APOC2_PANTA
ID APOC2_PANTA Reviewed; 101 AA.
AC T1W425; T1W2Z5;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 2.
DT 03-AUG-2022, entry version 26.
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 Panthera tigris altaica (Siberian tiger).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Pantherinae;
OC Panthera.
OX NCBI_TaxID=74533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24045858; DOI=10.1038/ncomms3433;
RA Cho Y.S., Hu L., Hou H., Lee H., Xu J., Kwon S., Oh S., Kim H.M., Jho S.,
RA Kim S., Shin Y.A., Kim B.C., Kim H., Kim C.U., Luo S.J., Johnson W.E.,
RA Koepfli K.P., Schmidt-Kuntzel A., Turner J.A., Marker L., Harper C.,
RA Miller S.M., Jacobs W., Bertola L.D., Kim T.H., Lee S., Zhou Q., Jung H.J.,
RA Xu X., Gadhvi P., Xu P., Xiong Y., Luo Y., Pan S., Gou C., Chu X.,
RA Zhang J., Liu S., He J., Chen Y., Yang L., Yang Y., He J., Liu S., Wang J.,
RA Kim C.H., Kwak H., Kim J.S., Hwang S., Ko J., Kim C.B., Kim S.,
RA Bayarlkhagva D., Paek W.K., Kim S.J., O'Brien S.J., Wang J., Bhak J.;
RT "The tiger genome and comparative analysis with lion and snow leopard
RT genomes.";
RL Nat. Commun. 4:2433-2433(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 78-101.
RC TISSUE=Kidney, and Liver;
RA Guan W., Lu T., Liu C., Bai C., Sun Y., Sun T., Li Q., Sun B., Wang K.;
RT "The study of functional genes in the Siberian tiger liver.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION.
RA Puppione D.L.;
RL Unpublished observations (SEP-2014).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, 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AGU01719.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; ATCQ01140320; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; KF051817; AGU01719.1; ALT_FRAME; mRNA.
DR EMBL; KF028906; AGU01736.1; -; mRNA.
DR RefSeq; XP_007096583.1; XM_007096521.2.
DR AlphaFoldDB; T1W425; -.
DR SMR; T1W425; -.
DR Ensembl; ENSPTIT00000029201; ENSPTIP00000024715; ENSPTIG00000020728.
DR GeneID; 102949268; -.
DR KEGG; ptg:102949268; -.
DR CTD; 344; -.
DR GeneTree; ENSGT00390000007913; -.
DR Proteomes; UP000675900; Unassembled WGS sequence.
DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR GO; GO:0034363; C:intermediate-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0055102; F:lipase inhibitor activity; IEA:Ensembl.
DR GO; GO:0008289; F:lipid binding; IEA:Ensembl.
DR GO; GO:0060230; F:lipoprotein lipase activator activity; IEA:Ensembl.
DR GO; GO:0016004; F:phospholipase activator activity; IEA:Ensembl.
DR GO; GO:0043274; F:phospholipase binding; IEA:Ensembl.
DR GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
DR GO; GO:0034382; P:chylomicron remnant clearance; IEA:Ensembl.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032375; P:negative regulation of cholesterol transport; IEA:Ensembl.
DR GO; GO:0045833; P:negative regulation of lipid metabolic process; IEA:Ensembl.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:0033700; P:phospholipid efflux; IEA:Ensembl.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IEA:Ensembl.
DR GO; GO:0010518; P:positive regulation of phospholipase activity; IEA:Ensembl.
DR GO; GO:0060697; P:positive regulation of phospholipid catabolic process; IEA:Ensembl.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IEA:Ensembl.
DR GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
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_0000430847"
FT PROPEP 23..28
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P02655"
FT /id="PRO_0000430848"
FT CHAIN 29..101
FT /note="Apolipoprotein C-II"
FT /evidence="ECO:0000250|UniProtKB:P02655"
FT /id="PRO_0000430849"
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"
FT CONFLICT 89
FT /note="L -> F (in Ref. 2; AGU01736)"
FT CONFLICT 95
FT /note="S -> F (in Ref. 2; AGU01736)"
SQ SEQUENCE 101 AA; 11175 MW; BE1369BBCEC0BA46 CRC64;
MGTRCLLVLL LVLLVLKCEV QGDDMARQDE ATGPTLLSQM QESLYGYWGS AKAAAQDLYE
KTYLTAMDEK IRDMYSTSTA AVRIYTGILT DQILSMLTGD P
