Serum amyloid A protein precursor - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P02735 (SAA_HUMAN)

Last modified November 24, 2009. Version 117. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Serum amyloid A protein
      Short name=SAA
Cleaved into the following 6 chains:
    1- Recommended name:
            Amyloid protein A
        Alternative name(s):
            Amyloid fibril protein AA
    2- Recommended name:
            Serum amyloid protein A(2-104)
    3- Recommended name:
            Serum amyloid protein A(3-104)
    4- Recommended name:
            Serum amyloid protein A(2-103)
    5- Recommended name:
            Serum amyloid protein A(2-102)
    6- Recommended name:
            Serum amyloid protein A(4-101)

Gene names

Name:	SAA1
AND
Name:	SAA2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	122 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Major acute phase reactant. Apolipoprotein of the HDL complex.
Subcellular location	Secreted.
Tissue specificity	Expressed by the liver; secreted in plasma. Ref.20
Induction	Upon cytokine stimulation.
Post-translational modification	This protein is the precursor of amyloid protein A, which is formed by the removal of approximately 24 residues from the C-terminal end.
Polymorphism	Both SAA1 and SAA2 have a number of alleles. We use here the nomenclature of Ref.11. The sequence shown is that of 1-alpha.
Involvement in disease	Reactive, secondary amyloidosis is characterized by the extracellular accumulation in various tissues of the SAA protein. These deposits are highly insoluble and resistant to proteolysis; they disrupt tissue structure and compromise function.
Miscellaneous	Elevated serum SSA protein levels may be associated with lung cancer.
Sequence similarities	Belongs to the SAA family.
Mass spectrometry	Molecular mass is 11702±14 Da from positions 19 - 122. Determined by MALDI. Ref.20 Molecular mass is 11682.7 Da from positions 19 - 122. Determined by MALDI. Ref.22 Molecular mass is 11526.5 Da from positions 20 - 122. Determined by MALDI. Ref.22 Molecular mass is 11439.6 Da from positions 21 - 122. Determined by MALDI. Ref.22 Molecular mass is 11363.6 Da from positions 20 - 121. Determined by MALDI. Ref.22 Molecular mass is 11235.6 Da from positions 20 - 120. Determined by MALDI. Ref.22 Molecular mass is 10872.6 Da from positions 22 - 119. Determined by MALDI. Ref.22 Molecular mass is 8337.5±0.8 Da from positions 19 - 94. Determined by ESI. With variants Ala-70, Val-75, Asn-78 and 86-Leu-Thr-87. Ref.16 Molecular mass is 8390.9±0.2 Da from positions 19 - 94. Determined by ESI. With variant Ala-70. Ref.16

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Ontologies

Keywords
Biological process	Acute phase
Cellular component	Amyloid HDL Secreted
Coding sequence diversity	Polymorphism
Disease	Amyloidosis
Domain	Signal
PTM	Methylation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	acute-phase response Non-traceable author statement. Source: UniProtKB elevation of cytosolic calcium ion concentration Inferred from direct assay. Source: UniProtKB lymphocyte chemotaxis Inferred from direct assay. Source: UniProtKB macrophage chemotaxis Inferred from direct assay. Source: UniProtKB negative regulation of inflammatory response Non-traceable author statement. Source: UniProtKB neutrophil chemotaxis Non-traceable author statement. Source: UniProtKB platelet activation Non-traceable author statement. Source: UniProtKB positive regulation of cell adhesion Inferred from direct assay. Source: UniProtKB positive regulation of interleukin-1 secretion Non-traceable author statement. Source: UniProtKB
Cellular component	high-density lipoprotein particle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	G-protein-coupled receptor binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

Ref.16 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18

Chain

19 – 122

104

Serum amyloid A protein

PRO_0000031575

Chain

19 – 94

Amyloid protein A

PRO_0000031576

Chain

20 – 122

103

Serum amyloid protein A(2-104)

