ID   APOC2_OTOGA             Reviewed;         100 AA.
AC   P0DMN9;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 13.
DE   RecName: Full=Apolipoprotein C-II;
DE            Short=Apo-CII;
DE            Short=ApoC-II;
DE   AltName: Full=Apolipoprotein C2;
DE   Contains:
DE     RecName: Full=Proapolipoprotein C-II;
DE              Short=ProapoC-II;
DE   Flags: Precursor;
GN   Name=APOC2;
OS   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=30611;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA   Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA   Walker B.J., Sharpe T., Hall G.;
RT   "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (JUL-2014).
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:0000250|UniProtKB:P02655}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02655}.
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:0000250|UniProtKB:P02655}.
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:0000250|UniProtKB:P02655}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein C2 family. {ECO:0000305}.
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DR   EMBL; AAQR03153639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003799547.1; XM_003799499.2.
DR   AlphaFoldDB; P0DMN9; -.
DR   SMR; P0DMN9; -.
DR   GeneID; 100956226; -.
DR   KEGG; oga:100956226; -.
DR   CTD; 344; -.
DR   OrthoDB; 1548460at2759; -.
DR   Proteomes; UP000005225; Unassembled WGS sequence.
DR   GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1440.10; -; 1.
DR   InterPro; IPR008019; Apo-CII.
DR   InterPro; IPR023121; ApoC-II_dom_sf.
DR   PANTHER; PTHR16566; PTHR16566; 1.
DR   Pfam; PF05355; Apo-CII; 1.
PE   3: Inferred from homology;
KW   Chylomicron; Glycoprotein; HDL; LDL; Lipid degradation; Lipid metabolism;
KW   Lipid transport; Reference proteome; Secreted; Sialic acid; Signal;
KW   Transport; VLDL.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..100
FT                   /note="Proapolipoprotein C-II"
FT                   /id="PRO_0000430328"
FT   CHAIN           29..100
FT                   /note="Apolipoprotein C-II"
FT                   /evidence="ECO:0000250|UniProtKB:P02655"
FT                   /id="PRO_0000430841"
FT   REGION          66..74
FT                   /note="Lipid binding"
FT                   /evidence="ECO:0000250|UniProtKB:P02655"
FT   REGION          78..100
FT                   /note="Lipoprotein lipase cofactor"
FT                   /evidence="ECO:0000250|UniProtKB:P02655"
SQ   SEQUENCE   100 AA;  11113 MW;  BBC97F0CB68086B0 CRC64;
     MGTRFLLALF LVLLVLGFEV QGAQLPQQDE PSSPTLLTQM QESLSSYWDS AKEAARGLYE
     KTYLPTVDEK LRDMYSKSTA AVSTYAGIFT DQLLTLLKGD