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 08-NOV-2023, entry version 89.
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 PaxDb; 9986-ENSOCUP00000002092; -.
DR GeneID; 100009138; -.
DR KEGG; ocu:100009138; -.
DR CTD; 20210; -.
DR eggNOG; ENOG502S4PB; Eukaryota.
DR InParanoid; P35543; -.
DR OrthoDB; 2958429at2759; -.
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 Gene3D; 1.10.132.110; Serum amyloid A protein; 1.
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
//
