SAMP_RAT
ID SAMP_RAT Reviewed; 228 AA.
AC P23680; Q63539;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Serum amyloid P-component;
DE Short=SAP;
DE Flags: Precursor;
GN Name=Apcs; Synonyms=Ptx2, Sap;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2400402; DOI=10.1042/bj2700553;
RA Dowton S.B., McGrew S.D.;
RT "Rat serum amyloid P component. Analysis of cDNA sequence and gene
RT expression.";
RL Biochem. J. 270:553-556(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Rassouli M., Murray R.K.;
RL Submitted (JUN-1993) 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; X55761; CAA39287.1; -; mRNA.
DR EMBL; M83177; AAB59696.1; -; mRNA.
DR PIR; S11473; S11473.
DR RefSeq; NP_058866.2; NM_017170.2.
DR AlphaFoldDB; P23680; -.
DR SMR; P23680; -.
DR BioGRID; 247998; 1.
DR IntAct; P23680; 1.
DR MINT; P23680; -.
DR STRING; 10116.ENSRNOP00000012092; -.
DR GlyGen; P23680; 1 site.
DR PaxDb; P23680; -.
DR PRIDE; P23680; -.
DR GeneID; 29339; -.
DR KEGG; rno:29339; -.
DR UCSC; RGD:68322; rat.
DR CTD; 325; -.
DR RGD; 68322; Apcs.
DR eggNOG; ENOG502S201; Eukaryota.
DR HOGENOM; CLU_032051_2_0_1; -.
DR InParanoid; P23680; -.
DR OrthoDB; 1088298at2759; -.
DR PhylomeDB; P23680; -.
DR TreeFam; TF330208; -.
DR PRO; PR:P23680; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P23680; RN.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0001849; F:complement component C1q complex binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046790; F:virion binding; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; ISO:RGD.
DR GO; GO:0044869; P:negative regulation by host of viral exo-alpha-sialidase activity; ISO:RGD.
DR GO; GO:0044871; P:negative regulation by host of viral glycoprotein metabolic process; ISO:RGD.
DR GO; GO:1903016; P:negative regulation of exo-alpha-sialidase activity; ISO:RGD.
DR GO; GO:1903019; P:negative regulation of glycoprotein metabolic process; ISO:RGD.
DR GO; GO:0045656; P:negative regulation of monocyte differentiation; ISO:RGD.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:RGD.
DR GO; GO:0048525; P:negative regulation of viral process; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IPI:RGD.
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..20
FT CHAIN 21..228
FT /note="Serum amyloid P-component"
FT /id="PRO_0000023544"
FT DOMAIN 25..224
FT /note="Pentraxin (PTX)"
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 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 156
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
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 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 56..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CONFLICT 86
FT /note="D -> A (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 88..89
FT /note="VG -> LE (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 228 AA; 26176 MW; E2314CBDA1103996 CRC64;
MDKLLLWMSV FTSLLSEAFA QTDLNQKVFV FPRESETDYV KLIPWLEKPL QNFTLCFRAY
SDLSRSQSLF SYSVNSRDNE LLIYKDKVGQ YSLYIGNSKV TVRGLEEFPS PIHFCTSWES
SSGIAEFWVN GKPWVKKGLQ KGYTVKSSPS IVLGQEQDTY GGGFDKTQSF VGEIADLYMW
DSVLTPENIH SVDRGFPPNP NILDWRALNY EINGYVVIKP RMWDNKSS
