ID   SAA1_RABIT              Reviewed;         122 AA.
AC   P53614;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Serum amyloid A-1 protein;
DE   Flags: Precursor;
GN   Name=SAA1;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY
RP   INFLAMMATORY STIMULI.
RX   PubMed=1721234; DOI=10.1111/j.1365-3083.1991.tb01597.x;
RA   Rygg M., Marhaug G., Husby G., Dowton S.B.;
RT   "Rabbit serum amyloid protein A: expression and primary structure deduced
RT   from cDNA sequences.";
RL   Scand. J. Immunol. 34:727-734(1991).
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:1721234}.
CC   -!- INDUCTION: Up-regulated by inflammatory stimuli.
CC       {ECO:0000269|PubMed:1721234}.
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; S71722; AAB20616.1; -; mRNA.
DR   PIR; I46981; I46981.
DR   RefSeq; NP_001075796.1; NM_001082327.2.
DR   RefSeq; XP_008273295.2; XM_008275073.2.
DR   RefSeq; XP_008273297.2; XM_008275075.2.
DR   RefSeq; XP_008273298.1; XM_008275076.2.
DR   AlphaFoldDB; P53614; -.
DR   SMR; P53614; -.
DR   STRING; 9986.ENSOCUP00000017760; -.
DR   PRIDE; P53614; -.
DR   GeneID; 100009168; -.
DR   KEGG; ocu:100009168; -.
DR   eggNOG; ENOG502S4PB; Eukaryota.
DR   InParanoid; P53614; -.
DR   OrthoDB; 1417043at2759; -.
DR   TreeFam; TF332544; -.
DR   Proteomes; UP000001811; 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..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..122
FT                   /note="Serum amyloid A-1 protein"
FT                   /id="PRO_0000031596"
FT   REGION          20..45
FT                   /note="Important for amyloid formation"
FT                   /evidence="ECO:0000250"
FT   REGION          87..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   122 AA;  13655 MW;  98822631B36B2B98 CRC64;
     MKLLSGLLLC SLVLGVSSQR WFSFIGEATQ GAWDMWRAYS DMREANYINA DKYFHARGNY
     DAAQRGPGGV WAAKVISDAR EDLQRLMGHG AEDSMADQAA NEWGRSGKDP NHFRPKGLPD
     KY