Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P09813 (APOA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

Involvement in disease

Defects in Apoa2 are the cause of senescence accelerated mouse (SAM), the senile amyloid is a mutated apolipoprotein A-II. Ref.2

Miscellaneous

The apo A-II stoichiometry in HDL molecules varies among inbred mice strains, because of structural polymorphisms affecting the apo A-II gene, which influence its translational efficiency.

The sequence presented here is that of strain BALB/c and C3H/HeJ.

Sequence similarities

Belongs to the apolipoprotein A2 family.

Mass spectrometry

Molecular mass is 8709.2±0.071 Da from positions 24 - 102. Determined by ESI. Strain C57BL/6. Without methionine sulfoxide. Ref.11

Molecular mass is 8719.5 Da from positions 24 - 102. Determined by ESI. Strain BALB/c. Without methionine sulfoxide. Ref.11

Molecular mass is 8725.3±0.283 Da from positions 24 - 102. Determined by ESI. Strain C57BL/6. With 1 methionine sulfoxide. Ref.11

Molecular mass is 8742 Da from positions 24 - 102. Determined by ESI. Strain C57BL/6. With 2 methionine sulfoxides. Ref.11

Molecular mass is 8735.2 Da from positions 24 - 102. Determined by ESI. Strain BALB/c. With 1 methionine sulfoxide. Ref.11

Molecular mass is 9294±0.707 Da from positions 19 - 102. Determined by ESI. Strain C57BL/6. Without methionine sulfoxide. Ref.11

Molecular mass is 9304 Da from positions 19 - 102. Determined by ESI. Strain BALB/c. Without methionine sulfoxide. Ref.11

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentAmyloid
HDL
Secreted
   DiseaseDisease mutation
   DomainSignal
   PTMCleavage on pair of basic residues
Oxidation
Phosphoprotein
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute inflammatory response

Inferred from electronic annotation. Source: Ensembl

beta-glucoside transport

Non-traceable author statement PubMed 12269810. Source: UniProtKB

cholesterol efflux

Inferred from electronic annotation. Source: Ensembl

cholesterol homeostasis

Inferred from direct assay PubMed 8422330. Source: MGI

cholesterol metabolic process

Inferred from mutant phenotype PubMed 10357838PubMed 8647961. Source: MGI

diacylglycerol catabolic process

Inferred from electronic annotation. Source: Ensembl

fatty acid metabolic process

Non-traceable author statement PubMed 12269810. Source: UniProtKB

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

lipid transport

Inferred from mutant phenotype PubMed 14729860. Source: MGI

lipoprotein metabolic process

Inferred from direct assay PubMed 7837794PubMed 9150245. Source: MGI

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 mutant phenotype PubMed 10357838. Source: MGI

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 electronic annotation. Source: Ensembl

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 mutant phenotype PubMed 8962133. Source: MGI

regulation of protein stability

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

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

cytosol

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 1596514PubMed 6403543PubMed 9186920. Source: MGI

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 electronic annotation. Source: Ensembl

high-density lipoprotein particle binding

Inferred from mutant phenotype PubMed 14729860. Source: MGI

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_0000425354
Chain24 – 10279Apolipoprotein A-II
PRO_0000002008

Amino acid modifications

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

Natural variations

Natural variant281P → Q in SAM. Ref.2

Experimental info

Sequence conflict431D → E in CAA27731. Ref.1
Sequence conflict431D → E in AAA37248. Ref.2
Sequence conflict431D → E in AAA37250. Ref.3
Sequence conflict431D → E in AAH31786. Ref.8
Sequence conflict481L → F in CAA44616. Ref.4
Sequence conflict491M → V in CAA27731. Ref.1
Sequence conflict491M → V in AAA37248. Ref.2
Sequence conflict491M → V in AAA37250. Ref.3
Sequence conflict491M → V in AAH31786. Ref.8
Sequence conflict611A → V in CAA27731. Ref.1
Sequence conflict611A → V in AAA37250. Ref.3
Sequence conflict611A → V in AAH31786. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P09813 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: F50142E0D118665B

FASTA10211,309
        10         20         30         40         50         60 
MKLLAMVALL VTICSLEGAL VKRQADGPDM QSLFTQYFQS MTDYGKDLME KAKTSEIQSQ 

