APOC2_HUMAN
ID APOC2_HUMAN Reviewed; 101 AA.
AC P02655; C0JYY4; Q9BS39; Q9UDE3; Q9UNK3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 225.
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; Synonyms=APC2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3030808; DOI=10.1016/0014-5793(87)81495-3;
RA Fojo S.S., Law S.W., Brewer H.B. Jr.;
RT "The human preproapolipoprotein C-II gene. Complete nucleic acid sequence
RT and genomic organization.";
RL FEBS Lett. 213:221-226(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=6593704; DOI=10.1073/pnas.81.20.6354;
RA Fojo S.S., Law S.W., Brewer H.B. Jr.;
RT "Human apolipoprotein C-II: complete nucleic acid sequence of
RT preapolipoprotein C-II.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:6354-6357(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6328445; DOI=10.1093/nar/12.9.3917;
RA Sharpe C.R., Sidoli A., Shelley C.S., Lucero M.A., Shoulders C.C.,
RA Baralle F.E.;
RT "Human apolipoproteins AI, AII, CII and CIII. cDNA sequences and mRNA
RT abundance.";
RL Nucleic Acids Res. 12:3917-3932(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3558370; DOI=10.1016/s0021-9258(18)61264-5;
RA Das H.K., Jackson C.L., Miller D.A., Leff T., Breslow J.L.;
RT "The human apolipoprotein C-II gene sequence contains a novel chromosome
RT 19-specific minisatellite in its third intron.";
RL J. Biol. Chem. 262:4787-4793(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=2415514; DOI=10.1016/s0021-9258(18)95724-8;
RA Wei C.F., Tsao Y.K., Robberson D.L., Gotto A.M. Jr., Brown K., Chan L.;
RT "The structure of the human apolipoprotein C-II gene. Electron microscopic
RT analysis of RNA:DNA hybrids, complete nucleotide sequence, and
RT identification of 5' homologous sequences among apolipoprotein genes.";
RL J. Biol. Chem. 260:15211-15221(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nickerson D.A., Smith J.D., Fullerton S.M., Clark A.G., Stengard J.H.,
RA Salomaa V., Boerwinkle E., Sing C.F., Weiss K.M.;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-101, AND TISSUE SPECIFICITY.
RX PubMed=6546757; DOI=10.1016/s0021-9258(17)43060-2;
RA Myklebost O., Williamson B., Markham A.F., Myklebost S.R., Rogers J.,
RA Woods D.E., Humphries S.E.;
RT "The isolation and characterization of cDNA clones for human apolipoprotein
RT CII.";
RL J. Biol. Chem. 259:4401-4404(1984).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 11-101.
RX PubMed=3014272; DOI=10.1016/0076-6879(86)28106-9;
RA Jackson C.L., Bruns G.A.P., Breslow J.L.;
RT "Isolation of cDNA and genomic clones for apolipoprotein C-II.";
RL Methods Enzymol. 128:788-800(1986).
RN [13]
RP PROTEIN SEQUENCE OF 23-101.
RX PubMed=6706938; DOI=10.1016/s0021-9258(17)43660-x;
RA Hospattankar A.V., Fairwell T., Ronan R., Brewer H.B. Jr.;
RT "Amino acid sequence of human plasma apolipoprotein C-II from normal and
RT hyperlipoproteinemic subjects.";
RL J. Biol. Chem. 259:318-322(1984).
RN [14]
RP PROTEIN SEQUENCE OF 23-101.
RX PubMed=194244; DOI=10.1073/pnas.74.5.1942;
RA Jackson R.L., Baker H.N., Gilliam E.B., Gotto A.M. Jr.;
RT "Primary structure of very low density apolipoprotein C-II of human
RT plasma.";
RL Proc. Natl. Acad. Sci. U.S.A. 74:1942-1945(1977).
RN [15]
RP PROTEIN SEQUENCE OF 29-35, PROTEOLYTIC PROCESSING, GLYCOSYLATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=3525527; DOI=10.1016/s0021-9258(18)67554-4;
RA Fojo S.S., Taam L., Fairwell T., Ronan R., Bishop C., Meng M.S., Hoeg J.M.,
RA Sprecher D.L., Brewer H.B. Jr.;
RT "Human preproapolipoprotein C-II. Analysis of major plasma isoforms.";
RL J. Biol. Chem. 261:9591-9594(1986).
