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Serum amyloid A-1 protein (SAA) [Cleaved into: Amyloid protein A (Amyloid fibril protein AA); Serum amyloid protein A(2-104); Serum amyloid protein A(3-104); Serum amyloid protein A(2-103); Serum amyloid protein A(2-102); Serum amyloid protein A(4-101)]

 SAA1_HUMAN              Reviewed;         122 AA.
P0DJI8; P02735; P02736; P02737; Q16730; Q16834; Q16835; Q16879;
Q3KRB3; Q6FG67; Q96QN0; Q9UCK9; Q9UCL0;
11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
11-JUL-2012, sequence version 1.
10-OCT-2018, entry version 55.
RecName: Full=Serum amyloid A-1 protein;
Short=SAA;
Contains:
RecName: Full=Amyloid protein A;
AltName: Full=Amyloid fibril protein AA;
Contains:
RecName: Full=Serum amyloid protein A(2-104);
Contains:
RecName: Full=Serum amyloid protein A(3-104);
Contains:
RecName: Full=Serum amyloid protein A(2-103);
Contains:
RecName: Full=Serum amyloid protein A(2-102);
Contains:
RecName: Full=Serum amyloid protein A(4-101);
Flags: Precursor;
Name=SAA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE SAA1.1).
PubMed=3839415; DOI=10.1021/bi00333a018;
Sipe J.D., Colten H.R., Goldberger G., Edge M.D., Tack B.F.,
Cohen A.S., Whitehead A.S.;
"Human serum amyloid A (SAA): biosynthesis and postsynthetic
processing of preSAA and structural variants defined by complementary
DNA.";
Biochemistry 24:2931-2936(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE SAA1.1).
TISSUE=Liver;
PubMed=3183061; DOI=10.1172/JCI113779;
Kluve-Beckerman B., Dwulet F.E., Benson M.D.;
"Human serum amyloid A. Three hepatic mRNAs and the corresponding
proteins in one person.";
J. Clin. Invest. 82:1670-1675(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE SAA1.5).
TISSUE=Liver;
PubMed=1656519; DOI=10.1111/j.1365-3083.1991.tb01570.x;
Betts J., Edbrooke M., Thakker R., Woo P.;
"The human acute-phase serum amyloid A gene family: structure,
evolution and expression in hepatoma cells.";
Scand. J. Immunol. 34:471-482(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE SAA1.5).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE SAA1.5).
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE SAA1.1).
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 73-122, AND VARIANTS VAL-75 AND ASN-78.
TISSUE=Liver;
PubMed=1971508; DOI=10.1042/bj2680187;
Steinkasserer A., Weiss E.H., Schwaeble W., Linke R.P.;
"Heterogeneity of human serum amyloid A protein. Five different
variants from one individual demonstrated by cDNA sequence analysis.";
Biochem. J. 268:187-193(1990).
[8]
PROTEIN SEQUENCE OF 19-122, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE
SPECIFICITY.
PubMed=7115671; DOI=10.1021/bi00257a008;
Parmelee D.C., Titani K., Ericsson L.H., Eriksen N., Benditt E.P.,
Walsh K.A.;
"Amino acid sequence of amyloid-related apoprotein (apoSAA1) from
human high-density lipoprotein.";
Biochemistry 21:3298-3303(1982).
[9]
PROTEIN SEQUENCE OF 19-122 (ALLELE SAA1.2).
PubMed=1546977; DOI=10.1042/bj2820615;
Beach C.M., de Beer M.C., Sipe J.D., Loose L.D., de Beer F.C.;
"Human serum amyloid A protein. Complete amino acid sequence of a new
variant.";
Biochem. J. 282:615-620(1992).
[10]
PROTEIN SEQUENCE OF 19-101.
