ID   SAA1_NEOVI              Reviewed;         129 AA.
AC   P18575;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Serum amyloid A-1 protein;
DE   Flags: Precursor;
GN   Name=SAA1;
OS   Neovison vison (American mink) (Mustela vison).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC   Neogale.
OX   NCBI_TaxID=452646;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY
RP   LIPOPOLYSACCHARIDE.
RC   TISSUE=Liver;
RX   PubMed=2351648; DOI=10.1016/s0021-9258(19)38777-0;
RA   Marhaug G., Husby G., Dowton S.B.;
RT   "Mink serum amyloid A protein. Expression and primary structure based on
RT   cDNA sequences.";
RL   J. Biol. Chem. 265:10049-10054(1990).
CC   -!- FUNCTION: Major acute phase protein. {ECO:0000250}.
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. {ECO:0000269|PubMed:2351648}.
CC   -!- INDUCTION: By bacterial lipopolysaccharide.
CC       {ECO:0000269|PubMed:2351648}.
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   -!- MISCELLANEOUS: SAA2 is more amyloidogenic than SAA1.
CC   -!- SIMILARITY: Belongs to the SAA family. {ECO:0000305}.
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DR   EMBL; M34953; AAA30968.1; -; mRNA.
DR   PIR; A36451; A36451.
DR   AlphaFoldDB; P18575; -.
DR   SMR; P18575; -.
DR   Ensembl; ENSNVIT00000028418; ENSNVIP00000024492; ENSNVIG00000018957.
DR   GeneTree; ENSGT00390000004737; -.
DR   Proteomes; UP000694425; 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..129
FT                   /note="Serum amyloid A-1 protein"
FT                   /id="PRO_0000031593"
FT   REGION          19..44
FT                   /note="Important for amyloid formation"
FT                   /evidence="ECO:0000250"
FT   REGION          92..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   129 AA;  14389 MW;  D73D3DD95519E068 CRC64;
     MKLFTGLIFC SLVLGVSSQW YSFIGEAAQG AWDMYRAYSD MIEAKYKNSD KYFHARGNYD
     AAQRGPGGAW AAKVISDARE RSQRITDLIK YGDSGHGVED SKADQAANEW GRSGKDPNHF
     RPPGLPDKY