RN [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 77-101.
RX PubMed=11310852;
RA Chun E.M., Park Y.J., Kang H.S., Cho H.M., Jun D.Y., Kim Y.H.;
RT "Expression of the apolipoprotein C-II gene during myelomonocytic
RT differentiation of human leukemic cells.";
RL J. Leukoc. Biol. 69:645-650(2001).
RN [17]
RP REGION LIPOPROTEIN LIPASE COFACTOR AND REGION LIPID BINDING.
RX PubMed=6772077; DOI=10.1111/j.1749-6632.1980.tb21300.x;
RA Sparrow J.T., Gotto A.M. Jr.;
RT "Phospholipid binding studies with synthetic apolipoprotein fragments.";
RL Ann. N. Y. Acad. Sci. 348:187-211(1980).
RN [18]
RP FUNCTION.
RX PubMed=2209608; DOI=10.1111/j.1432-1033.1990.tb19255.x;
RA Bengtsson-Olivecrona G., Sletten K.;
RT "Primary structure of the bovine analogues to human apolipoproteins CII and
RT CIII. Studies on isoforms and evidence for proteolytic processing.";
RL Eur. J. Biochem. 192:515-521(1990).
RN [19]
RP REVIEW.
RX PubMed=22304839; DOI=10.1016/j.metabol.2011.12.002;
RA Kei A.A., Filippatos T.D., Tsimihodimos V., Elisaf M.S.;
RT "A review of the role of apolipoprotein C-II in lipoprotein metabolism and
RT cardiovascular disease.";
RL Metabolism 61:906-921(2012).
RN [20]
RP GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP STRUCTURE BY NMR OF 72-101, AND REGION LIPOPROTEIN LIPASE COFACTOR.
RX PubMed=1555583; DOI=10.1111/j.1432-1033.1992.tb16772.x;
RA Lycksell P.-O., Oehman A., Bengtsson-Olivecrona G., Johansson L.B.-A.,
RA Wijmenga S.S., Wernic D., Graeslund A.;
RT "Sequence specific 1H-NMR assignments and secondary structure of a carboxy-
RT terminal functional fragment of apolipoprotein CII.";
RL Eur. J. Biochem. 205:223-231(1992).
RN [23]
RP STRUCTURE BY NMR OF 72-101.
RX PubMed=8112221; DOI=10.1007/bf00213558;
RA Oehman A., Lycksell P.-O., Graeslund A.;
RT "A refined three-dimensional solution structure of a carboxy terminal
RT fragment of apolipoprotein CII.";
RL Eur. Biophys. J. 22:351-357(1993).
RN [24]
RP VARIANT AFRICA GLN-77.
RX PubMed=3944271; DOI=10.1172/jci112342;
RA Menzel H.-J., Kane J.P., Malloy M.J., Havel R.J.;
RT "A variant primary structure of apolipoprotein C-II in individuals of
RT African descent.";
RL J. Clin. Invest. 77:595-601(1986).
RN [25]
RP VARIANT SAN FRANCISCO LYS-60.
RX PubMed=8490626; DOI=10.1093/hmg/2.1.69;
RA Pullinger C.R., Zysow B.R., Hennessy L.K., Frost P.H., Malloy M.J.,
RA Kanr J.P.;
RT "Molecular cloning and characteristics of a new apolipoprotein C-II mutant
RT identified in three unrelated individuals with hypercholesterolemia and
RT hypertriglyceridemia.";
RL Hum. Mol. Genet. 2:69-74(1993).
RN [26]
RP VARIANT THR-41.
RX PubMed=1782747;
RA Hegele R.A., Connelly P.W., Maguire G.F., Huff M.W., Leiter L., Wolfe B.M.,
RA Evans A.J., Little J.A.;
RT "An apolipoprotein CII mutation, CII Lys-19-->Thr identified in patients
RT with hyperlipidemia.";
RL Dis. Markers 9:73-80(1991).
RN [27]
RP VARIANT THR-41.