PubMed=6155694; DOI=10.1111/j.1365-3083.1980.tb00023.x;
Moyner K., Sletten K., Husby G., Natvig J.B.;
"An unusually large (83 amino acid residues) amyloid fibril protein AA
from a patient with Waldenstrom's macroglobulinaemia and
amyloidosis.";
Scand. J. Immunol. 11:549-554(1980).
[11]
PROTEIN SEQUENCE OF 19-94.
PubMed=5055786;
Ein D., Kimura S., Terry W.D., Magnotta J., Glenner G.G.;
"Amino acid sequence of an amyloid fibril protein of unknown origin.";
J. Biol. Chem. 247:5653-5655(1972).
[12]
PROTEIN SEQUENCE OF 19-94 (FAMILIAL MEDITERRANEAN FEVER PATIENT).
PubMed=5056669; DOI=10.1172/JCI107098;
Levin M., Franklin E.C., Frangione B., Pras M.;
"The amino acid sequence of a major nonimmunoglobulin component of
some amyloid fibrils.";
J. Clin. Invest. 51:2773-2776(1972).
[13]
PROTEIN SEQUENCE OF 19-94, AND TISSUE SPECIFICITY.
PubMed=4816450; DOI=10.1111/j.1432-1033.1974.tb03251.x;
Sletten K., Husby G.;
"The complete amino-acid sequence of non-immunoglobulin amyloid fibril
protein AS in rheumatoid arthritis.";
Eur. J. Biochem. 41:117-125(1974).
[14]
PROTEIN SEQUENCE OF 19-94, MASS SPECTROMETRY, DISEASE, VARIANTS
ALA-70; VAL-75 AND ASN-78, AND ALLELE SAA1.3.
TISSUE=Thyroid;
PubMed=1463770; DOI=10.1016/0925-4439(92)90068-X;
Baba S., Takahashi T., Kasama T., Shirasawa H.;
"Identification of two novel amyloid A protein subsets coexisting in
an individual patient of AA-amyloidosis.";
Biochim. Biophys. Acta 1180:195-200(1992).
[15]
PROTEIN SEQUENCE OF 19-82.
PubMed=1259755; DOI=10.1016/S0006-291X(76)80266-5;
Sletten K., Husby G., Natvig J.B.;
"The complete amino acid sequence of an amyloid fibril protein AA1 of
unusual size (64 residues).";
Biochem. Biophys. Res. Commun. 69:19-25(1976).
[16]
PROTEIN SEQUENCE OF 19-42.
PubMed=11946204; DOI=10.1016/0014-5793(71)80506-9;
Benditt E.P., Eriksen N., Hermodson M.A., Ericsson L.H.;
"The major proteins of human and monkey amyloid substance: common
properties including unusual N-terminal amino acid sequences.";
FEBS Lett. 19:169-173(1971).
[17]
PROTEIN SEQUENCE OF 20-100.
PubMed=3442653; DOI=10.1021/bi00399a035;
Prelli F., Pras M., Frangione B.;
"Degradation and deposition of amyloid AA fibrils are tissue
specific.";
Biochemistry 26:8251-8256(1987).
[18]
PROTEIN SEQUENCE OF 20-33; 44-57; 64-80 AND 86-122, TISSUE
SPECIFICITY, AND MASS SPECTROMETRY.
PubMed=12973732; DOI=10.1002/pmic.200300514;
Howard B.A., Wang M.Z., Campa M.J., Corro C., Fitzgerald M.C.,
Patz E.F. Jr.;
"Identification and validation of a potential lung cancer serum
biomarker detected by matrix-assisted laser desorption/ionization-time
of flight spectra analysis.";
Proteomics 3:1720-1724(2003).
[19]
PARTIAL PROTEIN SEQUENCE (VARIOUS FORMS), AND METHYLATION AT ASN-101.
PubMed=8783012; DOI=10.1002/elps.1150170508;
Ducret A., Bruun C.F., Bures E.J., Marhaug G., Husby G., Aebersold R.;
"Characterization of human serum amyloid A protein isoforms separated
by two-dimensional electrophoresis by liquid
chromatography/electrospray ionization tandem mass spectrometry.";
Electrophoresis 17:866-876(1996).
