Reviewed, UniProtKB/Swiss-Prot P04058 (ACES_TORCA)

Names and origin

Protein names

Recommended name:
    Acetylcholinesterase
      Short name=AChE
    EC=3.1.1.7

Gene names

Name:

ache

Organism

Torpedo californica (Pacific electric ray)

Taxonomic identifier

7787 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Chondrichthyes › Elasmobranchii › Squalea › Hypnosqualea › Pristiorajea › Batoidea › Torpediniformes › Torpedinoidei › Torpedinidae › Torpedo

Protein attributes

Sequence length	586 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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 activity	Acetylcholine + H2O = choline + acetate.
Enzyme regulation	Inhibited by substrate concentrations above 0.5 mM. Ref.22
Subunit structure	Isoform H form is an homodimer; the asymmetric form is a disulfide-bonded oligomer composed of a collagenic subunit (Q) and a variable number of T catalytic subunits. Ref.11
Subcellular location	Isoform H: Cell membrane; Lipid-anchor › GPI-anchor. Cell junction › synapse. Isoform T: Cell membrane; Peripheral membrane protein. Cell junction › synapse. Note: Attached to the membrane through disulfide linkage with the collagenic subunit, itself bound to the membrane.
Tissue specificity	Found in the synapses and to a lower extent in extrajunctional areas of muscle and nerve, and on erythrocyte membranes.
Post-translational modification	An interchain disulfide bond is present in what becomes position 593 of the T isoform.
Sequence similarities	Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
Biological process	Neurotransmitter degradation
Cellular component	Cell junction Cell membrane Membrane Synapse
Coding sequence diversity	Alternative splicing
Domain	Signal
Molecular function	Hydrolase Serine esterase
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	acetylcholine catabolic process in synaptic cleft Inferred from electronic annotation. Source: InterPro
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW cell junction Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acetylcholinesterase activity Inferred from electronic annotation. Source: EC cholinesterase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform H (identifier: P04058-1)

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.

Note: GPI-anchored form.

Isoform T (identifier: P04058-2)

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

Note: Attached to the membrane through disulfide linkage with the collagenic subunit, itself bound to the membrane.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Ref.3

Chain

22 – 564

543

Acetylcholinesterase

PRO_0000008595

Propeptide

565 – 586

22

Removed in mature form

PRO_0000008596

Sites

Active site

221

1

Acyl-ester intermediate Ref.22 Ref.11

Active site

348

1

Charge relay system Ref.22 Ref.11

Active site

461

1

Charge relay system Ref.22 Ref.11

Amino acid modifications

Lipidation

564

1

GPI-anchor amidated serine

Glycosylation

80

1

N-linked (GlcNAc...) Ref.22 Ref.18

Glycosylation

437

1

N-linked (GlcNAc...) Ref.22 Ref.11 Ref.18

Glycosylation

478

1

N-linked (GlcNAc...) Ref.18

Glycosylation

554

1

N-linked (GlcNAc...) Ref.18

Disulfide bond

88 ↔ 115

Ref.11 Ref.7

Disulfide bond

275 ↔ 286

Ref.11 Ref.7

Disulfide bond

423 ↔ 542

Ref.11 Ref.7

Disulfide bond

558

Interchain Ref.11 Ref.7

Natural variations

Alternative sequence

557 – 586

30

ACDGE…LYLIF → ETIDEAERQWKTEFHRWSSY MMHWKNQFDHYSRHESCAEL in isoform T.

VSP_001460

Experimental info

Mutagenesis

220

1

E → H: Loss of activity.

Mutagenesis

220

1

E → Q or D: Decrease in activity.

Mutagenesis

221

1

S → C: Loss of activity.

Mutagenesis

221

1

S → V: Loss of activity.

Mutagenesis

446

1

H → Q: Almost no loss of activity.

Mutagenesis

461

1

H → Q: Loss of activity.

Secondary structure

1

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586

Helix Strand Turn

Details...