RX PubMed=7923858; DOI=10.1111/j.1399-0004.1994.tb04033.x;
RA Zysow B.R., Pullinger C.R., Hennessy L.K., Farese R.V. Jr.,
RA Ghassemzadeh M., Kane J.P.;
RT "The apolipoprotein C-II variant apoC-II Lys-19-->Thr is not associated
RT with dyslipidemia in an affected kindred.";
RL Clin. Genet. 45:292-297(1994).
RN [28]
RP VARIANT HLPP1B WAKAYAMA ARG-48.
RX PubMed=8323539; DOI=10.1006/bbrc.1993.1749;
RA Inadera H., Hibino A., Kobayashi J., Kanzaki T., Shirai K., Yukawa S.,
RA Saito Y., Yoshida S.;
RT "A missense mutation (Trp 26-->Arg) in exon 3 of the apolipoprotein CII
RT gene in a patient with apolipoprotein CII deficiency (apo CII-Wakayama).";
RL Biochem. Biophys. Res. Commun. 193:1174-1183(1993).
RN [29]
RP VARIANT GLN-77.
RX PubMed=10391210; DOI=10.1038/10297;
RA Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A.,
RA Cooper R., Lipshutz R., Chakravarti A.;
RT "Patterns of single-nucleotide polymorphisms in candidate genes for blood-
RT pressure homeostasis.";
RL Nat. Genet. 22:239-247(1999).
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. In normolipidemic
CC individuals, it is mainly distributed in the HDL, whereas in
CC hypertriglyceridemic individuals, predominantly found in the VLDL and
CC LDL. {ECO:0000269|PubMed:2209608, ECO:0000303|PubMed:22304839}.
CC -!- INTERACTION:
CC P02655; P49638: TTPA; NbExp=3; IntAct=EBI-1223594, EBI-10210710;
CC PRO_0000002024; PRO_0000002024 [P02655]: APOC2; NbExp=16; IntAct=EBI-25338752, EBI-25338752;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3525527}.
CC -!- TISSUE SPECIFICITY: Liver and intestine. {ECO:0000269|PubMed:6546757}.
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:0000269|PubMed:3525527}.
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:0000269|PubMed:3525527}.
CC -!- DISEASE: Hyperlipoproteinemia 1B (HLPP1B) [MIM:207750]: Autosomal
CC recessive trait characterized by hypertriglyceridemia, xanthomas, and
CC increased risk of pancreatitis and early atherosclerosis.
CC {ECO:0000269|PubMed:8323539}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the apolipoprotein C2 family. {ECO:0000305}.
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DR EMBL; X05151; CAA28798.1; -; Genomic_DNA.
DR EMBL; X00568; CAA25234.1; -; mRNA.
DR EMBL; J02698; AAA98743.1; -; Genomic_DNA.
DR EMBL; AY422955; AAQ91814.1; -; Genomic_DNA.
DR EMBL; BT006708; AAP35354.1; -; mRNA.
DR EMBL; FJ525875; ACN81313.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57311.1; -; Genomic_DNA.
DR EMBL; BC005348; AAH05348.3; -; mRNA.
DR EMBL; M29844; AAA51743.1; -; mRNA.
DR EMBL; M10612; AAB59380.1; -; Genomic_DNA.
DR EMBL; AF113884; AAD28193.1; -; mRNA.
DR CCDS; CCDS12650.1; -.
DR PIR; A24238; LPHUC2.
DR RefSeq; NP_000474.2; NM_000483.4.
DR PDB; 1BY6; NMR; -; A=66-101.
DR PDB; 1I5J; NMR; -; A=23-101.
DR PDB; 1O8T; NMR; -; A=23-101.
DR PDB; 1SOH; NMR; -; A=23-101.
DR PDBsum; 1BY6; -.
DR PDBsum; 1I5J; -.
DR PDBsum; 1O8T; -.
DR PDBsum; 1SOH; -.
DR AlphaFoldDB; P02655; -.
DR BMRB; P02655; -.
DR SMR; P02655; -.
DR BioGRID; 106841; 43.
DR IntAct; P02655; 6.
DR MINT; P02655; -.
DR STRING; 9606.ENSP00000466775; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB11886; Infigratinib.