[20]
IDENTIFICATION OF ALLELE SAA1.4.
PubMed=8670280; DOI=10.1006/bbrc.1996.0892;
Westermark P., Sletten K., Westermark G.T., Raynes J., McAdam K.P.;
"A protein AA-variant derived from a novel serum AA protein, SAA1
delta, in an individual from Papua New Guinea.";
Biochem. Biophys. Res. Commun. 223:320-323(1996).
[21]
POLYMORPHISM, AND NOMENCLATURE OF ALLELES.
PubMed=10211414; DOI=10.3109/13506129908993291;
Sipe J.;
"Revised nomenclature for serum amyloid A (SAA). Nomenclature
Committee of the International Society of Amyloidosis. Part 2.";
Amyloid 6:67-70(1999).
[22]
MASS SPECTROMETRY.
PubMed=12606051; DOI=10.1016/S0014-5793(03)00097-8;
Kiernan U.A., Tubbs K.A., Nedelkov D., Niederkofler E.E., Nelson R.W.;
"Detection of novel truncated forms of human serum amyloid A protein
in human plasma.";
FEBS Lett. 537:166-170(2003).
[23]
IDENTIFICATION OF ALLELE SAA1.3.
PubMed=8512321; DOI=10.1006/abbi.1993.1296;
Baba S., Takahashi T., Kasama T., Fujie M., Shirasawa H.;
"A novel polymorphism of human serum amyloid A protein, SAA1 gamma, is
characterized by alanines at both residues 52 and 57.";
Arch. Biochem. Biophys. 303:361-366(1993).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 19-122, SUBUNIT, AND
MUTAGENESIS OF ARG-19; ARG-33; ARG-37; ARG-65; ARG-80 AND HIS-89.
PubMed=24706838; DOI=10.1073/pnas.1322357111;
Lu J., Yu Y., Zhu I., Cheng Y., Sun P.D.;
"Structural mechanism of serum amyloid A-mediated inflammatory
amyloidosis.";
Proc. Natl. Acad. Sci. U.S.A. 111:5189-5194(2014).
-!- FUNCTION: Major acute phase protein.
-!- SUBUNIT: Homohexamer; dimer of trimers. Can form amyloid fibrils
after partial proteolysis; the native, undenatured protein does
not form amyloid fibrils (in vitro). Apolipoprotein of the HDL
complex. Binds to heparin. {ECO:0000269|PubMed:24706838,
ECO:0000269|PubMed:7115671}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7115671}.
-!- TISSUE SPECIFICITY: Expressed by the liver; secreted in plasma (at
protein level). {ECO:0000269|PubMed:12973732,
ECO:0000269|PubMed:4816450, ECO:0000269|PubMed:7115671}.
-!- INDUCTION: Upon cytokine stimulation.
-!- PTM: This protein is the precursor of amyloid protein A, which is
formed by the removal of approximately 24 residues from the C-
terminal end.
