ID SAA1_HUMAN Reviewed; 122 AA. AC P0DJI8; E9PQD6; P02735; P02736; P02737; Q16730; Q16834; Q16835; Q16879; AC Q3KRB3; Q6FG67; Q96QN0; Q9UCK9; Q9UCL0; DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2024, sequence version 2. DT 27-MAR-2024, entry version 87. DE RecName: Full=Serum amyloid A-1 protein; DE Short=SAA; DE Contains: DE RecName: Full=Amyloid protein A; DE AltName: Full=Amyloid fibril protein AA; DE Contains: DE RecName: Full=Serum amyloid protein A(2-104); DE Contains: DE RecName: Full=Serum amyloid protein A(3-104); DE Contains: DE RecName: Full=Serum amyloid protein A(2-103); DE Contains: DE RecName: Full=Serum amyloid protein A(2-102); DE Contains: DE RecName: Full=Serum amyloid protein A(4-101); DE Flags: Precursor; GN Name=SAA1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE SAA1.1), AND VARIANTS VAL-70; ALA-75 AND RP SER-77. RX PubMed=3839415; DOI=10.1021/bi00333a018; RA Sipe J.D., Colten H.R., Goldberger G., Edge M.D., Tack B.F., Cohen A.S., RA Whitehead A.S.; RT "Human serum amyloid A (SAA): biosynthesis and postsynthetic processing of RT preSAA and structural variants defined by complementary DNA."; RL Biochemistry 24:2931-2936(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE SAA1.1), AND VARIANTS VAL-70; ALA-75 AND RP SER-77. RC TISSUE=Liver; RX PubMed=3183061; DOI=10.1172/jci113779; RA Kluve-Beckerman B., Dwulet F.E., Benson M.D.; RT "Human serum amyloid A. Three hepatic mRNAs and the corresponding proteins RT in one person."; RL J. Clin. Invest. 82:1670-1675(1988). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE SAA1.5), AND VARIANT SER-77. RC TISSUE=Liver; RX PubMed=1656519; DOI=10.1111/j.1365-3083.1991.tb01570.x; RA Betts J., Edbrooke M., Thakker R., Woo P.; RT "The human acute-phase serum amyloid A gene family: structure, evolution RT and expression in hepatoma cells."; RL Scand. J. Immunol. 34:471-482(1991). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE SAA1.5), AND VARIANT SER-77. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE SAA1.5). RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE SAA1.1), AND VARIANTS RP VAL-70; ALA-75 AND SER-77. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 73-122, AND VARIANTS ALA-75; SER-77 AND RP ASN-78. RC TISSUE=Liver; RX PubMed=1971508; DOI=10.1042/bj2680187; RA Steinkasserer A., Weiss E.H., Schwaeble W., Linke R.P.; RT "Heterogeneity of human serum amyloid A protein. Five different variants RT from one individual demonstrated by cDNA sequence analysis."; RL Biochem. J. 268:187-193(1990). RN [8] RP PROTEIN SEQUENCE OF 19-122, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE RP SPECIFICITY. RX PubMed=7115671; DOI=10.1021/bi00257a008; RA Parmelee D.C., Titani K., Ericsson L.H., Eriksen N., Benditt E.P., RA Walsh K.A.; RT "Amino acid sequence of amyloid-related apoprotein (apoSAA1) from human RT high-density lipoprotein."; RL Biochemistry 21:3298-3303(1982). RN [9] RP PROTEIN SEQUENCE OF 19-122 (ALLELE SAA1.2). RX PubMed=1546977; DOI=10.1042/bj2820615; RA Beach C.M., de Beer M.C., Sipe J.D., Loose L.D., de Beer F.C.; RT "Human serum amyloid A protein. Complete amino acid sequence of a new RT variant."; RL Biochem. J. 282:615-620(1992). RN [10] RP PROTEIN SEQUENCE OF 19-101. RX PubMed=6155694; DOI=10.1111/j.1365-3083.1980.tb00023.x; RA Moyner K., Sletten K., Husby G., Natvig J.B.; RT "An unusually large (83 amino acid residues) amyloid fibril protein AA from RT a patient with Waldenstrom's macroglobulinaemia and amyloidosis."; RL Scand. J. Immunol. 