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 16-JUN-2009, entry version 67. 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; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 17-31 AND RP 152-160. RC TISSUE=Liver; RX MEDLINE=93203287; PubMed=8454653; 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 RT intermediate stage in CRP evolution."; RL J. Biol. Chem. 268:6809-6815(1993). CC -!- FUNCTION: CRP displays several functions associated with host CC defense: it promotes agglutination, bacterial capsular swelling, CC phagocytosis, and complement fixation through its calcium- CC dependent binding to phosphorylcholine. CC -!- COFACTOR: Binds 2 calcium ions per subunit (By similarity). CC -!- SUBUNIT: Homodimer; disulfide-linked. It is not known if it CC assembles into a pentaxin (or pentraxin) structure. Pentaxins have CC a discoid arrangement of 5 non-covalently bound subunits. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- DEVELOPMENTAL STAGE: Is initially detected at the late tail bud CC stage when the liver appears. CC -!- PTM: Cys-89 or Cys-223 or Cys-236 could be involved in interchain CC disulfide linkage. CC -!- SIMILARITY: Belongs to the pentaxin family. CC -!- SIMILARITY: Contains 1 pentaxin domain. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=No more Christmas CC pudding? - Issue 30 of January 2003; CC URL="http://www.expasy.org/spotlight/back_issues/sptlt030.shtml"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L08166; AAA49692.1; -; Genomic_DNA. DR PIR; A45487; A45487. DR HSSP; P02741; 1B09. DR HOVERGEN; Q07203; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW. DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW. DR InterPro; IPR013320; ConA-like_subgrp. DR InterPro; IPR001759; Pentaxin. DR Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 1. DR Pfam; PF00354; Pentaxin; 1. DR PRINTS; PR00895; PENTAXIN. DR ProDom; PD002153; Pentaxin; 1. DR SMART; SM00159; PTX; 1. DR PROSITE; PS00289; PENTAXIN; 1. PE 1: Evidence at protein level; KW Acute phase; Calcium; Direct protein sequencing; Disulfide bond; KW Metal-binding; Pyrrolidone carboxylic acid; Secreted; Signal. FT SIGNAL 1 16 FT CHAIN 17 238 C-reactive protein. FT /FTId=PRO_0000023536. FT DOMAIN 17 238 Pentaxin. FT METAL 76 76 Calcium 1 (By similarity). FT METAL 77 77 Calcium 1 (By similarity). FT METAL 154 154 Calcium 1 (By similarity). FT METAL 154 154 Calcium 2 (By similarity). FT METAL 155 155 Calcium 1; via carbonyl oxygen (By FT similarity). FT METAL 156 156 Calcium 1 (By similarity). FT METAL 156 156 Calcium 2 (By similarity). FT METAL 166 166 Calcium 2 (By similarity). FT MOD_RES 17 17 Pyrrolidone carboxylic acid (By FT similarity). FT DISULFID 52 113 By similarity. FT VARIANT 40 40 P -> A. FT VARIANT 66 66 L -> F. FT VARIANT 151 151 Q -> L. FT VARIANT 181 181 V -> I. 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 //