-!- MASS SPECTROMETRY: Mass=11702; Mass_error=14; Method=MALDI;
Range=19-122; Evidence={ECO:0000269|PubMed:12973732};
-!- MASS SPECTROMETRY: Mass=11682.7; Method=MALDI; Range=19-122;
Evidence={ECO:0000269|PubMed:12606051};
-!- MASS SPECTROMETRY: Mass=11526.5; Method=MALDI; Range=20-122;
Evidence={ECO:0000269|PubMed:12606051};
-!- MASS SPECTROMETRY: Mass=11439.6; Method=MALDI; Range=21-122;
Evidence={ECO:0000269|PubMed:12606051};
-!- MASS SPECTROMETRY: Mass=11363.6; Method=MALDI; Range=20-121;
Evidence={ECO:0000269|PubMed:12606051};
-!- MASS SPECTROMETRY: Mass=11235.6; Method=MALDI; Range=20-120;
Evidence={ECO:0000269|PubMed:12606051};
-!- MASS SPECTROMETRY: Mass=10872.6; Method=MALDI; Range=22-119;
Evidence={ECO:0000269|PubMed:12606051};
-!- MASS SPECTROMETRY: Mass=8337.5; Mass_error=0.8;
Method=Electrospray; Range=19-94; Note=With variants Ala-70, Val-
75, Asn-78 and 86-Leu-Thr-87.;
Evidence={ECO:0000269|PubMed:1463770};
-!- MASS SPECTROMETRY: Mass=8390.9; Mass_error=0.2;
Method=Electrospray; Range=19-94; Note=With variant Ala-70.;
Evidence={ECO:0000269|PubMed:1463770};
-!- POLYMORPHISM: At least 5 different SAA1 alleles have been
described: SAA1.1 (SAA1alpha), SAA1.2 (SAA1beta), SAA1.3
(SAA1gamma), SAA1.4 (SAA1delta), SAA1.5 (also named SAA1beta but
which differs from SAA1.2). We use here the revised nomenclature
described in PubMed:10211414. The sequence shown is that of
SAA1.1.
-!- DISEASE: Note=Reactive, secondary amyloidosis is characterized by
the extracellular accumulation in various tissues of the SAA1
protein. These deposits are highly insoluble and resistant to
proteolysis; they disrupt tissue structure and compromise
function. {ECO:0000269|PubMed:1463770}.
-!- DISEASE: Note=Elevated serum SAA1 protein levels may be associated
with lung cancer. {ECO:0000269|PubMed:1463770}.
-!- SIMILARITY: Belongs to the SAA family. {ECO:0000305}.
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EMBL; M10906; AAA60297.1; -; mRNA.
EMBL; M23698; AAA64799.1; -; mRNA.
EMBL; X56652; CAA39974.1; -; Genomic_DNA.
EMBL; CR542241; CAG47037.1; -; mRNA.
EMBL; AC107948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007022; AAH07022.1; -; mRNA.
EMBL; BC105796; AAI05797.1; -; mRNA.
EMBL; X51439; CAA35804.1; -; mRNA.
EMBL; X51441; CAA35806.1; -; mRNA.
EMBL; X51442; CAA35807.1; -; mRNA.
CCDS; CCDS7835.1; -.
PIR; A22342; YLHUS.
PIR; I39456; I39456.
RefSeq; NP_000322.2; NM_000331.5.
RefSeq; NP_001171477.1; NM_001178006.2.
RefSeq; NP_954630.1; NM_199161.4.
UniGene; Hs.632144; -.
UniGene; Hs.731376; -.
UniGene; Hs.734161; -.
PDB; 4IP8; X-ray; 2.19 A; A/B/C/D=19-122.
PDB; 4IP9; X-ray; 2.50 A; A/B=19-122.
PDBsum; 4IP8; -.
PDBsum; 4IP9; -.
ProteinModelPortal; P0DJI8; -.
SMR; P0DJI8; -.
BioGrid; 112196; 2.
STRING; 9606.ENSP00000348918; -.
DrugBank; DB00062; Human Serum Albumin.
DrugBank; DB00064; Serum albumin iodonated.
iPTMnet; P0DJI8; -.
PhosphoSitePlus; P0DJI8; -.
BioMuta; SAA1; -.
DMDM; 395406826; -.
EPD; P0DJI8; -.
PaxDb; P0DJI8; -.
PeptideAtlas; P0DJI8; -.
PRIDE; P0DJI8; -.
ProteomicsDB; 52549; -.
Ensembl; ENST00000356524; ENSP00000348918; ENSG00000173432.
Ensembl; ENST00000405158; ENSP00000384906; ENSG00000173432.
GeneID; 6288; -.
KEGG; hsa:6288; -.
UCSC; uc057zpu.1; human.
