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Q07203 (CRP_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-reactive protein

Short name=CRP
Gene names
Name:crp
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length238 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

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

Secreted.

Developmental stage

Is initially detected at the late tail bud stage when the liver appears. Ref.1

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 processAcute phase
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Pyrrolidone carboxylic acid
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.1
Chain17 – 238222C-reactive protein
PRO_0000023536

Regions

Domain17 – 238222Pentaxin

Sites

Metal binding761Calcium 1 By similarity
Metal binding771Calcium 1 By similarity
Metal binding1541Calcium 1 By similarity
Metal binding1541Calcium 2 By similarity
Metal binding1551Calcium 1; via carbonyl oxygen By similarity
Metal binding1561Calcium 1 By similarity
Metal binding1561Calcium 2 By similarity
Metal binding1661Calcium 2 By similarity

Amino acid modifications

Modified residue171Pyrrolidone carboxylic acid By similarity
Disulfide bond52 ↔ 113 By similarity

Natural variations

Natural variant401P → A. Ref.1
Natural variant661L → F. Ref.1
Natural variant1511Q → L. Ref.1
Natural variant1811V → I. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q07203 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 495875AA4E2986A6

FASTA23827,085
        10         20         30         40         50         60 
MERFALWFIF LAGSLAQEDL VGNVFLFPKP SVTTYAILKP EVEKPLKNLT VCLRSYTTLT 

        70         80         90        100        110        120 
RFHSLLSLAT SNPLQDNAFL LFSKPPNQCS IYINQEENVF KVDPTAVEWK HTCVSWDSVS 

       130        140        150        160        170        180 
GVVELWIDGK LYPRTVSKKA SSIGFPSSII QGQEQDSFGG GFNIDQSFVG EISDVHMWDY 

       190        200        210        220        230 
VLTPDHIQKV LFANMDFNGN IISWRSLQYE LRGQATTQPK RQCKTLEHHY GLFAKCYK 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 17-31 AND 152-160, DEVELOPMENTAL STAGE, VARIANTS ALA-40; PHE-66; LEU-151 AND ILE-181.
Tissue: Liver.

Web resources

Protein Spotlight

No more Christmas pudding? - Issue 30 of January 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L08166 Genomic DNA. Translation: AAA49692.1.
PIRA45487.
RefSeqNP_001165686.1. NM_001172215.1.
UniGeneXl.87595.

3D structure databases

ProteinModelPortalQ07203.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100337615.
KEGGxla:100337615.

Organism-specific databases

CTD100337615.
XenbaseXB-GENE-6464307. crp.4.

Phylogenomic databases

HOVERGENHBG005405.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR001759. Pentaxin.
[Graphical view]
PfamPF00354. Pentaxin. 1 hit.
[Graphical view]
PRINTSPR00895. PENTAXIN.
SMARTSM00159. PTX. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS00289. PENTAXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCRP_XENLA
AccessionPrimary (citable) accession number: Q07203
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: February 19, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries