ID   SAA_FELCA               Reviewed;         129 AA.
AC   P19707; M3X0G8;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   26-NOV-2014, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Serum amyloid A protein {ECO:0000305};
DE            Short=SAA {ECO:0000305};
DE   Contains:
DE     RecName: Full=Amyloid protein A {ECO:0000303|PubMed:2598632};
DE     AltName: Full=Amyloid fibril protein AA {ECO:0000305};
DE   Flags: Precursor;
GN   Name=SAA1;
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian;
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2]
RP   PROTEIN SEQUENCE OF 19-111.
RX   PubMed=2598632; DOI=10.1016/0305-0491(89)90030-8;
RA   Kluve-Beckerman B., Dwulet F.E., Dibartola S.P., Benson M.D.;
RT   "Primary structures of dog and cat amyloid A proteins: comparison to human
RT   AA.";
RL   Comp. Biochem. Physiol. 94B:175-183(1989).
CC   -!- FUNCTION: Major acute phase reactant. Apolipoprotein of the HDL
CC       complex.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma.
CC   -!- INDUCTION: Upon cytokine stimulation.
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; AANG02169639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AANG02169640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AANG02169641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; JL0111; YLCTA.
DR   AlphaFoldDB; P19707; -.
DR   SMR; P19707; -.
DR   STRING; 9685.ENSFCAP00000011761; -.
DR   eggNOG; ENOG502S4PB; Eukaryota.
DR   InParanoid; P19707; -.
DR   OMA; HEDTIAD; -.
DR   OrthoDB; 1417043at2759; -.
DR   Proteomes; UP000011712; 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;
KW   Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:2598632"
FT   CHAIN           19..129
FT                   /note="Serum amyloid A protein"
FT                   /id="PRO_0000174667"
FT   CHAIN           19..111
FT                   /note="Amyloid protein A"
FT                   /evidence="ECO:0000269|PubMed:2598632"
FT                   /id="PRO_0000430938"
FT   PROPEP          112..129
FT                   /note="Often cleaved during amyloidogenesis"
FT                   /evidence="ECO:0000250|UniProtKB:P19708"
FT                   /id="PRO_0000430939"
FT   REGION          88..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         19
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P42819"
FT   CONFLICT        19
FT                   /note="Q -> E (in Ref. 2; AA sequence)"
FT   CONFLICT        106..108
FT                   /note="AAN -> EWG (in Ref. 2; AA sequence)"
SQ   SEQUENCE   129 AA;  14270 MW;  02CA07DF94584B51 CRC64;
     MKLFTGLVFC SLVLGVSSQW YSFLGEAAQG AWDMWRAYSD MREANYIGAD KYFHARGNYD
     AAQRGPGGAW AAKVISDARE NSQRVTDFFR HGNSGHGAED SKADQAANEW GRSGKDPNHF
     RPAGLPSKY