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Protein

C-reactive protein

Gene

crp

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis, and complement fixation through its calcium-dependent binding to phosphorylcholine.

Cofactori

Ca2+By similarityNote: Binds 2 calcium ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi76Calcium 1By similarity1
Metal bindingi77Calcium 1By similarity1
Metal bindingi154Calcium 1By similarity1
Metal bindingi154Calcium 2By similarity1
Metal bindingi155Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi156Calcium 1By similarity1
Metal bindingi156Calcium 2By similarity1
Metal bindingi166Calcium 2By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Acute phase

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
C-reactive protein
Short name:
CRP
Gene namesi
Name:crp
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6464307. crp.4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 161 PublicationAdd BLAST16
ChainiPRO_000002353617 – 238C-reactive proteinAdd BLAST222

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17Pyrrolidone carboxylic acidBy similarity1
Disulfide bondi52 ↔ 113By similarity

Post-translational modificationi

Cys-89 or Cys-223 or Cys-236 could be involved in interchain disulfide linkage.

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Expressioni

Developmental stagei

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

Interactioni

Subunit structurei

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.

Structurei

3D structure databases

ProteinModelPortaliQ07203.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 238PentaxinAdd BLAST222

Sequence similaritiesi

Belongs to the pentaxin family.Curated
Contains 1 pentaxin domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG005405.

Family and domain databases

CDDicd00152. PTX. 1 hit.
Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001759. Pentaxin-related.
IPR030476. Pentaxin_CS.
[Graphical view]
PfamiPF00354. Pentaxin. 1 hit.
[Graphical view]
PRINTSiPR00895. PENTAXIN.
SMARTiSM00159. PTX. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00289. PENTAXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q07203-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERFALWFIF LAGSLAQEDL VGNVFLFPKP SVTTYAILKP EVEKPLKNLT
60 70 80 90 100
VCLRSYTTLT RFHSLLSLAT SNPLQDNAFL LFSKPPNQCS IYINQEENVF
110 120 130 140 150
KVDPTAVEWK HTCVSWDSVS GVVELWIDGK LYPRTVSKKA SSIGFPSSII
160 170 180 190 200
QGQEQDSFGG GFNIDQSFVG EISDVHMWDY VLTPDHIQKV LFANMDFNGN
210 220 230
IISWRSLQYE LRGQATTQPK RQCKTLEHHY GLFAKCYK
Length:238
Mass (Da):27,085
Last modified:October 1, 1994 - v1
Checksum:i495875AA4E2986A6
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti40P → A.1 Publication1
Natural varianti66L → F.1 Publication1
Natural varianti151Q → L.1 Publication1
Natural varianti181V → I.1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08166 Genomic DNA. Translation: AAA49692.1.
PIRiA45487.
RefSeqiNP_001165686.1. NM_001172215.1.
UniGeneiXl.87595.

Genome annotation databases

GeneIDi100337615.
KEGGixla:100337615.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Protein Spotlight

No more Christmas pudding? - Issue 30 of January 2003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08166 Genomic DNA. Translation: AAA49692.1.
PIRiA45487.
RefSeqiNP_001165686.1. NM_001172215.1.
UniGeneiXl.87595.

3D structure databases

ProteinModelPortaliQ07203.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100337615.
KEGGixla:100337615.

Organism-specific databases

CTDi100337615.
XenbaseiXB-GENE-6464307. crp.4.

Phylogenomic databases

HOVERGENiHBG005405.

Family and domain databases

CDDicd00152. PTX. 1 hit.
Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001759. Pentaxin-related.
IPR030476. Pentaxin_CS.
[Graphical view]
PfamiPF00354. Pentaxin. 1 hit.
[Graphical view]
PRINTSiPR00895. PENTAXIN.
SMARTiSM00159. PTX. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00289. PENTAXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCRP_XENLA
AccessioniPrimary (citable) accession number: Q07203
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 30, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.