APOC1_HUMAN
ID APOC1_HUMAN Reviewed; 83 AA.
AC P02654; B2R526; Q6IB97;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 03-AUG-2022, entry version 200.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6328444; DOI=10.1093/nar/12.9.3909;
RA Knott T.J., Robertson M.E., Priestley L.M., Urdea M., Wallis S.C.,
RA Scott J.;
RT "Characterisation of mRNAs encoding the precursor for human apolipoprotein
RT CI.";
RL Nucleic Acids Res. 12:3909-3915(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=2835369; DOI=10.1016/s0021-9258(18)68638-7;
RA Lauer S.J., Walker D., Elshourbagy N.A., Reardon C.A., Levy-Wilson B.,
RA Taylor J.M.;
RT "Two copies of the human apolipoprotein C-I gene are linked closely to the
RT apolipoprotein E gene.";
RL J. Biol. Chem. 263:7277-7286(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10520737; DOI=10.3109/10425179809086433;
RA Freitas E.M., Zhang W.J., Lalonde J.P., Tay G.K., Gaudieri S.,
RA Ashworth L.K., Van Bockxmeer F.M., Dawkins R.L.;
RT "Sequencing of 42kb of the APO E-C2 gene cluster reveals a new gene:
RT PEREC1.";
RL DNA Seq. 9:89-100(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nickerson D.A., Smith J.D., Fullerton S.M., Clark A.G., Stengard J.H.,
RA Salomaa V., Boerwinkle E., Sing C.F., Weiss K.M.;
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Bechtel S., Schupp I., Duda A., Wellenreuther R., Mehrle A., Ruschke V.,
RA Poustka A., Wiemann S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-83.
RX PubMed=2985493; DOI=10.1007/bf00291654;
RA Tata F., Henry I., Markham A.F., Wallis S.C., Weil D., Grzeschik K.H.,
RA Junien C., Williamson R., Humphries S.E.;
RT "Isolation and characterisation of a cDNA clone for human apolipoprotein CI
RT and assignment of the gene to chromosome 19.";
RL Hum. Genet. 69:345-349(1985).
RN [13]
RP PROTEIN SEQUENCE OF 27-83.
RX PubMed=166984; DOI=10.1016/s0021-9258(19)41998-4;
RA Shulman R.S., Herbert P.N., Wehrly K., Fredrickson D.S.;
RT "The complete amino acid sequence of C-I (apoLp-Ser), an apolipoprotein
RT from human very low density lipoproteins.";
RL J. Biol. Chem. 250:182-190(1975).
RN [14]
RP PROTEIN SEQUENCE OF 27-83.
RX PubMed=4369340; DOI=10.1016/s0021-9258(19)42365-x;
RA Jackson R.L., Sparrow J.T., Baker H.N., Morrisett J.D., Taunton O.D.,
RA Gotto A.M. Jr.;
RT "The primary structure of apolipoprotein-serine.";
RL J. Biol. Chem. 249:5308-5313(1974).
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RX PubMed=2897845; DOI=10.1016/s0006-291x(88)80424-8;
RA Smit M.V.D., Kooij-Meijs E., Woudt L.P., Havekes L.M., Frants R.R.;
RT "Exact localization of the familial dysbetalipoproteinemia associated HpaI
RT restriction site in the promoter region of the APOC1 gene.";
RL Biochem. Biophys. Res. Commun. 152:1282-1288(1988).
RN [16]
RP FUNCTION.
RX PubMed=17339654; DOI=10.1194/jlr.m700024-jlr200;
RA Westerterp M., Berbee J.F., Delsing D.J., Jong M.C., Gijbels M.J.,
RA Dahlmans V.E., Offerman E.H., Romijn J.A., Havekes L.M., Rensen P.C.;
RT "Apolipoprotein C-I binds free fatty acids and reduces their intracellular
RT esterification.";
RL J. Lipid Res. 48:1353-1361(2007).
RN [17]
RP REVIEW.