PRO_0000031577

Chain

20 – 121

102

Serum amyloid protein A(2-103)

PRO_0000031578

Chain

20 – 120

101

Serum amyloid protein A(2-102)

PRO_0000031579

Chain

21 – 122

102

Serum amyloid protein A(3-104)

PRO_0000031580

Chain

22 – 119

Serum amyloid protein A(4-101)

PRO_0000031581

Propeptide

95 – 122

Often cleaved during amyloidogenesis

PRO_0000031582

Amino acid modifications

Modified residue

101

N4,N4-dimethylasparagine Probable

Natural variations

Natural variant

G → S: dbSNP rs712021.

VAR_006925

Natural variant

V → A in 2-alpha, 2-beta, 1-beta and 1-gamma. Ref.16 Ref.7

VAR_006926

Natural variant

A → V in 2-alpha, 2-beta and 1-beta. Ref.16 Ref.7

VAR_006927

Natural variant

D → N in 2-alpha and 2-beta. Ref.16

VAR_006928

Natural variant

86 – 87

FF → LT in 2-alpha and 2-beta.

VAR_006929

Natural variant

F → L: dbSNP rs1059559.

VAR_057167

Natural variant

H → R in 2-beta. dbSNP rs2229338.

VAR_006930

Natural variant

G → D in 1-beta.

VAR_006931

Natural variant

102

E → K in 2-alpha and 2-beta. dbSNP rs1059567.

VAR_006932

Natural variant

108

K → R in 2-alpha and 2-beta. dbSNP rs1059571.

VAR_006933

Experimental info

Sequence conflict

W → R AA sequence Ref.12

Sequence conflict

W → R AA sequence Ref.13

Sequence conflict

S → T in AC090099. Ref.8

Sequence conflict

96 – 101

ADQAAN → SEATVK AA sequence Ref.11

Sequence conflict

101

N → D in AAH07022. Ref.9

Sequence conflict

119

P → S in AAA60297. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P02735-1 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: 43A57D56B37CB173
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FASTA

122

13,532

        10         20         30         40         50         60 
MKLLTGLVFC SLVLGVSSRS FFSFLGEAFD GARDMWRAYS DMREANYIGS DKYFHARGNY 

        70         80         90        100        110        120 
DAAKRGPGGV WAAEAISDAR ENIQRFFGHG AEDSLADQAA NEWGRSGKDP NHFRPAGLPE 


