ID   APOC1_URSMA             Reviewed;          88 AA.
AC   P0DPH6;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2018, sequence version 1.
DT   03-AUG-2022, entry version 18.
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   Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=29073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24813606; DOI=10.1016/j.cell.2014.03.054;
RA   Liu S., Lorenzen E.D., Fumagalli M., Li B., Harris K., Xiong Z., Zhou L.,
RA   Korneliussen T.S., Somel M., Babbitt C., Wray G., Li J., He W., Wang Z.,
RA   Fu W., Xiang X., Morgan C.C., Doherty A., O'Connell M.J., McInerney J.O.,
RA   Born E.W., Dalen L., Dietz R., Orlando L., Sonne C., Zhang G., Nielsen R.,
RA   Willerslev E., Wang J.;
RT   "Population genomics reveal recent speciation and rapid evolutionary
RT   adaptation in polar bears.";
RL   Cell 157:785-794(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Malenfant R.M., Coltman D.W., Richardson E.S., Lunn N.J., Andriashek D.S.,
RA   Davis C.S.;
RT   "Transcriptome assembly and SNP discovery in polar bears (Ursus maritimus)
RT   of Western Hudson Bay.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   IDENTIFICATION.
RA   Puppione D.L.;
RL   Unpublished observations (MAY-2018).
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). Binds free fatty acids and reduces their intracellular
CC       esterification. Modulates the interaction of APOE with beta-migrating
CC       VLDL and inhibits binding of beta-VLDL to the LDL receptor-related
CC       protein. {ECO:0000250|UniProtKB:P02654, ECO:0000250|UniProtKB:P33047}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the apolipoprotein C1 family. {ECO:0000305}.
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DR   EMBL; AVOR01000000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; GAJD01000000; -; NOT_ANNOTATED_CDS; Transcribed_RNA.
DR   RefSeq; XP_008682671.1; XM_008684449.1.
DR   AlphaFoldDB; P0DPH6; -.
DR   SMR; P0DPH6; -.
DR   STRING; 29073.XP_008682671.1; -.
DR   Ensembl; ENSUMAT00000038279; ENSUMAP00000032380; ENSUMAG00000023318.
DR   GeneID; 103657040; -.
DR   KEGG; umr:103657040; -.
DR   CTD; 341; -.
DR   GeneTree; ENSGT00390000011584; -.
DR   OMA; NWFTEQF; -.
DR   Proteomes; UP000261680; Genome assembly.
DR   Proteomes; UP000814620; Genome assembly.
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_0000444596"
FT   CHAIN           29..88
FT                   /note="Truncated apolipoprotein C-I"
FT                   /evidence="ECO:0000250|UniProtKB:P86336"
FT                   /id="PRO_0000444597"
SQ   SEQUENCE   88 AA;  9676 MW;  9BED258A50CE3A0B CRC64;
     MRLFLSLPVW VAVLAMVLEG PAPAQAAPEI SSTLGSIPDK LKEFGNTLED KARAAIESIK
     QSDIPAKTRN WFSETFNKVK EQLKTAFS