CTD; 6288; -.
DisGeNET; 6288; -.
EuPathDB; HostDB:ENSG00000173432.10; -.
GeneCards; SAA1; -.
HGNC; HGNC:10513; SAA1.
MalaCards; SAA1; -.
MIM; 104750; gene.
neXtProt; NX_P0DJI8; -.
Orphanet; 85445; Secondary amyloidosis.
eggNOG; ENOG410IXU4; Eukaryota.
eggNOG; ENOG410YSBK; LUCA.
InParanoid; P0DJI8; -.
KO; K17310; -.
OrthoDB; EOG091G17YH; -.
PhylomeDB; P0DJI8; -.
TreeFam; TF332544; -.
Reactome; R-HSA-3000471; Scavenging by Class B Receptors.
Reactome; R-HSA-416476; G alpha (q) signalling events.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-444473; Formyl peptide receptors bind formyl peptides and many other ligands.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
Reactome; R-HSA-977225; Amyloid fiber formation.
ChiTaRS; SAA1; human.
GeneWiki; Serum_amyloid_A1; -.
GenomeRNAi; 6288; -.
PRO; PR:P0DJI8; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000173432; Expressed in 89 organ(s), highest expression level in liver.
CleanEx; HS_SAA1; -.
ExpressionAtlas; P0DJI8; baseline and differential.
Genevisible; P0DJI8; HS.
GO; GO:0005881; C:cytoplasmic microtubule; IDA:CACAO.
GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0042056; F:chemoattractant activity; IBA:GO_Central.
GO; GO:0001664; F:G-protein coupled receptor binding; IDA:UniProtKB.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0000187; P:activation of MAPK activity; IDA:CACAO.
GO; GO:0006953; P:acute-phase response; NAS:UniProtKB.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0045087; P:innate immune response; TAS:Reactome.
GO; GO:0048247; P:lymphocyte chemotaxis; IDA:UniProtKB.
GO; GO:0048246; P:macrophage chemotaxis; IDA:UniProtKB.
GO; GO:0050728; P:negative regulation of inflammatory response; NAS:UniProtKB.
GO; GO:0030593; P:neutrophil chemotaxis; NAS:UniProtKB.
GO; GO:0030168; P:platelet activation; NAS:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; IDA:UniProtKB.
GO; GO:0050715; P:positive regulation of cytokine secretion; IDA:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
GO; GO:0050716; P:positive regulation of interleukin-1 secretion; NAS:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0050708; P:regulation of protein secretion; NAS:UniProtKB.
InterPro; IPR000096; Serum_amyloid_A.
Pfam; PF00277; SAA; 1.
PIRSF; PIRSF002472; Serum_amyloid_A; 1.
PRINTS; PR00306; SERUMAMYLOID.
SMART; SM00197; SAA; 1.
PROSITE; PS00992; SAA; 1.
1: Evidence at protein level;
3D-structure; Acute phase; Amyloid; Amyloidosis; Complete proteome;
Direct protein sequencing; HDL; Heparin-binding; Methylation;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 18 {ECO:0000269|PubMed:11946204,
ECO:0000269|PubMed:1259755,
ECO:0000269|PubMed:1463770,
ECO:0000269|PubMed:1546977,
ECO:0000269|PubMed:4816450,
ECO:0000269|PubMed:5055786,
ECO:0000269|PubMed:5056669,
ECO:0000269|PubMed:6155694,
ECO:0000269|PubMed:7115671}.
CHAIN 19 122 Serum amyloid A-1 protein.
/FTId=PRO_0000031575.
CHAIN 19 94 Amyloid protein A.
/FTId=PRO_0000031576.
CHAIN 20 122 Serum amyloid protein A(2-104).
/FTId=PRO_0000031577.
CHAIN 20 121 Serum amyloid protein A(2-103).
/FTId=PRO_0000031578.
CHAIN 20 120 Serum amyloid protein A(2-102).
