O00748 · EST2_HUMAN
- ProteinCocaine esterase
- GeneCES2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids559 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs (PubMed:9169443).
Shows high catalytic efficiency for hydrolysis of cocaine, 4-methylumbelliferyl acetate, heroin and 6-monoacetylmorphine (PubMed:9169443).
Hydrolyzes aspirin, substrates with large alcohol group and small acyl group and endogenous lipids such as triacylglycerol (PubMed:28677105).
Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins (PubMed:21049984).
Shows high catalytic efficiency for hydrolysis of cocaine, 4-methylumbelliferyl acetate, heroin and 6-monoacetylmorphine (PubMed:9169443).
Hydrolyzes aspirin, substrates with large alcohol group and small acyl group and endogenous lipids such as triacylglycerol (PubMed:28677105).
Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins (PubMed:21049984).
Catalytic activity
- cocaine + H2O = benzoate + ecgonine methyl ester + H+
- 2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H+This reaction proceeds in the forward direction.
- H2O + prostaglandin E2 1-glyceryl ester = glycerol + H+ + prostaglandin E2This reaction proceeds in the forward direction.
- H2O + prostaglandin F2alpha 1-glyceryl ester = glycerol + H+ + prostaglandin F2alphaThis reaction proceeds in the forward direction.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.39 mM | cocaine | |||||
0.15 mM | 4-methylumbelliferyl acetate | |||||
6.8 mM | heroin | |||||
46 μM | 2-arachidonoylglycerol | |||||
750 μM | prostaglandin E2 1-glyceryl ester | |||||
35 μM | prostaglandin F2alpha 1-glyceryl ester | |||||
0.13 mM | 6-monoacetylmorphine |
kcat is 43 min-1, 49 min-1, 150 min-1 with 2-arachidonoylglycerol, prostaglandin F2alpha 1-glyceryl ester and prostaglandin E2 1-glyceryl ester as substrates, respectively.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 228 | Acyl-ester intermediate | ||||
Sequence: S | ||||||
Active site | 345 | Charge relay system | ||||
Sequence: E | ||||||
Active site | 457 | Charge relay system | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | intracellular membrane-bounded organelle | |
Molecular Function | carboxylesterase activity | |
Molecular Function | carboxylic ester hydrolase activity | |
Molecular Function | methylumbelliferyl-acetate deacetylase activity | |
Biological Process | catabolic process | |
Biological Process | prostaglandin metabolic process | |
Biological Process | xenobiotic metabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameCocaine esterase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00748
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_018396 | 34 | in dbSNP:rs72547531 | |||
Sequence: R → W | ||||||
Natural variant | VAR_018397 | 206 | in dbSNP:rs8192924 | |||
Sequence: R → H |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 630 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, modified residue, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-26 | |||||
Sequence: MRLHRLRARLSAVACGLLLLLVRGQG | ||||||
Modified residue | 27 | Pyrrolidone carboxylic acid | ||||
Sequence: Q | ||||||
Chain | PRO_0000008572 | 27-559 | Cocaine esterase | |||
Sequence: QDSASPIRTTHTGQVLGSLVHVKGANAGVQTFLGIPFAKPPLGPLRFAPPEPPESWSGVRDGTTHPAMCLQDLTAVESEFLSQFNMTFPSDSMSEDCLYLSIYTPAHSHEGSNLPVMVWIHGGALVFGMASLYDGSMLAALENVVVVIIQYRLGVLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIMESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEILAINKPFKMIPGVVDGVFLPRHPQELLASADFQPVPSIVGVNNNEFGWLIPKVMRIYDTQKEMDREASQAALQKMLTLLMLPPTFGDLLREEYIGDNGDPQTLQAQFQEMMADSMFVIPALQVAHFQCSRAPVYFYEFQHQPSWLKNIRPPHMKADHGDELPFVFRSFFGGNYIKFTEEEEQLSRKMMKYWANFARNGNPNGEGLPHWPLFDQEEQYLQLNLQPAVGRALKAHRLQFWKKALPQKIQELEEPEERHTEL | ||||||
Disulfide bond | 95↔123 | |||||
Sequence: CLQDLTAVESEFLSQFNMTFPSDSMSEDC | ||||||
Glycosylation | 111 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 276 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 280↔291 | |||||
Sequence: CDQVDSEALVGC |
Post-translational modification
Glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Preferentially expressed in intestine with moderate expression in liver. Within the intestine, highest expression is found in small intestine with lower expression in colon and rectum.
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 556-559 | Prevents secretion from ER | ||||
Sequence: HTEL |
Sequence similarities
Belongs to the type-B carboxylesterase/lipase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 4 isoforms produced by Alternative splicing & Alternative initiation.
O00748-1
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.
- Name1
- Length559
- Mass (Da)61,807
- Last updated1997-07-01 v1
- ChecksumE2EBCABA2995339A
O00748-2
- Name2
- Differences from canonical
- 458-474: GDELPFVFRSFFGGNYI → V
O00748-4
- Name3
- NoteProbably produced by alternative initiation of isoform 1. Does not contain a signal peptide. The biological function of the extra amino acids in the N-terminus remains to be determined.
- Differences from canonical
- 1-1: M → MTAQSRSPTTPTFPGPSQRTPLTPCPVQTPRLGKALIHCWTDPGQPLGEQQRVRRQRTETSEPTM
O00748-5
- Name4
- NoteProbably produced by alternative initiation of isoform 2. Does not contain a signal peptide. The biological function of the extra amino acids in the N-terminus remains to be determined.
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_059804 | 1 | in isoform 3 and isoform 4 | |||
Sequence: M → MTAQSRSPTTPTFPGPSQRTPLTPCPVQTPRLGKALIHCWTDPGQPLGEQQRVRRQRTETSEPTM | ||||||
Sequence conflict | 2-10 | in Ref. 2; AA sequence | ||||
Sequence: Missing | ||||||
Sequence conflict | 180 | in Ref. 4; BAF83171 | ||||
Sequence: G → S | ||||||
Sequence conflict | 239 | in Ref. 4; BAF83171 | ||||
Sequence: V → M | ||||||
Sequence conflict | 385 | in Ref. 5; CAD98009 | ||||
Sequence: F → S | ||||||
Alternative sequence | VSP_010161 | 458-474 | in isoform 2 and isoform 4 | |||
Sequence: GDELPFVFRSFFGGNYI → V | ||||||
Sequence conflict | 519 | in Ref. 5; CAD98009 | ||||
Sequence: Q → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y09616 EMBL· GenBank· DDBJ | CAA70831.1 EMBL· GenBank· DDBJ | mRNA | ||
D50579 EMBL· GenBank· DDBJ | BAA23606.1 EMBL· GenBank· DDBJ | mRNA | ||
U60553 EMBL· GenBank· DDBJ | AAB03611.1 EMBL· GenBank· DDBJ | mRNA | ||
AL713761 EMBL· GenBank· DDBJ | CAD28531.1 EMBL· GenBank· DDBJ | mRNA | ||
AK290482 EMBL· GenBank· DDBJ | BAF83171.1 EMBL· GenBank· DDBJ | mRNA | ||
BX538086 EMBL· GenBank· DDBJ | CAD98009.1 EMBL· GenBank· DDBJ | mRNA | ||
AY851164 EMBL· GenBank· DDBJ | AAW29943.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC009084 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471092 EMBL· GenBank· DDBJ | EAW83058.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471092 EMBL· GenBank· DDBJ | EAW83059.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC032095 EMBL· GenBank· DDBJ | AAH32095.1 EMBL· GenBank· DDBJ | mRNA |