SAA_HORSE
ID SAA_HORSE Reviewed; 110 AA.
AC P19857;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Serum amyloid A protein;
DE Short=SAA;
DE Contains:
DE RecName: Full=Amyloid protein A;
DE AltName: Full=Amyloid fibril protein AA;
GN Name=SAA1;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Blood;
RX PubMed=2502829; DOI=10.1111/j.1365-3083.1989.tb01195.x;
RA Sletten K., Husebekk A., Husby G.;
RT "The primary structure of equine serum amyloid A (SAA) protein.";
RL Scand. J. Immunol. 30:117-122(1989).
RN [2]
RP PROTEIN SEQUENCE OF 1-80.
RC TISSUE=Liver;
RX PubMed=3616485; DOI=10.1111/j.1365-3083.1987.tb02237.x;
RA Sletten K., Husebekk A., Husby G.;
RT "The amino acid sequence of an amyloid fibril protein AA isolated from the
RT horse.";
RL Scand. J. Immunol. 26:79-84(1987).
CC -!- FUNCTION: Major acute phase reactant. Apolipoprotein of the HDL
CC complex.
CC -!- TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma.
CC -!- INDUCTION: Upon cytokine stimulation.
CC -!- PTM: This protein is the precursor of amyloid protein A, which is
CC formed by the removal of residues from the C-terminal end.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A60430; A28573.
DR AlphaFoldDB; P19857; -.
DR SMR; P19857; -.
DR STRING; 9796.ENSECAP00000011472; -.
DR PaxDb; P19857; -.
DR PeptideAtlas; P19857; -.
DR PRIDE; P19857; -.
DR InParanoid; P19857; -.
DR Proteomes; UP000002281; 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 1: Evidence at protein level;
KW Acute phase; Amyloid; Direct protein sequencing; HDL; Reference proteome.
FT CHAIN 1..110
FT /note="Serum amyloid A protein"
FT /id="PRO_0000031573"
FT CHAIN 1..80
FT /note="Amyloid protein A"
FT /id="PRO_0000031574"
FT REGION 73..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 16
FT /note="I -> L"
FT VARIANT 44
FT /note="K -> Q"
FT VARIANT 59
FT /note="A -> G"
FT VARIANT 78
FT /note="G -> A"
SQ SEQUENCE 110 AA; 12289 MW; EAE7DBE7AB007E5B CRC64;
LLSFLGEAAR GTWDMIRAYN DMREANYIGA DKYFHARGNY DAAKRGPGGA WAAKVISDAR
ENFQRFTDRF SFGGSGRGAE DSRADQAANE WGRSGKDPNH FRPHGLPDKY