RX PubMed=28757862; DOI=10.1007/s11515-013-1278-7;
RA Puppione D., Whitelegge J.P.;
RT "Proteogenomic Review of the Changes in Primate apoC-I during Evolution.";
RL Front. Biol. 8:533-548(2013).
RN [18]
RP GENE DUPLICATION.
RX PubMed=25160599; DOI=10.1016/j.cbd.2014.08.001;
RA Puppione D.L.;
RT "Higher primates, but not New World monkeys, have a duplicate set of
RT enhancers flanking their apoC-I genes.";
RL Comp. Biochem. Physiol. 11:45-48(2014).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX DOI=10.4236/ojmn.2018.83021;
RA Groll M., Frenzel J., Krause M., Schaenzer A., Mueller W., Eschrich K.,
RA Nestler U.;
RT "MALDI-TOF mass spectrometric analysis of brain tumor cyst fluid reveals a
RT protein peak corresponding to ApoC1 and LuzP6.";
RL O. J. Mod. Neurosurg. 8:251-263(2018).
RN [21]
RP STRUCTURE BY NMR OF 33-50 AND 61-79.
RX PubMed=7779782; DOI=10.1021/bi00022a013;
RA Rozek A., Buchko G.W., Cushley R.J.;
RT "Conformation of two peptides corresponding to human apolipoprotein C-I
RT residues 7-24 and 35-53 in the presence of sodium dodecyl sulfate by CD and
RT NMR spectroscopy.";
RL Biochemistry 34:7401-7408(1995).
RN [22]
RP STRUCTURE BY NMR OF 27-64.
RX PubMed=9300485; DOI=10.1002/pro.5560060906;
RA Rozek A., Buchko G.W., Kanda P., Cushley R.J.;
RT "Conformational studies of the N-terminal lipid-associating domain of human
RT apolipoprotein C-I by CD and 1H NMR spectroscopy.";
RL Protein Sci. 6:1858-1868(1997).
RN [23]
RP STRUCTURE BY NMR OF 27-83.
RX PubMed=10545169; DOI=10.1021/bi982966h;
RA Rozek A., Sparrow J.T., Weisgraber K.H., Cushley R.J.;
RT "Conformation of human apolipoprotein C-I in a lipid-mimetic environment
RT determined by CD and NMR spectroscopy.";
RL Biochemistry 38:14475-14484(1999).
RN [24]
RP VARIANT MET-16.
RX PubMed=10391210; DOI=10.1038/10297;
RA Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A.,
RA Cooper R., Lipshutz R., Chakravarti A.;
RT "Patterns of single-nucleotide polymorphisms in candidate genes for blood-
RT pressure homeostasis.";
RL Nat. Genet. 22:239-247(1999).
RN [25]
RP VARIANT SER-71, AND CHARACTERIZATION OF VARIANT SER-71.
RX PubMed=16981907; DOI=10.1111/j.1742-4658.2006.05473.x;
RA Wroblewski M.S., Wilson-Grady J.T., Martinez M.B., Kasthuri R.S.,
RA McMillan K.R., Flood-Urdangarin C., Nelsestuen G.L.;
RT "A functional polymorphism of apolipoprotein C1 detected by mass
RT spectrometry.";
RL FEBS J. 273:4707-4715(2006).
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:0000269|PubMed:17339654, ECO:0000303|PubMed:25160599}.
