P36178 (CTRB2_LITVA) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 65.
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: Chymotrypsin BII EC=3.4.21.1 |
| Organism | Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei) |
| Taxonomic identifier | 6689 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Crustacea › Malacostraca › Eumalacostraca › Eucarida › Decapoda › Dendrobranchiata › Penaeoidea › Penaeidae › Litopenaeus |
Protein attributes
| Sequence length | 271 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 | Serine protease with chymotryptic and collagenolytic activities. |
| Catalytic activity | Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa. |
| Subcellular location | |
| Sequence similarities | Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Collagen degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase Protease Serine protease |
| PTM | Disulfide bond Zymogen |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | collagen catabolic process Inferred from electronic annotation. Source: UniProtKB-KW proteolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 15 | 15 | Potential | ||||||||
| Propeptide | 16 – 45 | 30 | Activation peptide | PRO_0000027652 | |||||||
| Chain | 46 – 271 | 226 | Chymotrypsin BII | PRO_0000027653 | |||||||
Regions | |||||||||||
| Domain | 46 – 268 | 223 | Peptidase S1 | ||||||||
Sites | |||||||||||
| Active site | 86 | 1 | Charge relay system By similarity | ||||||||
| Active site | 132 | 1 | Charge relay system By similarity | ||||||||
| Active site | 223 | 1 | Charge relay system By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 71 ↔ 87 | By similarity | |||||||||
| Disulfide bond | 196 ↔ 209 | By similarity | |||||||||
| Disulfide bond | 219 ↔ 245 | By similarity | |||||||||
Sequences
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References
| [1] | "Molecular cloning of a cDNA that encodes a serine protease with chymotryptic and collagenolytic activities in the hepatopancreas of the shrimp Penaeus vanameii (Crustacea, Decapoda)." Sellos D., van Wormhoudt A. FEBS Lett. 309:219-224(1992) [PubMed: 1516690] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Tissue: Hepatopancreas. |
| [2] | "Purification, biochemical characterization and N-terminal sequence of a serine-protease with chymotrypsic and collagenolytic activities in a tropical shrimp, Penaeus vannamei (Crustacea, Decapoda)." van Wormhoudt A., le Chevalier P., Sellos D. Comp. Biochem. Physiol. 103B:675-680(1992) [PubMed: 1458841] [Abstract] Cited for: PROTEIN SEQUENCE OF 46-65, CHARACTERIZATION. Tissue: Hepatopancreas. |
| + | Additional computationally mapped references. |
Cross-references
3D structure databases | |
|---|---|
| ProteinModelPortal | P36178. |
| SMR | P36178. Positions 46-271. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | S01.122. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
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 | CTRB2_LITVA | ||||||||
| Accession | Primary (citable) accession number: P36178 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with