2WLSX-ray2.60A/B32-574[»]
2WU3X-ray2.70A/B32-574[»]
2WU4X-ray2.40A/B32-574[»]
2XUDX-ray2.65A/B32-574[»]
2XUFX-ray2.55A/B32-575[»]
2XUGX-ray2.60A/B32-575[»]
2XUHX-ray2.65A/B32-574[»]
2XUIX-ray2.60A/B32-574[»]
2XUJX-ray2.65A/B32-574[»]
2XUKX-ray2.75A/B32-574[»]
2XUOX-ray2.80A/B32-574[»]
2XUPX-ray2.70A/B32-574[»]
2XUQX-ray2.70A/B32-574[»]
2Y2UX-ray2.60A/B32-574[»]
2Y2VX-ray2.45A/B32-574[»]
3DL4X-ray2.50A/B32-574[»]
3DL7X-ray2.50A/B32-574[»]
3ZLTX-ray2.60A/B32-574[»]
3ZLUX-ray2.60A/B32-574[»]
3ZLVX-ray2.50A/B32-574[»]
4A16X-ray2.65A/B/C/D35-574[»]
4A23X-ray2.40A/B32-574[»]
4ARAX-ray2.50A/B32-574[»]
4ARBX-ray2.25A/B32-574[»]
4B7ZX-ray2.30A/B32-574[»]
4B80X-ray2.50A/B32-574[»]
4B81X-ray2.80A/B32-574[»]
4B82X-ray2.10A/B32-574[»]
4B83X-ray2.40A/B32-574[»]
4B84X-ray2.60A/B32-574[»]
4B85X-ray2.10A/B32-574[»]
4BC0X-ray3.35A/B/C/D32-574[»]
4BC1X-ray2.95A/B/C/D32-574[»]
4BTLX-ray2.50A/B32-574[»]
5DTIX-ray2.00A/B32-573[»]
5DTJX-ray2.71A/B32-573[»]
5EHNX-ray2.60A/B32-574[»]
5EHQX-ray2.50A/B32-574[»]
5EHZX-ray2.50A/B32-574[»]
5EIAX-ray2.70A/B32-574[»]
5EIEX-ray2.10A/B32-574[»]
5EIHX-ray2.70A/B32-574[»]
5FKJX-ray3.13A/B/C/D32-574[»]
5FPPX-ray2.40A/B32-574[»]
5FUMX-ray2.50A/B32-574[»]
5HCUX-ray2.42A/B32-571[»]
ProteinModelPortaliP21836.
SMRiP21836.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21836.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4389. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiP21836.
KOiK01049.
OMAiHYSKQDR.
OrthoDBiEOG091G0I4G.
PhylomeDBiP21836.
TreeFamiTF315470.

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: P21836-1) [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
MRPPWYPLHT PSLAFPLLFL LLSLLGGGAR AEGREDPQLL VRVRGGQLRG
60 70 80 90 100
IRLKAPGGPV SAFLGIPFAE PPVGSRRFMP PEPKRPWSGV LDATTFQNVC
110 120 130 140 150
YQYVDTLYPG FEGTEMWNPN RELSEDCLYL NVWTPYPRPA SPTPVLIWIY
160 170 180 190 200
GGGFYSGAAS LDVYDGRFLA QVEGAVLVSM NYRVGTFGFL ALPGSREAPG
210 220 230 240 250
NVGLLDQRLA LQWVQENIAA FGGDPMSVTL FGESAGAASV GMHILSLPSR
260 270 280 290 300
SLFHRAVLQS GTPNGPWATV SAGEARRRAT LLARLVGCPP GGAGGNDTEL
310 320 330 340 350
IACLRTRPAQ DLVDHEWHVL PQESIFRFSF VPVVDGDFLS DTPEALINTG
360 370 380 390 400
DFQDLQVLVG VVKDEGSYFL VYGVPGFSKD NESLISRAQF LAGVRIGVPQ
410 420 430 440 450
ASDLAAEAVV LHYTDWLHPE DPTHLRDAMS AVVGDHNVVC PVAQLAGRLA
460 470 480 490 500
AQGARVYAYI FEHRASTLTW PLWMGVPHGY EIEFIFGLPL DPSLNYTTEE
510 520 530 540 550
RIFAQRLMKY WTNFARTGDP NDPRDSKSPQ WPPYTTAAQQ YVSLNLKPLE
560 570 580 590 600
VRRGLRAQTC AFWNRFLPKL LSATDTLDEA ERQWKAEFHR WSSYMVHWKN
610
QFDHYSKQER CSDL
Length:614
Mass (Da):68,169
Last modified:May 1, 1991 - v1
Checksum:i66E2512463C21172
GO
Isoform H (identifier: P21836-2)
Sequence is not available
Note: No experimental confirmation available.
Length:
Mass (Da):

