ID   APOC2_CAPHE             Reviewed;         101 AA.
AC   P0DN40;
DT   09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 1.
DT   25-MAY-2022, entry version 8.
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   Capra hircus aegagrus (Wild goat) (Capra aegagrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9923;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Streeter I.;
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (OCT-2015).
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; CBYH010014123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0DN40; -.
DR   SMR; P0DN40; -.
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; Secreted; Sialic acid; Signal; Transport; VLDL.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..101
FT                   /note="Proapolipoprotein C-II"
FT                   /id="PRO_0000435012"
FT   CHAIN           29..101
FT                   /note="Apolipoprotein C-II"
FT                   /evidence="ECO:0000250|UniProtKB:P02655"
FT                   /id="PRO_0000435013"
FT   REGION          66..74
FT                   /note="Lipid binding"
FT                   /evidence="ECO:0000250|UniProtKB:P02655"
FT   REGION          78..101
FT                   /note="Lipoprotein lipase cofactor"
FT                   /evidence="ECO:0000250|UniProtKB:P02655"
SQ   SEQUENCE   101 AA;  11118 MW;  A57CCF0CD35798E0 CRC64;
     MGTRYFLVGF LILLVLGFEA QGAHVPQQDE ASSPALLTKM QKSLLGYWDT AKAAAHKLYK
     KTYLPTVDEK IRDIYSKSTA AVTTYAGIIT DQVFSILSGE D