SAMP_CAVPO
ID SAMP_CAVPO Reviewed; 223 AA.
AC P49255;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Serum amyloid P-component;
DE Short=SAP;
DE Flags: Precursor;
GN Name=PTX2; Synonyms=SAP;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Hartley;
RX PubMed=8486600; DOI=10.1093/oxfordjournals.jbchem.a124039;
RA Rubio N., Sharp P.M., Rits M., Zahedi K., Whitehead A.S.;
RT "Structure, expression, and evolution of guinea pig serum amyloid P
RT component and C-reactive protein.";
RL J. Biochem. 113:277-284(1993).
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 -!- SIMILARITY: Belongs to the pentraxin family. {ECO:0000305}.
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DR EMBL; S60421; AAC60661.1; -; Genomic_DNA.
DR PIR; JX0260; JX0260.
DR RefSeq; XP_003466600.1; XM_003466552.2.
DR AlphaFoldDB; P49255; -.
DR SMR; P49255; -.
DR STRING; 10141.ENSCPOP00000019069; -.
DR Ensembl; ENSCPOT00000022170; ENSCPOP00000019069; ENSCPOG00000009766.
DR GeneID; 100726823; -.
DR KEGG; cpoc:100726823; -.
DR CTD; 325; -.
DR eggNOG; ENOG502S201; Eukaryota.
DR GeneTree; ENSGT01050000244822; -.
DR HOGENOM; CLU_032051_2_0_1; -.
DR InParanoid; P49255; -.
DR OMA; GFDKSQS; -.
DR OrthoDB; 1088298at2759; -.
DR TreeFam; TF330208; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000009766; Expressed in liver and 1 other tissue.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0001849; F:complement component C1q complex binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046790; F:virion binding; IEA:Ensembl.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:Ensembl.
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 3: Inferred from homology;
KW Acute phase; Amyloid; Calcium; Disulfide bond; Glycoprotein; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..223
FT /note="Serum amyloid P-component"
FT /id="PRO_0000023538"
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 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
SQ SEQUENCE 223 AA; 25453 MW; A6FF1C7C6904EBB5 CRC64;
MDKMLFWVSV FTIFLDVFAQ TDLDKKVFVF PRESSSDHVN LITKLETPLQ EFTVCLRAYS
DLSRHYSLFS YNTPGKDNEL LIYKEKLGEY SLYIGGTKVT ARVPEEILAP VHICTSWESS
SGIAEFWING KPLVKKGLKR GYSVAAHPKI ILGQEQDSYG GKFDRGQSFL GEIGDVYMWD
SVLSPDDVQA VYYGSYVNGS ILNWQALNYE LNDYVIIKPR VWD
