SAMP_MOUSE
ID SAMP_MOUSE Reviewed; 224 AA.
AC P12246;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Serum amyloid P-component;
DE Short=SAP;
DE Flags: Precursor;
GN Name=Apcs; Synonyms=Ptx2, Sap;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3263126; DOI=10.1016/s0006-291x(88)81292-0;
RA Nishiguchi S., Maeda S., Araki S., Shimada K.;
RT "Structure of the mouse serum amyloid P component gene.";
RL Biochem. Biophys. Res. Commun. 155:1366-1373(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBA/J;
RX PubMed=2481440; DOI=10.1042/bj2630025;
RA Whitehead A.S., Rits M.;
RT "Characterization of the gene encoding mouse serum amyloid P component.
RT Comparison with genes encoding other pentraxins.";
RL Biochem. J. 263:25-31(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DBA/2J; TISSUE=Liver;
RX PubMed=3183383;
RA Mole J.E., Beaulieu B.L., Geheran C.A., Carnazza J.A., Anderson J.K.;
RT "Isolation and analysis of murine serum amyloid P component cDNA clones.";
RL J. Immunol. 141:3642-3646(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=NZB; TISSUE=Liver;
RX PubMed=3658681; DOI=10.1093/nar/15.17.7186;
RA Ishikawa N., Shigemoto K., Maruyama N.;
RT "The complete nucleotide and deduced amino acid sequence of mouse serum
RT amyloid P component.";
RL Nucleic Acids Res. 15:7186-7186(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 159-224.
RC STRAIN=CBA/J; TISSUE=Liver;
RX PubMed=3169883; DOI=10.1007/bf00364241;
RA Whitehead A.S., Rits M., Michaelson J.;
RT "Molecular genetics of mouse serum amyloid P component (SAP): cloning and
RT gene mapping.";
RL Immunogenetics 28:388-390(1988).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-52.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; M23552; AAA40092.1; -; mRNA.
DR EMBL; M29535; AAA40093.1; -; Genomic_DNA.
DR EMBL; X16899; CAA34774.1; -; Genomic_DNA.
DR EMBL; X14079; CAA32243.1; -; mRNA.
DR EMBL; Y00426; CAA68488.1; -; mRNA.
DR EMBL; BC061125; AAH61125.1; -; mRNA.
DR EMBL; M23248; AAA40091.1; -; mRNA.
DR CCDS; CCDS15520.1; -.
DR PIR; A30528; A30528.
DR RefSeq; NP_035448.2; NM_011318.2.
DR AlphaFoldDB; P12246; -.
DR SMR; P12246; -.
DR BioGRID; 203069; 3.
DR IntAct; P12246; 1.
DR STRING; 10090.ENSMUSP00000027824; -.
DR GlyGen; P12246; 1 site.
DR iPTMnet; P12246; -.
DR PhosphoSitePlus; P12246; -.
DR CPTAC; non-CPTAC-3671; -.
DR CPTAC; non-CPTAC-5618; -.
DR PaxDb; P12246; -.
DR PeptideAtlas; P12246; -.
DR PRIDE; P12246; -.
DR ProteomicsDB; 260822; -.
DR Antibodypedia; 3590; 617 antibodies from 38 providers.
DR DNASU; 20219; -.
DR Ensembl; ENSMUST00000027824; ENSMUSP00000027824; ENSMUSG00000026542.
DR GeneID; 20219; -.
DR KEGG; mmu:20219; -.
DR UCSC; uc007dqy.2; mouse.
DR CTD; 325; -.
DR MGI; MGI:98229; Apcs.
DR VEuPathDB; HostDB:ENSMUSG00000026542; -.
DR eggNOG; ENOG502S201; Eukaryota.
DR GeneTree; ENSGT01050000244822; -.
DR HOGENOM; CLU_032051_2_0_1; -.
DR InParanoid; P12246; -.
DR OMA; GFDKSQS; -.
DR OrthoDB; 1088298at2759; -.
DR PhylomeDB; P12246; -.
DR TreeFam; TF330208; -.
DR BioGRID-ORCS; 20219; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Pitx2; mouse.
DR PRO; PR:P12246; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P12246; protein.
DR Bgee; ENSMUSG00000026542; Expressed in left lobe of liver and 35 other tissues.
DR ExpressionAtlas; P12246; baseline and differential.
DR Genevisible; P12246; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0001849; F:complement component C1q complex binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046790; F:virion binding; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0044869; P:negative regulation by host of viral exo-alpha-sialidase activity; ISO:MGI.
DR GO; GO:0044871; P:negative regulation by host of viral glycoprotein metabolic process; ISO:MGI.
DR GO; GO:1903016; P:negative regulation of exo-alpha-sialidase activity; ISO:MGI.
DR GO; GO:1903019; P:negative regulation of glycoprotein metabolic process; ISO:MGI.
DR GO; GO:0045656; P:negative regulation of monocyte differentiation; ISO:MGI.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:MGI.
DR GO; GO:0048525; P:negative regulation of viral process; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
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 1: Evidence at protein level;
KW Amyloid; Calcium; Disulfide bond; Glycoprotein; Lectin; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT CHAIN 21..224
FT /note="Serum amyloid P-component"
FT /id="PRO_0000023542"
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:0000269|PubMed:17330941"
FT DISULFID 56..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01172"
FT CONFLICT 151
FT /note="I -> V (in Ref. 3; AAA40092/CAA32243)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="G -> R (in Ref. 4; CAA68488)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 26247 MW; 1CDBC15F45E50DCA CRC64;
MDKLLLWMFV FTSLLSEAFC QTDLKRKVFV FPRESETDHV KLIPHLEKPL QNFTLCFRTY
SDLSRSQSLF SYSVKGRDNE LLIYKEKVGE YSLYIGQSKV TVRGMEEYLS PVHLCTTWES
SSGIVEFWVN GKPWVKKSLQ REYTVKAPPS IVLGQEQDNY GGGFQRSQSF VGEFSDLYMW
DYVLTPQDIL FVYRDSPVNP NILNWQALNY EINGYVVIRP RVWD
