ID   APOC1_MESAU             Reviewed;          88 AA.
AC   A0A1U7QUM6;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Apolipoprotein C-I;
DE            Short=Apo-CI;
DE            Short=ApoC-I;
DE   AltName: Full=Apolipoprotein C1;
DE   Contains:
DE     RecName: Full=Truncated apolipoprotein C-I;
DE   Flags: Precursor;
GN   Name=APOC1;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT   "The Draft Genome of Mesocricetus auratus.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (JUL-2021).
CC   -!- FUNCTION: Inhibitor of lipoprotein binding to the low density
CC       lipoprotein (LDL) receptor, LDL receptor-related protein, and very low
CC       density lipoprotein (VLDL) receptor. Associates with high density
CC       lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the
CC       plasma and makes up about 10% of the protein of the VLDL and 2% of that
CC       of HDL. Appears to interfere directly with fatty acid uptake and is
CC       also the major plasma inhibitor of cholesteryl ester transfer protein
CC       (CETP). Modulates the interaction of APOE with beta-migrating VLDL and
CC       inhibits binding of beta-VLDL to the LDL receptor-related protein (By
CC       similarity). Binds free fatty acids and reduces their intracellular
CC       esterification (By similarity). {ECO:0000250|UniProtKB:P02654,
CC       ECO:0000250|UniProtKB:P33047, ECO:0000250|UniProtKB:P34928}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02654}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein C1 family. {ECO:0000305}.
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DR   EMBL; APMT01188317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005086405.1; XM_005086348.3.
DR   RefSeq; XP_021078849.1; XM_021223190.1.
DR   STRING; 10036.XP_005086405.1; -.
DR   GeneID; 101825021; -.
DR   CTD; 341; -.
DR   eggNOG; ENOG502SEU4; Eukaryota.
DR   OrthoDB; 1558708at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IEA:Ensembl.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0005504; F:fatty acid binding; IEA:Ensembl.
DR   GO; GO:0004859; F:phospholipase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
DR   GO; GO:0034382; P:chylomicron remnant clearance; IEA:Ensembl.
DR   GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR   GO; GO:0032375; P:negative regulation of cholesterol transport; IEA:Ensembl.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; IEA:Ensembl.
DR   GO; GO:0010900; P:negative regulation of phosphatidylcholine catabolic process; IEA:Ensembl.
DR   GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IEA:Ensembl.
DR   GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; IEA:Ensembl.
DR   GO; GO:0033700; P:phospholipid efflux; IEA:Ensembl.
DR   GO; GO:0034369; P:plasma lipoprotein particle remodeling; IEA:Ensembl.
DR   GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
DR   GO; GO:0034447; P:very-low-density lipoprotein particle clearance; IEA:Ensembl.
DR   Gene3D; 4.10.260.30; -; 1.
DR   InterPro; IPR043081; ApoC-1_sf.
DR   InterPro; IPR006781; ApoC-I.
DR   PANTHER; PTHR16565; PTHR16565; 1.
DR   Pfam; PF04691; ApoC-I; 1.
PE   3: Inferred from homology;
KW   Lipid transport; Reference proteome; Secreted; Signal; Transport; VLDL.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..88
FT                   /note="Apolipoprotein C-I"
FT                   /id="PRO_5029134073"
FT   CHAIN           29..88
FT                   /note="Truncated apolipoprotein C-I"
FT                   /evidence="ECO:0000250|UniProtKB:P86336"
FT                   /id="PRO_0000453987"
SQ   SEQUENCE   88 AA;  9870 MW;  D9413A29557A2F49 CRC64;
     MRLLISLPVL IVVLAMALEG PAPAQATPDL SSAFENLPEK LKEFGNTLED KARAAIEHIK
     QKEILTKTRT WFSETFGKLK EKLKTTFD