Beta strand

28 – 31

4

Beta strand

34 – 37

4

Beta strand

39 – 43

5

Beta strand

46 – 55

10

Helix

62 – 64

3

Beta strand

76 – 80

5

Helix

100 – 103

4

Beta strand

117 – 122

6

Beta strand

128 – 136

9

Turn

140 – 142

3

Helix

149 – 151

3

Helix

154 – 160

7

Beta strand

163 – 166

4

Helix

172 – 176

5

Beta strand

183 – 185

3

Helix

189 – 204

16

Helix

205 – 208

4

Beta strand

210 – 220

11

Helix

222 – 232

11

Turn

234 – 236

3

Helix

237 – 239

3

Beta strand

241 – 247

7

Helix

259 – 272

14

Helix

280 – 289

10

Helix

292 – 296

5

Helix

297 – 302

6

Beta strand

304 – 306

3

Beta strand

319 – 324

6

Helix

326 – 332

7

Beta strand

340 – 345

6

Helix

350 – 356

7

Helix

370 – 380

11

Helix

386 – 396

11

Helix

405 – 420

16

Helix

422 – 435

14

Beta strand

439 – 444

6

Helix

455 – 457

3

Turn

461 – 464

4

Helix

465 – 468

4

Helix

471 – 473

3

Helix

475 – 477

3

Helix

481 – 500

20

Turn

518 – 520

3

Beta strand

522 – 529

8

Beta strand

533 – 536

4

Helix

539 – 546

8

Helix

548 – 555

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform H (Globular) [UniParc]. Last modified June 1, 1994. Version 2. Checksum: 731D5F0F3ABA62A8	FASTA	586	65,906
	10 20 30 40 50 60 MNLLVTSSLG VLLHLVVLCQ ADDHSELLVN TKSGKVMGTR VPVLSSHISA FLGIPFAEPP 70 80 90 100 110 120 VGNMRFRRPE PKKPWSGVWN ASTYPNNCQQ YVDEQFPGFS GSEMWNPNRE MSEDCLYLNI 130 140 150 160 170 180 WVPSPRPKST TVMVWIYGGG FYSGSSTLDV YNGKYLAYTE EVVLVSLSYR VGAFGFLALH 190 200 210 220 230 240 GSQEAPGNVG LLDQRMALQW VHDNIQFFGG DPKTVTIFGE SAGGASVGMH ILSPGSRDLF 250 260 270 280 290 300 RRAILQSGSP NCPWASVSVA EGRRRAVELG RNLNCNLNSD EELIHCLREK KPQELIDVEW 310 320 330 340 350 360 NVLPFDSIFR FSFVPVIDGE FFPTSLESML NSGNFKKTQI LLGVNKDEGS FFLLYGAPGF 370 380 390 400 410 420 SKDSESKISR EDFMSGVKLS VPHANDLGLD AVTLQYTDWM DDNNGIKNRD GLDDIVGDHN 430 440 450 460 470 480 VICPLMHFVN KYTKFGNGTY LYFFNHRASN LVWPEWMGVI HGYEIEFVFG LPLVKELNYT 490 500 510 520 530 540 AEEEALSRRI MHYWATFAKT GNPNEPHSQE SKWPLFTTKE QKFIDLNTEP MKVHQRLRVQ 550 560 570 580 MCVFWNQFLP KLLNATACDG ELSSSGTSSS KGIIFYVLFS ILYLIF
	Isoform T. Checksum: 36D5E9A30F9E6065	FASTA	596	67,818
	10 20 30 40 50 60 MNLLVTSSLG VLLHLVVLCQ ADDHSELLVN TKSGKVMGTR VPVLSSHISA FLGIPFAEPP 70 80 90 100 110 120 VGNMRFRRPE PKKPWSGVWN ASTYPNNCQQ YVDEQFPGFS GSEMWNPNRE MSEDCLYLNI 130 140 150 160 170 180 WVPSPRPKST TVMVWIYGGG FYSGSSTLDV YNGKYLAYTE EVVLVSLSYR VGAFGFLALH 190 200 210 220 230 240 GSQEAPGNVG LLDQRMALQW VHDNIQFFGG DPKTVTIFGE SAGGASVGMH ILSPGSRDLF 250 260 270 280 290 300 RRAILQSGSP NCPWASVSVA EGRRRAVELG RNLNCNLNSD EELIHCLREK KPQELIDVEW 310 320 330 340 350 360 NVLPFDSIFR FSFVPVIDGE FFPTSLESML NSGNFKKTQI LLGVNKDEGS FFLLYGAPGF 370 380 390 400 410 420 SKDSESKISR EDFMSGVKLS VPHANDLGLD AVTLQYTDWM DDNNGIKNRD GLDDIVGDHN 430 440 450 460 470 480 VICPLMHFVN KYTKFGNGTY LYFFNHRASN LVWPEWMGVI HGYEIEFVFG LPLVKELNYT 490 500 510 520 530 540 AEEEALSRRI MHYWATFAKT GNPNEPHSQE SKWPLFTTKE QKFIDLNTEP MKVHQRLRVQ 550 560 570 580 590 MCVFWNQFLP KLLNATETID EAERQWKTEF HRWSSYMMHW KNQFDHYSRH ESCAEL

