P02742 · CRP_RABIT
- ProteinC-reactive protein
- GeneCRP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids225 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells (By similarity).
Miscellaneous
Asp-61, Arg-76, Arg-77, and Glu-81 may be involved in the calcium-dependent binding of phosphorylcholine, a property that may be important for the biological function of this protein.
Cofactor
Note: Binds 2 calcium ions per subunit.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Molecular Function | complement component C1q complex binding | |
Molecular Function | low-density lipoprotein particle binding | |
Molecular Function | metal ion binding | |
Biological Process | acute-phase response | |
Biological Process | innate immune response | |
Biological Process | regulation of interleukin-8 production |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameC-reactive protein
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus
Accessions
- Primary accessionP02742
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 62 | |||||
Sequence: L → K | ||||||
Natural variant | 89 | |||||
Sequence: D → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MEKLLWCFLTLVSFSNMSDQ | ||||||
Chain | PRO_0000023531 | 21-225 | C-reactive protein | |||
Sequence: AGMHKKAFVFPKESDNSYVSLNAQLKKPLKAFTVCLYFYTDLSMTRGYSIFSYATRRQFNEILLFWSKDIGYSFSVGGDEIIFKVSDIPVDPTHLCASWESSTGIAELWVDGKPMVRKSLKKGYILGPEASIILGQDQDSFGGSFEKQQSLVGDIGNVNMWDYALSPEEINTIYAGGTFSPNVLDWRELTYQVRGEVHVKPQLWP | ||||||
Disulfide bond | 55↔116 | |||||
Sequence: CLYFYTDLSMTRGYSIFSYATRRQFNEILLFWSKDIGYSFSVGGDEIIFKVSDIPVDPTHLC |
Keywords
- PTM
Proteomic databases
Expression
Tissue specificity
Found in plasma.
Induction
The concentration of CRP in plasma increases greatly during acute phase response to tissue injury, infection or other inflammatory stimuli.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-225 | Pentraxin (PTX) | ||||
Sequence: HKKAFVFPKESDNSYVSLNAQLKKPLKAFTVCLYFYTDLSMTRGYSIFSYATRRQFNEILLFWSKDIGYSFSVGGDEIIFKVSDIPVDPTHLCASWESSTGIAELWVDGKPMVRKSLKKGYILGPEASIILGQDQDSFGGSFEKQQSLVGDIGNVNMWDYALSPEEINTIYAGGTFSPNVLDWRELTYQVRGEVHVKPQLWP |
Sequence similarities
Belongs to the pentraxin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length225
- Mass (Da)25,493
- Last updated1988-01-01 v1
- ChecksumC6D634FDE844438F
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 10 | in Ref. 2; AAA31206 | ||||
Sequence: T → I | ||||||
Sequence conflict | 46 | in Ref. 3; AA sequence | ||||
Sequence: K → T | ||||||
Sequence conflict | 50 | in Ref. 3; AA sequence | ||||
Sequence: K → L | ||||||
Sequence conflict | 76 | in Ref. 1; AAA75404 | ||||
Sequence: R → K | ||||||
Sequence conflict | 84-88 | in Ref. 3; AA sequence | ||||
Sequence: LFWSK → FFVKE | ||||||
Sequence conflict | 91 | in Ref. 3; AA sequence | ||||
Sequence: G → V | ||||||
Sequence conflict | 93-101 | in Ref. 3; AA sequence | ||||
Sequence: Missing | ||||||
Sequence conflict | 108 | in Ref. 2; AAA31206 | ||||
Sequence: I → V | ||||||
Sequence conflict | 167 | in Ref. 3; AA sequence | ||||
Sequence: K → W | ||||||
Sequence conflict | 177 | in Ref. 3; AA sequence | ||||
Sequence: N → D | ||||||
Sequence conflict | 193 | in Ref. 2; AAA31206 | ||||
Sequence: I → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M14538 EMBL· GenBank· DDBJ | AAA75403.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L47237 EMBL· GenBank· DDBJ | AAA75404.1 EMBL· GenBank· DDBJ | mRNA | ||
M13497 EMBL· GenBank· DDBJ | AAA31206.1 EMBL· GenBank· DDBJ | mRNA |