CRP_XENLA
ID CRP_XENLA Reviewed; 238 AA.
AC Q07203;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=C-reactive protein;
DE Short=CRP;
DE Flags: Precursor;
GN Name=crp;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 17-31 AND 152-160,
RP DEVELOPMENTAL STAGE, AND VARIANTS ALA-40; PHE-66; LEU-151 AND ILE-181.
RC TISSUE=Liver;
RX PubMed=8454653; DOI=10.1016/s0021-9258(18)53321-4;
RA Lin L., Liu T.-Y.;
RT "Isolation and characterization of C-reactive protein (CRP) cDNA and
RT genomic DNA from Xenopus laevis. A species representing an intermediate
RT stage in CRP evolution.";
RL J. Biol. Chem. 268:6809-6815(1993).
CC -!- FUNCTION: Displays several functions associated with host defense: it
CC promotes agglutination, bacterial capsular swelling, phagocytosis, and
CC complement fixation through its calcium-dependent binding to
CC phosphorylcholine.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer; disulfide-linked. It is not known if it assembles
CC into a pentraxin (or pentaxin) structure. Pentaxins have a discoid
CC arrangement of 5 non-covalently bound subunits.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DEVELOPMENTAL STAGE: Is initially detected at the late tail bud stage
CC when the liver appears. {ECO:0000269|PubMed:8454653}.
CC -!- PTM: Cys-89 or Cys-223 or Cys-236 could be involved in interchain
CC disulfide linkage.
CC -!- SIMILARITY: Belongs to the pentraxin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=No more Christmas pudding?
CC - Issue 30 of January 2003;
CC URL="https://web.expasy.org/spotlight/back_issues/030";
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DR EMBL; L08166; AAA49692.1; -; Genomic_DNA.
DR PIR; A45487; A45487.
DR RefSeq; NP_001165686.1; NM_001172215.1.
DR AlphaFoldDB; Q07203; -.
DR SMR; Q07203; -.
DR DNASU; 444374; -.
DR GeneID; 444374; -.
DR KEGG; xla:444374; -.
DR CTD; 444374; -.
DR Xenbase; XB-GENE-6464307; crp.4.L.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 444374; Expressed in spleen and 15 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR CDD; cd00152; PTX; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR030476; Pentaxin_CS.
DR InterPro; IPR001759; Pentraxin-related.
DR Pfam; PF00354; Pentaxin; 1.
DR PRINTS; PR00895; PENTAXIN.
DR SMART; SM00159; PTX; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00289; PTX_1; 1.
DR PROSITE; PS51828; PTX_2; 1.
PE 1: Evidence at protein level;
KW Acute phase; Calcium; Direct protein sequencing; Disulfide bond;
KW Metal-binding; Pyrrolidone carboxylic acid; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:8454653"
FT CHAIN 17..238
FT /note="C-reactive protein"
FT /id="PRO_0000023536"
FT DOMAIN 21..223
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT MOD_RES 17
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT DISULFID 52..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT VARIANT 40
FT /note="P -> A"
FT /evidence="ECO:0000269|PubMed:8454653"
FT VARIANT 66
FT /note="L -> F"
FT /evidence="ECO:0000269|PubMed:8454653"
FT VARIANT 151
FT /note="Q -> L"
FT /evidence="ECO:0000269|PubMed:8454653"
FT VARIANT 181
FT /note="V -> I"
FT /evidence="ECO:0000269|PubMed:8454653"
SQ SEQUENCE 238 AA; 27085 MW; 495875AA4E2986A6 CRC64;
MERFALWFIF LAGSLAQEDL VGNVFLFPKP SVTTYAILKP EVEKPLKNLT VCLRSYTTLT
RFHSLLSLAT SNPLQDNAFL LFSKPPNQCS IYINQEENVF KVDPTAVEWK HTCVSWDSVS
GVVELWIDGK LYPRTVSKKA SSIGFPSSII QGQEQDSFGG GFNIDQSFVG EISDVHMWDY
VLTPDHIQKV LFANMDFNGN IISWRSLQYE LRGQATTQPK RQCKTLEHHY GLFAKCYK