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56518 mRNA. Translation: CAA39867.1.
AF312033 Genomic DNA. Translation: AAK28816.1.
BC046327 mRNA. Translation: AAH46327.1.
CCDSiCCDS19763.1. [P21836-1]
PIRiJH0314.
RefSeqiNP_001276939.1. NM_001290010.1. [P21836-1]
NP_033729.1. NM_009599.4. [P21836-1]
UniGeneiMm.255464.
Mm.489229.

Genome annotation databases

EnsembliENSMUST00000024099; ENSMUSP00000024099; ENSMUSG00000023328. [P21836-1]
ENSMUST00000085934; ENSMUSP00000083097; ENSMUSG00000023328. [P21836-1]
GeneIDi11423.
KEGGimmu:11423.
UCSCiuc009abt.1. mouse. [P21836-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56518 mRNA. Translation: CAA39867.1.
AF312033 Genomic DNA. Translation: AAK28816.1.
BC046327 mRNA. Translation: AAH46327.1.
CCDSiCCDS19763.1. [P21836-1]
PIRiJH0314.
RefSeqiNP_001276939.1. NM_001290010.1. [P21836-1]
NP_033729.1. NM_009599.4. [P21836-1]
UniGeneiMm.255464.
Mm.489229.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C2BX-ray4.50A35-574[»]
1C2OX-ray4.20A/B/C/D36-574[»]
1J06X-ray2.35A/B32-574[»]
1J07X-ray2.35A/B32-574[»]
1KU6X-ray2.50A32-580[»]
1MAAX-ray2.90A/B/C/D32-578[»]
1MAHX-ray3.20A32-574[»]
1N5MX-ray2.20A/B32-572[»]
1N5RX-ray2.25A/B32-574[»]
1Q83X-ray2.65A/B1-580[»]
1Q84X-ray2.45A/B1-580[»]
2C0PX-ray2.50A/B32-574[»]
2C0QX-ray2.50A/B32-574[»]
2GYUX-ray2.20A/B32-574[»]
2GYVX-ray2.50A/B32-574[»]
2GYWX-ray2.40A/B32-574[»]
2H9YX-ray2.40A/B32-574[»]
2HA0X-ray2.20A/B32-574[»]
2HA2X-ray2.05A/B32-574[»]
2HA3X-ray2.25A/B32-574[»]
2HA4X-ray2.56A/B32-574[»]
2HA5X-ray2.15A/B32-574[»]
2HA6X-ray2.25A/B32-574[»]
2HA7X-ray2.66A/B32-574[»]
2JEYX-ray2.70A/B32-574[»]
2JEZX-ray2.60A/B32-574[»]
2JF0X-ray2.50A/B32-574[»]
2JGEX-ray2.60A/B32-574[»]
2JGFX-ray2.50A/B32-574[»]
2JGIX-ray2.90A/B32-574[»]
2JGJX-ray2.50A/B32-574[»]
2JGKX-ray2.90A/B32-574[»]
2JGLX-ray2.60A/B32-574[»]
2JGMX-ray2.90A/B32-574[»]
2WHPX-ray2.20A/B32-573[»]
2WHQX-ray2.15A/B32-574[»]
2WHRX-ray2.54A/B32-574[»]
2WLSX-ray2.60A/B32-574[»]
2WU3X-ray2.70A/B32-574[»]
2WU4X-ray2.40A/B32-574[»]
2XUDX-ray2.65A/B32-574[»]
2XUFX-ray2.55A/B32-575[»]
2XUGX-ray2.60A/B32-575[»]
2XUHX-ray2.65A/B32-574[»]
2XUIX-ray2.60A/B32-574[»]
2XUJX-ray2.65A/B32-574[»]
2XUKX-ray2.75A/B32-574[»]
2XUOX-ray2.80A/B32-574[»]
2XUPX-ray2.70A/B32-574[»]
2XUQX-ray2.70A/B32-574[»]
2Y2UX-ray2.60A/B32-574[»]
2Y2VX-ray2.45A/B32-574[»]
3DL4X-ray2.50A/B32-574[»]
3DL7X-ray2.50A/B32-574[»]
3ZLTX-ray2.60A/B32-574[»]
3ZLUX-ray2.60A/B32-574[»]
3ZLVX-ray2.50A/B32-574[»]
4A16X-ray2.65A/B/C/D35-574[»]
4A23X-ray2.40A/B32-574[»]
4ARAX-ray2.50A/B32-574[»]
4ARBX-ray2.25A/B32-574[»]
4B7ZX-ray2.30A/B32-574[»]
4B80X-ray2.50A/B32-574[»]
4B81X-ray2.80A/B32-574[»]
4B82X-ray2.10A/B32-574[»]
4B83X-ray2.40A/B32-574[»]
4B84X-ray2.60A/B32-574[»]
4B85X-ray2.10A/B32-574[»]
4BC0X-ray3.35A/B/C/D32-574[»]
4BC1X-ray2.95A/B/C/D32-574[»]
4BTLX-ray2.50A/B32-574[»]
5DTIX-ray2.00A/B32-573[»]
5DTJX-ray2.71A/B32-573[»]
5EHNX-ray2.60A/B32-574[»]
5EHQX-ray2.50A/B32-574[»]
5EHZX-ray2.50A/B32-574[»]
5EIAX-ray2.70A/B32-574[»]
5EIEX-ray2.10A/B32-574[»]
5EIHX-ray2.70A/B32-574[»]
5FKJX-ray3.13A/B/C/D32-574[»]
5FPPX-ray2.40A/B32-574[»]
5FUMX-ray2.50A/B32-574[»]
5HCUX-ray2.42A/B32-571[»]
ProteinModelPortaliP21836.
SMRiP21836.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi197921. 1 interactor.
IntActiP21836. 2 interactors.
MINTiMINT-1206315.
STRINGi10090.ENSMUSP00000024099.