CC -!- INTERACTION:
CC P02654; Q13085-4: ACACA; NbExp=3; IntAct=EBI-1220105, EBI-12562760;
CC P02654; Q96CM8: ACSF2; NbExp=3; IntAct=EBI-1220105, EBI-2876502;
CC P02654; P56378-2: ATP5MPL; NbExp=3; IntAct=EBI-1220105, EBI-17870477;
CC P02654; Q92843: BCL2L2; NbExp=3; IntAct=EBI-1220105, EBI-707714;
CC P02654; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-1220105, EBI-7062247;
CC P02654; Q8N5I4: DHRSX; NbExp=3; IntAct=EBI-1220105, EBI-3923585;
CC P02654; Q6VB84: FOXD4L3; NbExp=3; IntAct=EBI-1220105, EBI-11961494;
CC P02654; Q96QA5: GSDMA; NbExp=3; IntAct=EBI-1220105, EBI-11320924;
CC P02654; Q99525: H4C7; NbExp=3; IntAct=EBI-1220105, EBI-10294329;
CC P02654; A8MV81: HIGD1C; NbExp=3; IntAct=EBI-1220105, EBI-12809676;
CC P02654; Q6P1Q0: LETMD1; NbExp=3; IntAct=EBI-1220105, EBI-1549822;
CC P02654; Q8WWC4: MAIP1; NbExp=3; IntAct=EBI-1220105, EBI-1042937;
CC P02654; Q5XKP0: MICOS13; NbExp=3; IntAct=EBI-1220105, EBI-1053887;
CC P02654; O95563: MPC2; NbExp=3; IntAct=EBI-1220105, EBI-719403;
CC P02654; Q9Y6C9: MTCH2; NbExp=3; IntAct=EBI-1220105, EBI-6164522;
CC P02654; Q96E29: MTERF3; NbExp=3; IntAct=EBI-1220105, EBI-7825321;
CC P02654; Q9UMS0: NFU1; NbExp=3; IntAct=EBI-1220105, EBI-725252;
CC P02654; Q96JH8: RADIL; NbExp=3; IntAct=EBI-1220105, EBI-744267;
CC P02654; Q8WXG1: RSAD2; NbExp=3; IntAct=EBI-1220105, EBI-12736320;
CC P02654; Q14D33: RTP5; NbExp=3; IntAct=EBI-1220105, EBI-10217913;
CC P02654; O00241-2: SIRPB1; NbExp=3; IntAct=EBI-1220105, EBI-10179231;
CC P02654; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-1220105, EBI-742688;
CC P02654; Q17RD7: SYT16; NbExp=3; IntAct=EBI-1220105, EBI-10238936;
CC P02654; Q53QW1: TEX44; NbExp=5; IntAct=EBI-1220105, EBI-10278496;
CC P02654; Q6ZUI0: TPRG1; NbExp=3; IntAct=EBI-1220105, EBI-17249488;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:2835369}.
CC -!- TISSUE SPECIFICITY: Synthesized mainly in liver and to a minor degree
CC in intestine. Also found in the lung and spleen.
CC {ECO:0000269|PubMed:2835369}.
CC -!- MISCELLANEOUS: Apolipoprotein C-I is present in acidic (APOC1A) and
CC basic (APOC1B) forms in P.paniscus, P.abelii and P.troglodytes and
CC perhaps also in baboons and macaques. The two genes for ApoC-I arose
CC through a duplication process that occurred after the divergence of New
CC World monkeys from the human lineage. In human, the acidic form has
CC become a pseudogene sometime between the divergence of bonobos and
CC chimpanzees from the human lineage and the appearance of the
CC Denisovans. Pseudogenization resulted when the codon for the
CC penultimate amino acid in the signal sequence was changed to a stop
CC codon. {ECO:0000303|PubMed:25160599}.
CC -!- SIMILARITY: Belongs to the apolipoprotein C1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Apolipoprotein C1 entry;
CC URL="https://en.wikipedia.org/wiki/Apolipoprotein_C1";
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DR EMBL; X00570; CAA25235.1; -; mRNA.
DR EMBL; M20843; AAA51763.1; -; Genomic_DNA.
DR EMBL; AF050154; AAD02506.1; -; Genomic_DNA.
DR EMBL; AY422954; AAQ91813.1; -; Genomic_DNA.
DR EMBL; BT007142; AAP35806.1; -; mRNA.
DR EMBL; AK312036; BAG34973.1; -; mRNA.
DR EMBL; CR456907; CAG33188.1; -; mRNA.
DR EMBL; AM392727; CAL37605.1; -; mRNA.
DR EMBL; FJ525874; ACN81312.1; -; Genomic_DNA.
DR EMBL; CH471126; EAW57307.1; -; Genomic_DNA.
DR EMBL; BC009698; AAH09698.1; -; mRNA.
DR EMBL; BC055093; AAH55093.1; -; mRNA.