KY

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human serum amyloid A (SAA): biosynthesis and postsynthetic processing of preSAA and structural variants defined by complementary DNA." Sipe J.D., Colten H.R., Goldberger G., Edge M.D., Tack B.F., Cohen A.S., Whitehead A.S. Biochemistry 24:2931-2936(1985) [PubMed: 3839415] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"DNA sequence evidence for polymorphic forms of human serum amyloid A (SAA)." Kluve-Beckerman B., Long G.L., Benson M.D. Biochem. Genet. 24:795-803(1986) [PubMed: 3800865] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Structure of a human serum amyloid A gene and modulation of its expression in transfected L cells." Woo P., Sipe J., Dinarello C.A., Colten H.R. J. Biol. Chem. 262:15790-15795(1987) [PubMed: 2890635] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Human serum amyloid A. Three hepatic mRNAs and the corresponding proteins in one person." Kluve-Beckerman B., Dwulet F.E., Benson M.D. J. Clin. Invest. 82:1670-1675(1988) [PubMed: 3183061] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (SAA1 AND SAA2). Tissue: Liver.
[5]	"Heterogeneity of human serum amyloid A protein. Five different variants from one individual demonstrated by cDNA sequence analysis." Steinkasserer A., Weiss E.H., Schwaeble W., Linke R.P. Biochem. J. 268:187-193(1990) [PubMed: 1971508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[6]	"The human acute-phase serum amyloid A gene family: structure, evolution and expression in hepatoma cells." Betts J., Edbrooke M., Thakker R., Woo P. Scand. J. Immunol. 34:471-482(1991) [PubMed: 1656519] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Liver.
[7]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." 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. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ALA-70 AND VAL-75.
[8]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." 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. Sakaki Y. Nature 440:497-500(2006) [PubMed: 16554811] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS ALA-70 AND VAL-75.
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (SAA1 AND SAA2 ALPHA). Tissue: Liver.
[10]	"Amino acid sequence of amyloid-related apoprotein (apoSAA1) from human high-density lipoprotein." Parmelee D.C., Titani K., Ericsson L.H., Eriksen N., Benditt E.P., Walsh K.A. Biochemistry 21:3298-3303(1982) [PubMed: 7115671] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-122.
[11]	"Human serum amyloid A protein. Complete amino acid sequence of a new variant." Beach C.M., de Beer M.C., Sipe J.D., Loose L.D., de Beer F.C. Biochem. J. 282:615-620(1992) [PubMed: 1546977] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-122 (VARIANT 1-BETA).
[12]	"An unusually large (83 amino acid residues) amyloid fibril protein AA from a patient with Waldenstrom's macroglobulinaemia and amyloidosis." Moyner K., Sletten K., Husby G., Natvig J.B. Scand. J. Immunol. 11:549-554(1980) [PubMed: 6155694] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-101.
[13]	"Amino acid sequence of an amyloid fibril protein of unknown origin." Ein D., Kimura S., Terry W.D., Magnotta J., Glenner G.G. J. Biol. Chem. 247:5653-5655(1972) [PubMed: 5055786] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-94.
[14]	"The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils." Levin M., Franklin E.C., Frangione B., Pras M. J. Clin. Invest. 51:2773-2776(1972) [PubMed: 5056669] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-94 (FAMILIAL MEDITERRANEAN FEVER PATIENT).
[15]	"The complete amino-acid sequence of non-immunoglobulin amyloid fibril protein AS in rheumatoid arthritis." Sletten K., Husby G. Eur. J. Biochem. 41:117-125(1974) [PubMed: 4816450] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-94.
[16]	"Identification of two novel amyloid A protein subsets coexisting in an individual patient of AA-amyloidosis." Baba S., Takahashi T., Kasama T., Shirasawa H. Biochim. Biophys. Acta 1180:195-200(1992) [PubMed: 1463770] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-94, MASS SPECTOMETRY, VARIANTS ALA-70; VAL-75; ASN-78 AND 86-LEU-THR-87. Tissue: Thyroid.
[17]	"The complete amino acid sequence of an amyloid fibril protein AA1 of unusual size (64 residues)." Sletten K., Husby G., Natvig J.B. Biochem. Biophys. Res. Commun. 69:19-25(1976) [PubMed: 1259755] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-82.
