APOC3_PANTA
ID APOC3_PANTA Reviewed; 100 AA.
AC P0DMP9;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 26.
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 Panthera tigris altaica (Siberian tiger).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Pantherinae;
OC Panthera.
OX NCBI_TaxID=74533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24045858; DOI=10.1038/ncomms3433;
RA Cho Y.S., Hu L., Hou H., Lee H., Xu J., Kwon S., Oh S., Kim H.M., Jho S.,
RA Kim S., Shin Y.A., Kim B.C., Kim H., Kim C.U., Luo S.J., Johnson W.E.,
RA Koepfli K.P., Schmidt-Kuntzel A., Turner J.A., Marker L., Harper C.,
RA Miller S.M., Jacobs W., Bertola L.D., Kim T.H., Lee S., Zhou Q., Jung H.J.,
RA Xu X., Gadhvi P., Xu P., Xiong Y., Luo Y., Pan S., Gou C., Chu X.,
RA Zhang J., Liu S., He J., Chen Y., Yang L., Yang Y., He J., Liu S., Wang J.,
RA Kim C.H., Kwak H., Kim J.S., Hwang S., Ko J., Kim C.B., Kim S.,
RA Bayarlkhagva D., Paek W.K., Kim S.J., O'Brien S.J., Wang J., Bhak J.;
RT "The tiger genome and comparative analysis with lion and snow leopard
RT genomes.";
RL Nat. Commun. 4:2433-2433(2013).
RN [2]
RP IDENTIFICATION.
RA Puppione D.L.;
RL Unpublished observations (SEP-2014).
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 -!- PTM: The most abundant glycoforms are characterized by an O-linked
CC disaccharide galactose linked to N-acetylgalactosamine (Gal-GalNAc),
CC further modified with up to 3 sialic acid residues. Less abundant
CC glycoforms are characterized by more complex and fucosylated glycan
CC moieties. O-glycosylated on Thr-94 with a core 1 or possibly core 8
CC glycan. {ECO:0000250|UniProtKB:P02656}.
CC -!- SIMILARITY: Belongs to the apolipoprotein C3 family. {ECO:0000305}.
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DR EMBL; ATCQ01045855; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR RefSeq; XP_015392270.1; XM_015536784.1.
DR RefSeq; XP_015392271.1; XM_015536785.1.
DR AlphaFoldDB; P0DMP9; -.
DR SMR; P0DMP9; -.
DR Ensembl; ENSPTIT00000004544; ENSPTIP00000001596; ENSPTIG00000004093.
DR GeneID; 102952151; -.
DR KEGG; ptg:102952151; -.
DR CTD; 345; -.
DR GeneTree; ENSGT00390000015395; -.
DR Proteomes; UP000675900; Unassembled WGS sequence.
DR GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR GO; GO:0034363; C:intermediate-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IEA:Ensembl.
DR GO; GO:0055102; F:lipase inhibitor activity; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0034382; P:chylomicron remnant clearance; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR GO; GO:0060621; P:negative regulation of cholesterol import; IEA:Ensembl.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0010987; P:negative regulation of high-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; IEA:Ensembl.
DR GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IEA:Ensembl.
DR GO; GO:0010897; P:negative regulation of triglyceride catabolic process; IEA:Ensembl.
DR GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; IEA:Ensembl.
DR GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0033700; P:phospholipid efflux; IEA:Ensembl.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IEA:Ensembl.
DR GO; GO:0019433; P:triglyceride catabolic process; IEA:Ensembl.
DR GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
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; Glycoprotein; Lipid degradation; Lipid metabolism;
KW Lipid transport; Reference proteome; Secreted; Sialic acid; Signal;
KW Transport; VLDL.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..100
FT /note="Apolipoprotein C-III"
FT /id="PRO_0000430846"
FT REGION 68..99
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 CARBOHYD 94
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P02656"
SQ SEQUENCE 100 AA; 10986 MW; 42CCBC776C0EE069 CRC64;
MQSRVLLVTA LLVLLASARA TEGEDPSLLG LMQGYVQHAT KTAQDTLTTM REFPVAQQAR
DWVTGRFSSL KDYWSTLTGK FSGFWDSTFA VTPTPASEAK
