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Protein

Apolipoprotein A-II

Gene

APOA2

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

Functioni

May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism.

GO - Molecular functioni

  • apolipoprotein receptor binding Source: BHF-UCL
  • cholesterol binding Source: BHF-UCL
  • cholesterol transporter activity Source: Ensembl
  • high-density lipoprotein particle binding Source: GO_Central
  • high-density lipoprotein particle receptor binding Source: BHF-UCL
  • lipase inhibitor activity Source: BHF-UCL
  • lipid binding Source: BHF-UCL
  • lipid transporter activity Source: BHF-UCL
  • phosphatidylcholine binding Source: BHF-UCL
  • phosphatidylcholine-sterol O-acyltransferase activator activity Source: BHF-UCL
  • phospholipid binding Source: BHF-UCL
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  • acute inflammatory response Source: Ensembl
  • animal organ regeneration Source: Ensembl
  • cholesterol efflux Source: BHF-UCL
  • cholesterol homeostasis Source: BHF-UCL
  • cholesterol metabolic process Source: GO_Central
  • diacylglycerol catabolic process Source: BHF-UCL
  • high-density lipoprotein particle assembly Source: BHF-UCL
  • high-density lipoprotein particle clearance Source: BHF-UCL
  • high-density lipoprotein particle remodeling Source: BHF-UCL
  • lipoprotein biosynthetic process Source: Reactome
  • lipoprotein metabolic process Source: GO_Central
  • low-density lipoprotein particle remodeling Source: BHF-UCL
  • negative regulation of cholesterol import Source: BHF-UCL
  • negative regulation of cholesterol transport Source: BHF-UCL
  • negative regulation of cholesterol transporter activity Source: BHF-UCL
  • negative regulation of cytokine secretion involved in immune response Source: BHF-UCL
  • negative regulation of lipase activity Source: BHF-UCL
  • negative regulation of lipid catabolic process Source: BHF-UCL
  • negative regulation of very-low-density lipoprotein particle remodeling Source: BHF-UCL
  • peptidyl-methionine modification Source: UniProtKB
  • phosphatidylcholine biosynthetic process Source: BHF-UCL
  • phospholipid catabolic process Source: BHF-UCL
  • phospholipid efflux Source: BHF-UCL
  • positive regulation of cholesterol esterification Source: BHF-UCL
  • positive regulation of interleukin-8 biosynthetic process Source: UniProtKB
  • positive regulation of lipid catabolic process Source: BHF-UCL
  • protein oxidation Source: UniProtKB
  • regulation of intestinal cholesterol absorption Source: Ensembl
  • regulation of protein stability Source: BHF-UCL
  • response to drug Source: Ensembl
  • response to estrogen Source: Ensembl
  • response to glucocorticoid Source: Ensembl
  • response to glucose Source: BHF-UCL
  • retinoid metabolic process Source: Reactome
  • reverse cholesterol transport Source: BHF-UCL
  • triglyceride metabolic process Source: BHF-UCL
  • triglyceride-rich lipoprotein particle remodeling Source: BHF-UCL
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Lipid transport, Transport

Enzyme and pathway databases

BioCyciZFISH:ENSG00000158874-MONOMER.
ReactomeiR-HSA-174800. Chylomicron-mediated lipid transport.
R-HSA-1989781. PPARA activates gene expression.
R-HSA-975634. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Apolipoprotein A-II
Short name:
Apo-AII
Short name:
ApoA-II
Alternative name(s):
Apolipoprotein A2
Cleaved into the following 2 chains:
Proapolipoprotein A-II
Short name:
ProapoA-II
Alternative name(s):
Apolipoprotein A-II(1-76)
Gene namesi
Name:APOA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:601. APOA2.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • chylomicron Source: BHF-UCL
  • cytosol Source: Reactome
  • early endosome Source: Reactome
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • high-density lipoprotein particle Source: BHF-UCL
  • spherical high-density lipoprotein particle Source: BHF-UCL
  • very-low-density lipoprotein particle Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

HDL, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi336.
MalaCardsiAPOA2.
MIMi107670. gene+phenotype.
OpenTargetsiENSG00000158874.
Orphaneti238269. Familial renal amyloidosis due to Apolipoprotein AII variant.
PharmGKBiPA24886.

