ID H6X2W4_RAT Unreviewed; 230 AA.
AC H6X2W4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Pentraxin family member {ECO:0000256|RuleBase:RU362112};
GN Name=Crp {ECO:0000313|RGD:2411};
GN Synonyms=crp {ECO:0000313|EMBL:AFA37863.1};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|EMBL:AFA37863.1};
RN [1] {ECO:0000313|EMBL:AFA37863.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RnYan-06 {ECO:0000313|EMBL:AFA37863.1};
RX PubMed=22306119; DOI=10.1016/j.febslet.2012.01.048;
RA Li Y., Robins J.H., Ye J., Huang Z., Wen Q., Zhang G.;
RT "Adaptive diversity of innate immune receptor family short pentraxins in
RT Murinae.";
RL FEBS Lett. 586:798-803(2012).
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. Can interact with DNA and histones and may scavenge
CC nuclear material released from damaged circulating cells.
CC {ECO:0000256|ARBA:ARBA00037561}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|RuleBase:RU362112};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|RuleBase:RU362112};
CC -!- SUBUNIT: Homopentamer. Pentaxin (or pentraxin) have a discoid
CC arrangement of 5 non-covalently bound subunits.
CC {ECO:0000256|RuleBase:RU362112}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU362112}.
CC -!- SIMILARITY: Belongs to the pentraxin family.
CC {ECO:0000256|ARBA:ARBA00038102, ECO:0000256|RuleBase:RU362112}.
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DR EMBL; JQ438891; AFA37863.1; -; Genomic_DNA.
DR AlphaFoldDB; H6X2W4; -.
DR RGD; 2411; Crp.
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 Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR030476; Pentaxin_CS.
DR InterPro; IPR001759; Pentraxin-related.
DR PANTHER; PTHR45869:SF7; C-REACTIVE PROTEIN; 1.
DR PANTHER; PTHR45869; C-REACTIVE PROTEIN-RELATED; 1.
DR Pfam; PF00354; Pentaxin; 1.
DR PRINTS; PR00895; PENTAXIN.
DR SMART; SM00159; PTX; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00289; PTX_1; 1.
DR PROSITE; PS51828; PTX_2; 1.
PE 3: Inferred from homology;
KW Acute phase {ECO:0000256|ARBA:ARBA00022486};
KW Calcium {ECO:0000256|RuleBase:RU362112};
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU01172};
KW Metal-binding {ECO:0000256|RuleBase:RU362112};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU362112}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU362112"
FT CHAIN 20..230
FT /note="Pentraxin family member"
FT /evidence="ECO:0000256|RuleBase:RU362112"
FT /id="PRO_5005134538"
FT DISULFID 55..114
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01172"
SQ SEQUENCE 230 AA; 25436 MW; 227ED1FF788D6204 CRC64;
MEKLLWCLLI TISFSQAFGH EDVSKQAFVF PGVSATAYVS LEAESKKPLE AFTVCLYAHA
DVSRSFSIFS YATKTSFNEI LLFWTRGQGF SIAVGGPEIL FSASEIPEVP THICATWESA
TGIVELWLDG KPRVRKSLQK GYIVGTNASI ILGQEQDSYG GGFDANQSLV GDIGDVNMWD
FVLSPEQINA VYVGRVFSPN VLNWRALKYE THGDVFIKPQ LWPLTDCCES
//
