A7WPL7 (CMA1_CAVPO) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 30.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Chymase EC=3.4.21.39 Alternative name(s): Alpha-chymase | ||
| Gene names |
| ||
| Organism | Cavia porcellus (Guinea pig) | ||
| Taxonomic identifier | 10141 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia |
Protein attributes
| Sequence length | 247 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 | Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion By similarity. UniProtKB P23946 |
| Catalytic activity | Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa > Leu-|-Xaa. UniProtKB P23946 |
| Subcellular location | Secreted By similarity. Cytoplasmic granule By similarity. Note: Mast cell granules By similarity. UniProtKB P23946 |
| Sequence similarities | Belongs to the peptidase S1 family. Granzyme subfamily. Contains 1 peptidase S1 domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Disulfide bond Glycoprotein Zymogen |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | proteolysis 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 – 17 | 17 | Potential | ||||||||
| Propeptide | 18 – 21 | 4 | Activation peptide | PRO_0000312843 | |||||||
| Chain | 22 – 247 | 226 | Chymase Ref.2 | PRO_5000271615 | |||||||
Regions | |||||||||||
| Domain | 22 – 245 | 224 | Peptidase S1 | ||||||||
Sites | |||||||||||
| Active site | 66 | 1 | Charge relay system By similarity UniProtKB P23946 | ||||||||
| Active site | 110 | 1 | Charge relay system By similarity UniProtKB P23946 | ||||||||
| Active site | 203 | 1 | Charge relay system By similarity UniProtKB P23946 | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 103 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 121 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 51 ↔ 67 | By similarity UniProtKB P23946 | |||||||||
| Disulfide bond | 144 ↔ 209 | By similarity UniProtKB P23946 | |||||||||
| Disulfide bond | 175 ↔ 188 | By similarity UniProtKB P23946 | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 52 | 1 | G → S AA sequence Ref.2 | ||||||||
Sequences
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References
| [1] | "Guinea pig chymase is leucine-specific: a novel example of functional plasticity in the chymase/granzyme family of immune cell serine peptidases." Beauchamp J.C., Caughey G.H., Fingerle J., Schliemann K. Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart. |
| [2] | "Structural basis for elastolytic substrate specificity in rodent alpha-chymases." Kervinen J., Abad M., Crysler C., Kolpak M., Mahan A.D., Masucci J.A., Bayoumy S., Cummings M.D., Yao X., Olson M., de Garavilla L., Kuo L., Deckman I., Spurlino J. J. Biol. Chem. 283:427-436(2008) [PubMed: 17981788] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-247. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM851020 mRNA. Translation: CAO99144.1. |
| RefSeq | NP_001166403.1. NM_001172932.1. |
3D structure databases | |
| ProteinModelPortal | A7WPL7. |
| SMR | A7WPL7. Positions 22-247. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A7WPL7. |
Protein family/group databases | |
| MEROPS | S01.140. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSCPOT00000012522; ENSCPOP00000011161; ENSCPOG00000012404. |
| GeneID | 100135503. |
Organism-specific databases | |
| CTD | 1215. |
Phylogenomic databases | |
| eggNOG | roNOG06568. |
| GeneTree | ENSGT00580000081281. |
| HOVERGEN | HBG013304. |
| InParanoid | A7WPL7. |
| OrthoDB | EOG4R23VK. |
Enzyme and pathway databases | |
| BRENDA | 3.4.21.39. 1225. |
Family and domain databases | |
| InterPro | IPR009003. Pept_cys/ser_Trypsin-like. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view] |
| Pfam | PF00089. Trypsin. 1 hit. [Graphical view] |
| PRINTS | PR00722. CHYMOTRYPSIN. |
| SMART | SM00020. Tryp_SPc. 1 hit. [Graphical view] |
| SUPFAM | SSF50494. Pept_Ser_Cys. 1 hit. |
| PROSITE | PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CMA1_CAVPO | ||||||||
| Accession | Primary (citable) accession number: A7WPL7 Secondary accession number(s): P85201 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

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