[18]	"The major proteins of human and monkey amyloid substance: common properties including unusual N-terminal amino acid sequences." Benditt E.P., Eriksen N., Hermodson M.A., Ericsson L.H. FEBS Lett. 19:169-173(1971) [PubMed: 11946204] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-42.
[19]	"Degradation and deposition of amyloid AA fibrils are tissue specific." Prelli F., Pras M., Frangione B. Biochemistry 26:8251-8256(1987) [PubMed: 3442653] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-100.
[20]	"Identification and validation of a potential lung cancer serum biomarker detected by matrix-assisted laser desorption/ionization-time of flight spectra analysis." Howard B.A., Wang M.Z., Campa M.J., Corro C., Fitzgerald M.C., Patz E.F. Jr. Proteomics 3:1720-1724(2003) [PubMed: 12973732] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-33; 44-57; 64-80 AND 86-122, TISSUE SPECIFICITY, MASS SPECTROMETRY.
[21]	"Characterization of human serum amyloid A protein isoforms separated by two-dimensional electrophoresis by liquid chromatography/electrospray ionization tandem mass spectrometry." Ducret A., Bruun C.F., Bures E.J., Marhaug G., Husby G., Aebersold R. Electrophoresis 17:866-876(1996) [PubMed: 8783012] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE (VARIOUS FORMS), METHYLATION AT ASN-101.
[22]	"Detection of novel truncated forms of human serum amyloid A protein in human plasma." Kiernan U.A., Tubbs K.A., Nedelkov D., Niederkofler E.E., Nelson R.W. FEBS Lett. 537:166-170(2003) [PubMed: 12606051] [Abstract] Cited for: MASS SPECTROMETRY.
[23]	"A novel polymorphism of human serum amyloid A protein, SAA1 gamma, is characterized by alanines at both residues 52 and 57." Baba S., Takahashi T., Kasama T., Fujie M., Shirasawa H. Arch. Biochem. Biophys. 303:361-366(1993) [PubMed: 8512321] [Abstract] Cited for: VARIANT 1-GAMMA.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	M10906 mRNA. Translation: AAA60297.1. M26152 mRNA. Translation: AAA85338.1. J03474 Genomic DNA. Translation: AAB59539.1. M23698 mRNA. Translation: AAA64799.1. M23699 mRNA. Translation: AAA64800.1. M23700 mRNA. Translation: AAA64801.1. X51439 mRNA. Translation: CAA35804.1. X51440 mRNA. Translation: CAA35805.1. X51441 mRNA. Translation: CAA35806.1. X51442 mRNA. Translation: CAA35807.1. X51444 mRNA. Translation: CAA35809.1. X51445 mRNA. Translation: CAA35810.1. X56652 Genomic DNA. Translation: CAA39974.1. X56653 Genomic DNA. Translation: CAA39975.1. CR542241 mRNA. Translation: CAG47037.1. AC090099 Genomic DNA. No translation available. BC007022 mRNA. Translation: AAH07022.1. BC020795 mRNA. Translation: AAH20795.1. BC105796 mRNA. Translation: AAI05797.1.
IPI	IPI00552578.
PIR	YLHUS. A22342. YLHUA. A27902. I39456.
RefSeq	NP_000322.2. NP_001120852.1. NP_110381.2. NP_954630.1.
UniGene	Hs.1955 Hs.632144
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P02735.
Proteomic databases
PeptideAtlas	P02735.
PRIDE	P02735.
Genome annotation databases
Ensembl	ENST00000356524; ENSP00000348918; ENSG00000173432; Homo sapiens. [Genome view] ENST00000405158; ENSP00000384906; ENSG00000173432; Homo sapiens. [Genome view]
GeneID	6288. 6289.
KEGG	hsa:6288. hsa:6289.
Organism-specific databases
CTD	6288. 6289.
GeneCards	GC11M018223. GC11P018244.
H-InvDB	HIX0009484.
HGNC	HGNC:10513. SAA1. HGNC:10514. SAA2.
MIM	104750. gene. 104751. gene.
PharmGKB	PA34921.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P02735.
Gene expression databases
ArrayExpress	P02735.
Bgee	P02735.
CleanEx	HS_SAA1.
Genevestigator	P02735.
GermOnline	ENSG00000173432. Homo sapiens.
Family and domain databases
InterPro	IPR000096. Serum_amyloid_A. [Graphical view]
PANTHER	PTHR23424. Serum_amyloid_A. 1 hit.
Pfam	PF00277. SAA. 1 hit. [Graphical view]
PIRSF	PIRSF002472. Serum_amyloid_A. 1 hit.
PRINTS	PR00306. SERUMAMYLOID.
SMART	SM00197. SAA. 1 hit. [Graphical view]
PROSITE	PS00992. SAA. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00062. Human Serum Albumin. DB00064. Serum albumin iodonated.
NextBio	24415.
SOURCE	Search...

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Entry information

Entry name

SAA_HUMAN

Accession

Primary (citable) accession number: P02735
Secondary accession number(s): P02736

Q9UCL0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 1, 1990
Last modified:	November 24, 2009
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

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Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents