Reviewed,
UniProtKB/Swiss-Prot Q9N2D4 (PEPA_CALJA)
Last modified
February 9, 2010.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Pepsin A EC=3.4.23.1 | ||
| Gene names |
| ||
| Organism | Callithrix jacchus (Common marmoset) | ||
| Taxonomic identifier | 9483 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Platyrrhini › Cebidae › Callitrichinae › Callithrix |
Protein attributes
| Sequence length | 387 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 | Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent. Ref.1 |
| Catalytic activity | Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin. |
| Enzyme regulation | Inhibited by pepstatin. Ref.1 |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase A1 family. |
| Biophysicochemical properties | pH dependence: Optimum pH is about 2. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Digestion |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Aspartyl protease Hydrolase Protease |
| PTM | Disulfide bond Phosphoprotein Zymogen |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | digestion Inferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: InterPro |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 15 | 15 | Ref.1 | ||||||||
| Propeptide | 16 – 61 | 46 | Activation peptide By similarity | PRO_0000026009 | |||||||
| Chain | 62 – 387 | 326 | Pepsin A | PRO_0000026010 | |||||||
Sites | |||||||||||
| Active site | 93 | 1 | By similarity | ||||||||
| Active site | 276 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 129 | 1 | Phosphoserine By similarity | ||||||||
| Disulfide bond | 106 ↔ 111 | By similarity | |||||||||
| Disulfide bond | 267 ↔ 271 | By similarity | |||||||||
| Disulfide bond | 310 ↔ 343 | By similarity | |||||||||
Sequences
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References
| [1] | "New World monkey pepsinogens A and C, and prochymosins. Purification, characterization of enzymatic properties, cDNA cloning, and molecular evolution." Kageyama T. J. Biochem. 127:761-770(2000) [PubMed: 10788784] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 16-25, FUNCTION, ENZYME REGULATION. Tissue: Gastric mucosa. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB038384 mRNA. Translation: BAA90871.1. |
| PIR | JC7245. |
3D structure databases | |
| SMR | Q9N2D4. Positions 16-387. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | A01.001. |
Genome annotation databases | |
| Ensembl | ENSCJAT00000038063; ENSCJAP00000036045; ENSCJAG00000019394; Callithrix jacchus. [Genome view] |
Phylogenomic databases | |
| HOVERGEN | Q9N2D4. |
Enzyme and pathway databases | |
| BRENDA | 3.4.23.1. 265156. |
Family and domain databases | |
| InterPro | IPR001461. Peptidase_A1. IPR021109. Peptidase_aspartic. IPR001969. Peptidase_aspartic_AS. IPR009007. Peptidase_aspartic_catalytic. IPR012848. Propep_A1. [Graphical view] |
| Gene3D | G3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits. |
| PANTHER | PTHR13683. Peptidase_A1. 1 hit. |
| Pfam | PF07966. A1_Propeptide. 1 hit. PF00026. Asp. 1 hit. [Graphical view] |
| PRINTS | PR00792. PEPSIN. |
| PROSITE | PS00141. ASP_PROTEASE. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PEPA_CALJA | ||||||||
| Accession | Primary (citable) accession number: Q9N2D4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