/FTId=PRO_0000031579.
CHAIN 21 122 Serum amyloid protein A(3-104).
/FTId=PRO_0000031580.
CHAIN 22 119 Serum amyloid protein A(4-101).
/FTId=PRO_0000031581.
PROPEP 95 122 Often cleaved during amyloidogenesis.
/FTId=PRO_0000031582.
REGION 19 45 Important for amyloid formation; forms
amyloid fibrils in vitro.
MOD_RES 101 101 N4,N4-dimethylasparagine.
{ECO:0000305|PubMed:8783012}.
VARIANT 15 15 G -> S (in dbSNP:rs712021).
/FTId=VAR_006925.
VARIANT 70 70 V -> A (in allele SAA1.2, SAA1.3, SAA1.4
and SAA1.5).
{ECO:0000269|PubMed:1463770}.
/FTId=VAR_006926.
VARIANT 75 75 A -> V (in allele SAA1.2, SAA1.4 and
SAA1.5). {ECO:0000269|PubMed:1463770,
ECO:0000269|PubMed:1971508}.
/FTId=VAR_006927.
VARIANT 78 78 D -> N (in allele SAA1.4).
{ECO:0000269|PubMed:1463770,
ECO:0000269|PubMed:1971508}.
/FTId=VAR_006928.
VARIANT 86 86 F -> L (in dbSNP:rs1059559).
/FTId=VAR_057167.
VARIANT 90 90 G -> D (in allele SAA1.2).
/FTId=VAR_006931.
MUTAGEN 19 19 R->A: Reduces affinity for heparin and
nearly abolishes association with HDL;
when associated with A-80 and A-89.
{ECO:0000269|PubMed:24706838}.
MUTAGEN 33 33 R->A: Reduces affinity for heparin; when
associated with A-37 and A-65.
{ECO:0000269|PubMed:24706838}.
MUTAGEN 37 37 R->A: Reduces affinity for heparin; when
associated with A-33 and A-65.
{ECO:0000269|PubMed:24706838}.
MUTAGEN 65 65 R->A: Reduces affinity for heparin; when
associated with A-33 and A-37.
{ECO:0000269|PubMed:24706838}.
MUTAGEN 80 80 R->A: Reduces affinity for heparin and
nearly abolishes association with HDL;
when associated with A-18 and A-89.
{ECO:0000269|PubMed:24706838}.
MUTAGEN 89 89 H->A: Reduces affinity for heparin and
nearly abolishes association with HDL;
when associated with A-18 and A-80.
{ECO:0000269|PubMed:24706838}.
CONFLICT 71 71 W -> R (in Ref. 10; AA sequence and 11;
AA sequence). {ECO:0000305}.
CONFLICT 77 77 S -> T (in Ref. 5; AC107948).
{ECO:0000305}.
CONFLICT 96 101 ADQAAN -> SEATVK (in Ref. 9; AA
sequence). {ECO:0000305}.
CONFLICT 101 101 N -> D (in Ref. 6; AAH07022).
{ECO:0000305}.
CONFLICT 119 119 P -> S (in Ref. 1; AAA60297).
{ECO:0000305}.
HELIX 19 45 {ECO:0000244|PDB:4IP8}.
HELIX 51 65 {ECO:0000244|PDB:4IP8}.
HELIX 67 86 {ECO:0000244|PDB:4IP8}.
HELIX 91 105 {ECO:0000244|PDB:4IP8}.
HELIX 110 113 {ECO:0000244|PDB:4IP8}.
SEQUENCE 122 AA; 13532 MW; 43A57D56B37CB173 CRC64;
MKLLTGLVFC SLVLGVSSRS FFSFLGEAFD GARDMWRAYS DMREANYIGS DKYFHARGNY
DAAKRGPGGV WAAEAISDAR ENIQRFFGHG AEDSLADQAA NEWGRSGKDP NHFRPAGLPE
KY


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