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P02742

- CRP_RABIT

UniProt

P02742 - CRP_RABIT

Protein

C-reactive protein

Gene

CRP

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    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. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells By similarity.By similarity

    Cofactori

    Binds 2 calcium ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi80 – 801Calcium 1By similarity
    Metal bindingi158 – 1581Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi159 – 1591Calcium 1By similarity
    Metal bindingi159 – 1591Calcium 2By similarity
    Metal bindingi169 – 1691Calcium 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. acute-phase response Source: UniProtKB-KW
    2. regulation of interleukin-8 secretion Source: UniProtKB

    Keywords - Biological processi

    Acute phase

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    C-reactive protein
    Gene namesi
    Name:CRP
    Synonyms:PTX1
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20201 PublicationAdd
    BLAST
    Chaini21 – 225205C-reactive protein1 PublicationPRO_0000023531Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi55 ↔ 1161 Publication

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Found in plasma.

    Inductioni

    The concentration of CRP in plasma increases greatly during acute phase response to tissue injury, infection or other inflammatory stimuli.

    Interactioni

    Subunit structurei

    Homopentamer. Pentaxin (or pentraxin) have a discoid arrangement of 5 non-covalently bound subunits. Interacts with FCN1; may regulate monocyte activation by FCN1 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000004059.

    Structurei

    3D structure databases

    ProteinModelPortaliP02742.
    SMRiP02742. Positions 20-225.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 225205PentaxinAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG113288.
    HOGENOMiHOG000247043.
    HOVERGENiHBG005405.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR001759. Pentaxin.
    [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.

    P02742-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKLLWCFLT LVSFSNMSDQ AGMHKKAFVF PKESDNSYVS LNAQLKKPLK    50
    AFTVCLYFYT DLSMTRGYSI FSYATRRQFN EILLFWSKDI GYSFSVGGDE 100
    IIFKVSDIPV DPTHLCASWE SSTGIAELWV DGKPMVRKSL KKGYILGPEA 150
    SIILGQDQDS FGGSFEKQQS LVGDIGNVNM WDYALSPEEI NTIYAGGTFS 200
    PNVLDWRELT YQVRGEVHVK PQLWP 225
    Length:225
    Mass (Da):25,493
    Last modified:January 1, 1988 - v1
    Checksum:iC6D634FDE844438F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101T → I in AAA31206. (PubMed:3007506)Curated
    Sequence conflicti46 – 461K → T AA sequence (PubMed:6754715)Curated
    Sequence conflicti50 – 501K → L AA sequence (PubMed:6754715)Curated
    Sequence conflicti76 – 761R → K in AAA75404. (PubMed:3026463)Curated
    Sequence conflicti84 – 885LFWSK → FFVKE AA sequence (PubMed:6754715)Curated
    Sequence conflicti91 – 911G → V AA sequence (PubMed:6754715)Curated
    Sequence conflicti93 – 1019Missing AA sequence (PubMed:6754715)Curated
    Sequence conflicti108 – 1081I → V in AAA31206. (PubMed:3007506)Curated
    Sequence conflicti167 – 1671K → W AA sequence (PubMed:6754715)Curated
    Sequence conflicti177 – 1771N → D AA sequence (PubMed:6754715)Curated
    Sequence conflicti193 – 1931I → V in AAA31206. (PubMed:3007506)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti62 – 621L → K.
    Natural varianti89 – 891D → V.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14538 Genomic DNA. Translation: AAA75403.1.
    L47237 mRNA. Translation: AAA75404.1.
    M13497 mRNA. Translation: AAA31206.1.
    PIRiA25605. CJRB.
    RefSeqiNP_001075734.1. NM_001082265.1.
    UniGeneiOcu.1848.

    Genome annotation databases

    GeneIDi100009091.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    No more Christmas pudding? - Issue 30 of January 2003

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14538 Genomic DNA. Translation: AAA75403.1 .
    L47237 mRNA. Translation: AAA75404.1 .
    M13497 mRNA. Translation: AAA31206.1 .
    PIRi A25605. CJRB.
    RefSeqi NP_001075734.1. NM_001082265.1.
    UniGenei Ocu.1848.

    3D structure databases

    ProteinModelPortali P02742.
    SMRi P02742. Positions 20-225.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9986.ENSOCUP00000004059.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100009091.

    Organism-specific databases

    CTDi 1401.

    Phylogenomic databases

    eggNOGi NOG113288.
    HOGENOMi HOG000247043.
    HOVERGENi HBG005405.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR001759. Pentaxin.
    [Graphical view ]
    Pfami PF00354. Pentaxin. 1 hit.
    [Graphical view ]
    PRINTSi PR00895. PENTAXIN.
    SMARTi SM00159. PTX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS00289. PENTAXIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of the gene for rabbit C-reactive protein."
      Hu S.-I., Miller S.M., Samols D.
      Biochemistry 25:7834-7839(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: New Zealand white.
      Tissue: Liver.
    2. "Rabbit C-reactive protein. Biosynthesis and characterization of cDNA clones."
      Syin C., Gotschlich E.C., Liu T.-Y.
      J. Biol. Chem. 261:5473-5479(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Primary structure of rabbit C-reactive protein."
      Wang C.-M., Nguyen N.Y., Yonaha K., Robey F., Liu T.-Y.
      J. Biol. Chem. 257:13610-13615(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-225.

    Entry informationi

    Entry nameiCRP_RABIT
    AccessioniPrimary (citable) accession number: P02742
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 116 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3