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 27-MAR-2024, entry version 234. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 44. DR IntAct; P02655; 7. DR MINT; P02655; -. DR STRING; 9606.ENSP00000466775; -. DR DrugBank; DB09130; Copper. DR DrugBank; DB11886; Infigratinib. DR DrugBank; DB00877; Sirolimus. DR GlyCosmos; P02655; 3 sites, 2 glycans. DR GlyGen; P02655; 4 sites, 4 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 CPTAC; non-CPTAC-1084; -. DR CPTAC; non-CPTAC-2625; -. DR EPD; P02655; -. DR jPOST; P02655; -. DR MassIVE; P02655; -. DR MaxQB; P02655; -. DR PaxDb; 9606-ENSP00000252490; -. DR PeptideAtlas; P02655; -. DR ProteomicsDB; 51540; -. DR Pumba; P02655; -. DR TopDownProteomics; P02655; -. DR Antibodypedia; 31235; 176 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 AGR; HGNC:609; -. 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; GTHEPQE; -. DR OrthoDB; 4640492at2759; -. 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 1055 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 97 other cell types or tissues. DR ExpressionAtlas; P02655; baseline and differential. 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: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:0140677; F:molecular function activator activity; EXP:DisProt. 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; Apolipoprotein C-II; 1. DR InterPro; IPR008019; Apo-CII. DR InterPro; IPR023121; ApoC-II_dom_sf. DR PANTHER; PTHR16566; APOLIPOPROTEIN C-II; 1. DR PANTHER; PTHR16566:SF0; APOLIPOPROTEIN C-II; 1. DR Pfam; PF05355; Apo-CII; 1. DR SWISS-2DPAGE; P02655; -. DR Genevisible; P02655; HS. 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 //