References

[1]	"Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence." Schumacher M., Camp S., Maulet Y., Newton M., McPhee-Quigley K., Taylor S.S., Friedmann T., Taylor P. Nature 319:407-409(1986) [PubMed: 3753747] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-586.
[2]	"Multiple messenger RNA species give rise to the structural diversity in acetylcholinesterase." Schumacher M. J. Biol. Chem. 263:18979-18987(1988) [PubMed: 3198606] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
[3]	"Primary structures of the catalytic subunits from two molecular forms of acetylcholinesterase. A comparison of NH2-terminal and active center sequences." MacPhee-Quigley K., Taylor P., Taylor S. J. Biol. Chem. 260:12185-12189(1985) [PubMed: 3900071] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-45 AND 214-237.
[4]	"Anionic subsites of the catalytic center of acetylcholinesterase from Torpedo and from cobra venom." Kreienkamp H.J., Weise C., Raba R., Aaviksaar A., Hucho F. Proc. Natl. Acad. Sci. U.S.A. 88:6117-6121(1991) [PubMed: 2068091] [Abstract] Cited for: PROTEIN SEQUENCE OF 100-108.
[5]	"Divergence in primary structure between the molecular forms of acetylcholinesterase." Gibney G., Macphee-Quigley K., Thompson B., Vedvick T., Low M.G., Taylor S.S., Taylor P. J. Biol. Chem. 263:1140-1145(1988) [PubMed: 3335534] [Abstract] Cited for: PROTEIN SEQUENCE OF 552-558.
[6]	"Single gene encodes glycophospholipid-anchored and asymmetric acetylcholinesterase forms: alternative coding exons contain inverted repeat sequences." Maulet Y., Camp S., Gibney G., Rachinsky T.L., Ekstroem T.J., Taylor P. Neuron 4:289-301(1990) [PubMed: 2306366] [Abstract] Cited for: ALTERNATIVE SPLICING.
[7]	"Profile of the disulfide bonds in acetylcholinesterase." McPhee-Quigley K., Vedvick T.S., Taylor P., Taylor S.S. J. Biol. Chem. 261:13565-13570(1986) [PubMed: 3759980] [Abstract] Cited for: DISULFIDE BONDS.
[8]	"Structure of the glycosyl-phosphatidylinositol membrane anchor of acetylcholinesterase from the electric organ of the electric-fish, Torpedo californica." Mehlert A., Varon L., Silman I., Homans S.W., Ferguson M.A. Biochem. J. 296:473-479(1993) [PubMed: 8257440] [Abstract] Cited for: STRUCTURE OF THE GPI-ANCHOR.
[9]	"Residues in Torpedo californica acetylcholinesterase necessary for processing to a glycosyl phosphatidylinositol-anchored form." Bucht G., Hjalmarsson K. Biochim. Biophys. Acta 1292:223-232(1996) [PubMed: 8597567] [Abstract] Cited for: GPI-ANCHOR AT SER-564.
[10]	"Mutagenesis of essential functional residues in acetylcholinesterase." Gibney G., Camp S., Dionne M., McPhee-Quigley K., Taylor P. Proc. Natl. Acad. Sci. U.S.A. 87:7546-7550(1990) [PubMed: 2217185] [Abstract] Cited for: MUTAGENESIS.
[11]	"Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein." Sussman J.L., Harel M., Frolow F., Oefner C., Goldman A., Toker L., Silman I. Science 253:872-879(1991) [PubMed: 1678899] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-558, ACTIVE SITE, GLYCOSYLATION AT ASN-437, DISULFIDE BONDS, SUBUNIT.
[12]	"Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase." Harel M., Schalk I., Ehret-Sabatier L., Bouet F., Goeldner M., Hirth C., Axelsen P.H., Silman I., Sussman J.L. Proc. Natl. Acad. Sci. U.S.A. 90:9031-9035(1993) [PubMed: 8415649] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 22-556 IN COMPLEX WITH SUBSTRATE ANALOGS.
[13]	"Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target." Harel M., Kleywegt G.J., Ravelli R.B., Silman I., Sussman J.L. Structure 3:1355-1366(1995) [PubMed: 8747462] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 22-558 IN COMPLEX WITH FASCICULIN.
