ID   APOC2_ELLLU             Reviewed;         100 AA.
AC   P0DUX6;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 1.
DT   03-AUG-2022, entry version 3.
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   Ellobius lutescens (Transcaucasian mole vole).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Arvicolinae; Ellobius.
OX   NCBI_TaxID=39086;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=27510564; DOI=10.1101/gr.201665.115;
RA   Mulugeta E., Wassenaar E., Sleddens-Linkels E., Van Ijcken W.F., Heard E.,
RA   Grootegoed J.A., Just W., Gribnau J., Baarends W.M.;
RT   "Genomes of Ellobius species provide insight into the evolutionary dynamics
RT   of mammalian sex chromosomes.";
RL   Genome Res. 26:1202-1210(2016).
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. {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; LOJG01068708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
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; HDL; LDL; Lipid degradation; Lipid metabolism;
KW   Lipid transport; Secreted; Signal; Transport; VLDL.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..100
FT                   /note="Proapolipoprotein C-II"
FT                   /id="PRO_0000453992"
FT   CHAIN           29..100
FT                   /note="Apolipoprotein C-II"
FT                   /evidence="ECO:0000250|UniProtKB:P02655"
FT                   /id="PRO_0000453993"
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;  11035 MW;  CBB2DF9C7B69E60F CRC64;
     MGSRFLLALF LVLLVLGCEV QAAQQLQQDD PGSPALLDKV QESISSYWDT AKAAAQGLYQ
     KTYLTSVDEK LRDMYSKSSA AMTTYASIFT DQIFTLLKGE