ID   APOC2_ACIJB             Reviewed;         101 AA.
AC   P0DP52;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 1.
DT   03-AUG-2022, entry version 11.
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   Acinonyx jubatus (Cheetah).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Acinonychinae;
OC   Acinonyx.
OX   NCBI_TaxID=32536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dobrynin P., Liu S., Tamazian G., Xiong Z., Yurchenko A.,
RA   Krasheninnikova K., Kliver S., Koepfli K.-P., Johnson W., Kuderna L.,
RA   Garcia-Perez R., Montero M.D.M., Godinez R., Makunin A., Komissarov A.,
RA   Brukhin V., Qiu W., Zhou L., Li F., Yi J., Driscoll C., Antunes A.,
RA   Oleksyk T.K., Eizirik E., Perelman P., Roelke' M., Wildt D., Diekhans M.,
RA   Marques-Bonet T., Schmidt-Kuntzel A., Marker L., Bhak J., Wang J.,
RA   Zhang G., Obrien S.;
RT   "Genomic legacy of the African cheetah, Acinonyx jubatus.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (APR-2017).
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, the enzyme which hydrolyzes the
CC       triacylglycerols on chylomicrons and VLDL.
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 the
CC       mature form apolipoprotein C-II, which occurs as the minor form in
CC       plasma. {ECO:0000250|UniProtKB:P02655}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein C2 family. {ECO:0000305}.
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DR   EMBL; LLWD01000328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P0DP52; -.
DR   SMR; P0DP52; -.
DR   PRIDE; P0DP52; -.
DR   Proteomes; UP000504626; Unplaced.
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..101
FT                   /note="Proapolipoprotein C-II"
FT                   /id="PRO_0000440147"
FT   PROPEP          23..28
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250|UniProtKB:P02655"
FT                   /id="PRO_0000440148"
FT   CHAIN           29..101
FT                   /note="Apolipoprotein C-II"
FT                   /evidence="ECO:0000250|UniProtKB:P02655"
FT                   /id="PRO_0000440149"
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;  11163 MW;  50DBE06536442714 CRC64;
     MGTRCLLVLL LVLLVLRCDV QGDDMARQDE ATGPTLLSQM QESLYSYWGS AKAAAQDLYE
     KTYLTAVDEK IRDMYSTSTA AVRIYTGILT DQILSMLSGD S