Reviewed,
UniProtKB/Swiss-Prot Q07203 (CRP_XENLA)
Last modified
June 16, 2009.
Version 67.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: C-reactive protein Short name=CRP | ||
| Gene names |
| ||
| Organism | Xenopus laevis (African clawed frog) | ||
| Taxonomic identifier | 8355 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus |
Protein attributes
| Sequence length | 238 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 | CRP displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis, and complement fixation through its calcium-dependent binding to phosphorylcholine. |
| Cofactor | Binds 2 calcium ions per subunit By similarity. |
| Subunit structure | Homodimer; disulfide-linked. It is not known if it assembles into a pentaxin (or pentraxin) structure. Pentaxins have a discoid arrangement of 5 non-covalently bound subunits. |
| Subcellular location | |
| Developmental stage | Is initially detected at the late tail bud stage when the liver appears. |
| Post-translational modification | Cys-89 or Cys-223 or Cys-236 could be involved in interchain disulfide linkage. |
| Sequence similarities | Belongs to the pentaxin family. Contains 1 pentaxin domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Acute phase |
| Cellular component | Secreted |
| Domain | Signal |
| Ligand | Calcium Metal-binding |
| PTM | Disulfide bond Pyrrolidone carboxylic acid |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | acute-phase response Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | calcium ion binding 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 – 16 | 16 | Ref.1 | ||||||||
| Chain | 17 – 238 | 222 | C-reactive protein | PRO_0000023536 | |||||||
Regions | |||||||||||
| Domain | 17 – 238 | 222 | Pentaxin | ||||||||
Sites | |||||||||||
| Metal binding | 76 | 1 | Calcium 1 By similarity | ||||||||
| Metal binding | 77 | 1 | Calcium 1 By similarity | ||||||||
| Metal binding | 154 | 1 | Calcium 1 By similarity | ||||||||
| Metal binding | 154 | 1 | Calcium 2 By similarity | ||||||||
| Metal binding | 155 | 1 | Calcium 1; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 156 | 1 | Calcium 1 By similarity | ||||||||
| Metal binding | 156 | 1 | Calcium 2 By similarity | ||||||||
| Metal binding | 166 | 1 | Calcium 2 By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 17 | 1 | Pyrrolidone carboxylic acid By similarity | ||||||||
| Disulfide bond | 52 ↔ 113 | By similarity | |||||||||
Natural variations | |||||||||||
| Natural variant | 40 | 1 | P → A | ||||||||
| Natural variant | 66 | 1 | L → F | ||||||||
| Natural variant | 151 | 1 | Q → L | ||||||||
| Natural variant | 181 | 1 | V → I | ||||||||
Sequences
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References
| [1] | "Isolation and characterization of C-reactive protein (CRP) cDNA and genomic DNA from Xenopus laevis. A species representing an intermediate stage in CRP evolution." Lin L., Liu T.-Y. J. Biol. Chem. 268:6809-6815(1993) [PubMed: 8454653] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 17-31 AND 152-160. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| L08166 Genomic DNA. Translation: AAA49692.1. | |
| PIR | A45487. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1B09 based on UniProtKB P02741. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | Q07203. |
Family and domain databases | |
| InterPro | IPR013320. ConA-like_subgrp. IPR001759. Pentaxin. [Graphical view] |
| Gene3D | G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit. |
| Pfam | PF00354. Pentaxin. 1 hit. [Graphical view] |
| PRINTS | PR00895. PENTAXIN. |
| ProDom | PD002153. Pentaxin. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00159. PTX. 1 hit. [Graphical view] |
| PROSITE | PS00289. PENTAXIN. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | CRP_XENLA | ||||||||
| Accession | Primary (citable) accession number: Q07203 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Xenopus annotation project | ||||||||

Clusters with


