APOC2_LEPWE
ID APOC2_LEPWE Reviewed; 101 AA.
AC A0A2U3Y4D7;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 1.
DT 25-MAY-2022, entry version 10.
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 Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Phocidae; Leptonychotes.
OX NCBI_TaxID=9713;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION.
RA Puppione D.L.;
RL Unpublished observations (SEP-2019).
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; APMU01085777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006738588.1; XM_006738525.1.
DR RefSeq; XP_006738589.1; XM_006738526.1.
DR AlphaFoldDB; A0A2U3Y4D7; -.
DR SMR; A0A2U3Y4D7; -.
DR STRING; 9713.XP_006738588.1; -.
DR GeneID; 102732291; -.
DR CTD; 344; -.
DR Proteomes; UP000245341; 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; Lipoprotein; Reference proteome; Secreted; Sialic acid;
KW Signal; Transport; VLDL.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..101
FT /note="Proapolipoprotein C-II"
FT /id="PRO_5015818369"
FT CHAIN 29..101
FT /note="Apolipoprotein C-II"
FT /evidence="ECO:0000250|UniProtKB:P02655"
FT /id="PRO_0000448499"
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; 11285 MW; A8FDEB51AC95B280 CRC64;
MGIRYLLVLV LVLLVLGCEV QGAHMPQQDE ATTSSLFTQM QESFYGYWGI AKSAAQGLYE
KTYLTTMDEK IREIYNKSTA AVSTYAGIFT DQLLSMLKGD Q