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Apolipoprotein A-II (Apo-AII) (ApoA-II) (Apolipoprotein A2) [Cleaved into: Proapolipoprotein A-II (ProapoA-II); Truncated apolipoprotein A-II]

 APOA2_PANTR             Reviewed;         100 AA.
Q8MIQ5;
07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
23-MAY-2018, entry version 99.
RecName: Full=Apolipoprotein A-II;
Short=Apo-AII;
Short=ApoA-II;
AltName: Full=Apolipoprotein A2;
Contains:
RecName: Full=Proapolipoprotein A-II;
Short=ProapoA-II;
Contains:
RecName: Full=Truncated apolipoprotein A-II;
Flags: Precursor;
Name=APOA2;
Pan troglodytes (Chimpanzee).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pan.
NCBI_TaxID=9598;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12136239; DOI=10.1007/s00439-002-0763-x;
Fullerton S.M., Clark A.G., Weiss K.M., Taylor S.L., Stengard J.H.,
Salomaa V., Boerwinkle E., Nickerson D.A.;
"Sequence polymorphism at the human apolipoprotein AII gene (APOA2):
unexpected deficit of variation in an African-American sample.";
Hum. Genet. 111:75-87(2002).
[2]
MASS SPECTROMETRY, AND SUBUNIT.
PubMed=21298813; DOI=10.1016/j.cbd.2009.09.001;
Puppione D.L., Della Donna L., Laganowsky A.D., Bassilian S.,
Souda P., Ryder O.A., Whitelegge J.P.;
"Mass spectral analyses of the two major apolipoproteins of great ape
high density lipoproteins.";
Comp. Biochem. Physiol. 4:305-309(2009).
-!- FUNCTION: May stabilize HDL (high density lipoprotein) structure
by its association with lipids, and affect the HDL metabolism.
-!- SUBUNIT: Homodimer; disulfide-linked (PubMed:21298813). Interacts
with APOA1BP and NDRG1 (By similarity).
{ECO:0000250|UniProtKB:P02652, ECO:0000269|PubMed:21298813}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02652}.
-!- TISSUE SPECIFICITY: Plasma.
-!- MASS SPECTROMETRY: Mass=17469.7; Mass_error=1.15;
Method=Electrospray; Range=24-100; Note=Homodimer.;
Evidence={ECO:0000269|PubMed:21298813};
-!- MASS SPECTROMETRY: Mass=17342.0; Method=Electrospray; Range=24-99;
Note=Homodimer.; Evidence={ECO:0000269|PubMed:21298813};
-!- SIMILARITY: Belongs to the apolipoprotein A2 family.
{ECO:0000305}.
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EMBL; AY100525; AAM49808.1; -; Genomic_DNA.
RefSeq; NP_001008976.1; NM_001008976.1.
RefSeq; XP_009431992.2; XM_009433717.2.
UniGene; Ptr.6287; -.
ProteinModelPortal; Q8MIQ5; -.
STRING; 9598.ENSPTRP00000002645; -.
PaxDb; Q8MIQ5; -.
PRIDE; Q8MIQ5; -.
Ensembl; ENSPTRT00000002882; ENSPTRP00000002645; ENSPTRG00000001580.
GeneID; 449498; -.
KEGG; ptr:449498; -.
CTD; 336; -.
VGNC; VGNC:8240; APOA2.
eggNOG; ENOG410KCI2; Eukaryota.
eggNOG; ENOG4110NY0; LUCA.
GeneTree; ENSGT00390000003306; -.
HOGENOM; HOG000033999; -.
HOVERGEN; HBG050544; -.
InParanoid; Q8MIQ5; -.
KO; K08758; -.
Proteomes; UP000002277; Chromosome 1.
GO; GO:0072562; C:blood microparticle; IBA:GO_Central.
GO; GO:0042627; C:chylomicron; IBA:GO_Central.
GO; GO:0034366; C:spherical high-density lipoprotein particle; IBA:GO_Central.
GO; GO:0034361; C:very-low-density lipoprotein particle; IBA:GO_Central.
GO; GO:0034190; F:apolipoprotein receptor binding; IBA:GO_Central.
GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
GO; GO:0008035; F:high-density lipoprotein particle binding; IBA:GO_Central.
GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IBA:GO_Central.
GO; GO:0055102; F:lipase inhibitor activity; IBA:GO_Central.
GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
GO; GO:0008203; P:cholesterol metabolic process; IBA:GO_Central.
GO; GO:0030301; P:cholesterol transport; IEA:GOC.
GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
GO; GO:0034375; P:high-density lipoprotein particle remodeling; IBA:GO_Central.
GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
GO; GO:0034374; P:low-density lipoprotein particle remodeling; IBA:GO_Central.
GO; GO:0060192; P:negative regulation of lipase activity; IBA:GO_Central.
GO; GO:0018206; P:peptidyl-methionine modification; ISS:UniProtKB.
GO; GO:0045416; P:positive regulation of interleukin-8 biosynthetic process; ISS:UniProtKB.
GO; GO:0018158; P:protein oxidation; ISS:UniProtKB.
GO; GO:0034370; P:triglyceride-rich lipoprotein particle remodeling; IBA:GO_Central.
InterPro; IPR006801; ApoA-II.
InterPro; IPR036172; ApoA-II_sf.
PANTHER; PTHR11027; PTHR11027; 1.
Pfam; PF04711; ApoA-II; 1.
ProDom; PD010397; ApoA-II; 1.
SUPFAM; SSF82936; SSF82936; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
HDL; Lipid transport; Oxidation; Phosphoprotein; Reference proteome;
Secreted; Signal; Transport.
SIGNAL 1 18 {ECO:0000250}.
CHAIN 19 100 Proapolipoprotein A-II.
/FTId=PRO_0000425358.
CHAIN 24 100 Apolipoprotein A-II.
{ECO:0000305|PubMed:21298813}.
/FTId=PRO_0000002010.
CHAIN 24 99 Truncated apolipoprotein A-II.
{ECO:0000305|PubMed:21298813}.
/FTId=PRO_0000416582.
MOD_RES 49 49 Methionine sulfoxide.
{ECO:0000250|UniProtKB:P02652}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000250|UniProtKB:P02652}.
MOD_RES 68 68 Phosphoserine.
{ECO:0000250|UniProtKB:P02652}.
SEQUENCE 100 AA; 11220 MW; 9037748A340C7B53 CRC64;
MKLLAATVLL LTICSLEGAL VRRQAKEPCV DNLVSQYFQT VTDYGKDLME KVKSPELQAE
AKSYFEKSKE QLTPLIKKAG TELVNFLSYF MELGTQPATQ


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