ID APOC3_CAVPO Reviewed; 91 AA. AC Q9Z2R5; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 23-MAY-2018, entry version 95. DE RecName: Full=Apolipoprotein C-III; DE Short=Apo-CIII; DE Short=ApoC-III; DE AltName: Full=Apolipoprotein C3; DE Flags: Precursor; GN Name=APOC3; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricomorpha; Caviidae; Cavia. OX NCBI_TaxID=10141; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX PubMed=10584299; DOI=10.1016/S0305-0491(99)00097-8; RA Yin Y., Olivecrona G.; RT "Apolipoprotein CIII from guinea pig (Cavia porcellus) is shorter and RT less homologous than apolipoprotein CIII from other mammals."; RL Comp. Biochem. Physiol. 124B:157-161(1999). CC -!- FUNCTION: Component of triglyceride-rich very low density CC lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma. CC Plays a multifaceted role in triglyceride homeostasis. CC Intracellularly, promotes hepatic very low density lipoprotein 1 CC (VLDL1) assembly and secretion; extracellularly, attenuates CC hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs). CC Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and CC the hepatic uptake of TRLs by remnant receptors. Formed of several CC curved helices connected via semiflexible hinges, so that it can CC wrap tightly around the curved micelle surface and easily adapt to CC the different diameters of its natural binding partners. CC {ECO:0000250|UniProtKB:P02656}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02656}. CC -!- SIMILARITY: Belongs to the apolipoprotein C3 family. CC {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; AF030571; AAD01908.1; -; mRNA. DR RefSeq; NP_001166386.1; NM_001172915.1. DR RefSeq; XP_013010825.1; XM_013155371.1. DR ProteinModelPortal; Q9Z2R5; -. DR SMR; Q9Z2R5; -. DR STRING; 10141.ENSCPOP00000016494; -. DR PRIDE; Q9Z2R5; -. DR Ensembl; ENSCPOT00000027097; ENSCPOP00000016494; ENSCPOG00000025900. DR GeneID; 100135481; -. DR CTD; 345; -. DR eggNOG; ENOG410JE3N; Eukaryota. DR eggNOG; ENOG4111APE; LUCA. DR GeneTree; ENSGT00390000015395; -. DR HOGENOM; HOG000247042; -. DR HOVERGEN; HBG050549; -. DR InParanoid; Q9Z2R5; -. DR OMA; SLKDYWS; -. DR OrthoDB; EOG091G15XY; -. DR TreeFam; TF338209; -. DR Proteomes; UP000005447; Unassembled WGS sequence. DR Bgee; ENSCPOG00000025900; -. DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW. DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW. DR GO; GO:0008289; F:lipid binding; IEA:InterPro. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW. DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro. DR Gene3D; 1.10.225.30; -; 1. DR InterPro; IPR008403; Apo-CIII. DR InterPro; IPR038195; Apo_CIII_sf. DR PANTHER; PTHR14225; PTHR14225; 1. DR Pfam; PF05778; Apo-CIII; 1. DR ProDom; PD010414; Apo-CIII; 1. PE 3: Inferred from homology; KW Chylomicron; Complete proteome; Lipid degradation; Lipid metabolism; KW Lipid transport; Oxidation; Reference proteome; Secreted; Signal; KW Transport; VLDL. FT SIGNAL 1 20 {ECO:0000250}. FT CHAIN 21 91 Apolipoprotein C-III. FT /FTId=PRO_0000002030. FT REGION 68 91 Lipid-binding. {ECO:0000250}. FT SITE 41 41 May interact with the LDL receptor. FT {ECO:0000250|UniProtKB:P02656}. FT MOD_RES 63 63 Methionine sulfoxide. FT {ECO:0000250|UniProtKB:P33622}. SQ SEQUENCE 91 AA; 10099 MW; 849C2BBD4783E8FF CRC64; MQPRVLLAVT LLALLVSARA EEIQESSLLG VMKDYMQQAS KTANEMLTKV QESQVAENAR EWMTESLDSM KGYWTSLIGR LSGFLDSTPS S //