DR DrugBank; DB00877; Sirolimus.
DR GlyGen; P02655; 4 sites, 3 O-linked glycans (4 sites).
DR iPTMnet; P02655; -.
DR MetOSite; P02655; -.
DR PhosphoSitePlus; P02655; -.
DR BioMuta; APOC2; -.
DR DMDM; 114022; -.
DR DOSAC-COBS-2DPAGE; P02655; -.
DR SWISS-2DPAGE; P02655; -.
DR CPTAC; non-CPTAC-1084; -.
DR CPTAC; non-CPTAC-2625; -.
DR EPD; P02655; -.
DR jPOST; P02655; -.
DR MassIVE; P02655; -.
DR MaxQB; P02655; -.
DR PaxDb; P02655; -.
DR PeptideAtlas; P02655; -.
DR PRIDE; P02655; -.
DR ProteomicsDB; 51540; -.
DR TopDownProteomics; P02655; -.
DR Antibodypedia; 31235; 148 antibodies from 22 providers.
DR DNASU; 344; -.
DR Ensembl; ENST00000252490.7; ENSP00000252490.5; ENSG00000234906.11.
DR Ensembl; ENST00000590360.2; ENSP00000466775.1; ENSG00000234906.11.
DR GeneID; 344; -.
DR KEGG; hsa:344; -.
DR MANE-Select; ENST00000252490.7; ENSP00000252490.5; NM_000483.5; NP_000474.2.
DR UCSC; uc060zuu.1; human.
DR CTD; 344; -.
DR DisGeNET; 344; -.
DR GeneCards; APOC2; -.
DR HGNC; HGNC:609; APOC2.
DR HPA; ENSG00000234906; Tissue enriched (liver).
DR MalaCards; APOC2; -.
DR MIM; 207750; phenotype.
DR MIM; 608083; gene.
DR neXtProt; NX_P02655; -.
DR OpenTargets; ENSG00000234906; -.
DR Orphanet; 309020; Familial apolipoprotein C-II deficiency.
DR PharmGKB; PA52; -.
DR VEuPathDB; HostDB:ENSG00000234906; -.
DR eggNOG; ENOG502SEJB; Eukaryota.
DR GeneTree; ENSGT00390000007913; -.
DR HOGENOM; CLU_180154_0_0_1; -.
DR InParanoid; P02655; -.
DR OMA; EVQGAHL; -.
DR OrthoDB; 1548460at2759; -.
DR PhylomeDB; P02655; -.
DR PathwayCommons; P02655; -.
DR Reactome; R-HSA-8963888; Chylomicron assembly.
DR Reactome; R-HSA-8963889; Assembly of active LPL and LIPC lipase complexes.
DR Reactome; R-HSA-8963901; Chylomicron remodeling.
DR Reactome; R-HSA-8964058; HDL remodeling.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SignaLink; P02655; -.
DR SIGNOR; P02655; -.
DR BioGRID-ORCS; 344; 11 hits in 996 CRISPR screens.
DR EvolutionaryTrace; P02655; -.
DR GeneWiki; Apolipoprotein_C2; -.
DR GenomeRNAi; 344; -.
DR Pharos; P02655; Tbio.
DR PRO; PR:P02655; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P02655; protein.
DR Bgee; ENSG00000234906; Expressed in right lobe of liver and 95 other tissues.
DR ExpressionAtlas; P02655; baseline and differential.
DR Genevisible; P02655; HS.
DR GO; GO:0042627; C:chylomicron; IDA:BHF-UCL.
DR GO; GO:0005769; C:early endosome; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0034363; C:intermediate-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0034362; C:low-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0055102; F:lipase inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0008289; F:lipid binding; IDA:BHF-UCL.
DR GO; GO:0060230; F:lipoprotein lipase activator activity; IDA:BHF-UCL.
DR GO; GO:0016004; F:phospholipase activator activity; IDA:BHF-UCL.
DR GO; GO:0043274; F:phospholipase binding; IPI:BHF-UCL.
DR GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL.
DR GO; GO:0042632; P:cholesterol homeostasis; IC:BHF-UCL.
DR GO; GO:0034382; P:chylomicron remnant clearance; IDA:BHF-UCL.