11:549-554(1980). RN [11] RP PROTEIN SEQUENCE OF 19-94. RX PubMed=5055786; DOI=10.1016/s0021-9258(20)81154-5; RA Ein D., Kimura S., Terry W.D., Magnotta J., Glenner G.G.; RT "Amino acid sequence of an amyloid fibril protein of unknown origin."; RL J. Biol. Chem. 247:5653-5655(1972). RN [12] RP PROTEIN SEQUENCE OF 19-94 (FAMILIAL MEDITERRANEAN FEVER PATIENT). RX PubMed=5056669; DOI=10.1172/jci107098; RA Levin M., Franklin E.C., Frangione B., Pras M.; RT "The amino acid sequence of a major nonimmunoglobulin component of some RT amyloid fibrils."; RL J. Clin. Invest. 51:2773-2776(1972). RN [13] RP PROTEIN SEQUENCE OF 19-94, AND TISSUE SPECIFICITY. RX PubMed=4816450; DOI=10.1111/j.1432-1033.1974.tb03251.x; RA Sletten K., Husby G.; RT "The complete amino-acid sequence of non-immunoglobulin amyloid fibril RT protein AS in rheumatoid arthritis."; RL Eur. J. Biochem. 41:117-125(1974). RN [14] RP PROTEIN SEQUENCE OF 19-94, MASS SPECTROMETRY, DISEASE, VARIANTS ALA-75 AND RP ASN-78, AND ALLELE SAA1.3. RC TISSUE=Thyroid; RX PubMed=1463770; DOI=10.1016/0925-4439(92)90068-x; RA Baba S., Takahashi T., Kasama T., Shirasawa H.; RT "Identification of two novel amyloid A protein subsets coexisting in an RT individual patient of AA-amyloidosis."; RL Biochim. Biophys. Acta 1180:195-200(1992). RN [15] RP PROTEIN SEQUENCE OF 19-82. RX PubMed=1259755; DOI=10.1016/s0006-291x(76)80266-5; RA Sletten K., Husby G., Natvig J.B.; RT "The complete amino acid sequence of an amyloid fibril protein AA1 of RT unusual size (64 residues)."; RL Biochem. Biophys. Res. Commun. 69:19-25(1976). RN [16] RP PROTEIN SEQUENCE OF 19-42. RX PubMed=11946204; DOI=10.1016/0014-5793(71)80506-9; RA Benditt E.P., Eriksen N., Hermodson M.A., Ericsson L.H.; RT "The major proteins of human and monkey amyloid substance: common RT properties including unusual N-terminal amino acid sequences."; RL FEBS Lett. 19:169-173(1971). RN [17] RP PROTEIN SEQUENCE OF 20-100. RX PubMed=3442653; DOI=10.1021/bi00399a035; RA Prelli F., Pras M., Frangione B.; RT "Degradation and deposition of amyloid AA fibrils are tissue specific."; RL Biochemistry 26:8251-8256(1987). RN [18] RP PROTEIN SEQUENCE OF 20-33; 44-57; 64-80 AND 86-122, TISSUE SPECIFICITY, AND RP MASS SPECTROMETRY. RX PubMed=12973732; DOI=10.1002/pmic.200300514; RA Howard B.A., Wang M.Z., Campa M.J., Corro C., Fitzgerald M.C., RA Patz E.F. Jr.; RT "Identification and validation of a potential lung cancer serum biomarker RT detected by matrix-assisted laser desorption/ionization-time of flight RT spectra analysis."; RL Proteomics 3:1720-1724(2003). RN [19] RP PARTIAL PROTEIN SEQUENCE (VARIOUS FORMS), AND METHYLATION AT ASN-101. RX PubMed=8783012; DOI=10.1002/elps.1150170508; RA Ducret A., Bruun C.F., Bures E.J., Marhaug G., Husby G., Aebersold R.; RT "Characterization of human serum amyloid A protein isoforms separated by RT two-dimensional electrophoresis by liquid chromatography/electrospray RT ionization tandem mass spectrometry."; RL Electrophoresis 17:866-876(1996). RN [20] RP IDENTIFICATION OF ALLELE SAA1.4. RX PubMed=8670280; DOI=10.1006/bbrc.1996.0892; RA Westermark P., Sletten K., Westermark G.T., Raynes J., McAdam K.P.; RT "A protein AA-variant derived from a novel serum AA protein, SAA1 delta, in RT an individual from Papua New Guinea."; RL Biochem. Biophys. Res. Commun. 