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 27-MAR-2024, entry version 121. 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; CC Method=Electrospray; Note=Homodimer.; CC Evidence={ECO:0000269|PubMed:21298813}; CC -!- SIMILARITY: Belongs to the apolipoprotein A2 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSPTRP00000069102; -. DR PaxDb; 9598-ENSPTRP00000002645; -. DR Ensembl; ENSPTRT00000002882.2; ENSPTRP00000002645.2; ENSPTRG00000001580.5. 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; 4610750at2759; -. DR Proteomes; UP000002277; Chromosome 1. DR Bgee; ENSPTRG00000001580; Expressed in liver and 12 other cell types or 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: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 Gene3D; 6.10.250.100; -; 1. DR InterPro; IPR006801; ApoA-II. DR InterPro; IPR036172; ApoA-II_sf. DR PANTHER; PTHR11027; APOLIPOPROTEIN A-II; 1. DR PANTHER; PTHR11027:SF0; APOLIPOPROTEIN A-II; 1. DR Pfam; PF04711; ApoA-II; 1. DR SUPFAM; SSF82936; Apolipoprotein A-II; 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 //