SAA3_MOUSE
ID SAA3_MOUSE Reviewed; 122 AA.
AC P04918; Q62201;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Serum amyloid A-3 protein;
DE Flags: Precursor;
GN Name=Saa3;
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 [GENOMIC DNA / MRNA].
RX PubMed=3003697; DOI=10.1093/nar/14.2.797;
RA Stearman R.S., Lowell C.A., Peltzman C.G., Morrow J.F.;
RT "The sequence and structure of a new serum amyloid A gene.";
RL Nucleic Acids Res. 14:797-809(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SWR/J;
RX PubMed=3013853; DOI=10.1016/s0021-9258(19)83932-7;
RA Lowell C.A., Potter D.A., Stearman R.S., Morrow J.F.;
RT "Structure of the murine serum amyloid A gene family. Gene conversion.";
RL J. Biol. Chem. 261:8442-8452(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-64.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=6953913; DOI=10.1111/j.1749-6632.1982.tb22128.x;
RA Stearman R.S., Lowell C.A., Pearson W.R., Morrow J.F.;
RT "Regulation of synthesis of amyloid A-related protein.";
RL Ann. N. Y. Acad. Sci. 389:106-115(1982).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-122.
RX PubMed=3624868;
RA Yamamoto K., Goto N., Kosaka J., Shiroo M., Yeul Y.D., Migita S.;
RT "Structural diversity of murine serum amyloid A genes. Evolutionary
RT implications.";
RL J. Immunol. 139:1683-1688(1987).
CC -!- FUNCTION: Major acute phase reactant. Apolipoprotein of the HDL
CC complex. In vitro exhibits antimicrobial activity against Escherichia
CC coli, Streptococcus uberis and Pseudomonas aeruginosa (By similarity).
CC {ECO:0000250|UniProtKB:Q8SQ28}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8SQ28}.
CC -!- TISSUE SPECIFICITY: Found in various tissues.
CC -!- INDUCTION: Upon cytokine stimulation.
CC -!- SIMILARITY: Belongs to the SAA family. {ECO:0000305}.
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DR EMBL; X03479; CAA27199.1; -; mRNA.
DR EMBL; X03505; CAA27219.1; -; Genomic_DNA.
DR EMBL; X03506; CAA27219.1; JOINED; Genomic_DNA.
DR EMBL; X03507; CAA27219.1; JOINED; Genomic_DNA.
DR EMBL; BC055885; AAH55885.1; -; mRNA.
DR EMBL; M25467; AAA37231.1; -; mRNA.
DR EMBL; M17792; AAA40088.1; -; Genomic_DNA.
DR CCDS; CCDS21282.1; -.
DR PIR; A23521; A23521.
DR PIR; I71950; I71950.
DR RefSeq; NP_035445.1; NM_011315.3.
DR PDB; 4Q5G; X-ray; 2.06 A; A/B=19-122.
DR PDB; 6PXZ; X-ray; 1.70 A; A/B/C=19-122.
DR PDB; 6PY0; X-ray; 2.20 A; A/B/C=19-122.
DR PDBsum; 4Q5G; -.
DR PDBsum; 6PXZ; -.
DR PDBsum; 6PY0; -.
DR AlphaFoldDB; P04918; -.
DR SMR; P04918; -.
DR IntAct; P04918; 1.
DR MINT; P04918; -.
DR STRING; 10090.ENSMUSP00000006956; -.
DR iPTMnet; P04918; -.
DR PhosphoSitePlus; P04918; -.
DR MaxQB; P04918; -.
DR PaxDb; P04918; -.
DR PRIDE; P04918; -.
DR ProteomicsDB; 256580; -.
DR DNASU; 20210; -.
DR Ensembl; ENSMUST00000006956; ENSMUSP00000006956; ENSMUSG00000040026.
DR GeneID; 20210; -.
DR KEGG; mmu:20210; -.
DR UCSC; uc009gyw.1; mouse.
DR CTD; 20210; -.
DR MGI; MGI:98223; Saa3.
DR VEuPathDB; HostDB:ENSMUSG00000040026; -.
DR eggNOG; ENOG502S4PB; Eukaryota.
DR GeneTree; ENSGT00390000004737; -.
DR HOGENOM; CLU_129936_0_0_1; -.
DR InParanoid; P04918; -.
DR OMA; NYFRPAG; -.
DR OrthoDB; 1417043at2759; -.
DR PhylomeDB; P04918; -.
DR TreeFam; TF332544; -.
DR BioGRID-ORCS; 20210; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Saa3; mouse.
DR PRO; PR:P04918; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P04918; protein.
DR Bgee; ENSMUSG00000040026; Expressed in ankle joint and 90 other tissues.
DR ExpressionAtlas; P04918; baseline and differential.
DR Genevisible; P04918; MM.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0042056; F:chemoattractant activity; IDA:MGI.
DR GO; GO:0035662; F:Toll-like receptor 4 binding; IPI:MGI.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0060326; P:cell chemotaxis; IDA:MGI.
DR GO; GO:0071347; P:cellular response to interleukin-1; IDA:MGI.
DR GO; GO:0007252; P:I-kappaB phosphorylation; IDA:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB.
DR InterPro; IPR000096; Serum_amyloid_A.
DR Pfam; PF00277; SAA; 1.
DR PIRSF; PIRSF002472; Serum_amyloid_A; 1.
DR PRINTS; PR00306; SERUMAMYLOID.
DR SMART; SM00197; SAA; 1.
DR PROSITE; PS00992; SAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acute phase; HDL; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..122
FT /note="Serum amyloid A-3 protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000031591"
FT REGION 87..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 57
FT /note="R -> G (in Ref. 5; AAA40088)"
FT /evidence="ECO:0000305"
FT HELIX 21..45
FT /evidence="ECO:0007829|PDB:6PXZ"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:6PXZ"
FT HELIX 67..87
FT /evidence="ECO:0007829|PDB:6PXZ"
FT HELIX 94..105
FT /evidence="ECO:0007829|PDB:6PXZ"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:6PXZ"
SQ SEQUENCE 122 AA; 13774 MW; B9435F82D1B0B705 CRC64;
MKPSIAIILC ILILGVDSQR WVQFMKEAGQ GSRDMWRAYS DMKKANWKNS DKYFHARGNY
DAARRGPGGA WAAKVISDAR EAVQKFTGHG AEDSRADQFA NEWGRSGKDP NHFRPAGLPK
RY
