SAA_ANAPL
ID SAA_ANAPL Reviewed; 127 AA.
AC P02740; Q92034;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Serum amyloid A protein;
DE Short=SAA;
DE Flags: Precursor;
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Pekin breed; TISSUE=Liver;
RX PubMed=8962089; DOI=10.1073/pnas.93.25.14548;
RA Guo J.T., Aldrich C., Mason W.S., Pugh J.C.;
RT "Characterization of serum amyloid A protein mRNA expression and secondary
RT amyloidosis in the domestic duck.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14548-14553(1996).
RN [2]
RP PROTEIN SEQUENCE OF 19-124.
RX PubMed=3109944; DOI=10.1016/0014-5793(87)81008-6;
RA Ericsson L.H., Eriksen N., Walsh K.A., Benditt E.P.;
RT "Primary structure of duck amyloid protein A. The form deposited in tissues
RT may be identical to its serum precursor.";
RL FEBS Lett. 218:11-16(1987).
RN [3]
RP PROTEIN SEQUENCE OF 19-99.
RX PubMed=845435;
RA Gorevic P.D., Greenwald M., Frangione B., Pras M., Franklin E.C.;
RT "The amino acid sequence of duck amyloid A (AA) protein.";
RL J. Immunol. 118:1113-1118(1977).
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. Also
CC present in the liver and lung irrespective of induction.
CC -!- INDUCTION: Upon cytokine stimulation.
CC -!- PTM: This protein is the precursor of amyloid protein A, which is
CC formed by the removal of approximately 3 residues from the C-terminal
CC end.
CC -!- POLYMORPHISM: At least two alleles exist. The sequence of the B allele
CC is shown here.
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; U59909; AAC60058.1; -; Genomic_DNA.
DR EMBL; U59908; AAC60057.1; -; mRNA.
DR EMBL; U64985; AAC60059.1; -; Genomic_DNA.
DR PIR; A03200; YLDKA.
DR PIR; A27227; A27227.
DR RefSeq; NP_001297733.1; NM_001310804.1.
DR RefSeq; XP_005028466.2; XM_005028409.2.
DR AlphaFoldDB; P02740; -.
DR SMR; P02740; -.
DR GeneID; 101798523; -.
DR KEGG; apla:101798523; -.
DR CTD; 6289; -.
DR OrthoDB; 1417043at2759; -.
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; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:3109944,
FT ECO:0000269|PubMed:845435"
FT CHAIN 19..127
FT /note="Serum amyloid A protein"
FT /id="PRO_0000031567"
FT REGION 88..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 89
FT /note="G -> S (in allele A)"
FT VARIANT 107
FT /note="A -> V (in allele A)"
FT CONFLICT 81..82
FT /note="SD -> AN (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="T -> R (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 127 AA; 13873 MW; 6F61476AEAB9EB6F CRC64;
MRLCICFVLL AVIVCASADN PFTRGGRFVL DAAGGAWDML RAYRDMREAN HIGADKYFHA
RGNYDAARRG PGGAWAARVI SDARENWQGG VSGRGAEDTR ADQEANAWGR NGGDPNRYRP
PGLPSKY