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 07-OCT-2020, entry version 106. 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; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae; OC 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 less RT homologous than apolipoprotein CIII from other mammals."; RL Comp. Biochem. Physiol. 124B:157-161(1999). CC -!- FUNCTION: Component of triglyceride-rich very low density lipoproteins CC (VLDL) and high density lipoproteins (HDL) in plasma. Plays a CC multifaceted role in triglyceride homeostasis. Intracellularly, CC promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and CC secretion; extracellularly, attenuates hydrolysis and clearance of CC triglyceride-rich lipoproteins (TRLs). Impairs the lipolysis of TRLs by CC inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant CC receptors. Formed of several curved helices connected via semiflexible CC hinges, so that it can wrap tightly around the curved micelle surface CC and easily adapt to the different diameters of its natural binding CC partners. {ECO:0000250|UniProtKB:P02656}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02656}. CC -!- SIMILARITY: Belongs to the apolipoprotein C3 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; AF030571; AAD01908.1; -; mRNA. DR RefSeq; NP_001166386.1; NM_001172915.1. DR RefSeq; XP_013010825.1; XM_013155371.1. DR SMR; Q9Z2R5; -. DR STRING; 10141.ENSCPOP00000016494; -. DR Ensembl; ENSCPOT00000027097; ENSCPOP00000016494; ENSCPOG00000025900. DR GeneID; 100135481; -. DR CTD; 345; -. DR GeneTree; ENSGT00390000015395; -. DR HOGENOM; CLU_154694_0_0_1; -. DR InParanoid; Q9Z2R5; -. DR OMA; YWSTFKG; -. DR OrthoDB; 1613530at2759; -. DR TreeFam; TF338209; -. DR Proteomes; UP000005447; Unassembled WGS sequence. DR Bgee; ENSCPOG00000025900; Expressed in liver and 3 other tissues. 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. PE 3: Inferred from homology; KW Chylomicron; Lipid degradation; Lipid metabolism; Lipid transport; KW Oxidation; Reference proteome; Secreted; Signal; Transport; VLDL. FT SIGNAL 1..20 FT /evidence="ECO:0000250" FT CHAIN 21..91 FT /note="Apolipoprotein C-III" FT /id="PRO_0000002030" FT REGION 68..91 FT /note="Lipid-binding" FT /evidence="ECO:0000250" FT SITE 41 FT /note="May interact with the LDL receptor" FT /evidence="ECO:0000250|UniProtKB:P02656" FT MOD_RES 63 FT /note="Methionine sulfoxide" FT /evidence="ECO:0000250|UniProtKB:P33622" SQ SEQUENCE 91 AA; 10099 MW; 849C2BBD4783E8FF CRC64; MQPRVLLAVT LLALLVSARA EEIQESSLLG VMKDYMQQAS KTANEMLTKV QESQVAENAR EWMTESLDSM KGYWTSLIGR LSGFLDSTPS S //