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Protein

Serum amyloid A-1 protein

Gene

SAA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Major acute phase protein.

GO - Molecular functioni

  • chemoattractant activity Source: GO_Central
  • G-protein coupled receptor binding Source: UniProtKB
  • heparin binding Source: UniProtKB-KW

GO - Biological processi

  • activation of MAPK activity Source: CACAO
  • acute-phase response Source: UniProtKB
  • cellular protein metabolic process Source: Reactome
  • innate immune response Source: Reactome
  • lymphocyte chemotaxis Source: UniProtKB
  • macrophage chemotaxis Source: UniProtKB
  • negative regulation of inflammatory response Source: UniProtKB
  • neutrophil chemotaxis Source: UniProtKB
  • platelet activation Source: UniProtKB
  • positive regulation of cell adhesion Source: UniProtKB
  • positive regulation of cytokine secretion Source: UniProtKB
  • positive regulation of cytosolic calcium ion concentration Source: UniProtKB
  • positive regulation of interleukin-1 secretion Source: UniProtKB
  • receptor-mediated endocytosis Source: Reactome
  • regulation of protein secretion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Acute phase

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiR-HSA-1810476. RIP-mediated NFkB activation via ZBP1.
R-HSA-3000471. Scavenging by Class B Receptors.
R-HSA-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-HSA-416476. G alpha (q) signalling events.
R-HSA-418594. G alpha (i) signalling events.
R-HSA-444473. Formyl peptide receptors bind formyl peptides and many other ligands.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-879415. Advanced glycosylation endproduct receptor signaling.
R-HSA-933542. TRAF6 mediated NF-kB activation.
R-HSA-977225. Amyloid fiber formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Serum amyloid A-1 protein
Short name:
SAA
Cleaved into the following 6 chains:
Gene namesi
Name:SAA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:10513. SAA1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic microtubule Source: CACAO
  • endocytic vesicle lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: GO_Central
  • high-density lipoprotein particle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Amyloid, HDL, Secreted

Pathology & Biotechi

Involvement in diseasei

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.

Elevated serum SAA1 protein levels may be associated with lung cancer.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi19R → A: Reduces affinity for heparin and nearly abolishes association with HDL; when associated with A-80 and A-89. 1 Publication1
Mutagenesisi33R → A: Reduces affinity for heparin; when associated with A-37 and A-65. 1 Publication1
Mutagenesisi37R → A: Reduces affinity for heparin; when associated with A-33 and A-65. 1 Publication1
Mutagenesisi65R → A: Reduces affinity for heparin; when associated with A-33 and A-37. 1 Publication1
Mutagenesisi80R → A: Reduces affinity for heparin and nearly abolishes association with HDL; when associated with A-18 and A-89. 1 Publication1
Mutagenesisi89H → A: Reduces affinity for heparin and nearly abolishes association with HDL; when associated with A-18 and A-80. 1 Publication1

Keywords - Diseasei

Amyloidosis

Organism-specific databases

DisGeNETi6288.
MalaCardsiSAA1.
Orphaneti85445. Secondary amyloidosis.

Chemistry databases

DrugBankiDB00062. Human Serum Albumin.
DB00064. Serum albumin iodonated.

Polymorphism and mutation databases

BioMutaiSAA1.
DMDMi395406826.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 189 PublicationsAdd BLAST18
ChainiPRO_000003157519 – 122Serum amyloid A-1 proteinAdd BLAST104
ChainiPRO_000003157619 – 94Amyloid protein AAdd BLAST76
ChainiPRO_000003157720 – 122Serum amyloid protein A(2-104)Add BLAST103
ChainiPRO_000003157820 – 121Serum amyloid protein A(2-103)Add BLAST102
ChainiPRO_000003157920 – 120Serum amyloid protein A(2-102)Add BLAST101
ChainiPRO_000003158021 – 122Serum amyloid protein A(3-104)Add BLAST102
ChainiPRO_000003158122 – 119Serum amyloid protein A(4-101)Add BLAST98
PropeptideiPRO_000003158295 – 122Often cleaved during amyloidogenesisAdd BLAST28

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei101N4,N4-dimethylasparagine1 Publication1

Post-translational modificationi

This protein is the precursor of amyloid protein A, which is formed by the removal of approximately 24 residues from the C-terminal end.

Keywords - PTMi

Methylation

Proteomic databases

EPDiP0DJI8.
PaxDbiP0DJI8.
PeptideAtlasiP0DJI8.
PRIDEiP0DJI8.

2D gel databases

UCD-2DPAGEP02735.

PTM databases

iPTMnetiP0DJI8.
PhosphoSitePlusiP0DJI8.

Miscellaneous databases

PMAP-CutDBQ6FG67.

Expressioni

Tissue specificityi

Expressed by the liver; secreted in plasma (at protein level).3 Publications

Inductioni

Upon cytokine stimulation.

