P09813 (APOA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Apolipoprotein A-II
Short name=Apo-AII
Short name=ApoA-II

Alternative name(s):
Apolipoprotein A2

Gene names

Name:

Apoa2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	102 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Homodimer; disulfide-linked. 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.

Ontologies

Keywords
Biological process	Lipid transport Transport
Cellular component	Amyloid HDL Secreted
Disease	Disease mutation
Domain	Signal
PTM	Cleavage on pair of basic residues Disulfide bond Phosphoprotein Pyrrolidone carboxylic acid
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acute inflammatory response Inferred from electronic annotation. Source: Compara beta-glucoside transport Non-traceable author statement PubMed 12269810. Source: UniProtKB cholesterol efflux Inferred from electronic annotation. Source: Compara 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: Compara fatty acid metabolic process Non-traceable author statement PubMed 12269810. Source: UniProtKB high-density lipoprotein particle assembly Inferred from electronic annotation. Source: Compara high-density lipoprotein particle clearance Inferred from electronic annotation. Source: Compara high-density lipoprotein particle remodeling Inferred from electronic annotation. Source: Compara 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: Compara negative regulation of cholesterol import Inferred from electronic annotation. Source: Compara negative regulation of cholesterol transporter activity Inferred from electronic annotation. Source: Compara negative regulation of cytokine secretion involved in immune response Inferred from electronic annotation. Source: Compara negative regulation of lipase activity Inferred from mutant phenotype PubMed 10357838. Source: MGI negative regulation of lipid catabolic process Inferred from electronic annotation. Source: Compara negative regulation of very-low-density lipoprotein particle remodeling Inferred from electronic annotation. Source: Compara organ regeneration Inferred from electronic annotation. Source: Compara peptidyl-methionine modification Inferred from electronic annotation. Source: Compara phosphatidylcholine biosynthetic process Inferred from electronic annotation. Source: Compara phospholipid catabolic process Inferred from electronic annotation. Source: Compara phospholipid efflux Inferred from electronic annotation. Source: Compara positive regulation of cholesterol esterification Inferred from electronic annotation. Source: Compara 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: Compara protein folding Inferred from electronic annotation. Source: Compara protein oxidation Inferred from electronic annotation. Source: Compara regulation of intestinal cholesterol absorption Inferred from mutant phenotype PubMed 8962133. Source: MGI regulation of protein stability Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to estrogen stimulus Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara response to glucose stimulus Inferred from electronic annotation. Source: Compara reverse cholesterol transport Inferred from electronic annotation. Source: Compara triglyceride-rich lipoprotein particle remodeling Inferred from electronic annotation. Source: Compara
Cellular_component	chylomicron Inferred from electronic annotation. Source: Compara extracellular space Inferred from direct assay PubMed 1596514PubMed 6403543PubMed 9186920. Source: MGI spherical high-density lipoprotein particle Inferred from electronic annotation. Source: Compara very-low-density lipoprotein particle Inferred from electronic annotation. Source: Compara
Molecular_function	cholesterol binding Inferred from electronic annotation. Source: Compara cholesterol transporter activity Inferred from electronic annotation. Source: Compara high-density lipoprotein particle binding Inferred from mutant phenotype PubMed 14729860. Source: MGI lipase inhibitor activity Inferred from electronic annotation. Source: Compara phosphatidylcholine binding Inferred from electronic annotation. Source: Compara phosphatidylcholine-sterol O-acyltransferase activator activity Inferred from electronic annotation. Source: Compara protein heterodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18
	Propeptide	19 – 23	5			PRO_0000002007
	Chain	24 – 102	79	Apolipoprotein A-II		PRO_0000002008
Amino acid modifications
	Modified residue	24	1	Pyrrolidone carboxylic acid By similarity
Natural variations
	Natural variant	28	1	P → Q in SAM. Ref.2
Experimental info
	Sequence conflict	43	1	D → E in CAA27731. Ref.1
	Sequence conflict	43	1	D → E in AAA37248. Ref.2
	Sequence conflict	43	1	D → E in AAA37250. Ref.3
	Sequence conflict	43	1	D → E in AAH31786. Ref.8
	Sequence conflict	48	1	L → F in CAA44616. Ref.4
	Sequence conflict	49	1	M → V in CAA27731. Ref.1
	Sequence conflict	49	1	M → V in AAA37248. Ref.2
	Sequence conflict	49	1	M → V in AAA37250. Ref.3
	Sequence conflict	49	1	M → V in AAH31786. Ref.8
	Sequence conflict	61	1	A → V in CAA27731. Ref.1
	Sequence conflict	61	1	A → V in AAA37250. Ref.3
	Sequence conflict	61	1	A → V in AAH31786. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P09813 [UniParc]. Last modified October 3, 2012. Version 2. Checksum: F50142E0D118665B	FASTA	102	11,309
	10 20 30 40 50 60 MKLLAMVALL VTICSLEGAL VKRQADGPDM QSLFTQYFQS MTDYGKDLME KAKTSEIQSQ 70 80 90 100 AKAYFEKTHE QLTPLVRSAG TSLVNFFSSL MNLEEKPAPA AK

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
+	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.
IPI	IPI00111315. IPI00869381.
PIR	A37887. B23594. B37887. I48250. A23594. JS0392.
RefSeq	NP_038502.2. NM_013474.2.
UniGene	Mm.389209.
3D structure databases
ProteinModelPortal	P09813.
SMR	P09813. Positions 28-98.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000106951.
PTM databases
PhosphoSite	P09813.
Proteomic databases
PaxDb	P09813.
PRIDE	P09813.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000005824; ENSMUSP00000005824; ENSMUSG00000005681. ENSMUST00000111319; ENSMUSP00000106951; ENSMUSG00000005681. ENSMUST00000111320; ENSMUSP00000106952; ENSMUSG00000005681. ENSMUST00000111321; ENSMUSP00000106953; ENSMUSG00000005681.
GeneID	11807.
KEGG	mmu:11807.
Organism-specific databases
CTD	336.
MGI	MGI:88050. Apoa2.
Phylogenomic databases
eggNOG	NOG40617.
GeneTree	ENSGT00390000003306.
HOGENOM	HOG000033999.
HOVERGEN	HBG050544.
InParanoid	P09813.
KO	K08758.
OMA	TICSLEG.
OrthoDB	EOG42NJ1Z.
Gene expression databases
CleanEx	MM_APOA2.
Genevestigator	P09813.
GermOnline	ENSMUSG00000005681. Mus musculus.
Family and domain databases
InterPro	IPR006801. ApoA-II. [Graphical view]
PANTHER	PTHR11027. PTHR11027. 1 hit.
Pfam	PF04711. ApoA-II. 1 hit. [Graphical view]
ProDom	PD010397. ApoA-II. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...
Other
ChiTaRS	APOA2. mouse.
NextBio	279671.
SOURCE	Search...

Entry information

Entry name

APOA2_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program