ID SAMP_MESAU Reviewed; 234 AA.
AC P07629;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 24-JAN-2024, entry version 120.
DE RecName: Full=Serum amyloid P-component;
DE AltName: Full=Female protein;
DE Short=FP;
DE AltName: Full=SAP(FP);
DE Flags: Precursor;
GN Name=APCS; Synonyms=PTX2, SAP;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=7691816; DOI=10.1016/s0021-9258(20)80608-5;
RA Rudnick C.M., Dowton S.B.;
RT "Serum amyloid P (female protein) of the Syrian hamster. Gene structure and
RT expression.";
RL J. Biol. Chem. 268:21760-21769(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-234.
RX PubMed=2408337; DOI=10.1126/science.2408337;
RA Dowton S.B., Woods D.E., Mantzouranis E.C., Colten H.R.;
RT "Syrian hamster female protein: analysis of female protein primary
RT structure and gene expression.";
RL Science 228:1206-1208(1985).
RN [3]
RP PROTEIN SEQUENCE OF 25-48.
RX PubMed=6166709; DOI=10.1084/jem.153.4.977;
RA Coe J.E., Margossian S.S., Slayter H.S., Sogn J.A.;
RT "Hamster female protein. A new Pentraxin structurally and functionally
RT similar to C-reactive protein and amyloid P component.";
RL J. Exp. Med. 153:977-991(1981).
RN [4]
RP 3D-STRUCTURE MODELING.
RX PubMed=7881902; DOI=10.1016/s0969-2126(94)00105-7;
RA Srinivasan N., White H.E., Emsley J., Wood S.P., Pepys M.B., Blundell T.L.;
RT "Comparative analyses of pentraxins: implications for protomer assembly and
RT ligand binding.";
RL Structure 2:1017-1027(1994).
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; L22024; AAA03577.1; -; Unassigned_DNA.
DR EMBL; M11342; AAA36980.1; -; mRNA.
DR PIR; A19828; A19828.
DR PIR; A44177; A44177.
DR PIR; A48593; A48593.
DR AlphaFoldDB; P07629; -.
DR SMR; P07629; -.
DR STRING; 10036.ENSMAUP00000010068; -.
DR UniLectin; P07629; -.
DR GlyCosmos; P07629; 1 site, No reported glycans.
DR eggNOG; ENOG502S201; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
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; C-REACTIVE PROTEIN-RELATED; 1.
DR PANTHER; PTHR45869:SF5; SERUM AMYLOID P-COMPONENT; 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 1: Evidence at protein level;
KW Acute phase; Amyloid; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Lectin; Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..234
FT /note="Serum amyloid P-component"
FT /id="PRO_0000023539"
FT DOMAIN 27..226
FT /note="Pentraxin (PTX)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CONFLICT 27
FT /note="T -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="K -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="A -> T (in Ref. 2; AAA36980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 26463 MW; 6161F0383062D2DB CRC64;
MDKLLSLLGV SILAGLLLEA FAQTDLTGKV FVFPRQSETD YVKLIPRLDK PLQNFTVCFR
AYSDLSRPHS LFSYNAEYGE NELLIYKERI GEYELYIGNQ GTKVHGVEEF ASPVHFCTSW
ESSSGIAEFW VNGKPWVKKG LQKGYTVKNK PSIILGQEQD NYGGGFDNYQ SFVGEIGDLN
MWDSVLTPEE IKSVYQGVPL EPNILDWQAL NYEMNGYAVI RPRCVALSSY NKIS
//