[14]	"Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A." Raves M.L., Harel M., Pang Y.P., Silman I., Kozikowski A.P., Sussman J.L. Nat. Struct. Biol. 4:57-63(1997) [PubMed: 8989325] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-558 IN COMPLEX WITH THE INHIBITOR HUPERZINE A.
[15]	"'Back door' opening implied by the crystal structure of a carbamoylated acetylcholinesterase." Bartolucci C., Perola E., Cellai L., Brufani M., Lamba D. Biochemistry 38:5714-5719(1999) [PubMed: 10231521] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-558.
[16]	"Crystal structures of aged phosphonylated acetylcholinesterase: nerve agent reaction products at the atomic level." Millard C.B., Kryger G., Ordentlich A., Greenblatt H.M., Harel M., Raves M.L., Segall Y., Barak D., Shafferman A., Silman I., Sussman J.L. Biochemistry 38:7032-7039(1999) [PubMed: 10353814] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-558.
[17]	"Structure of acetylcholinesterase complexed with (-)-galanthamine at 2.3-A resolution." Greenblatt H.M., Kryger G., Lewis T., Silman I., Sussman J.L. FEBS Lett. 463:321-326(1999) [PubMed: 10606746] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 22-564 IN COMPLEX WITH GALANTHAMINE.
[18]	"Structure of acetylcholinesterase complexed with E2020 (Aricept(R)): implications for the design of new anti-Alzheimer drugs." Kryger G., Silman I., Sussman J.L. Structure 7:297-307(1999) [PubMed: 10368299] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE SYNTHETIC INHIBITOR ARICEPT, GLYCOSYLATION AT ASN-80; ASN-437; ASN-478 AND ASN-554.
[19]	"3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 A resolution: kinetic and molecular dynamic correlates." Dvir H., Wong D.M., Harel M., Barril X., Orozco M., Luque F.J., Munoz-Torrero D., Camps P., Rosenberry T.L., Silman I., Sussman J.L. Biochemistry 41:2970-2981(2002) [PubMed: 11863435] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE SYNTHETIC INHIBITOR HUPRINE.
[20]	"Kinetic and structural studies on the interaction of cholinesterases with the anti-Alzheimer drug rivastigmine." Bar-On P., Millard C.B., Harel M., Dvir H., Enz A., Sussman J.L., Silman I. Biochemistry 41:3555-3564(2002) [PubMed: 11888271] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-556 IN COMPLEX WITH THE SYNTHETIC INHIBITOR RIVASTIGMINE.
[21]	"The crystal structure of the complex of the anticancer prodrug 7-ethyl-10-[4-(1-piperidino)-1-piperidino]-carbonyloxycamptothecin (CPT-11) with Torpedo californica acetylcholinesterase provides a molecular explanation for its cholinergic action." Harel M., Hyatt J.L., Brumshtein B., Morton C.L., Yoon K.J., Wadkins R.M., Silman I., Sussman J.L., Potter P.M. Mol. Pharmacol. 67:1874-1881(2005) [PubMed: 15772291] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 22-564 IN COMPLEX WITH THE SYNTHETIC INHIBITOR CPT-11.
[22]	"Structural insights into substrate traffic and inhibition in acetylcholinesterase." Colletier J.-P., Fournier D., Greenblatt H.M., Stojan J., Sussman J.L., Zaccai G., Silman I., Weik M. EMBO J. 25:2746-2756(2006) [PubMed: 16763558] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 22-558 IN COMPLEXES WITH SUBSTRATE AND SUBSTRATE ANALOGS, GLYCOSYLATION AT ASN-80 AND ASN-437, ACTIVE SITE, ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X03439 mRNA. Translation: CAA27169.1.
X56516 Genomic DNA. No translation available.
X56517 Genomic DNA. No translation available.

