APOA2_GORGO
ID APOA2_GORGO Reviewed; 100 AA.
AC P0DJG2;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 58.
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 Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
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 [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RL Unpublished observations (FEB-2012).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 -!- TISSUE SPECIFICITY: Plasma.
CC -!- MASS SPECTROMETRY: [Apolipoprotein A-II]: Mass=17380.7;
CC Mass_error=0.58; Method=Electrospray; Note=Homodimer.;
CC Evidence={ECO:0000269|PubMed:21298813};
CC -!- MASS SPECTROMETRY: [Truncated apolipoprotein A-II]: Mass=17258;
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 RefSeq; XP_004027815.1; XM_004027766.2.
DR AlphaFoldDB; P0DJG2; -.
DR SMR; P0DJG2; -.
DR STRING; 9593.ENSGGOP00000005597; -.
DR Ensembl; ENSGGOT00000005742; ENSGGOP00000005597; ENSGGOG00000005718.
DR GeneID; 101126351; -.
DR KEGG; ggo:101126351; -.
DR CTD; 336; -.
DR eggNOG; ENOG502SVYZ; Eukaryota.
DR GeneTree; ENSGT00390000003306; -.
DR HOGENOM; CLU_157351_0_0_1; -.
DR InParanoid; P0DJG2; -.
DR OrthoDB; 1612564at2759; -.
DR Proteomes; UP000001519; Chromosome 1.
DR Bgee; ENSGGOG00000005718; Expressed in liver and 3 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: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: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:0000255"
FT CHAIN 19..100
FT /note="Proapolipoprotein A-II"
FT /id="PRO_0000425350"
FT CHAIN 24..100
FT /note="Apolipoprotein A-II"
FT /evidence="ECO:0000305|PubMed:21298813"
FT /id="PRO_0000416569"
FT CHAIN 24..99
FT /note="Truncated apolipoprotein A-II"
FT /evidence="ECO:0000305|PubMed:21298813"
FT /id="PRO_0000424747"
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; 11175 MW; 1247868A25EC3AF2 CRC64;
MKLLAATVLL LTICSLEGAL VRRQAKEPCV ESLVSQYFQT VTDYGKDLME KVKSPELQAE
AKSYFEKSKE QLTPLIKKAG TELVNFLSYF VELGTQPATQ
