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Protein

Apolipoprotein A-II

Gene

Apoa2

Organism
Mus musculus (Mouse)
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

  1. apolipoprotein receptor binding Source: MGI
  2. cholesterol binding Source: MGI
  3. cholesterol transporter activity Source: Ensembl
  4. high-density lipoprotein particle binding Source: MGI
  5. high-density lipoprotein particle receptor binding Source: MGI
  6. lipase inhibitor activity Source: MGI
  7. lipid binding Source: MGI
  8. lipid transporter activity Source: MGI
  9. phosphatidylcholine binding Source: MGI
  10. phosphatidylcholine-sterol O-acyltransferase activator activity Source: MGI
  11. phospholipid binding Source: MGI
  12. protein heterodimerization activity Source: UniProtKB
  13. protein homodimerization activity Source: MGI

GO - Biological processi

  1. acute inflammatory response Source: Ensembl
  2. beta-glucoside transport Source: UniProtKB
  3. cholesterol efflux Source: MGI
  4. cholesterol homeostasis Source: MGI
  5. cholesterol metabolic process Source: MGI
  6. diacylglycerol catabolic process Source: MGI
  7. fatty acid metabolic process Source: UniProtKB
  8. high-density lipoprotein particle assembly Source: MGI
  9. high-density lipoprotein particle clearance Source: MGI
  10. high-density lipoprotein particle remodeling Source: MGI
  11. lipid transport Source: MGI
  12. lipoprotein metabolic process Source: MGI
  13. low-density lipoprotein particle remodeling Source: MGI
  14. negative regulation of cholesterol import Source: MGI
  15. negative regulation of cholesterol transport Source: MGI
  16. negative regulation of cholesterol transporter activity Source: MGI
  17. negative regulation of cytokine secretion involved in immune response Source: MGI
  18. negative regulation of lipase activity Source: MGI
  19. negative regulation of lipid catabolic process Source: MGI
  20. negative regulation of very-low-density lipoprotein particle remodeling Source: MGI
  21. organ regeneration Source: Ensembl
  22. peptidyl-methionine modification Source: MGI
  23. phosphatidylcholine biosynthetic process Source: MGI
  24. phospholipid catabolic process Source: MGI
  25. phospholipid efflux Source: MGI
  26. positive regulation of catalytic activity Source: MGI
  27. positive regulation of cholesterol esterification Source: MGI
  28. positive regulation of interleukin-8 biosynthetic process Source: UniProtKB
  29. positive regulation of lipid catabolic process Source: MGI
  30. protein folding Source: MGI
  31. protein oxidation Source: MGI
  32. regulation of intestinal cholesterol absorption Source: MGI
  33. regulation of protein stability Source: MGI
  34. response to drug Source: Ensembl
  35. response to estrogen Source: Ensembl
  36. response to glucocorticoid Source: Ensembl
  37. response to glucose Source: MGI
  38. reverse cholesterol transport Source: MGI
  39. triglyceride-rich lipoprotein particle remodeling Source: MGI
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Enzyme and pathway databases

ReactomeiREACT_272139. PPARA activates gene expression.
REACT_295031. Retinoid metabolism and transport.
REACT_314625. Chylomicron-mediated lipid 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 chain:
Proapolipoprotein A-II
Short name:
ProapoA-II
Gene namesi
Name:Apoa2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:88050. Apoa2.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: MGI
  2. chylomicron Source: MGI
  3. cytosol Source: Reactome
  4. extracellular region Source: Reactome
  5. extracellular space Source: MGI
  6. extracellular vesicular exosome Source: MGI
  7. high-density lipoprotein particle Source: MGI
  8. spherical high-density lipoprotein particle Source: MGI
  9. very-low-density lipoprotein particle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Amyloid, HDL, Secreted

Pathology & Biotechi

Involvement in diseasei

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

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 10284Proapolipoprotein A-IIPRO_0000425354Add
BLAST
Chaini24 – 10279Apolipoprotein A-IIPRO_0000002008Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Pyrrolidone carboxylic acid; in Apolipoprotein A-IIBy similarity
Modified residuei49 – 491Methionine sulfoxideBy similarity

Post-translational modificationi

Phosphorylation sites are present in the extracellular medium.By similarity

Keywords - PTMi

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

Proteomic databases

MaxQBiP09813.
PaxDbiP09813.
PRIDEiP09813.

PTM databases

PhosphoSiteiP09813.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

CleanExiMM_APOA2.
GenevestigatoriP09813.

Interactioni

Subunit structurei

Monomer. Interacts with APOA1BP and NDRG1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi198156. 1 interaction.
IntActiP09813. 5 interactions.
MINTiMINT-1855567.
STRINGi10090.ENSMUSP00000106951.

Structurei

3D structure databases

ProteinModelPortaliP09813.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the apolipoprotein A2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40617.
GeneTreeiENSGT00390000003306.
HOGENOMiHOG000033999.
HOVERGENiHBG050544.
InParanoidiP09813.
KOiK08758.
OMAiAYFEKTQ.
OrthoDBiEOG7G4QHG.
TreeFamiTF338165.

