ID   SAA3_RABIT              Reviewed;         122 AA.
AC   P35543;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Serum amyloid A-3 protein;
DE   Flags: Precursor;
GN   Name=SAA3;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   INDUCTION BY CYTOKINES.
RC   TISSUE=Fibroblast;
RX   PubMed=1849144; DOI=10.1172/jci115116;
RA   Mitchell T.I., Coon C.I., Brinckerhoff C.E.;
RT   "Serum amyloid A (SAA3) produced by rabbit synovial fibroblasts treated
RT   with phorbol esters or interleukin 1 induces synthesis of collagenase and
RT   is neutralized with specific antiserum.";
RL   J. Clin. Invest. 87:1177-1185(1991).
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:0000269|PubMed:1849144}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma.
CC       Expressed in synovial fibroblasts (PubMed:1849144).
CC       {ECO:0000269|PubMed:1849144}.
CC   -!- INDUCTION: Up-regulated by cytokine stimulation.
CC       {ECO:0000269|PubMed:1849144}.
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; M64696; AAA31464.1; -; mRNA.
DR   PIR; S32574; S32574.
DR   RefSeq; NP_001075771.1; NM_001082302.2.
DR   AlphaFoldDB; P35543; -.
DR   SMR; P35543; -.
DR   STRING; 9986.ENSOCUP00000002092; -.
DR   GeneID; 100009138; -.
DR   KEGG; ocu:100009138; -.
DR   CTD; 20210; -.
DR   eggNOG; ENOG502S4PB; Eukaryota.
DR   InParanoid; P35543; -.
DR   OrthoDB; 1417043at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0034364; C:high-density lipoprotein particle; 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; 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_0000031598"
FT   REGION          88..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   122 AA;  13806 MW;  77E0F502D4284C0B CRC64;
     MKLSIGIIFC FLILGVNSRE WLTFLKEAGQ GAKDMWRAYS DMKEANYKNS DKYFHARGNY
     DAAKRGPGGV WAAEVISDAR ENYQKLIGRG AEDSKADQEA NQWGRSGNDP NHFRPKGLPD
     KY