SAA2_MOUSE
ID SAA2_MOUSE Reviewed; 122 AA.
AC P05367;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Serum amyloid A-2 protein {ECO:0000305};
DE Contains:
DE RecName: Full=Amyloid protein A {ECO:0000250|UniProtKB:P02739};
DE Flags: Precursor;
GN Name=Saa2 {ECO:0000312|MGI:MGI:98222};
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], AND TISSUE SPECIFICITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3857624; DOI=10.1073/pnas.82.9.2915;
RA Yamamoto K., Migita S.;
RT "Complete primary structures of two major murine serum amyloid A proteins
RT deduced from cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2915-2919(1985).
RN [3]
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).
RN [4]
RP PROTEIN SEQUENCE OF 20-122.
RC STRAIN=SJL/J;
RX PubMed=1590757; DOI=10.1042/bj2830673;
RA de Beer M.C., de Beer F.C., Beach C.M., Carreras I., Sipe J.D.;
RT "Mouse serum amyloid A protein. Complete amino acid sequence and mRNA
RT analysis of a new isoform.";
RL Biochem. J. 283:673-678(1992).
CC -!- FUNCTION: Major acute phase reactant. {ECO:0000250|UniProtKB:P05366}.
CC -!- SUBUNIT: Apolipoprotein of the HDL complex.
CC {ECO:0000250|UniProtKB:P0DJI8}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0DJI8}.
CC -!- TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma.
CC {ECO:0000269|PubMed:3013853}.
CC -!- SIMILARITY: Belongs to the SAA family. {ECO:0000305}.
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DR EMBL; M13522; AAA40086.1; -; Genomic_DNA.
DR EMBL; M11130; AAA40085.1; -; mRNA.
DR EMBL; M17791; AAA40087.1; -; Genomic_DNA.
DR CCDS; CCDS21285.1; -.
DR PIR; B23843; B23843.
DR RefSeq; NP_035444.1; NM_011314.2.
DR RefSeq; XP_006540790.1; XM_006540727.2.
DR PDB; 6DSO; EM; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=20-102.
DR PDB; 6ZCF; EM; 2.73 A; A/B/C/D/E/F/G/H/I/J/K/L=20-122.
DR PDB; 6ZCG; EM; 2.95 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=20-122.
DR PDB; 6ZCH; EM; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=20-102.
DR PDB; 7OVT; EM; 2.69 A; A/B/C/D/E/F/G/H/I/J/K/L=20-122.
DR PDBsum; 6DSO; -.
DR PDBsum; 6ZCF; -.
DR PDBsum; 6ZCG; -.
DR PDBsum; 6ZCH; -.
DR PDBsum; 7OVT; -.
DR AlphaFoldDB; P05367; -.
DR SMR; P05367; -.
DR BioGRID; 203062; 1.
DR STRING; 10090.ENSMUSP00000075365; -.
DR PhosphoSitePlus; P05367; -.
DR CPTAC; non-CPTAC-3944; -.
DR MaxQB; P05367; -.
DR PaxDb; P05367; -.
DR PeptideAtlas; P05367; -.
DR PRIDE; P05367; -.
DR ProteomicsDB; 255451; -.
DR DNASU; 20209; -.
DR Ensembl; ENSMUST00000075982; ENSMUSP00000075365; ENSMUSG00000057465.
DR Ensembl; ENSMUST00000210769; ENSMUSP00000147751; ENSMUSG00000057465.
DR GeneID; 20209; -.
DR KEGG; mmu:20209; -.
DR UCSC; uc009gzb.2; mouse.
DR CTD; 6289; -.
DR MGI; MGI:98222; Saa2.
DR VEuPathDB; HostDB:ENSMUSG00000057465; -.
DR eggNOG; ENOG502S4PB; Eukaryota.
DR GeneTree; ENSGT00390000004737; -.
DR HOGENOM; CLU_129936_0_0_1; -.
DR InParanoid; P05367; -.
DR OMA; MREANWI; -.
DR OrthoDB; 1417043at2759; -.
DR PhylomeDB; P05367; -.
DR TreeFam; TF332544; -.
DR BioGRID-ORCS; 20209; 5 hits in 40 CRISPR screens.
DR ChiTaRS; Saa1; mouse.
DR PRO; PR:P05367; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P05367; protein.
DR Bgee; ENSMUSG00000057465; Expressed in left lobe of liver and 71 other tissues.
DR ExpressionAtlas; P05367; baseline and differential.
DR Genevisible; P05367; MM.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0048247; P:lymphocyte chemotaxis; ISO:MGI.
DR GO; GO:0048246; P:macrophage chemotaxis; ISO:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO: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; Amyloid; Direct protein sequencing; HDL;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1590757"
FT CHAIN 20..122
FT /note="Serum amyloid A-2 protein"
FT /evidence="ECO:0000269|PubMed:1590757"
FT /id="PRO_0000031589"
FT CHAIN 20..94
FT /note="Amyloid protein A"
FT /evidence="ECO:0000250|UniProtKB:P0DJI9"
FT /id="PRO_0000031590"
FT REGION 89..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 120
FT /note="A -> D (in strain: SJL/J)"
FT STRAND 21..33
FT /evidence="ECO:0007829|PDB:6ZCF"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:6ZCF"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:6ZCF"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:6ZCF"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6DSO"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6DSO"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:6DSO"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:6DSO"
SQ SEQUENCE 122 AA; 13622 MW; 99E79D6FF97E96E0 CRC64;
MKLLTSLVFC SLLLGVCHGG FFSFIGEAFQ GAGDMWRAYT DMKEAGWKDG DKYFHARGNY
DAAQRGPGGV WAAEKISDAR ESFQEFFGRG HEDTMADQEA NRHGRSGKDP NYYRPPGLPA
KY