ID   PXN1_XENLA              Reviewed;         416 AA.
AC   P49263;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Pentraxin fusion protein;
DE   Flags: Precursor;
GN   Name=pxn1;
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 [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7694301; DOI=10.1098/rspb.1993.0112;
RA   Seery L.T., Schoenberg D.R., Barbaux S., Sharp P.M., Whitehead A.S.;
RT   "Identification of a novel member of the pentraxin family in Xenopus
RT   laevis.";
RL   Proc. R. Soc. B 253:263-270(1993).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000250};
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DR   EMBL; L19881; AAC38013.1; -; mRNA.
DR   AlphaFoldDB; P49263; -.
DR   SMR; P49263; -.
DR   CAZy; CBM47; Carbohydrate-Binding Module Family 47.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0042806; F:fucose binding; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0010185; P:regulation of cellular defense response; IEA:UniProt.
DR   GO; GO:0001868; P:regulation of complement activation, lectin pathway; IEA:UniProt.
DR   CDD; cd00152; PTX; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR006585; FTP1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR030476; Pentaxin_CS.
DR   InterPro; IPR001759; Pentraxin-related.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF00354; Pentaxin; 1.
DR   PRINTS; PR00895; PENTAXIN.
DR   SMART; SM00607; FTP; 1.
DR   SMART; SM00159; PTX; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00289; PTX_1; 1.
DR   PROSITE; PS51828; PTX_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Glycoprotein; Metal-binding; Reference proteome;
KW   Signal.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..416
FT                   /note="Pentraxin fusion protein"
FT                   /id="PRO_0000023554"
FT   DOMAIN          220..416
FT                   /note="Pentraxin (PTX)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   REGION          184..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         275
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         353
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         354
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         354
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         364
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        129
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        251..311
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
SQ   SEQUENCE   416 AA;  47242 MW;  62EDE45E913A2BD7 CRC64;
     MKSLLLFLKS QVFGLTVETL NGERNGDFEQ QKENHGAKNV APQGIPYQSS YYGQKEQAKR
     VIDGSLASNY MEGDCCHTEK QMHPWWQLDM KSKMRVHSVA ITNRGDCCRE RINGAEIRIG
     NSKKEGGLNS TRCGVVFKMN YEETLSFNCK ELEGRYVTVT IPDRIEYLTL CEVQVFADPL
     EVDGTEASDS SESVDGTEAP ASPESDVELP IASGMNVDLT NKSFMFPKES DINHVKLLPE
     KAMSLKAFTL CMKVLLNVPE NRETILFSYR TMFYDELNLW IERDGRIGLY MSGDGIIFPR
     MKFKSEWNHL CLTWESKYGR TEFWLNGRRS ATKVYHQKNT VRSGGIVLLG QDQDSYGGDF
     DKTQSFVGQI KDLKMWNKVL PLRSLKSLFK GREIGNGNIF DWSSLSYSMI GNVAEV