APOA2_PONAB
ID APOA2_PONAB Reviewed; 93 AA.
AC P0DJD2;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 39.
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 Flags: Precursor;
GN Name=APOA2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP MASS SPECTROMETRY, SUBUNIT, AND OXIDATION AT MET-49.
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).
RN [2]
RP IDENTIFICATION.
RA Puppione D.L.;
RL Unpublished observations (FEB-2012).
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 -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=16060.5;
CC Mass_error=0.71; Method=Electrospray; Note=Homodimer, without
CC methionine sulfoxide.; Evidence={ECO:0000269|PubMed:21298813};
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=16076.0;
CC Method=Electrospray; Note=Homodimer, with 1 methionine sulfoxide.;
CC Evidence={ECO:0000269|PubMed:21298813};
CC -!- SIMILARITY: Belongs to the apolipoprotein A2 family. {ECO:0000305}.
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DR AlphaFoldDB; P0DJD2; -.
DR SMR; P0DJD2; -.
DR PRIDE; P0DJD2; -.
DR InParanoid; P0DJD2; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
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:0000255"
FT CHAIN 19..93
FT /note="Proapolipoprotein A-II"
FT /id="PRO_0000425359"
FT CHAIN 24..93
FT /note="Apolipoprotein A-II"
FT /evidence="ECO:0000305|PubMed:21298813"
FT /id="PRO_0000415503"
FT MOD_RES 49
FT /note="Methionine sulfoxide"
FT /evidence="ECO:0000269|PubMed:21298813"
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 93 AA; 10516 MW; E20ECA2B08F0763B CRC64;
MKLLAATVLL LTICSLEGAL VRRQAKEPCV ESPVSQYFQT VTDYGKDLME KVKSPELQAE
AKSYFEKSKE QLTPLIKKAG TELVNFLNYF LEL
