ID   SAA1_MESAU              Reviewed;         122 AA.
AC   P20726;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Serum amyloid A-1 protein;
DE   Flags: Precursor;
GN   Name=SAA1;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY INFLAMMATORY STIMULI,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=2765510; DOI=10.1021/bi00437a040;
RA   Webb C.F., Tucker P.W., Dowton S.B.;
RT   "Expression and sequence analyses of serum amyloid A in the Syrian
RT   hamster.";
RL   Biochemistry 28:4785-4790(1989).
CC   -!- FUNCTION: Major acute phase protein. {ECO:0000269|PubMed:2765510}.
CC   -!- SUBUNIT: Homohexamer; dimer of trimers. Can form amyloid fibrils after
CC       partial proteolysis; the native, undenatured protein does not form
CC       amyloid fibrils (in vitro). Apolipoprotein of the HDL complex. Binds to
CC       heparin (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Detected in liver, spleen and kidney.
CC       {ECO:0000269|PubMed:2765510}.
CC   -!- INDUCTION: Up-regulated by inflammatory stimuli.
CC       {ECO:0000269|PubMed:2765510}.
CC   -!- DISEASE: Note=Reactive, secondary amyloidosis is characterized by the
CC       extracellular accumulation in various tissues of the SAA protein. These
CC       deposits are highly insoluble and resistant to proteolysis; they
CC       disrupt tissue structure and compromise function.
CC   -!- SIMILARITY: Belongs to the SAA family. {ECO:0000305}.
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DR   EMBL; M27242; AAA37095.1; -; mRNA.
DR   PIR; B30248; B30248.
DR   AlphaFoldDB; P20726; -.
DR   SMR; P20726; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Acute phase; Amyloid; HDL; Heparin-binding; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..122
FT                   /note="Serum amyloid A-1 protein"
FT                   /id="PRO_0000031585"
FT   REGION          19..45
FT                   /note="Important for amyloid formation"
FT                   /evidence="ECO:0000250"
FT   REGION          100..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   122 AA;  14021 MW;  12F36DB7310A1E68 CRC64;
     MKPFVAIIFC FLILGVDSQR WFQFMKEAGQ GTRDMWRAYT DMREANWKNS DKYFHARGNY
     DAAQRGPGGA WAAKVISDAR EGFKRITGRG IEDSRADQFA NEWGRSGKDP NFFRPPGLPS
     KY