ID   APOA2_PANPA             Reviewed;         100 AA.
AC   P0DM95;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2013, sequence version 1.
DT   03-AUG-2022, entry version 43.
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 paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9597;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22722832; DOI=10.1038/nature11128;
RA   Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA   Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA   Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA   Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA   Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA   Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA   Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA   Paabo S.;
RT   "The bonobo genome compared with the chimpanzee and human genomes.";
RL   Nature 486:527-531(2012).
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).
RN   [3]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (OCT-2013).
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=17471.0; Mass_error=1.0;
CC       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; AJFE01037512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003811880.1; XM_003811832.2.
DR   AlphaFoldDB; P0DM95; -.
DR   SMR; P0DM95; -.
DR   STRING; 9597.XP_003811880.1; -.
DR   Ensembl; ENSPPAT00000050602; ENSPPAP00000027759; ENSPPAG00000036949.
DR   GeneID; 100977422; -.
DR   KEGG; pps:100977422; -.
DR   CTD; 336; -.
DR   eggNOG; ENOG502SVYZ; Eukaryota.
DR   GeneTree; ENSGT00390000003306; -.
DR   OMA; LTICSFE; -.
DR   OrthoDB; 1612564at2759; -.
DR   Proteomes; UP000240080; Chromosome 1.
DR   Bgee; ENSPPAG00000036949; Expressed in liver and 4 other tissues.
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..100
FT                   /note="Proapolipoprotein A-II"
FT                   /id="PRO_0000425356"
FT   CHAIN           24..100
FT                   /note="Apolipoprotein A-II"
FT                   /evidence="ECO:0000305|PubMed:21298813"
FT                   /id="PRO_0000424682"
FT   CHAIN           24..99
FT                   /note="Truncated apolipoprotein A-II"
FT                   /evidence="ECO:0000305|PubMed:21298813"
FT                   /id="PRO_0000424750"
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