Q07203 (CRP_XENLA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
C-reactive protein
Short name=CRP

Gene names

Name:

crp

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amphibia › Batrachia › Anura › 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	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 process	Acute phase
Cellular component	Secreted
Coding sequence diversity	Polymorphism
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	metal 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. Ref.1
	Natural variant	66	1	L → F. Ref.1
	Natural variant	151	1	Q → L. Ref.1
	Natural variant	181	1	V → I. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q07203 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 495875AA4E2986A6	FASTA	238	27,085
	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

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.
PIR	A45487.
RefSeq	NP_001165686.1. NM_001172215.1.
UniGene	Xl.87595.
3D structure databases
ProteinModelPortal	Q07203.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100337615.
KEGG	xla:100337615.
Organism-specific databases
CTD	100337615.
Xenbase	XB-GENE-6464307. crp.4.
Phylogenomic databases
HOVERGEN	HBG005405.
Family and domain databases
Gene3D	2.60.120.200. 1 hit.
InterPro	IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR001759. Pentaxin. [Graphical view]
Pfam	PF00354. Pentaxin. 1 hit. [Graphical view]
PRINTS	PR00895. PENTAXIN.
SMART	SM00159. PTX. 1 hit. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS00289. PENTAXIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CRP_XENLA

Accession

Primary (citable) accession number: Q07203

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	May 29, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program