P04058 (ACES_TORCA) Reviewed, UniProtKB/Swiss-Prot

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

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Chondrichthyes › Elasmobranchii › Batoidea › Torpediniformes › 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 a 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-KW plasma membrane 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 carboxylesterase activity Inferred from electronic annotation. Source: UniProtKB-KW
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

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.11 Ref.22 Ref.23

Active site

348

1

Charge relay system Ref.11 Ref.22 Ref.23

Active site

461

1

Charge relay system Ref.11 Ref.22 Ref.23

Amino acid modifications

Lipidation

564

1

GPI-anchor amidated serine Ref.8 Ref.9

Glycosylation

80

1

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

Glycosylation

437

1

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

Glycosylation

478

1

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

Glycosylation

554

1

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

Disulfide bond

88 ↔ 115

Ref.7 Ref.11 Ref.23

Disulfide bond

275 ↔ 286

Ref.7 Ref.11 Ref.23

Disulfide bond

423 ↔ 542

Ref.7 Ref.11 Ref.23

Disulfide bond

558

Interchain Ref.7 Ref.11 Ref.23

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

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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

Beta strand

87 – 89

3

Beta strand

95 – 98

4

Helix

100 – 103

4

Beta strand

111 – 113

3

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

Helix

234 – 237

4

Beta strand

241 – 247

7

Turn

253 – 255

3

Helix

259 – 272

14

Helix

280 – 289

10

Helix

292 – 298

7

Helix

299 – 302

4

Beta strand

304 – 306

3

Beta strand

319 – 324

6

Helix

326 – 332

7

Beta strand

340 – 345

6

Beta strand

347 – 349

3

Helix

350 – 356

7

Beta strand

362 – 364

3

Helix

370 – 380

11

Helix

386 – 395

10

Turn

399 – 401

3

Helix

405 – 420

16

Helix

422 – 433

12

Beta strand

435 – 437

3

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

Beta strand

501 – 504

4

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 [UniParc]. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
[23]	"Crystallographic snapshots of nonaged and aged conjugates of soman with acetylcholinesterase, and of a ternary complex of the aged conjugate with pralidoxime." Sanson B., Nachon F., Colletier J.P., Froment M.T., Toker L., Greenblatt H.M., Sussman J.L., Ashani Y., Masson P., Silman I., Weik M. J. Med. Chem. 52:7593-7603(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-558 IN COMPLEX WITH SOMAN, ACTIVE SITE, DISULFIDE BONDS.
[24]	"Probing Torpedo californica acetylcholinesterase catalytic gorge with two novel bis-functional galanthamine derivatives." Bartolucci C., Haller L.A., Jordis U., Fels G., Lamba D. J. Med. Chem. 53:745-751(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 23-556 IN COMPLEX WITH GALANTHAMINE DERIVATIVES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

PIR

ACRYE. A00773.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
2W9I	X-ray	2.43	A	1-586	[»]
2WFZ	X-ray	1.95	A	22-558	[»]
2WG0	X-ray	2.20	A	22-558	[»]
2WG1	X-ray	2.20	A	22-558	[»]
2WG2	X-ray	1.95	A	22-558	[»]
2XI4	X-ray	2.30	A/B	22-558	[»]
3ACE	model	-	A	22-558	[»]
3GEL	X-ray	2.39	A	25-556	[»]
3I6M	X-ray	2.26	A	23-556	[»]
3I6Z	X-ray	2.19	A	23-556	[»]
3M3D	X-ray	2.34	A	22-564	[»]
3ZV7	X-ray	2.26	A	22-564	[»]
4ACE	model	-	A	22-558	[»]

ProteinModelPortal

P04058.

SMR

P04058. Positions 23-556.

ModBase

Search...

Protein family/group databases

MEROPS

S09.979.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG008839.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-16823.

Family and domain databases

InterPro

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

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

Search...

Other

BindingDB

P04058.

ChEMBL

CHEMBL4780.

DrugBank

DB00674. Galantamine.

EvolutionaryTrace

P04058.

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:	April 3, 2013
This is version 125 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program