APOA2_PANTR
ID APOA2_PANTR Reviewed; 100 AA.
AC Q8MIQ5;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Apolipoprotein A-II;
DE Short=Apo-AII;
DE Short=ApoA-II;
DE AltName: Full=Apolipoprotein A2;
DE Contains:
DE RecName: Full=Proapolipoprotein A-II;
DE Short=ProapoA-II;
DE Contains:
DE RecName: Full=Truncated apolipoprotein A-II;
DE Flags: Precursor;
GN Name=APOA2;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12136239; DOI=10.1007/s00439-002-0763-x;
RA Fullerton S.M., Clark A.G., Weiss K.M., Taylor S.L., Stengard J.H.,
RA Salomaa V., Boerwinkle E., Nickerson D.A.;
RT "Sequence polymorphism at the human apolipoprotein AII gene (APOA2):
RT unexpected deficit of variation in an African-American sample.";
RL Hum. Genet. 111:75-87(2002).
RN [2]
RP MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=21298813; DOI=10.1016/j.cbd.2009.09.001;
RA Puppione D.L., Della Donna L., Laganowsky A.D., Bassilian S., Souda P.,
RA Ryder O.A., Whitelegge J.P.;
RT "Mass spectral analyses of the two major apolipoproteins of great ape high
RT density lipoproteins.";
RL Comp. Biochem. Physiol. 4:305-309(2009).
CC -!- FUNCTION: May stabilize HDL (high density lipoprotein) structure by its
CC association with lipids, and affect the HDL metabolism.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:21298813). Interacts with
CC NAXE and NDRG1 (By similarity). {ECO:0000250|UniProtKB:P02652,
CC ECO:0000269|PubMed:21298813}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02652}.
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=17469.7;
CC Mass_error=1.15; Method=Electrospray; Note=Homodimer.;
CC Evidence={ECO:0000269|PubMed:21298813};
CC -!- MASS SPECTROMETRY: [Truncated apolipoprotein A-II]: Mass=17342.0;
CC Method=Electrospray; Note=Homodimer.;
CC Evidence={ECO:0000269|PubMed:21298813};
CC -!- SIMILARITY: Belongs to the apolipoprotein A2 family. {ECO:0000305}.
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DR EMBL; AY100525; AAM49808.1; -; Genomic_DNA.
DR RefSeq; NP_001008976.1; NM_001008976.1.
DR RefSeq; XP_009431992.2; XM_009433717.2.
DR AlphaFoldDB; Q8MIQ5; -.
DR SMR; Q8MIQ5; -.
DR STRING; 9598.ENSPTRP00000002645; -.
DR PaxDb; Q8MIQ5; -.
DR PRIDE; Q8MIQ5; -.
DR Ensembl; ENSPTRT00000002882; ENSPTRP00000002645; ENSPTRG00000001580.
DR GeneID; 449498; -.
DR KEGG; ptr:449498; -.
DR CTD; 336; -.
DR VGNC; VGNC:8240; APOA2.
DR eggNOG; ENOG502SVYZ; Eukaryota.
DR GeneTree; ENSGT00390000003306; -.
DR InParanoid; Q8MIQ5; -.
DR OMA; LTICSFE; -.
DR OrthoDB; 1612564at2759; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000001580; Expressed in liver and 12 other tissues.
DR GO; GO:0042627; C:chylomicron; IBA:GO_Central.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; IBA:GO_Central.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IBA:GO_Central.
DR GO; GO:0034190; F:apolipoprotein receptor binding; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
DR GO; GO:0008035; F:high-density lipoprotein particle binding; IBA:GO_Central.
DR GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IBA:GO_Central.
DR GO; GO:0055102; F:lipase inhibitor activity; IBA:GO_Central.
DR GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IBA:GO_Central.
DR GO; GO:0008203; P:cholesterol metabolic process; IBA:GO_Central.
DR GO; GO:0030301; P:cholesterol transport; IBA:GO_Central.
DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IBA:GO_Central.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IBA:GO_Central.
DR GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IBA:GO_Central.
DR GO; GO:0060192; P:negative regulation of lipase activity; IBA:GO_Central.
DR GO; GO:0018206; P:peptidyl-methionine modification; ISS:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0018158; P:protein oxidation; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0034370; P:triglyceride-rich lipoprotein particle remodeling; IBA:GO_Central.
DR InterPro; IPR006801; ApoA-II.
DR InterPro; IPR036172; ApoA-II_sf.
DR PANTHER; PTHR11027; PTHR11027; 1.
DR Pfam; PF04711; ApoA-II; 1.
DR SUPFAM; SSF82936; SSF82936; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Disulfide bond; HDL; Lipid transport;
KW Oxidation; Phosphoprotein; Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..100
FT /note="Proapolipoprotein A-II"
FT /id="PRO_0000425358"
FT CHAIN 24..100
FT /note="Apolipoprotein A-II"
FT /evidence="ECO:0000305|PubMed:21298813"
FT /id="PRO_0000002010"
FT CHAIN 24..99
FT /note="Truncated apolipoprotein A-II"
FT /evidence="ECO:0000305|PubMed:21298813"
FT /id="PRO_0000416582"
FT MOD_RES 49
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000250|UniProtKB:P02652"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02652"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02652"
SQ SEQUENCE 100 AA; 11220 MW; 9037748A340C7B53 CRC64;
MKLLAATVLL LTICSLEGAL VRRQAKEPCV DNLVSQYFQT VTDYGKDLME KVKSPELQAE
AKSYFEKSKE QLTPLIKKAG TELVNFLSYF MELGTQPATQ