223:320-323(1996). RN [21] RP POLYMORPHISM, AND NOMENCLATURE OF ALLELES. RX PubMed=10211414; DOI=10.3109/13506129908993291; RA Sipe J.; RT "Revised nomenclature for serum amyloid A (SAA). Nomenclature Committee of RT the International Society of Amyloidosis. Part 2."; RL Amyloid 6:67-70(1999). RN [22] RP MASS SPECTROMETRY. RX PubMed=12606051; DOI=10.1016/s0014-5793(03)00097-8; RA Kiernan U.A., Tubbs K.A., Nedelkov D., Niederkofler E.E., Nelson R.W.; RT "Detection of novel truncated forms of human serum amyloid A protein in RT human plasma."; RL FEBS Lett. 537:166-170(2003). RN [23] RP IDENTIFICATION OF ALLELE SAA1.3. RX PubMed=8512321; DOI=10.1006/abbi.1993.1296; RA Baba S., Takahashi T., Kasama T., Fujie M., Shirasawa H.; RT "A novel polymorphism of human serum amyloid A protein, SAA1 gamma, is RT characterized by alanines at both residues 52 and 57."; RL Arch. Biochem. Biophys. 303:361-366(1993). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 19-122, SUBUNIT, AND MUTAGENESIS RP OF ARG-19; ARG-33; ARG-37; ARG-65; ARG-80 AND HIS-89. RX PubMed=24706838; DOI=10.1073/pnas.1322357111; RA Lu J., Yu Y., Zhu I., Cheng Y., Sun P.D.; RT "Structural mechanism of serum amyloid A-mediated inflammatory RT amyloidosis."; RL Proc. Natl. Acad. Sci. U.S.A. 111:5189-5194(2014). CC -!- FUNCTION: Major acute phase protein. CC -!- SUBUNIT: Homohexamer; dimer of trimers. Can form amyloid fibrils after CC partial proteolysis; the native, undenatured protein does not form CC amyloid fibrils (in vitro). Apolipoprotein of the HDL complex. Binds to CC heparin. {ECO:0000269|PubMed:24706838, ECO:0000269|PubMed:7115671}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7115671}. CC -!- TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma (at CC protein level). {ECO:0000269|PubMed:12973732, CC ECO:0000269|PubMed:4816450, ECO:0000269|PubMed:7115671}. 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 24 residues from the C-terminal CC end. CC -!- MASS SPECTROMETRY: [Serum amyloid A-1 protein]: Mass=11702; CC Mass_error=14; Method=MALDI; Evidence={ECO:0000269|PubMed:12973732}; CC -!- MASS SPECTROMETRY: [Serum amyloid A-1 protein]: Mass=11682.7; CC Method=MALDI; Evidence={ECO:0000269|PubMed:12606051}; CC -!- MASS SPECTROMETRY: [Serum amyloid protein A(2-104)]: Mass=11526.5; CC Method=MALDI; Evidence={ECO:0000269|PubMed:12606051}; CC -!- MASS SPECTROMETRY: [Serum amyloid protein A(3-104)]: Mass=11439.6; CC Method=MALDI; Evidence={ECO:0000269|PubMed:12606051}; CC -!- MASS SPECTROMETRY: [Serum amyloid protein A(2-103)]: Mass=11363.6; CC Method=MALDI; Evidence={ECO:0000269|PubMed:12606051}; CC -!- MASS SPECTROMETRY: [Serum amyloid protein A(2-102)]: Mass=11235.6; CC Method=MALDI; Evidence={ECO:0000269|PubMed:12606051}; CC -!- MASS SPECTROMETRY: [Serum amyloid protein A(4-101)]: Mass=10872.6; CC Method=MALDI; Evidence={ECO:0000269|PubMed:12606051}; CC -!- MASS SPECTROMETRY: [Amyloid protein A]: Mass=8337.5; Mass_error=0.8; CC Method=Electrospray; Note=With variants Asn-78 and 86-Leu-Thr-87.; CC Evidence={ECO:0000269|PubMed:1463770}; CC -!- MASS SPECTROMETRY: [Amyloid protein A]: Mass=8390.9; Mass_error=0.2; CC Method=Electrospray; Evidence={ECO:0000269|PubMed:1463770}; CC -!- POLYMORPHISM: At least 5 different SAA1 alleles have been described: CC SAA1.1 (SAA1alpha), SAA1.2 (SAA1beta), SAA1.3 (SAA1gamma), SAA1.4 CC (SAA1delta), SAA1.5 (also named SAA1beta but which differs from CC SAA1.2). We use here the revised nomenclature described in CC PubMed:10211414. The sequence shown is that of SAA1.2. CC -!- DISEASE: Note=Reactive, secondary amyloidosis is characterized by the CC extracellular accumulation in various tissues of the SAA1 protein. CC These deposits are highly insoluble and resistant to proteolysis; they CC disrupt tissue structure and compromise function. CC {ECO:0000269|PubMed:1463770}. CC -!- DISEASE: Note=Elevated serum SAA1 protein levels may be associated with CC lung cancer. {ECO:0000269|PubMed:1463770}. 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 EMBL; M10906; AAA60297.1; -; mRNA. DR EMBL; M23698; AAA64799.1; -; mRNA. DR EMBL; X56652; CAA39974.1; -; Genomic_DNA. DR EMBL; CR542241; CAG47037.1; -; mRNA. DR EMBL; AC107948; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC007022; AAH07022.1; -; mRNA. DR EMBL; BC105796; AAI05797.1; -; mRNA. DR EMBL; X51439; CAA35804.1; -; mRNA. DR EMBL; X51441; CAA35806.1; -; mRNA. DR EMBL; X51442; CAA35807.1; -; mRNA. DR CCDS; CCDS7835.1; -. DR PIR; A22342; YLHUS. DR PIR; I39456; I39456. DR RefSeq; NP_000322.2; NM_000331.5. DR RefSeq; NP_001171477.1; NM_001178006.2. DR RefSeq; NP_954630.1; NM_199161.4. DR PDB; 4IP8; X-ray; 2.19 A; A/B/C/D=19-122. DR PDB; 4IP9; X-ray; 2.50 A; A/B=19-122. DR PDB; 6MST; EM; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=20-85. DR PDB; 7ZKY; EM; 2.56 A; A/B/C/D/E/F/G/H/I/J/K/L=20-87. DR PDBsum; 4IP8; -. DR PDBsum; 4IP9; -. DR PDBsum; 6MST; -. DR PDBsum; 7ZKY; -. DR AlphaFoldDB; P0DJI8; -. DR EMDB; EMD-14771; -. DR EMDB; EMD-9232; -. DR SMR; P0DJI8; -. DR BioGRID; 112196; 45. DR STRING; 9606.ENSP00000384906; -. DR iPTMnet; P0DJI8; -. DR PhosphoSitePlus; P0DJI8; -. DR BioMuta; SAA1; -. DR DMDM; 395406826; -. DR EPD; P0DJI8; -. DR jPOST; P0DJI8; -. DR MassIVE; P0DJI8; -. DR PaxDb; 9606-ENSP00000384906; -. DR PeptideAtlas; P0DJI8; -. DR ProteomicsDB; 22986; -. DR ProteomicsDB; 52549; -. DR ABCD; P0DJI8; 3 sequenced antibodies. DR Antibodypedia; 12220; 699 antibodies from 35 providers. DR DNASU; 6288; -. DR Ensembl; ENST00000356524.9; ENSP00000348918.4; ENSG00000173432.13. DR Ensembl; ENST00000405158.2; ENSP00000384906.2; ENSG00000173432.13. DR Ensembl; ENST00000532858.5; ENSP00000436866.1; ENSG00000173432.13. DR Ensembl; ENST00000672418.1; ENSP00000500630.1; ENSG00000288411.1. DR Ensembl; ENST00000672662.1; ENSP00000500281.1; ENSG00000288411.1. DR Ensembl; ENST00000672712.1; ENSP00000500639.1; ENSG00000288411.1. DR GeneID; 6288; -. DR KEGG; hsa:6288; -. DR MANE-Select; ENST00000356524.9; ENSP00000348918.4; NM_199161.5; NP_954630.2. DR UCSC; uc057zpu.1; human. DR AGR; HGNC:10513; -. DR CTD; 6288; -. DR DisGeNET; 6288; -. DR GeneCards; SAA1; -. DR HGNC; HGNC:10513; SAA1. DR HPA; ENSG00000173432; Tissue enriched (liver). DR MalaCards; SAA1; -. DR MIM; 104750; gene. DR neXtProt; NX_P0DJI8; -. DR OpenTargets; ENSG00000173432; -. DR Orphanet; 85445; AA amyloidosis. DR VEuPathDB; HostDB:ENSG00000173432; -. DR eggNOG; ENOG502S4PB; Eukaryota. DR GeneTree; ENSGT00390000004737; -. DR HOGENOM; CLU_129936_0_0_1; -. DR InParanoid; P0DJI8; -. DR OMA; HEDTIAD; -. DR OrthoDB; 2958429at2759; -. DR PhylomeDB; P0DJI8; -. DR TreeFam; TF332544; -. DR PathwayCommons; P0DJI8; -. DR Reactome; R-HSA-3000471; Scavenging by Class B Receptors. DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR Reactome; R-HSA-444473; Formyl peptide receptors bind formyl peptides and many other ligands. DR Reactome; R-HSA-445989; TAK1-dependent IKK and NF-kappa-B activation. DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling. DR Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling. DR Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation. DR Reactome; R-HSA-977225; Amyloid fiber formation. DR SignaLink; P0DJI8; -. DR BioGRID-ORCS; 6288; 15 hits in 1063 CRISPR screens. DR ChiTaRS; SAA1; human. DR GeneWiki; Serum_amyloid_A1; -. DR GenomeRNAi; 6288; -. DR Pharos; P0DJI8; Tbio. DR PRO; PR:P0DJI8; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P0DJI8; Protein. DR Bgee; ENSG00000173432; Expressed in right lobe of liver and 88 other cell types or tissues. DR ExpressionAtlas; P0DJI8; baseline and differential. DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:CACAO. DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW. DR GO; GO:0001664; F:G protein-coupled receptor binding; IDA:UniProtKB. DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW. DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW. DR GO; GO:0048247; P:lymphocyte chemotaxis; IDA:UniProtKB. DR GO; GO:0048246; P:macrophage chemotaxis; IDA:UniProtKB. DR GO; GO:0050728; P:negative regulation of inflammatory response; NAS:UniProtKB. DR GO; GO:0030593; P:neutrophil chemotaxis; NAS:UniProtKB. DR GO; GO:0030168; P:platelet activation; NAS:UniProtKB. DR GO; GO:0045785; P:positive regulation of cell adhesion; IDA:UniProtKB. DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB. DR GO; GO:0032732; P:positive regulation of interleukin-1 production; NAS:UniProtKB. DR GO; GO:0050708; P:regulation of protein secretion; NAS:UniProtKB. 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. DR Genevisible; P0DJI8; HS. PE 1: Evidence at protein level; KW 3D-structure; Acute phase; Amyloid; Amyloidosis; Direct protein sequencing; KW HDL; Heparin-binding; Methylation; Reference proteome; Secreted; Signal. FT SIGNAL 1..18 FT /evidence="ECO:0000269|PubMed:11946204, FT ECO:0000269|PubMed:1259755, ECO:0000269|PubMed:1463770, FT ECO:0000269|PubMed:1546977, ECO:0000269|PubMed:4816450, FT ECO:0000269|PubMed:5055786, ECO:0000269|PubMed:5056669, FT ECO:0000269|PubMed:6155694, ECO:0000269|PubMed:7115671" FT CHAIN 19..122 FT /note="Serum amyloid A-1 protein" FT /id="PRO_0000031575" FT CHAIN 19..94 FT /note="Amyloid protein A" FT /id="PRO_0000031576" FT CHAIN 20..122 FT /note="Serum amyloid protein A(2-104)" FT /id="PRO_0000031577" FT CHAIN 20..121 FT /note="Serum amyloid protein A(2-103)" FT /id="PRO_0000031578" FT CHAIN 20..120 FT /note="Serum amyloid protein A(2-102)" FT /id="PRO_0000031579" FT CHAIN 21..122 FT /note="Serum amyloid protein A(3-104)" FT /id="PRO_0000031580" FT CHAIN 22..119 FT /note="Serum amyloid protein A(4-101)" FT /id="PRO_0000031581" FT PROPEP 95..122 FT /note="Often