ID A0A7E6CSA1_9CHIR Unreviewed; 110 AA. AC A0A7E6CSA1; DT 10-FEB-2021, integrated into UniProtKB/TrEMBL. DT 10-FEB-2021, sequence version 1. DT 24-JUL-2024, entry version 18. DE RecName: Full=Apolipoprotein C-II {ECO:0000256|ARBA:ARBA00013947, ECO:0000256|RuleBase:RU368054}; DE Short=Apo-CII {ECO:0000256|RuleBase:RU368054}; DE Short=ApoC-II {ECO:0000256|RuleBase:RU368054}; DE AltName: Full=Apolipoprotein C2 {ECO:0000256|ARBA:ARBA00031176, ECO:0000256|RuleBase:RU368054}; GN Name=APOC2 {ECO:0000313|RefSeq:XP_035868984.1, GN ECO:0000313|RefSeq:XP_035868985.1}; GN ORFNames=HJG60_000833 {ECO:0000313|EMBL:KAF6076584.1}; OS Phyllostomus discolor (pale spear-nosed bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Phyllostomidae; OC Phyllostominae; Phyllostomus. OX NCBI_TaxID=89673 {ECO:0000313|Proteomes:UP000504628, ECO:0000313|RefSeq:XP_035868984.1}; RN [1] {ECO:0000313|EMBL:KAF6076584.1, ECO:0000313|Proteomes:UP000664940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bat1K_MPI-CBG_1 {ECO:0000313|EMBL:KAF6076584.1}; RX PubMed=32699395; RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P., RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L., RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M., RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N., RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M., RA Vernes S.C., Myers E.W., Teeling E.C.; RT "Six reference-quality genomes reveal evolution of bat adaptations."; RL Nature 583:578-584(2020). RN [2] {ECO:0000313|RefSeq:XP_035868984.1, ECO:0000313|RefSeq:XP_035868985.1} RP IDENTIFICATION. RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_035868984.1, RC ECO:0000313|RefSeq:XP_035868985.1}; RG RefSeq; RL Submitted (APR-2024) to UniProtKB. 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. {ECO:0000256|RuleBase:RU368054}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613, CC ECO:0000256|RuleBase:RU368054}. CC -!- SIMILARITY: Belongs to the apolipoprotein C2 family. CC {ECO:0000256|ARBA:ARBA00007221, ECO:0000256|RuleBase:RU368054}. 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; JABVXQ010000014; KAF6076584.1; -; Genomic_DNA. DR RefSeq; XP_035868984.1; XM_036013091.1. DR RefSeq; XP_035868985.1; XM_036013092.1. DR OrthoDB; 4640492at2759; -. DR Proteomes; UP000504628; Chromosome 12. DR Proteomes; UP000664940; Unassembled WGS sequence. DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-UniRule. DR GO; GO:0034363; C:intermediate-density lipoprotein particle; IEA:TreeGrafter. DR GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-UniRule. DR GO; GO:0034366; C:spherical high-density lipoprotein particle; IEA:TreeGrafter. DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-UniRule. DR GO; GO:0008289; F:lipid binding; IEA:TreeGrafter. DR GO; GO:0060230; F:lipoprotein lipase activator activity; IEA:TreeGrafter. DR GO; GO:0016004; F:phospholipase activator activity; IEA:TreeGrafter. DR GO; GO:0043274; F:phospholipase binding; IEA:TreeGrafter. DR GO; GO:0034382; P:chylomicron remnant clearance; IEA:TreeGrafter. DR GO; GO:0034384; P:high-density lipoprotein particle clearance; IEA:TreeGrafter. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-UniRule. DR GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; IEA:TreeGrafter. DR GO; GO:0060697; P:positive regulation of phospholipid catabolic process; IEA:TreeGrafter. 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. PE 3: Inferred from homology; KW Chylomicron {ECO:0000256|ARBA:ARBA00022513, ECO:0000256|RuleBase:RU368054}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00022981}; KW HDL {ECO:0000256|ARBA:ARBA00022850, ECO:0000256|RuleBase:RU368054}; KW LDL {ECO:0000256|ARBA:ARBA00022710, ECO:0000256|RuleBase:RU368054}; KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963, KW ECO:0000256|RuleBase:RU368054}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, KW ECO:0000256|RuleBase:RU368054}; KW Lipid transport {ECO:0000256|ARBA:ARBA00023055, KW ECO:0000256|RuleBase:RU368054}; KW Lipoprotein {ECO:0000313|EMBL:KAF6076584.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000504628}; KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU368054}; KW Sialic acid {ECO:0000256|ARBA:ARBA00022981}; KW Signal {ECO:0000256|RuleBase:RU368054, ECO:0000256|SAM:SignalP}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368054}; KW VLDL {ECO:0000256|ARBA:ARBA00023313, ECO:0000256|RuleBase:RU368054}. FT SIGNAL 1..22 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 23..110 FT /note="Apolipoprotein C-II" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5041832422" FT REGION 80..110 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 80..100 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 110 AA; 12376 MW; 1852753F23D25165 CRC64; MGTRYFLALF LILLVLGFEV QGVPLTQEDE TSSPSLFSQM QESLYSYWDT AKTTAQDLYK KTYLPSVDES IRSFLFWRET SNDGTPRTGE EIVQSPATLS LPTTPPLPTS //