ID   APOC1_PANTA             Reviewed;          78 AA.
AC   P0DM84;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2013, 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   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RL   Unpublished observations (OCT-2013).
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 {ECO:0000250|UniProtKB:P02654}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein C1 family. {ECO:0000305}.
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DR   EMBL; ATCQ01140317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_007096579.1; XM_007096517.2.
DR   AlphaFoldDB; P0DM84; -.
DR   SMR; P0DM84; -.
DR   Ensembl; ENSPTIT00000028839; ENSPTIP00000024361; ENSPTIG00000020485.
DR   GeneID; 102972544; -.
DR   KEGG; ptg:102972544; -.
DR   CTD; 341; -.
DR   GeneTree; ENSGT01050000247924; -.
DR   Proteomes; UP000675900; Unassembled WGS sequence.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR   InterPro; IPR006781; ApoC-I.
DR   PANTHER; PTHR16565; PTHR16565; 1.
PE   3: Inferred from homology;
KW   Lipid transport; Reference proteome; Secreted; Signal; Transport; VLDL.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000250"
FT   CHAIN           27..78
FT                   /note="Apolipoprotein C-I"
FT                   /id="PRO_0000424552"
FT   CHAIN           29..78
FT                   /note="Truncated apolipoprotein C-I"
FT                   /evidence="ECO:0000250|UniProtKB:P86336"
FT                   /id="PRO_0000424553"
SQ   SEQUENCE   78 AA;  8738 MW;  242216175E6184BF CRC64;
     MRLILWLPVL VVVLLMVTEG PAPAQGAPDV ASTFRNIPNS LKEFGNNLKD TFESIPEATR
     KLMTSFAERL KNFRIPLL