ID   A0A2K6AFA0_MANLE        Unreviewed;        72 AA.
AC   A0A2K6AFA0;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   14-DEC-2022, entry version 23.
DE   RecName: Full=Apolipoprotein C-II {ECO:0000256|ARBA:ARBA00013947, ECO:0000256|RuleBase:RU368054};
DE            Short=Apo-CII {ECO:0000256|RuleBase:RU368054};
DE            Short=ApoC-II {ECO:0000256|RuleBase:RU368054};
DE   AltName: Full=Apolipoprotein C2 {ECO:0000256|ARBA:ARBA00031176, ECO:0000256|RuleBase:RU368054};
GN   Name=APOC2 {ECO:0000313|Ensembl:ENSMLEP00000038715.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000038715.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000038715.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2022) to UniProtKB.
CC   -!- FUNCTION: Component of chylomicrons, very low-density lipoproteins
CC       (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins
CC       (HDL) in plasma. Plays an important role in lipoprotein metabolism as
CC       an activator of lipoprotein lipase. Both proapolipoprotein C-II and
CC       apolipoprotein C-II can activate lipoprotein lipase.
CC       {ECO:0000256|ARBA:ARBA00002160}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       ECO:0000256|RuleBase:RU368054}.
CC   -!- PTM: Proapolipoprotein C-II is synthesized as a sialic acid containing
CC       glycoprotein which is subsequently desialylated prior to its
CC       proteolytic processing. {ECO:0000256|RuleBase:RU368054}.
CC   -!- PTM: Proapolipoprotein C-II, the major form found in plasma undergoes
CC       proteolytic cleavage of its N-terminal hexapeptide to generate
CC       apolipoprotein C-II, which occurs as the minor form in plasma.
CC       {ECO:0000256|RuleBase:RU368054}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein C2 family.
CC       {ECO:0000256|ARBA:ARBA00007221, ECO:0000256|RuleBase:RU368054}.
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DR   RefSeq; XP_011830461.1; XM_011975071.1.
DR   AlphaFoldDB; A0A2K6AFA0; -.
DR   STRING; 9568.ENSMLEP00000038715; -.
DR   Ensembl; ENSMLET00000062328.1; ENSMLEP00000038715.1; ENSMLEG00000043412.1.
DR   GeneID; 105535841; -.
DR   CTD; 344; -.
DR   GeneTree; ENSGT00390000007913; -.
DR   OMA; GYWATAK; -.
DR   OrthoDB; 1548460at2759; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0042627; C:chylomicron; IEA:UniProtKB-UniRule.
DR   GO; GO:0034363; C:intermediate-density lipoprotein particle; IEA:Ensembl.
DR   GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-UniRule.
DR   GO; GO:0034366; C:spherical high-density lipoprotein particle; IEA:Ensembl.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-UniRule.
DR   GO; GO:0055102; F:lipase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0008289; F:lipid binding; IEA:Ensembl.
DR   GO; GO:0060230; F:lipoprotein lipase activator activity; IEA:Ensembl.
DR   GO; GO:0016004; F:phospholipase activator activity; IEA:Ensembl.
DR   GO; GO:0043274; F:phospholipase binding; IEA:Ensembl.
DR   GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
DR   GO; GO:0034382; P:chylomicron remnant clearance; IEA:Ensembl.
DR   GO; GO:0034384; P:high-density lipoprotein particle clearance; IEA:Ensembl.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0032375; P:negative regulation of cholesterol transport; IEA:Ensembl.
DR   GO; GO:0045833; P:negative regulation of lipid metabolic process; IEA:Ensembl.
DR   GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IEA:Ensembl.
DR   GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; IEA:Ensembl.
DR   GO; GO:0033700; P:phospholipid efflux; IEA:Ensembl.
DR   GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IEA:Ensembl.
DR   GO; GO:0010518; P:positive regulation of phospholipase activity; IEA:Ensembl.
DR   GO; GO:0060697; P:positive regulation of phospholipid catabolic process; IEA:Ensembl.
DR   GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IEA:Ensembl.
DR   GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
DR   Gene3D; 1.10.1440.10; -; 1.
DR   InterPro; IPR008019; Apo-CII.
DR   InterPro; IPR023121; ApoC-II_dom_sf.
DR   PANTHER; PTHR16566; APOLIPOPROTEIN C-II; 1.
DR   Pfam; PF05355; Apo-CII; 1.
PE   3: Inferred from homology;
KW   Chylomicron {ECO:0000256|ARBA:ARBA00022513, ECO:0000256|RuleBase:RU368054};
KW   HDL {ECO:0000256|ARBA:ARBA00022850, ECO:0000256|RuleBase:RU368054};
KW   LDL {ECO:0000256|ARBA:ARBA00022710, ECO:0000256|RuleBase:RU368054};
KW   Lipid degradation {ECO:0000256|RuleBase:RU368054};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU368054};
KW   Lipid transport {ECO:0000256|RuleBase:RU368054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW   Secreted {ECO:0000256|RuleBase:RU368054};
KW   Signal {ECO:0000256|RuleBase:RU368054, ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|RuleBase:RU368054};
KW   VLDL {ECO:0000256|ARBA:ARBA00023313, ECO:0000256|RuleBase:RU368054}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..72
FT                   /note="Apolipoprotein C-II"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014434678"
SQ   SEQUENCE   72 AA;  8038 MW;  F893A91EDB3FC1F2 CRC64;
     MGTRFLLALC LVLLVLGFEV QGAQLPQQDE RPSPALLSQV QESLSSYWES AKAAAQKLYE
     KTYLPAVDEK LR
//