SAMP_PIG
ID SAMP_PIG Reviewed; 224 AA.
AC O19063;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Serum amyloid P-component;
DE Short=SAP;
DE Flags: Precursor;
GN Name=APCS;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Landrace; TISSUE=Liver;
RA Ozawa A., Matsumoto M., Kajikawa M., Hanazono M., Yasue H.;
RT "Complementary DNA sequence of porcine serum amyloid P component (SAP).";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
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 -!- DISEASE: Note=SAP is a precursor of amyloid component P which is found
CC in basement membrane and associated with amyloid deposits.
CC -!- SIMILARITY: Belongs to the pentraxin family. {ECO:0000305}.
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DR EMBL; AB005546; BAA21474.1; -; mRNA.
DR RefSeq; NP_999052.1; NM_213887.1.
DR AlphaFoldDB; O19063; -.
DR SMR; O19063; -.
DR PeptideAtlas; O19063; -.
DR PRIDE; O19063; -.
DR Ensembl; ENSSSCT00000044230; ENSSSCP00000035458; ENSSSCG00000037268.
DR Ensembl; ENSSSCT00005004288; ENSSSCP00005002541; ENSSSCG00005002808.
DR Ensembl; ENSSSCT00025007433; ENSSSCP00025003025; ENSSSCG00025005551.
DR Ensembl; ENSSSCT00035029252; ENSSSCP00035011297; ENSSSCG00035022411.
DR Ensembl; ENSSSCT00045006466; ENSSSCP00045004397; ENSSSCG00045003904.
DR Ensembl; ENSSSCT00055055822; ENSSSCP00055044564; ENSSSCG00055028179.
DR Ensembl; ENSSSCT00070054127; ENSSSCP00070045888; ENSSSCG00070026993.
DR GeneID; 396921; -.
DR KEGG; ssc:396921; -.
DR CTD; 325; -.
DR VGNC; VGNC:85407; APCS.
DR GeneTree; ENSGT01050000244822; -.
DR InParanoid; O19063; -.
DR OMA; GFDKSQS; -.
DR OrthoDB; 1088298at2759; -.
DR Proteomes; UP000008227; Chromosome 4.
DR Proteomes; UP000314985; Chromosome 4.
DR Bgee; ENSSSCG00000037268; Expressed in liver and 13 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0001849; F:complement component C1q complex binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046790; F:virion binding; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0044869; P:negative regulation by host of viral exo-alpha-sialidase activity; IEA:Ensembl.
DR GO; GO:0044871; P:negative regulation by host of viral glycoprotein metabolic process; IEA:Ensembl.
DR GO; GO:1903016; P:negative regulation of exo-alpha-sialidase activity; IEA:Ensembl.
DR GO; GO:0045656; P:negative regulation of monocyte differentiation; IEA:Ensembl.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IEA:Ensembl.
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 Amyloid; Calcium; Disulfide bond; Glycoprotein; Lectin; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..224
FT /note="Serum amyloid P-component"
FT /id="PRO_0000023543"
FT DOMAIN 24..224
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 224 AA; 25641 MW; 9D1867691EBEDC66 CRC64;
MERLLLWVSV LASLPEAFAH RDLTGKVFVF PRESATDHVK LITKLEKPLQ NFTLCFRAYS
DLSRGYSLFS YNLQGKDNEL LVFKHRIGEY SLYIGKTKVT FKVREVFPRP VHICTSWESS
TGIAEFWING EPLVKKGLRQ GYSVGAYPRI VLGQEQDSYG GGFDKTQSFV GEIGDLYMWG
SVLSPNEIRL VYQGLSFPHP TILDWQALNY EMNGYVVIKP RVWS