Family and domain databases

InterProiIPR006801. ApoA-II.
[Graphical view]
PANTHERiPTHR11027. PTHR11027. 1 hit.
PfamiPF04711. ApoA-II. 1 hit.
[Graphical view]
ProDomiPD010397. ApoA-II. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

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

P09813-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLAMVALL VTICSLEGAL VKRQADGPDM QSLFTQYFQS MTDYGKDLME
60 70 80 90 100
KAKTSEIQSQ AKAYFEKTHE QLTPLVRSAG TSLVNFFSSL MNLEEKPAPA

AK
Length:102
Mass (Da):11,309
Last modified:October 3, 2012 - v2
Checksum:iF50142E0D118665B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431D → E in CAA27731 (PubMed:2426658).Curated
Sequence conflicti43 – 431D → E in AAA37248 (PubMed:2514123).Curated
Sequence conflicti43 – 431D → E in AAA37250 (PubMed:2118905).Curated
Sequence conflicti43 – 431D → E in AAH31786 (PubMed:15489334).Curated
Sequence conflicti48 – 481L → F in CAA44616 (PubMed:1683229).Curated
Sequence conflicti49 – 491M → V in CAA27731 (PubMed:2426658).Curated
Sequence conflicti49 – 491M → V in AAA37248 (PubMed:2514123).Curated
Sequence conflicti49 – 491M → V in AAA37250 (PubMed:2118905).Curated
Sequence conflicti49 – 491M → V in AAH31786 (PubMed:15489334).Curated
Sequence conflicti61 – 611A → V in CAA27731 (PubMed:2426658).Curated
Sequence conflicti61 – 611A → V in AAA37250 (PubMed:2118905).Curated
Sequence conflicti61 – 611A → V in AAH31786 (PubMed:15489334).Curated

Mass spectrometryi

Molecular mass is 8709.2±0.071 Da from positions 24 - 102. Determined by ESI. Strain C57BL/6. Without methionine sulfoxide.1 Publication
Molecular mass is 8719.5 Da from positions 24 - 102. Determined by ESI. Strain BALB/c. Without methionine sulfoxide.1 Publication
Molecular mass is 8725.3±0.283 Da from positions 24 - 102. Determined by ESI. Strain C57BL/6. With 1 methionine sulfoxide.1 Publication
Molecular mass is 8742 Da from positions 24 - 102. Determined by ESI. Strain C57BL/6. With 2 methionine sulfoxides.1 Publication
Molecular mass is 8735.2 Da from positions 24 - 102. Determined by ESI. Strain BALB/c. With 1 methionine sulfoxide.1 Publication
Molecular mass is 9294±0.707 Da from positions 19 - 102. Determined by ESI. Strain C57BL/6. Without methionine sulfoxide.1 Publication
Molecular mass is 9304 Da from positions 19 - 102. Determined by ESI. Strain BALB/c. Without methionine sulfoxide.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281P → Q in SAM. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35773.1.
PIRiA37887.
B37887. B23594.
I48250.
JS0392. A23594.
RefSeqiNP_038502.2. NM_013474.2.
XP_006496688.1. XM_006496625.1.
UniGeneiMm.389209.

Genome annotation databases

EnsembliENSMUST00000005824; ENSMUSP00000005824; ENSMUSG00000005681.
ENSMUST00000111319; ENSMUSP00000106951; ENSMUSG00000005681.
ENSMUST00000111320; ENSMUSP00000106952; ENSMUSG00000005681.
ENSMUST00000111321; ENSMUSP00000106953; ENSMUSG00000005681.
GeneIDi11807.
KEGGimmu:11807.
UCSCiuc007dnk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35773.1.
PIRiA37887.
B37887. B23594.
I48250.
JS0392. A23594.
RefSeqiNP_038502.2. NM_013474.2.
XP_006496688.1. XM_006496625.1.
UniGeneiMm.389209.

3D structure databases

ProteinModelPortaliP09813.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198156. 1 interaction.
IntActiP09813. 5 interactions.
MINTiMINT-1855567.
STRINGi10090.ENSMUSP00000106951.

PTM databases

PhosphoSiteiP09813.

Proteomic databases

MaxQBiP09813.
PaxDbiP09813.
PRIDEiP09813.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005824; ENSMUSP00000005824; ENSMUSG00000005681.
ENSMUST00000111319; ENSMUSP00000106951; ENSMUSG00000005681.
ENSMUST00000111320; ENSMUSP00000106952; ENSMUSG00000005681.
ENSMUST00000111321; ENSMUSP00000106953; ENSMUSG00000005681.
GeneIDi11807.
KEGGimmu:11807.
UCSCiuc007dnk.2. mouse.

Organism-specific databases

CTDi336.
MGIiMGI:88050. Apoa2.

Phylogenomic databases

eggNOGiNOG40617.
GeneTreeiENSGT00390000003306.
HOGENOMiHOG000033999.
HOVERGENiHBG050544.
InParanoidiP09813.
KOiK08758.
OMAiAYFEKTQ.
OrthoDBiEOG7G4QHG.
TreeFamiTF338165.

Enzyme and pathway databases

ReactomeiREACT_272139. PPARA activates gene expression.
REACT_295031. Retinoid metabolism and transport.
REACT_314625. Chylomicron-mediated lipid transport.

Miscellaneous databases

ChiTaRSiApoa2. mouse.
NextBioi279671.
PROiP09813.
SOURCEiSearch...

Gene expression databases

CleanExiMM_APOA2.
GenevestigatoriP09813.

Family and domain databases

InterProiIPR006801. ApoA-II.
[Graphical view]
PANTHERiPTHR11027. PTHR11027. 1 hit.
PfamiPF04711. ApoA-II. 1 hit.
[Graphical view]
ProDomiPD010397. ApoA-II. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1985) [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(1988) [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(1989) [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(1990) [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.
    , 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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Amnion.
  6. 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 (AUG-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(2003) [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(1985) [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(1985) [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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 54-62 AND 68-77, MASS SPECTROMETRY, OXIDATION.

Entry informationi

Entry nameiAPOA2_MOUSE
AccessioniPrimary (citable) accession number: P09813
Secondary accession number(s): Q3UKX6, Q61317
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 3, 2012
Last modified: April 1, 2015
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.