        70         80         90        100 
AKAYFEKTHE QLTPLVRSAG TSLVNFFSSL MNLEEKPAPA AK 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and nucleotide sequence of cDNA for murine senile amyloid protein: nucleotide substitutions found in apolipoprotein A-II cDNA of senescence accelerated mouse (SAM)."
Kunisada T., Higuchi K., Aota S., Takeda T., Yamagishi H.
Nucleic Acids Res. 14:5729-5740(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structural organization of the gene encoding apolipoprotein A-II in an amyloidotic strain of senescence-accelerated mouse."
Yonezu T., Toda M., Yamagishi H., Higuchi K., Takeda T.
Gene 84:187-191(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SAM GLN-28.
[3]"A polymorphism affecting apolipoprotein A-II translational efficiency determines high density lipoprotein size and composition."
Doolittle M.H., Leboeuf R.C., Warden C.H., Bee L.M., Lusis A.J.
J. Biol. Chem. 265:16380-16388(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/cJ, C3H/HeJ, C57BL/6J and DBA/2J.
Tissue: Liver.
[4]"Polymorphism of apolipoprotein A-II (apoA-II) among inbred strains of mice. Relationship between the molecular type of apoA-II and mouse senile amyloidosis."
Higuchi K., Kitagawa K., Naiki H., Hanada K., Hosakawa M., Takeda T.
Biochem. J. 279:427-433(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Amnion.
[6]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[7]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[9]"The single proline-glutamine substitution at position 5 enhances the potency of amyloid fibril formation of murine apo A-II."
Higuchi K., Yonezu T., Tsunasawa S., Sakiyama F., Takeda T.
FEBS Lett. 207:23-27(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-102.
[10]"High homology is present in the primary structures between murine senile amyloid protein (ASSAM) and human apolipoprotein A-II."
Yonezu T., Higuchi K., Tsunasawa S., Takagi S., Sakiyama F., Takeda T.
FEBS Lett. 203:149-152(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-102.
[11]"Mass spectral analysis of the apolipoproteins on mouse high density lipoproteins. Detection of post-translational modifications."
Puppione D.L., Yam L.M., Bassilian S., Souda P., Castellani L.W., Schumaker V.N., Whitelegge J.P.
Biochim. Biophys. Acta 1764:1363-1371(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 54-62 AND 68-77, MASS SPECTROMETRY, OXIDATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04119 mRNA. Translation: CAA27731.1.
M32360 Genomic DNA. Translation: AAA37248.1.
M79361 mRNA. Translation: AAA37249.1.
M79362 mRNA. Translation: AAA37250.1.
X62772 mRNA. Translation: CAA44616.1.
AK145823 mRNA. Translation: BAE26675.1.
AC084821 Genomic DNA. No translation available.
CH466520 Genomic DNA. Translation: EDL39118.1.
CH466520 Genomic DNA. Translation: EDL39119.1.
CH466520 Genomic DNA. Translation: EDL39120.1.
CH466520 Genomic DNA. Translation: EDL39121.1.
BC031786 mRNA. Translation: AAH31786.1.
PIRA37887.
B23594. B37887.
I48250.
A23594. JS0392.
RefSeqNP_038502.2. NM_013474.2.
XP_006496688.1. XM_006496625.1.
UniGeneMm.389209.

3D structure databases

ProteinModelPortalP09813.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198156. 1 interaction.
IntActP09813. 5 interactions.
MINTMINT-1855567.
STRING10090.ENSMUSP00000106951.

PTM databases

PhosphoSiteP09813.

Proteomic databases

PaxDbP09813.
PRIDEP09813.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005824; ENSMUSP00000005824; ENSMUSG00000005681.
ENSMUST00000111319; ENSMUSP00000106951; ENSMUSG00000005681.
ENSMUST00000111320; ENSMUSP00000106952; ENSMUSG00000005681.
ENSMUST00000111321; ENSMUSP00000106953; ENSMUSG00000005681.
GeneID11807.
KEGGmmu:11807.
UCSCuc007dnk.2. mouse.

Organism-specific databases

CTD336.
MGIMGI:88050. Apoa2.

Phylogenomic databases

eggNOGNOG40617.
GeneTreeENSGT00390000003306.
HOGENOMHOG000033999.
HOVERGENHBG050544.
InParanoidP09813.
KOK08758.
OMAAYFEKTQ.
OrthoDBEOG7G4QHG.
TreeFamTF338165.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.
REACT_189085. Disease.

Gene expression databases

CleanExMM_APOA2.
GenevestigatorP09813.

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

ChiTaRSAPOA2. mouse.
NextBio279671.
PROP09813.
SOURCESearch...

Entry information

Entry nameAPOA2_MOUSE
AccessionPrimary (citable) accession number: P09813
Secondary accession number(s): Q3UKX6, Q61317
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 3, 2012
Last modified: April 16, 2014
This is version 133 of the entry and version 2 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot