Serum amyloid A1

Serum amyloid A1

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
4IP8, 4IP9

Identifiers

SAA1 ; PIG4; SAA; SAA2; TP53I4

External IDs

OMIM: 104750 MGI: 98221 HomoloGene: 128033 GeneCards: SAA1 Gene

Gene ontology
Molecular function	• G-protein coupled receptor binding • heparin binding
Cellular component	• extracellular region • high-density lipoprotein particle • extracellular vesicular exosome • endocytic vesicle lumen
Biological process	• acute-phase response • positive regulation of cytosolic calcium ion concentration • platelet activation • neutrophil chemotaxis • innate immune response • positive regulation of cell adhesion • macrophage chemotaxis • lymphocyte chemotaxis • regulation of protein secretion • positive regulation of cytokine secretion • positive regulation of interleukin-1 secretion • negative regulation of inflammatory response
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

ENSG00000173432

ENSMUSG00000074115

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
18.29 – 18.29 Mb

Chr 7:
46.74 – 46.74 Mb

PubMed search

Serum amyloid A protein is a protein that in humans is encoded by the SAA1 gene.^[1]^[2]^[3]

References

↑ Glaser T, Housman D, Lewis WH, Gerhard D, Jones C (Jan 1990). "A fine-structure deletion map of human chromosome 11p: analysis of J1 series hybrids". Somat Cell Mol Genet 15 (6): 477–501. doi:10.1007/BF01534910. PMID 2595451.
↑ Polyak K, Xia Y, Zweier JL, Kinzler KW, Vogelstein B (Sep 1997). "A model for p53-induced apoptosis". Nature 389 (6648): 300–5. doi:10.1038/38525. PMID 9305847.
↑ "Entrez Gene: SAA1 serum amyloid A1".

Further reading

Kisilevsky R, Tam SP (2002). "Acute phase serum amyloid A, cholesterol metabolism, and cardiovascular disease.". Pediatric pathology & molecular medicine 21 (3): 291–305. doi:10.1080/02770930290056523. PMID 12056504.
Sletten K, Husby G, Natvig JB (1976). "The complete amino acid sequence of an amyloid fibril protein AA1 of unusual size (64 residues).". Biochem. Biophys. Res. Commun. 69 (1): 19–25. doi:10.1016/S0006-291X(76)80266-5. PMID 1259755.
Beach CM, De Beer MC, Sipe JD et al. (1992). "Human serum amyloid A protein. Complete amino acid sequence of a new variant.". Biochem. J. 282 (2): 615–20. PMC 1130826. PMID 1546977.
Betts JC, Edbrooke MR, Thakker RV, Woo P (1991). "The human acute-phase serum amyloid A gene family: structure, evolution and expression in hepatoma cells.". Scand. J. Immunol. 34 (4): 471–82. doi:10.1111/j.1365-3083.1991.tb01570.x. PMID 1656519.
Zimlichman S, Danon A, Nathan I et al. (1990). "Serum amyloid A, an acute phase protein, inhibits platelet activation.". J. Lab. Clin. Med. 116 (2): 180–6. PMID 1697614.
Steinkasserer A, Weiss EH, Schwaeble W, Linke RP (1990). "Heterogeneity of human serum amyloid A protein. Five different variants from one individual demonstrated by cDNA sequence analysis.". Biochem. J. 268 (1): 187–93. PMC 1131410. PMID 1971508.
Sack GH, Talbot CC (1991). "Highly polymorphic domains of the human serum amyloid A (SAA) gene GSAA1.". Scand. J. Immunol. 33 (4): 485–8. doi:10.1111/j.1365-3083.1991.tb01797.x. PMID 2017667.
Woo P, Sipe J, Dinarello CA, Colten HR (1987). "Structure of a human serum amyloid A gene and modulation of its expression in transfected L cells.". J. Biol. Chem. 262 (32): 15790–5. PMID 2890635.
Kluve-Beckerman B, Dwulet FE, Benson MD (1988). "Human serum amyloid A. Three hepatic mRNAs and the corresponding proteins in one person.". J. Clin. Invest. 82 (5): 1670–5. doi:10.1172/JCI113779. PMC 442736. PMID 3183061.
Prelli F, Pras M, Frangione B (1988). "Degradation and deposition of amyloid AA fibrils are tissue specific.". Biochemistry 26 (25): 8251–6. doi:10.1021/bi00399a035. PMID 3442653.
Kluve-Beckerman B, Long GL, Benson MD (1987). "DNA sequence evidence for polymorphic forms of human serum amyloid A (SAA).". Biochem. Genet. 24 (11-12): 795–803. doi:10.1007/BF00554519. PMID 3800865.
Sipe JD, Colten HR, Goldberger G et al. (1985). "Human serum amyloid A (SAA): biosynthesis and postsynthetic processing of preSAA and structural variants defined by complementary DNA.". Biochemistry 24 (12): 2931–6. doi:10.1021/bi00333a018. PMID 3839415.
Sletten K, Husby G (1974). "The complete amino-acid sequence of non-immunoglobulin amyloid fibril protein AS in rheumatoid arthritis.". Eur. J. Biochem. 41 (1): 117–25. doi:10.1111/j.1432-1033.1974.tb03251.x. PMID 4816450.
Ein D, Kimura S, Terry WD et al. (1972). "Amino acid sequence of an amyloid fibril protein of unknown origin.". J. Biol. Chem. 247 (17): 5653–5. PMID 5055786.
Levin M, Franklin EC, Frangione B, Pras M (1972). "The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils.". J. Clin. Invest. 51 (10): 2773–6. doi:10.1172/JCI107098. PMC 332979. PMID 5056669.
Møyner K, Sletten K, Husby G, Natvig JB (1980). "An unusually large (83 amino acid residues) amyloid fibril protein AA from a patient with Waldenström's macroglobulinaemia and amyloidosis.". Scand. J. Immunol. 11 (5): 549–54. doi:10.1111/j.1365-3083.1980.tb00023.x. PMID 6155694.
Parmelee DC, Titani K, Ericsson LH et al. (1982). "Amino acid sequence of amyloid-related apoprotein (apoSAA1) from human high-density lipoprotein.". Biochemistry 21 (14): 3298–303. doi:10.1021/bi00257a008. PMID 7115671.
Badolato R, Wang JM, Murphy WJ et al. (1994). "Serum amyloid A is a chemoattractant: induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes.". J. Exp. Med. 180 (1): 203–9. doi:10.1084/jem.180.1.203. PMC 2191543. PMID 7516407.
Badolato R, Johnston JA, Wang JM et al. (1995). "Serum amyloid A induces calcium mobilization and chemotaxis of human monocytes by activating a pertussis toxin-sensitive signaling pathway.". J. Immunol. 155 (8): 4004–10. PMID 7561109.