Chemistry databases

BindingDBiP21836.
ChEMBLiCHEMBL3198.

Protein family/group databases

ESTHERimouse-ACHE. AChE.
MEROPSiS09.979.

PTM databases

PhosphoSitePlusiP21836.

Proteomic databases

PaxDbiP21836.
PRIDEiP21836.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024099; ENSMUSP00000024099; ENSMUSG00000023328. [P21836-1]
ENSMUST00000085934; ENSMUSP00000083097; ENSMUSG00000023328. [P21836-1]
GeneIDi11423.
KEGGimmu:11423.
UCSCiuc009abt.1. mouse. [P21836-1]

Organism-specific databases

CTDi43.
MGIiMGI:87876. Ache.

Phylogenomic databases

eggNOGiKOG4389. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiP21836.
KOiK01049.
OMAiHYSKQDR.
OrthoDBiEOG091G0I4G.
PhylomeDBiP21836.
TreeFamiTF315470.

Enzyme and pathway databases

BRENDAi3.1.1.7. 3474.
ReactomeiR-MMU-112311. Neurotransmitter Clearance In The Synaptic Cleft.
R-MMU-1483191. Synthesis of PC.
SABIO-RKP21836.

Miscellaneous databases

EvolutionaryTraceiP21836.
PROiP21836.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000023328.
CleanExiMM_ACHE.
ExpressionAtlasiP21836. baseline and differential.
GenevisibleiP21836. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: P21836
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: November 2, 2016
This is version 158 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.