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P04638 (APOA2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apolipoprotein A-II

Short name=Apo-AII
Short name=ApoA-II
Alternative name(s):
Apolipoprotein A2

Cleaved into the following chain:

  1. Proapolipoprotein A-II
    Short name=ProapoA-II
Gene names
Name:Apoa2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length102 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Subunit structure

Monomer. Interacts with APOA1BP and NDRG1 By similarity.

Subcellular location

Secreted.

Tissue specificity

Plasma.

Post-translational modification

Phosphorylation sites are present in the extracellular medium By similarity.

Sequence similarities

Belongs to the apolipoprotein A2 family.

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentHDL
Secreted
   DomainSignal
   PTMCleavage on pair of basic residues
Oxidation
Phosphoprotein
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacute inflammatory response

Inferred from expression pattern PubMed 3108158. Source: RGD

cholesterol efflux

Inferred from electronic annotation. Source: Ensembl

cholesterol homeostasis

Inferred from electronic annotation. Source: Ensembl

cholesterol metabolic process

Inferred from electronic annotation. Source: Ensembl

cholesterol transport

Inferred from direct assay PubMed 1537840. Source: RGD

diacylglycerol catabolic process

Inferred from electronic annotation. Source: Ensembl

high-density lipoprotein particle assembly

Inferred from electronic annotation. Source: Ensembl

high-density lipoprotein particle clearance

Inferred from electronic annotation. Source: Ensembl

high-density lipoprotein particle remodeling

Inferred from electronic annotation. Source: Ensembl

lipoprotein metabolic process

Inferred from electronic annotation. Source: Ensembl

low-density lipoprotein particle remodeling

Inferred from electronic annotation. Source: Ensembl

negative regulation of cholesterol import

Inferred from electronic annotation. Source: Ensembl

negative regulation of cholesterol transporter activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of cytokine secretion involved in immune response

Inferred from electronic annotation. Source: Ensembl

negative regulation of lipase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of lipid catabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of very-low-density lipoprotein particle remodeling

Inferred from electronic annotation. Source: Ensembl

organ regeneration

Inferred from direct assay PubMed 2123716. Source: RGD

peptidyl-methionine modification

Inferred from electronic annotation. Source: Ensembl

phosphatidylcholine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

phospholipid catabolic process

Inferred from electronic annotation. Source: Ensembl

phospholipid efflux

Inferred from electronic annotation. Source: Ensembl

positive regulation of cholesterol esterification

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-8 biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of lipid catabolic process

Inferred from electronic annotation. Source: Ensembl

protein folding

Inferred from electronic annotation. Source: Ensembl

protein oxidation

Inferred from electronic annotation. Source: Ensembl

regulation of intestinal cholesterol absorption

Inferred from electronic annotation. Source: Ensembl

regulation of protein stability

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from expression pattern PubMed 1547188. Source: RGD

response to estrogen

Inferred from expression pattern PubMed 2504861. Source: RGD

response to glucocorticoid

Inferred from expression pattern PubMed 1903065. Source: RGD

response to glucose

Inferred from electronic annotation. Source: Ensembl

reverse cholesterol transport

Inferred from electronic annotation. Source: Ensembl

triglyceride-rich lipoprotein particle remodeling

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentchylomicron

Inferred from electronic annotation. Source: Ensembl

spherical high-density lipoprotein particle

Inferred from electronic annotation. Source: Ensembl

very-low-density lipoprotein particle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncholesterol binding

Inferred from electronic annotation. Source: Ensembl

cholesterol transporter activity

Inferred from direct assay PubMed 1537840. Source: RGD

high-density lipoprotein particle binding

Inferred from electronic annotation. Source: Ensembl

lipase inhibitor activity

Inferred from electronic annotation. Source: Ensembl

phosphatidylcholine binding

Inferred from electronic annotation. Source: Ensembl

phosphatidylcholine-sterol O-acyltransferase activator activity

Inferred from electronic annotation. Source: Ensembl

protein heterodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 10284Proapolipoprotein A-II
PRO_0000425360
Chain24 – 10279Apolipoprotein A-II
PRO_0000002012

Amino acid modifications

Modified residue241Pyrrolidone carboxylic acid; in Apolipoprotein A-II By similarity
Modified residue491Methionine sulfoxide By similarity

Sequences

Sequence LengthMass (Da)Tools
P04638 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 94A29508DFE7A813

FASTA10211,439
        10         20         30         40         50         60 
MKLLAMVALL VTICSLEGAL VRRQAAETDV QTLFSQYLQS LTDYGKDLME KAQPSEIQNQ 

        70         80         90        100 
AKAYFQNAQE RLTPFVQRTG TNLMDFLSRL MSPEEKPAPA AK 

« Hide

References

[1]"Structure and evolution of the apolipoprotein multigene family."
Luo C.-C., Li W.-H., Moore M.N., Chan L.
J. Mol. Biol. 187:325-340(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Amino acid sequence of rat apolipoprotein A-II deduced from the nucleotide sequence of cloned cDNA."
Nagashima M., Morris G., Howlett G., Fidge N., Schreiber G.
J. Lipid Res. 27:706-712(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-102.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03468 mRNA. Translation: CAA27185.1.
M28615 mRNA. Translation: AAA40750.1.
PIRA24846.
RefSeqNP_037244.1. NM_013112.1.
XP_006250300.1. XM_006250238.1.
XP_006250301.1. XM_006250239.1.
UniGeneRn.89304.

3D structure databases

ProteinModelPortalP04638.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000004662.

PTM databases

PhosphoSiteP04638.

Proteomic databases

PaxDbP04638.
PRIDEP04638.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000004662; ENSRNOP00000004662; ENSRNOG00000003500.
GeneID25649.
KEGGrno:25649.
UCSCRGD:2131. rat.

Organism-specific databases

CTD336.
RGD2131. Apoa2.

Phylogenomic databases

eggNOGNOG40617.
GeneTreeENSGT00390000003306.
HOGENOMHOG000033999.
HOVERGENHBG050544.
InParanoidP04638.
KOK08758.
OMAAYFEKTQ.
OrthoDBEOG7G4QHG.
PhylomeDBP04638.
TreeFamTF338165.

Gene expression databases

GenevestigatorP04638.

Family and domain databases

InterProIPR006801. ApoA-II.
[Graphical view]
PANTHERPTHR11027. PTHR11027. 1 hit.
PfamPF04711. ApoA-II. 1 hit.
[Graphical view]
ProDomPD010397. ApoA-II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

NextBio607515.
PROP04638.

Entry information

Entry nameAPOA2_RAT
AccessionPrimary (citable) accession number: P04638
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families