Q96KN2 · CNDP1_HUMAN
- ProteinBeta-Ala-His dipeptidase
- GeneCNDP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids507 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the peptide bond hydrolysis in Xaa-His dipeptides, displaying the highest activity toward carnosine (beta-alanyl-L-histidine) and anserine (beta-alanyl-3-methyl-histidine).
Catalytic activity
- carnosine + H2O = beta-alanine + L-histidineThis reaction proceeds in the forward direction.
- H2O + L-alanyl-L-histidine = L-alanine + L-histidineThis reaction proceeds in the forward direction.
- glycyl-L-histidine + H2O = glycine + L-histidineThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Activity regulation
Activated by cadmium ions (PubMed:12473676).
Inhibited by the metal chelator 1,10-o-phenantrolin. The inhibitory concentration 50% (IC50) is 5 uM.
Inhibited by the metal chelator 1,10-o-phenantrolin. The inhibitory concentration 50% (IC50) is 5 uM.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.27 μM | carnosine | 30 | in the absence of cadmium ions | |||
11 μM | carnosine | 30 | in the presence of 200 uM cadmium ions | |||
0.13 mM | carnosine | |||||
0.2 μM | homocarnosine | 30 | in the absence of cadmium ions | |||
1 μM | homocarnosine | 30 | in the presence of 200 uM cadmium ions | |||
8.7 mM | homocarnosine |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
8.5 μmol/min/mg | toward carnosine | ||||
0.36 μmol/min/mg | toward homocarnosine |
1 hour incubation in 50 mM Tris-HCl, pH 7.5.
pH Dependence
Optimum pH is 8.5.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 132 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 134 | |||||
Sequence: D | ||||||
Binding site | 165 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 165 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 199 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 200 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 228 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 478 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extracellular region | |
Molecular Function | carboxypeptidase activity | |
Molecular Function | dipeptidase activity | |
Molecular Function | metal ion binding | |
Molecular Function | metallodipeptidase activity | |
Biological Process | proteolysis | |
Biological Process | regulation of protein metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBeta-Ala-His dipeptidase
- 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 accessionQ96KN2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_027147 | 6 | in dbSNP:rs11151964 | |||
Sequence: G → R | ||||||
Natural variant | VAR_027148 | 20 | ||||
Sequence: L → LL | ||||||
Natural variant | VAR_027149 | 113 | in dbSNP:rs4263028 | |||
Sequence: V → I | ||||||
Mutagenesis | 132 | Loss of activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 165 | Loss of activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 200 | Loss of activity. | ||||
Sequence: E → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 633 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-26 | |||||
Sequence: MDPKLGRMAASLLAVLLLLLERGMFS | ||||||
Chain | PRO_0000026809 | 27-507 | Beta-Ala-His dipeptidase | |||
Sequence: SPSPPPALLEKVFQYIDLHQDEFVQTLKEWVAIESDSVQPVPRFRQELFRMMAVAADTLQRLGARVASVDMGPQQLPDGQSLPIPPVILAELGSDPTKGTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAFRALEQDLPVNIKFIIEGMEEAGSVALEELVEKEKDRFFSGVDYIVISDNLWISQRKPAITYGTRGNSYFMVEVKCRDQDFHSGTFGGILHEPMADLVALLGSLVDSSGHILVPGIYDEVVPLTEEEINTYKAIHLDLEEYRNSSRVEKFLFDTKEEILMHLWRYPSLSIHGIEGAFDEPGTKTVIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEDVFSKRNSSNKMVVSMTLGLHPWIANIDDTQYLAAKRAIRTVFGTEPDMIRDGSTIPIAKMFQEIVHKSVVLIPLGAVDDGEHSQNEKINRWNYIEGTKLFAAFFLEMAQLH | ||||||
Modified residue | 219 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 322 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 382 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Found in serum and adult nervous central system. Absent in serum from patients with homocarnosinosis.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q96KN2 | CNDP2 Q96KP4 | 2 | EBI-21014506, EBI-1190734 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length507
- Mass (Da)56,692
- Last updated2022-02-23 v5
- ChecksumF3B51A9123C927C0
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 155 | in Ref. 1; CAD10388 and 5; AAI10296 | ||||
Sequence: D → G | ||||||
Sequence conflict | 237 | in Ref. 1; CAD10388 | ||||
Sequence: P → L | ||||||
Sequence conflict | 272 | in Ref. 1; CAD10388 | ||||
Sequence: P → L |
Polymorphism
The number of trinucleotide (CTG) repeat varies among different alleles leading to insertion of Leu residues in the signal peptide. The allele with 5 leucines (as shown in the reference entry) is known as the Mannheim allele. Diabetic patients with the CNDP1 Mannheim allele are less susceptible for nephropathy.
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ417564 EMBL· GenBank· DDBJ | CAD10388.1 EMBL· GenBank· DDBJ | mRNA | ||
AY358756 EMBL· GenBank· DDBJ | AAQ89116.1 EMBL· GenBank· DDBJ | mRNA | ||
BC004271 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BC110295 EMBL· GenBank· DDBJ | AAI10296.1 EMBL· GenBank· DDBJ | mRNA | ||
BC113512 EMBL· GenBank· DDBJ | AAI13513.1 EMBL· GenBank· DDBJ | mRNA | ||
BC117122 EMBL· GenBank· DDBJ | AAI17123.1 EMBL· GenBank· DDBJ | mRNA |