P48052 · CBPA2_HUMAN
- ProteinCarboxypeptidase A2
- GeneCPA2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids419 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Carboxypeptidase that catalyzes the release of a C-terminal amino acid, with a preference for large aromatic C-terminal residues.
Catalytic activity
Cofactor
Note: Binds 1 zinc ion per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
36.4 μM | 3-(2-furyl)acryloyl-Phe-Phe | 25 | ||||
16.3 μM | 3-(2-furyl)acryloyl-Phe-Trp | 25 | ||||
393 μM | 3-(2-furyl)acryloyl-Phe-Leu | 25 | ||||
460 μM | 3-(2-furyl)acryloyl-Phe-Ile | 25 |
kcat is 121 sec-1 with 3-(2-furyl)acryloyl-Phe-Phe as substrate (at 25 degrees Celsius) (PubMed:20385563).
kcat is 65.3 sec-1 with 3-(2-furyl)acryloyl-Phe-Trp as substrate (at 25 degrees Celsius) (PubMed:20385563).
kcat is 18.6 sec-1 with 3-(2-furyl)acryloyl-Phe-Leu as substrate (at 25 degrees Celsius) (PubMed:20385563).
kcat is 5.37 sec-1 with 3-(2-furyl)acryloyl-Phe-Ile as substrate (at 25 degrees Celsius) (PubMed:20385563).
kcat is 65.3 sec-1 with 3-(2-furyl)acryloyl-Phe-Trp as substrate (at 25 degrees Celsius) (PubMed:20385563).
kcat is 18.6 sec-1 with 3-(2-furyl)acryloyl-Phe-Leu as substrate (at 25 degrees Celsius) (PubMed:20385563).
kcat is 5.37 sec-1 with 3-(2-furyl)acryloyl-Phe-Ile as substrate (at 25 degrees Celsius) (PubMed:20385563).
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 179 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 179-182 | substrate | ||||
Sequence: HARE | ||||||
Binding site | 182 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 237 | substrate | ||||
Sequence: R | ||||||
Binding site | 254-255 | substrate | ||||
Sequence: NR | ||||||
Binding site | 306 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 307-308 | substrate | ||||
Sequence: SY | ||||||
Binding site | 358 | substrate | ||||
Sequence: Y | ||||||
Active site | 380 | Proton donor/acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | vacuole | |
Molecular Function | carboxypeptidase activity | |
Molecular Function | metallocarboxypeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | protein catabolic process in the vacuole | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCarboxypeptidase A2
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP48052
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_031204 | 82 | in dbSNP:rs17850135 | |||
Sequence: E → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 484 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, propeptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MAMRLILFFGALFGHIYC | ||||||
Propeptide | PRO_0000004353 | 19-114 | Activation peptide | |||
Sequence: LETFVGDQVLEIVPSNEEQIKNLLQLEAQEHLQLDFWKSPTTPGETAHVRVPFVNVQAVKVFLESQGIAYSIMIEDVQVLLDKENEEMLFNRRRER | ||||||
Chain | PRO_0000004354 | 115-419 | Carboxypeptidase A2 | |||
Sequence: SGNFNFGAYHTLEEISQEMDNLVAEHPGLVSKVNIGSSFENRPMNVLKFSTGGDKPAIWLDAGIHAREWVTQATALWTANKIVSDYGKDPSITSILDALDIFLLPVTNPDGYVFSQTKNRMWRKTRSKVSGSLCVGVDPNRNWDAGFGGPGASSNPCSDSYHGPSANSEVEVKSIVDFIKSHGKVKAFITLHSYSQLLMFPYGYKCTKLDDFDELSEVAQKAAQSLRSLHGTKYKVGPICSVIYQASGGSIDWSYDYGIKYSFAFELRDTGRYGFLLPARQILPTAEETWLGLKAIMEHVRDHPY | ||||||
Disulfide bond | 248↔271 | |||||
Sequence: CVGVDPNRNWDAGFGGPGASSNPC | ||||||
Disulfide bond | 320↔354 | |||||
Sequence: CTKLDDFDELSEVAQKAAQSLRSLHGTKYKVGPIC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 122-414 | Peptidase M14 | ||||
Sequence: AYHTLEEISQEMDNLVAEHPGLVSKVNIGSSFENRPMNVLKFSTGGDKPAIWLDAGIHAREWVTQATALWTANKIVSDYGKDPSITSILDALDIFLLPVTNPDGYVFSQTKNRMWRKTRSKVSGSLCVGVDPNRNWDAGFGGPGASSNPCSDSYHGPSANSEVEVKSIVDFIKSHGKVKAFITLHSYSQLLMFPYGYKCTKLDDFDELSEVAQKAAQSLRSLHGTKYKVGPICSVIYQASGGSIDWSYDYGIKYSFAFELRDTGRYGFLLPARQILPTAEETWLGLKAIMEHV |
Sequence similarities
Belongs to the peptidase M14 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length419
- Mass (Da)47,030
- Last updated2010-04-20 v3
- Checksum00269F2AE50CA38D
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
J3QT58 | J3QT58_HUMAN | CPA2 | 182 |
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 19 | in Ref. 7; AA sequence | ||||
Sequence: L → S | ||||||
Sequence conflict | 39 | in Ref. 7; AA sequence | ||||
Sequence: K → N | ||||||
Sequence conflict | 304 | in Ref. 4; AAA74425 | ||||
Sequence: T → I |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC024085 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH236950 EMBL· GenBank· DDBJ | EAL24092.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
BC007009 EMBL· GenBank· DDBJ | AAH07009.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC014571 EMBL· GenBank· DDBJ | AAH14571.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC015140 EMBL· GenBank· DDBJ | AAH15140.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
U19977 EMBL· GenBank· DDBJ | AAA74425.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BT007403 EMBL· GenBank· DDBJ | AAP36067.1 EMBL· GenBank· DDBJ | mRNA |