PIR

ACRYE. A00773.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ACJ	X-ray	2.80	A	22-556	[»]
1ACL	X-ray	2.80	A	22-556	[»]
1AMN	X-ray	2.80	A	22-558	[»]
1AX9	X-ray	2.80	A	22-558	[»]
1CFJ	X-ray	2.60	A	22-558	[»]
1DX6	X-ray	2.30	A	22-564	[»]
1E3Q	X-ray	2.85	A	22-564	[»]
1E66	X-ray	2.10	A	22-564	[»]
1EA5	X-ray	1.80	A	22-558	[»]
1EEA	X-ray	4.50	A	22-555	[»]
1EVE	X-ray	2.50	A	22-564	[»]
1FSS	X-ray	3.00	A	22-558	[»]
1GPK	X-ray	2.10	A	22-558	[»]
1GPN	X-ray	2.35	A	22-558	[»]
1GQR	X-ray	2.20	A	25-556	[»]
1GQS	X-ray	3.00	A	25-556	[»]
1H22	X-ray	2.15	A	22-564	[»]
1H23	X-ray	2.15	A	22-564	[»]
1HBJ	X-ray	2.50	A	22-564	[»]
1JGA	model	-	A	1-586	[»]
1JGB	model	-	A	1-586	[»]
1JJB	X-ray	2.30	A	25-556	[»]
1OCE	X-ray	2.70	A	22-558	[»]
1ODC	X-ray	2.20	A	22-564	[»]
1QID	X-ray	2.05	A	22-558	[»]
1QIE	X-ray	2.10	A	22-558	[»]
1QIF	X-ray	2.10	A	22-558	[»]
1QIG	X-ray	2.30	A	22-558	[»]
1QIH	X-ray	2.50	A	22-558	[»]
1QII	X-ray	2.65	A	22-558	[»]
1QIJ	X-ray	2.80	A	22-558	[»]
1QIK	X-ray	2.90	A	22-558	[»]
1QIM	X-ray	3.00	A	22-558	[»]
1QTI	X-ray	2.50	A	22-537	[»]
1SOM	X-ray	2.20	A	22-564	[»]
1U65	X-ray	2.61	A	22-564	[»]
1UT6	X-ray	2.40	A	22-556	[»]
1VOT	X-ray	2.50	A	22-558	[»]
1VXO	X-ray	2.40	A	22-558	[»]
1VXR	X-ray	2.20	A	22-558	[»]
1W4L	X-ray	2.16	A	22-564	[»]
1W6R	X-ray	2.05	A	22-564	[»]
1W75	X-ray	2.40	A/B	22-564	[»]
1W76	X-ray	2.30	A/B	22-564	[»]
1ZGB	X-ray	2.30	A	22-564	[»]
1ZGC	X-ray	2.10	A/B	22-564	[»]
2ACE	X-ray	2.50	A	22-558	[»]
2ACK	X-ray	2.40	A	22-558	[»]
2BAG	X-ray	2.40	A	22-564	[»]
2C4H	X-ray	2.15	A	22-558	[»]
2C58	X-ray	2.30	A	22-558	[»]
2C5F	X-ray	2.60	A	22-558	[»]
2C5G	X-ray	1.95	A	22-558	[»]
2CEK	X-ray	2.20	A	22-556	[»]
2CKM	X-ray	2.15	A	22-564	[»]
2CMF	X-ray	2.50	A	22-564	[»]
2DFP	X-ray	2.30	A	23-556	[»]
2J3D	X-ray	2.60	A	22-564	[»]
2J3Q	X-ray	2.80	A	22-564	[»]
2J4F	X-ray	2.80	A	22-564	[»]
2V96	X-ray	2.40	A/B	22-558	[»]
2V97	X-ray	2.40	A/B	22-558	[»]
2V98	X-ray	3.00	A/B	22-558	[»]
2VA9	X-ray	2.40	A/B	22-558	[»]
2VJA	X-ray	2.30	A/B	22-558	[»]
2VJB	X-ray	2.39	A/B	22-558	[»]
2VJC	X-ray	2.20	A/B	22-558	[»]
2VJD	X-ray	2.30	A/B	22-558	[»]
2VQ6	X-ray	2.71	A	22-564	[»]
2VT6	X-ray	2.40	A/B	22-558	[»]
2VT7	X-ray	2.20	A/B	22-558	[»]
2W6C	X-ray	2.69	X	1-586	[»]
3ACE	model	-	A	22-558	[»]
4ACE	model	-	A	22-558	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S09.979.

Phylogenomic databases

HOVERGEN

P04058.

Enzyme and pathway databases

BRENDA

3.1.1.7. 74507.

Family and domain databases

InterPro

IPR000908. Acylcholinesterase_fish/snake.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]

PANTHER

PTHR11559. CarbesteraseB. 1 hit.

Pfam

PF00135. COesterase. 1 hit.
[Graphical view]

PRINTS

PR00879. ACHEFISH.
PR00878. CHOLNESTRASE.

PROSITE

PS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

DrugBank

DB00674. Galantamine.

Entry information

Entry name

ACES_TORCA

Accession

Primary (citable) accession number: P04058

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	June 1, 1994
Last modified:	June 16, 2009
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)