Polymorphism and mutation databases

BioMutaiAPOA2.
DMDMi114000.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 181 PublicationAdd BLAST18
ChainiPRO_000042535119 – 100Proapolipoprotein A-IIAdd BLAST82
ChainiPRO_000000200324 – 100Apolipoprotein A-II1 PublicationAdd BLAST77
ChainiPRO_000000200424 – 99Truncated apolipoprotein A-II1 PublicationAdd BLAST76

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei24Pyrrolidone carboxylic acid2 Publications1
Disulfide bondi29Interchain (with C-136 in APOD); in heterodimeric form1 Publication
Modified residuei49Methionine sulfoxide1 Publication1
Modified residuei54Phosphoserine; by FAM20C1 Publication1
Modified residuei68Phosphoserine; by FAM20CCombined sources1 Publication1

Post-translational modificationi

Phosphorylation sites are present in the extracellular medium.1 Publication
Apolipoprotein A-II is O-glycosylated.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Oxidation, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP02652.
PaxDbiP02652.
PeptideAtlasiP02652.
PRIDEiP02652.
TopDownProteomicsiP02652.

2D gel databases

SWISS-2DPAGEP02652.

PTM databases

iPTMnetiP02652.
PhosphoSitePlusiP02652.

Miscellaneous databases

PMAP-CutDBP02652.

Expressioni

Tissue specificityi

Plasma; synthesized in the liver and intestine.

Gene expression databases

BgeeiENSG00000158874.
CleanExiHS_APOA2.
ExpressionAtlasiP02652. baseline and differential.
GenevisibleiP02652. HS.

Organism-specific databases

HPAiCAB025885.

Interactioni

Subunit structurei

Monomer. Homodimer; disulfide-linked. Also forms a disulfide-linked heterodimer with APOD. Interacts with HCV core protein. Interacts with APOA1BP and NDRG1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CATSPER1Q8NEC55EBI-1171525,EBI-744545

GO - Molecular functioni

  • apolipoprotein receptor binding Source: BHF-UCL
  • high-density lipoprotein particle receptor binding Source: BHF-UCL
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi106833. 14 interactors.
IntActiP02652. 9 interactors.
MINTiMINT-106326.
STRINGi9606.ENSP00000356969.

Structurei

Secondary structure

1100
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi31 – 56Combined sources26
Beta strandi58 – 60Combined sources3
Helixi63 – 69Combined sources7
Turni70 – 72Combined sources3
Helixi74 – 77Combined sources4
Helixi79 – 82Combined sources4
Helixi88 – 95Combined sources8
Turni96 – 98Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L6LX-ray2.301/2/3/4/5/6/7/8/A/B/C/D/E/F/G/H/I/J/K/L/M/N/P/Q/S/T/U/V/W/X/Y/Z24-100[»]
2OU1X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L24-100[»]
ProteinModelPortaliP02652.
SMRiP02652.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02652.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni32 – 43O-glycosylated at one siteAdd BLAST12

Sequence similaritiesi

Belongs to the apolipoprotein A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410KCI2. Eukaryota.
ENOG4110NY0. LUCA.
GeneTreeiENSGT00390000003306.
HOGENOMiHOG000033999.
HOVERGENiHBG050544.
InParanoidiP02652.
KOiK08758.
PhylomeDBiP02652.
TreeFamiTF338165.

Family and domain databases

InterProiIPR006801. ApoA-II.
[Graphical view]
PANTHERiPTHR11027. PTHR11027. 1 hit.
ProDomiPD010397. ApoA-II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF82936. SSF82936. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P02652-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLAATVLL LTICSLEGAL VRRQAKEPCV ESLVSQYFQT VTDYGKDLME
60 70 80 90 100
KVKSPELQAE AKSYFEKSKE QLTPLIKKAG TELVNFLSYF VELGTQPATQ
Length:100
Mass (Da):11,175
Last modified:August 13, 1987 - v1
Checksum:i1247868A25EC3AF2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti96Q → H in CAA28583 (PubMed:6428397).Curated1

Mass spectrometryi

Molecular mass is 17252 Da from positions 24 - 100. Determined by ESI. Homodimer, without methionine sulfoxide.1 Publication
Molecular mass is 17269 Da from positions 24 - 100. Determined by ESI. Homodimer, with 1 methionine sulfoxide, oxidation at Met-49.1 Publication
Molecular mass is 8701.2 Da from positions 24 - 100. Determined by MALDI. Monomer.1 Publication
Molecular mass is 8823.4 Da from positions 24 - 100. Determined by MALDI. Cysteinylated ApoA-II monomer.1 Publication
Molecular mass is 17421.3 Da from positions 24 - 100. Determined by MALDI. Homodimer.1 Publication
Molecular mass is 17293.4 Da from positions 24 - 100. Determined by MALDI. Heterodimer with truncated apolipoprotein A-II.1 Publication
Molecular mass is 8578.3 Da from positions 24 - 99. Determined by MALDI. Monomer.1 Publication
Molecular mass is 17166.2 Da from positions 24 - 99. Determined by MALDI. Homodimer.1 Publication
Molecular mass is 17380 Da from positions 25 - 100. Determined by MALDI. Homodimer.1 Publication

