APOC2_MACFA
ID APOC2_MACFA Reviewed; 101 AA.
AC P18658;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 105.
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 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2481808; DOI=10.1007/bf00225222;
RA Whitted B.E., Castle C.K., Polites H.G., Melchior G.W., Marotti K.R.;
RT "Purification, cloning and nucleotide sequence determination of cynomolgus
RT monkey apolipoprotein C-II: comparison to the human sequence.";
RL Mol. Cell. Biochem. 90:69-79(1989).
RN [2]
RP PROTEIN SEQUENCE OF 23-49.
RX PubMed=3105581; DOI=10.1021/bi00379a037;
RA Herbert P.N., Bausserman L.L., Lynch K.M., Saritelli A.L., Kantor M.A.,
RA Nicolosi R.J., Shulman R.S.;
RT "Homologues of the human C and A apolipoproteins in the Macaca fascicularis
RT (cynomolgus) monkey.";
RL Biochemistry 26:1457-1463(1987).
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; M86345; AAA36835.1; -; mRNA.
DR PIR; E26627; E26627.
DR PIR; I57492; I57492.
DR RefSeq; NP_001271640.1; NM_001284711.1.
DR RefSeq; XP_015300138.1; XM_015444652.1.
DR AlphaFoldDB; P18658; -.
DR SMR; P18658; -.
DR STRING; 9541.XP_005595586.1; -.
DR Ensembl; ENSMFAT00000058527; ENSMFAP00000012478; ENSMFAG00000024498.
DR GeneID; 102116264; -.
DR KEGG; mcf:102116264; -.
DR CTD; 344; -.
DR VEuPathDB; HostDB:ENSMFAG00000024498; -.
DR eggNOG; ENOG502SEJB; Eukaryota.
DR GeneTree; ENSGT00390000007913; -.
DR OMA; EVQGAHL; -.
DR OrthoDB; 1548460at2759; -.
DR Proteomes; UP000233100; Chromosome 19.
DR Bgee; ENSMFAG00000024498; Expressed in liver and 3 other tissues.
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 1: Evidence at protein level;
KW Chylomicron; Direct protein sequencing; Glycoprotein; HDL; LDL;
KW Lipid degradation; Lipid metabolism; Lipid transport; Reference proteome;
KW Secreted; Sialic acid; Signal; Transport; VLDL.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:3105581"
FT CHAIN 23..101
FT /note="Proapolipoprotein C-II"
FT /id="PRO_0000002025"
FT CHAIN 29..101
FT /note="Apolipoprotein C-II"
FT /evidence="ECO:0000250|UniProtKB:P02655"
FT /id="PRO_0000430840"
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 25
FT /note="L -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="R -> Q (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 101 AA; 11145 MW; F599316E5073F628 CRC64;
MGTRFLLALC LVLLVLGFEV QGAQLPQQDE PPSPALLSRV QESLSSYWES AKAAAQKLYE
KTYLPAVDEK LRDLYSKSTA AMSTYTGIFT DQVLSVLKGE E
