ID   FP_CRIMI                Reviewed;         231 AA.
AC   P15697;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Female protein;
DE            Short=FP;
DE   AltName: Full=Serum amyloid P-component;
DE   Flags: Precursor;
OS   Cricetulus migratorius (Gray dwarf hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10032;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2479691;
RA   Dowton S.B., Waggoner D.J.;
RT   "Armenian hamster female protein (serum amyloid P component). Comparison
RT   with the sex-regulated homolog in Syrian hamster.";
RL   J. Immunol. 143:3776-3780(1989).
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: Homopentamer. Pentraxin (or pentaxin) have a discoid
CC       arrangement of 5 non-covalently bound subunits.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MISCELLANEOUS: Plasma concentration of FP are altered by sex steroids
CC       and by stimuli that elicit an acute phase response.
CC   -!- SIMILARITY: Belongs to the pentraxin family. {ECO:0000305}.
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DR   EMBL; M31610; AAA36981.1; -; mRNA.
DR   PIR; A45814; A45814.
DR   AlphaFoldDB; P15697; -.
DR   SMR; P15697; -.
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   2: Evidence at transcript level;
KW   Acute phase; Calcium; Disulfide bond; Glycoprotein; Metal-binding;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT   CHAIN           20..231
FT                   /note="Female protein"
FT                   /id="PRO_0000023537"
FT   DOMAIN          24..223
FT                   /note="Pentraxin (PTX)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   BINDING         77
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   BINDING         78
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
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:0000255|PROSITE-ProRule:PRU01172"
FT   BINDING         155
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   BINDING         156
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   BINDING         157
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   BINDING         157
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   BINDING         167
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        55..114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
SQ   SEQUENCE   231 AA;  26353 MW;  A4D12A9DDE70B823 CRC64;
     MDKMLLLLGV SILLSEVFAQ TDLTGKVFVF PRESESDYVK LIPRLEKPLE NFTLCFRTYT
     DLSRPHSLFS YNTKNKDNEL LIYKERMGEY GLYIENLGAI VRGVEEFASP VHFCTSWESS
     SGIAEFWVNG IPWVKKGLKK GYTVKTQPSI ILGQEQDNYG GGFDKSQSFV GEMGDLNMWD
     SVLTPEEIKS VYEGSWLEAN ILDWRTLNYE MSGYAVIRPR CVALSSYNKI S