Gene expression databases

BgeeiENSG00000173432.
CleanExiHS_SAA1.
ExpressionAtlasiP0DJI8. baseline and differential.
GenevisibleiP0DJI8. HS.

Interactioni

Subunit structurei

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.2 Publications

GO - Molecular functioni

  • G-protein coupled receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112196. 2 interactors.
STRINGi9606.ENSP00000348918.

Structurei

Secondary structure

1122
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi19 – 45Combined sources27
Helixi51 – 65Combined sources15
Helixi67 – 86Combined sources20
Helixi91 – 105Combined sources15
Helixi110 – 113Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IP8X-ray2.19A/B/C/D19-122[»]
4IP9X-ray2.50A/B19-122[»]
ProteinModelPortaliP0DJI8.
SMRiP0DJI8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni19 – 45Important for amyloid formation; forms amyloid fibrils in vitroAdd BLAST27

Sequence similaritiesi

Belongs to the SAA family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IXU4. Eukaryota.
ENOG410YSBK. LUCA.
HOVERGENiHBG016327.
InParanoidiP0DJI8.
KOiK17310.
OrthoDBiEOG091G17YH.
PhylomeDBiP0DJI8.
TreeFamiTF332544.

Family and domain databases

InterProiIPR000096. Serum_amyloid_A.
[Graphical view]
PfamiPF00277. SAA. 1 hit.
[Graphical view]
PIRSFiPIRSF002472. Serum_amyloid_A. 1 hit.
PRINTSiPR00306. SERUMAMYLOID.
SMARTiSM00197. SAA. 1 hit.
[Graphical view]
PROSITEiPS00992. SAA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0DJI8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLTGLVFC SLVLGVSSRS FFSFLGEAFD GARDMWRAYS DMREANYIGS
60 70 80 90 100
DKYFHARGNY DAAKRGPGGV WAAEAISDAR ENIQRFFGHG AEDSLADQAA
110 120
NEWGRSGKDP NHFRPAGLPE KY
Length:122
Mass (Da):13,532
Last modified:July 11, 2012 - v1
Checksum:i43A57D56B37CB173
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti71W → R AA sequence (PubMed:6155694).Curated1
Sequence conflicti71W → R AA sequence (PubMed:5055786).Curated1
Sequence conflicti77S → T in AC107948 (PubMed:16554811).Curated1
Sequence conflicti96 – 101ADQAAN → SEATVK AA sequence (PubMed:1546977).Curated6
Sequence conflicti101N → D in AAH07022 (PubMed:15489334).Curated1
Sequence conflicti119P → S in AAA60297 (PubMed:3839415).Curated1

Mass spectrometryi

Molecular mass is 11702±14 Da from positions 19 - 122. Determined by MALDI. 1 Publication
Molecular mass is 11682.7 Da from positions 19 - 122. Determined by MALDI. 1 Publication
Molecular mass is 11526.5 Da from positions 20 - 122. Determined by MALDI. 1 Publication
Molecular mass is 11439.6 Da from positions 21 - 122. Determined by MALDI. 1 Publication
Molecular mass is 11363.6 Da from positions 20 - 121. Determined by MALDI. 1 Publication
Molecular mass is 11235.6 Da from positions 20 - 120. Determined by MALDI. 1 Publication
Molecular mass is 10872.6 Da from positions 22 - 119. Determined by MALDI. 1 Publication
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-87.1 Publication
Molecular mass is 8390.9±0.2 Da from positions 19 - 94. Determined by ESI. With variant Ala-70.1 Publication

Polymorphismi

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.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00692515G → S.Corresponds to variant rs712021dbSNPEnsembl.1
Natural variantiVAR_00692670V → A in allele SAA1.2, SAA1.3, SAA1.4 and SAA1.5. 1 Publication1
Natural variantiVAR_00692775A → V in allele SAA1.2, SAA1.4 and SAA1.5. 2 Publications1
Natural variantiVAR_00692878D → N in allele SAA1.4. 2 Publications1
Natural variantiVAR_05716786F → L.Corresponds to variant rs1059559dbSNPEnsembl.1
Natural variantiVAR_00693190G → D in allele SAA1.2. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10906 mRNA. Translation: AAA60297.1.
M23698 mRNA. Translation: AAA64799.1.
X56652 Genomic DNA. Translation: CAA39974.1.
CR542241 mRNA. Translation: CAG47037.1.
AC107948 Genomic DNA. No translation available.
BC007022 mRNA. Translation: AAH07022.1.
BC105796 mRNA. Translation: AAI05797.1.
X51439 mRNA. Translation: CAA35804.1.
X51441 mRNA. Translation: CAA35806.1.
X51442 mRNA. Translation: CAA35807.1.
CCDSiCCDS7835.1.
PIRiA22342. YLHUS.
I39456.
RefSeqiNP_000322.2. NM_000331.5.
NP_001171477.1. NM_001178006.2.
NP_954630.1. NM_199161.4.
UniGeneiHs.632144.
Hs.731376.
Hs.734161.

