SAA1_HUMAN
ID SAA1_HUMAN Reviewed; 122 AA.
AC P0DJI8; P02735; P02736; P02737; Q16730; Q16834; Q16835; Q16879; Q3KRB3;
AC Q6FG67; Q96QN0; Q9UCK9; Q9UCL0;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2012, sequence version 1.
DT 03-AUG-2022, entry version 79.
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).
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).
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).
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).
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).
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 VAL-75 AND 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-70;
RP VAL-75 AND 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 Ala-70, Val-75, Asn-78 and 86-
CC Leu-Thr-87.; Evidence={ECO:0000269|PubMed:1463770};
CC -!- MASS SPECTROMETRY: [Amyloid protein A]: Mass=8390.9; Mass_error=0.2;
CC Method=Electrospray; Note=With variant Ala-70.;
CC 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 SAA1.1.
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}.
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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 PDBsum; 4IP8; -.
DR PDBsum; 4IP9; -.
DR PDBsum; 6MST; -.
DR AlphaFoldDB; P0DJI8; -.
DR SMR; P0DJI8; -.
DR BioGRID; 112196; 44.
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; P0DJI8; -.
DR PeptideAtlas; P0DJI8; -.
DR PRIDE; P0DJI8; -.
DR ProteomicsDB; 52549; -.
DR ABCD; P0DJI8; 3 sequenced antibodies.
DR Antibodypedia; 12220; 600 antibodies from 35 providers.
DR DNASU; 6288; -.
DR Ensembl; ENST00000356524.9; ENSP00000348918.4; ENSG00000173432.13.
DR Ensembl; ENST00000405158.2; ENSP00000384906.2; ENSG00000173432.13.
DR GeneID; 6288; -.
DR KEGG; hsa:6288; -.
DR UCSC; uc057zpu.1; human.
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 Orphanet; 85445; AA amyloidosis.
DR VEuPathDB; HostDB:ENSG00000173432; -.
DR eggNOG; ENOG502S4PB; Eukaryota.
DR HOGENOM; CLU_129936_0_0_1; -.
DR InParanoid; P0DJI8; -.
DR OrthoDB; 1417043at2759; -.
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; 12 hits in 1000 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 87 other tissues.
DR ExpressionAtlas; P0DJI8; baseline and differential.
DR Genevisible; P0DJI8; HS.
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 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 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="V -> A (in allele SAA1.2, SAA1.3, SAA1.4 and
FT SAA1.5)"
FT /evidence="ECO:0000269|PubMed:1463770"
FT /id="VAR_006926"
FT VARIANT 75
FT /note="A -> V (in allele SAA1.2, SAA1.4 and SAA1.5)"
FT /evidence="ECO:0000269|PubMed:1463770,
FT ECO:0000269|PubMed:1971508"
FT /id="VAR_006927"
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 77
FT /note="S -> T (in Ref. 5; AC107948)"
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:6MST"
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; 13532 MW; 43A57D56B37CB173 CRC64;
MKLLTGLVFC SLVLGVSSRS FFSFLGEAFD GARDMWRAYS DMREANYIGS DKYFHARGNY
DAAKRGPGGV WAAEAISDAR ENIQRFFGHG AEDSLADQAA NEWGRSGKDP NHFRPAGLPE
KY
