APOC3_CAVPO
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 03-AUG-2022, entry version 110.
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}.
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DR EMBL; AF030571; AAD01908.1; -; mRNA.
DR RefSeq; NP_001166386.1; NM_001172915.1.
DR RefSeq; XP_013010825.1; XM_013155371.1.
DR AlphaFoldDB; Q9Z2R5; -.
DR SMR; Q9Z2R5; -.
DR STRING; 10141.ENSCPOP00000016494; -.
DR Ensembl; ENSCPOT00000027097; ENSCPOP00000016494; ENSCPOG00000025900.
DR GeneID; 100135481; -.
DR KEGG; cpoc: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 10 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; 6.10.90.10; -; 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