Genome annotation databases

EnsembliENST00000356524; ENSP00000348918; ENSG00000173432.
ENST00000405158; ENSP00000384906; ENSG00000173432.
GeneIDi6288.
KEGGihsa:6288.
UCSCiuc057zpu.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10906 mRNA. Translation: AAA60297.1.
M23698 mRNA. Translation: AAA64799.1.
X56652 Genomic DNA. Translation: CAA39974.1.
CR542241 mRNA. Translation: CAG47037.1.
AC107948 Genomic DNA. No translation available.
BC007022 mRNA. Translation: AAH07022.1.
BC105796 mRNA. Translation: AAI05797.1.
X51439 mRNA. Translation: CAA35804.1.
X51441 mRNA. Translation: CAA35806.1.
X51442 mRNA. Translation: CAA35807.1.
CCDSiCCDS7835.1.
PIRiA22342. YLHUS.
I39456.
RefSeqiNP_000322.2. NM_000331.5.
NP_001171477.1. NM_001178006.2.
NP_954630.1. NM_199161.4.
UniGeneiHs.632144.
Hs.731376.
Hs.734161.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4IP8X-ray2.19A/B/C/D19-122[»]
4IP9X-ray2.50A/B19-122[»]
ProteinModelPortaliP0DJI8.
SMRiP0DJI8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112196. 2 interactors.
STRINGi9606.ENSP00000348918.

Chemistry databases

DrugBankiDB00062. Human Serum Albumin.
DB00064. Serum albumin iodonated.

PTM databases

iPTMnetiP0DJI8.
PhosphoSitePlusiP0DJI8.

Polymorphism and mutation databases

BioMutaiSAA1.
DMDMi395406826.

2D gel databases

UCD-2DPAGEP02735.

Proteomic databases

EPDiP0DJI8.
PaxDbiP0DJI8.
PeptideAtlasiP0DJI8.
PRIDEiP0DJI8.

Protocols and materials databases

DNASUi6288.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356524; ENSP00000348918; ENSG00000173432.
ENST00000405158; ENSP00000384906; ENSG00000173432.
GeneIDi6288.
KEGGihsa:6288.
UCSCiuc057zpu.1. human.

Organism-specific databases

CTDi6288.
DisGeNETi6288.
GeneCardsiSAA1.
H-InvDBHIX0009484.
HGNCiHGNC:10513. SAA1.
MalaCardsiSAA1.
MIMi104750. gene.
neXtProtiNX_P0DJI8.
Orphaneti85445. Secondary amyloidosis.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IXU4. Eukaryota.
ENOG410YSBK. LUCA.
HOVERGENiHBG016327.
InParanoidiP0DJI8.
KOiK17310.
OrthoDBiEOG091G17YH.
PhylomeDBiP0DJI8.
TreeFamiTF332544.

Enzyme and pathway databases

ReactomeiR-HSA-1810476. RIP-mediated NFkB activation via ZBP1.
R-HSA-3000471. Scavenging by Class B Receptors.
R-HSA-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-HSA-416476. G alpha (q) signalling events.
R-HSA-418594. G alpha (i) signalling events.
R-HSA-444473. Formyl peptide receptors bind formyl peptides and many other ligands.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-879415. Advanced glycosylation endproduct receptor signaling.
R-HSA-933542. TRAF6 mediated NF-kB activation.
R-HSA-977225. Amyloid fiber formation.

Miscellaneous databases

ChiTaRSiSAA1. human.
GeneWikiiSerum_amyloid_A1.
GenomeRNAii6288.
PMAP-CutDBQ6FG67.
PROiP0DJI8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000173432.
CleanExiHS_SAA1.
ExpressionAtlasiP0DJI8. baseline and differential.
GenevisibleiP0DJI8. HS.

Family and domain databases

InterProiIPR000096. Serum_amyloid_A.
[Graphical view]
PfamiPF00277. SAA. 1 hit.
[Graphical view]
PIRSFiPIRSF002472. Serum_amyloid_A. 1 hit.
PRINTSiPR00306. SERUMAMYLOID.
SMARTiSM00197. SAA. 1 hit.
[Graphical view]
PROSITEiPS00992. SAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSAA1_HUMAN
AccessioniPrimary (citable) accession number: P0DJI8
Secondary accession number(s): P02735
, P02736, P02737, Q16730, Q16834, Q16835, Q16879, Q3KRB3, Q6FG67, Q96QN0, Q9UCK9, Q9UCL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2012
Last sequence update: July 11, 2012
Last modified: November 2, 2016
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.