Polymorphismi

A homozygous transition at position 1 of intron 3 of APOA2 results in deficiency of apolipoprotein A-II, without significant influence either on lipid and lipoprotein profiles or on the occurrence of coronary artery disease [MIMi:107670].1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04898 Genomic DNA. Translation: CAA28583.1.
X00955 mRNA. Translation: CAA25467.1.
X02905 Genomic DNA. Translation: CAA26665.1.
X02619 Genomic DNA. Translation: CAA26474.1.
M29882 mRNA. Translation: AAA51701.1.
AY100524 Genomic DNA. Translation: AAM49807.1.
AK312034 mRNA. Translation: BAG34971.1.
BT006786 mRNA. Translation: AAP35432.1.
AL590714 Genomic DNA. Translation: CAH72151.1.
BC005282 mRNA. Translation: AAH05282.1.
CCDSiCCDS1226.1.
PIRiA93586. LPHUA2.
RefSeqiNP_001634.1. NM_001643.1.
UniGeneiHs.237658.

Genome annotation databases

EnsembliENST00000367990; ENSP00000356969; ENSG00000158874.
GeneIDi336.
KEGGihsa:336.
UCSCiuc001fzc.2. human.

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04898 Genomic DNA. Translation: CAA28583.1.
X00955 mRNA. Translation: CAA25467.1.
X02905 Genomic DNA. Translation: CAA26665.1.
X02619 Genomic DNA. Translation: CAA26474.1.
M29882 mRNA. Translation: AAA51701.1.
AY100524 Genomic DNA. Translation: AAM49807.1.
AK312034 mRNA. Translation: BAG34971.1.
BT006786 mRNA. Translation: AAP35432.1.
AL590714 Genomic DNA. Translation: CAH72151.1.
BC005282 mRNA. Translation: AAH05282.1.
CCDSiCCDS1226.1.
PIRiA93586. LPHUA2.
RefSeqiNP_001634.1. NM_001643.1.
UniGeneiHs.237658.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1L6LX-ray2.301/2/3/4/5/6/7/8/A/B/C/D/E/F/G/H/I/J/K/L/M/N/P/Q/S/T/U/V/W/X/Y/Z24-100[»]
2OU1X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L24-100[»]
ProteinModelPortaliP02652.
SMRiP02652.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106833. 14 interactors.
IntActiP02652. 9 interactors.
MINTiMINT-106326.
STRINGi9606.ENSP00000356969.

PTM databases

iPTMnetiP02652.
PhosphoSitePlusiP02652.

Polymorphism and mutation databases

BioMutaiAPOA2.
DMDMi114000.

2D gel databases

SWISS-2DPAGEP02652.

Proteomic databases

MaxQBiP02652.
PaxDbiP02652.
PeptideAtlasiP02652.
PRIDEiP02652.
TopDownProteomicsiP02652.

Protocols and materials databases

DNASUi336.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000367990; ENSP00000356969; ENSG00000158874.
GeneIDi336.
KEGGihsa:336.
UCSCiuc001fzc.2. human.

Organism-specific databases

CTDi336.
DisGeNETi336.
GeneCardsiAPOA2.
HGNCiHGNC:601. APOA2.
HPAiCAB025885.
MalaCardsiAPOA2.
MIMi107670. gene+phenotype.
neXtProtiNX_P02652.
OpenTargetsiENSG00000158874.
Orphaneti238269. Familial renal amyloidosis due to Apolipoprotein AII variant.
PharmGKBiPA24886.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410KCI2. Eukaryota.
ENOG4110NY0. LUCA.
GeneTreeiENSGT00390000003306.
HOGENOMiHOG000033999.
HOVERGENiHBG050544.
InParanoidiP02652.
KOiK08758.
PhylomeDBiP02652.
TreeFamiTF338165.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000158874-MONOMER.
ReactomeiR-HSA-174800. Chylomicron-mediated lipid transport.
R-HSA-1989781. PPARA activates gene expression.
R-HSA-975634. Retinoid metabolism and transport.

Miscellaneous databases

ChiTaRSiAPOA2. human.
EvolutionaryTraceiP02652.
GeneWikiiAPOA2.
GenomeRNAii336.
PMAP-CutDBP02652.
PROiP02652.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000158874.
CleanExiHS_APOA2.
ExpressionAtlasiP02652. baseline and differential.
GenevisibleiP02652. HS.

Family and domain databases

InterProiIPR006801. ApoA-II.
[Graphical view]
PANTHERiPTHR11027. PTHR11027. 1 hit.
ProDomiPD010397. ApoA-II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF82936. SSF82936. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAPOA2_HUMAN
AccessioniPrimary (citable) accession number: P02652
Secondary accession number(s): B2R524
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: August 13, 1987
Last modified: November 30, 2016
This is version 200 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.