cleaved during amyloidogenesis" FT /id="PRO_0000031582" FT REGION 19..45 FT /note="Important for amyloid formation; forms amyloid FT fibrils in vitro" FT REGION 98..122 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 101 FT /note="N4,N4-dimethylasparagine" FT /evidence="ECO:0000305|PubMed:8783012" FT VARIANT 15 FT /note="G -> S (in dbSNP:rs1232745554)" FT /id="VAR_006925" FT VARIANT 70 FT /note="A -> V (in allele SAA1.1)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:3183061, ECO:0000269|PubMed:3839415" FT /id="VAR_006926" FT VARIANT 75 FT /note="V -> A (in allele SAA1.1 and allele SAA1.3)" FT /evidence="ECO:0000269|PubMed:1463770, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1971508, FT ECO:0000269|PubMed:3183061, ECO:0000269|PubMed:3839415" FT /id="VAR_006927" FT VARIANT 77 FT /note="T -> S (requires 2 nucleotide substitutions; FT dbSNP:rs1671926)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16554811, ECO:0000269|PubMed:1656519, FT ECO:0000269|PubMed:1971508, ECO:0000269|PubMed:3183061, FT ECO:0000269|PubMed:3839415, ECO:0000269|Ref.4" FT /id="VAR_088562" FT VARIANT 78 FT /note="D -> N (in allele SAA1.4; dbSNP:rs557915415)" FT /evidence="ECO:0000269|PubMed:1463770, FT ECO:0000269|PubMed:1971508" FT /id="VAR_006928" FT VARIANT 86 FT /note="F -> L (in dbSNP:rs1059559)" FT /id="VAR_057167" FT VARIANT 90 FT /note="G -> D (in allele SAA1.2; dbSNP:rs79681911)" FT /id="VAR_006931" FT MUTAGEN 19 FT /note="R->A: Reduces affinity for heparin and nearly FT abolishes association with HDL; when associated with A-80 FT and A-89." FT /evidence="ECO:0000269|PubMed:24706838" FT MUTAGEN 33 FT /note="R->A: Reduces affinity for heparin; when associated FT with A-37 and A-65." FT /evidence="ECO:0000269|PubMed:24706838" FT MUTAGEN 37 FT /note="R->A: Reduces affinity for heparin; when associated FT with A-33 and A-65." FT /evidence="ECO:0000269|PubMed:24706838" FT MUTAGEN 65 FT /note="R->A: Reduces affinity for heparin; when associated FT with A-33 and A-37." FT /evidence="ECO:0000269|PubMed:24706838" FT MUTAGEN 80 FT /note="R->A: Reduces affinity for heparin and nearly FT abolishes association with HDL; when associated with A-18 FT and A-89." FT /evidence="ECO:0000269|PubMed:24706838" FT MUTAGEN 89 FT /note="H->A: Reduces affinity for heparin and nearly FT abolishes association with HDL; when associated with A-18 FT and A-80." FT /evidence="ECO:0000269|PubMed:24706838" FT CONFLICT 71 FT /note="W -> R (in Ref. 10; AA sequence and 11; AA FT sequence)" FT /evidence="ECO:0000305" FT CONFLICT 96..101 FT /note="ADQAAN -> SEATVK (in Ref. 9; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 101 FT /note="N -> D (in Ref. 6; AAH07022)" FT /evidence="ECO:0000305" FT CONFLICT 119 FT /note="P -> S (in Ref. 1; AAA60297)" FT /evidence="ECO:0000305" FT HELIX 19..45 FT /evidence="ECO:0007829|PDB:4IP8" FT STRAND 47..49 FT /evidence="ECO:0007829|PDB:7ZKY" FT HELIX 51..65 FT /evidence="ECO:0007829|PDB:4IP8" FT HELIX 67..86 FT /evidence="ECO:0007829|PDB:4IP8" FT HELIX 91..105 FT /evidence="ECO:0007829|PDB:4IP8" FT HELIX 110..113 FT /evidence="ECO:0007829|PDB:4IP8" SQ SEQUENCE 122 AA; 13546 MW; 8C43BF06AA47B179 CRC64; MKLLTGLVFC SLVLGVSSRS FFSFLGEAFD GARDMWRAYS DMREANYIGS DKYFHARGNY DAAKRGPGGA WAAEVITDAR ENIQRFFGHG AEDSLADQAA NEWGRSGKDP NHFRPAGLPE KY //