DR GO; GO:0034371; P:chylomicron remodeling; IC:BHF-UCL.
DR GO; GO:0034384; P:high-density lipoprotein particle clearance; IMP:BHF-UCL.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032375; P:negative regulation of cholesterol transport; IMP:BHF-UCL.
DR GO; GO:0045833; P:negative regulation of lipid metabolic process; IDA:BHF-UCL.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IDA:BHF-UCL.
DR GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; IDA:BHF-UCL.
DR GO; GO:0033700; P:phospholipid efflux; IDA:BHF-UCL.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IDA:BHF-UCL.
DR GO; GO:0010518; P:positive regulation of phospholipase activity; IDA:BHF-UCL.
DR GO; GO:0060697; P:positive regulation of phospholipid catabolic process; IDA:BHF-UCL.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:BHF-UCL.
DR GO; GO:0010902; P:positive regulation of very-low-density lipoprotein particle remodeling; IC:BHF-UCL.
DR GO; GO:0043691; P:reverse cholesterol transport; IC:BHF-UCL.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:BHF-UCL.
DR GO; GO:0034370; P:triglyceride-rich lipoprotein particle remodeling; TAS:BHF-UCL.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; TAS:BHF-UCL.
DR DisProt; DP01883; -.
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 3D-structure; Chylomicron; Direct protein sequencing; Disease variant;
KW Glycoprotein; HDL; Hyperlipidemia; LDL; Lipid degradation;
KW Lipid metabolism; Lipid transport; Reference proteome; Secreted;
KW Sialic acid; Signal; Transport; VLDL.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:194244,
FT ECO:0000269|PubMed:6706938"
FT CHAIN 23..101
FT /note="Proapolipoprotein C-II"
FT /evidence="ECO:0000269|PubMed:194244,
FT ECO:0000269|PubMed:6706938"
FT /id="PRO_0000002024"
FT CHAIN 29..101
FT /note="Apolipoprotein C-II"
FT /evidence="ECO:0000305|PubMed:3525527"
FT /id="PRO_0000430839"
FT REGION 23..38
FT /note="O-glycosylated at one site"
FT REGION 66..74
FT /note="Lipid binding"
FT /evidence="ECO:0000269|PubMed:6772077"
FT REGION 78..101
FT /note="Lipoprotein lipase cofactor"
FT /evidence="ECO:0000269|PubMed:1555583,
FT ECO:0000269|PubMed:6772077"
FT VARIANT 41
FT /note="K -> T (in dbSNP:rs120074114)"
FT /evidence="ECO:0000269|PubMed:1782747,
FT ECO:0000269|PubMed:7923858"
FT /id="VAR_000639"
FT VARIANT 48
FT /note="W -> R (in HLPP1B; variant Wakayama;
FT dbSNP:rs120074115)"
FT /evidence="ECO:0000269|PubMed:8323539"
FT /id="VAR_000640"
FT VARIANT 60
FT /note="E -> K (in San Francisco; found in hyperlipidemic
FT patients; dbSNP:rs5122)"
FT /evidence="ECO:0000269|PubMed:8490626"
FT /id="VAR_000641"
FT VARIANT 77
FT /note="K -> Q (in Africa; dbSNP:rs5126)"
FT /evidence="ECO:0000269|PubMed:10391210,
FT ECO:0000269|PubMed:3944271"
FT /id="VAR_000642"
FT CONFLICT 36
FT /note="F -> L (in Ref. 7; AAP35354 and 8; ACN81313)"
FT /evidence="ECO:0000305"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1O8T"
FT HELIX 37..57
FT /evidence="ECO:0007829|PDB:1I5J"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:1I5J"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1I5J"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:1SOH"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1I5J"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:1BY6"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1BY6"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1BY6"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1BY6"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1BY6"
SQ SEQUENCE 101 AA; 11284 MW; 51CB86FEDB174D84 CRC64;
MGTRLLPALF LVLLVLGFEV QGTQQPQQDE MPSPTFLTQV KESLSSYWES AKTAAQNLYE
KTYLPAVDEK LRDLYSKSTA AMSTYTGIFT DQVLSVLKGE E