DR EMBL; M20902; AAA88018.1; -; Genomic_DNA.
DR EMBL; M27359; AAA51762.1; -; mRNA.
DR CCDS; CCDS12648.1; -.
DR PIR; A28057; LPHUC1.
DR RefSeq; NP_001307994.1; NM_001321065.1.
DR RefSeq; NP_001307995.1; NM_001321066.1.
DR RefSeq; NP_001636.1; NM_001645.4.
DR PDB; 1ALE; NMR; -; A=33-50.
DR PDB; 1ALF; NMR; -; A=61-79.
DR PDB; 1IOJ; NMR; -; A=27-83.
DR PDB; 1OPP; NMR; -; A=27-64.
DR PDB; 6DVU; X-ray; 1.80 A; A/B=1-83.
DR PDB; 6DXR; X-ray; 2.00 A; A/B=1-83.
DR PDB; 6DZ6; X-ray; 3.00 A; A/B=1-83.
DR PDB; 6NF3; X-ray; 2.33 A; A/B=1-83.
DR PDBsum; 1ALE; -.
DR PDBsum; 1ALF; -.
DR PDBsum; 1IOJ; -.
DR PDBsum; 1OPP; -.
DR PDBsum; 6DVU; -.
DR PDBsum; 6DXR; -.
DR PDBsum; 6DZ6; -.
DR PDBsum; 6NF3; -.
DR AlphaFoldDB; P02654; -.
DR SMR; P02654; -.
DR BioGRID; 106838; 32.
DR IntAct; P02654; 30.
DR MINT; P02654; -.
DR STRING; 9606.ENSP00000465356; -.
DR CarbonylDB; P02654; -.
DR PhosphoSitePlus; P02654; -.
DR BioMuta; APOC1; -.
DR DMDM; 114016; -.
DR CPTAC; non-CPTAC-1085; -.
DR CPTAC; non-CPTAC-2623; -.
DR EPD; P02654; -.
DR jPOST; P02654; -.
DR MassIVE; P02654; -.
DR MaxQB; P02654; -.
DR PaxDb; P02654; -.
DR PeptideAtlas; P02654; -.
DR PRIDE; P02654; -.
DR ProteomicsDB; 51539; -.
DR TopDownProteomics; P02654; -.
DR Antibodypedia; 17780; 367 antibodies from 35 providers.
DR DNASU; 341; -.
DR Ensembl; ENST00000588750.5; ENSP00000465356.1; ENSG00000130208.10.
DR Ensembl; ENST00000588802.5; ENSP00000468029.1; ENSG00000130208.10.
DR Ensembl; ENST00000592535.6; ENSP00000468276.2; ENSG00000130208.10.
DR GeneID; 341; -.
DR KEGG; hsa:341; -.
DR MANE-Select; ENST00000592535.6; ENSP00000468276.2; NM_001645.5; NP_001636.1.
DR UCSC; uc002pac.2; human.
DR CTD; 341; -.
DR DisGeNET; 341; -.
DR GeneCards; APOC1; -.
DR HGNC; HGNC:607; APOC1.
DR HPA; ENSG00000130208; Tissue enriched (liver).
DR MIM; 107710; gene.
DR neXtProt; NX_P02654; -.
DR OpenTargets; ENSG00000130208; -.
DR PharmGKB; PA51; -.
DR VEuPathDB; HostDB:ENSG00000130208; -.
DR eggNOG; ENOG502SEU4; Eukaryota.
DR GeneTree; ENSGT00390000011584; -.
DR InParanoid; P02654; -.
DR OMA; NWFTEQF; -.
DR OrthoDB; 1558708at2759; -.
DR PhylomeDB; P02654; -.
DR PathwayCommons; P02654; -.
DR Reactome; R-HSA-8866423; VLDL assembly.
DR Reactome; R-HSA-8964046; VLDL clearance.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR SignaLink; P02654; -.
DR BioGRID-ORCS; 341; 18 hits in 1070 CRISPR screens.
DR ChiTaRS; APOC1; human.
DR EvolutionaryTrace; P02654; -.
DR GeneWiki; Apolipoprotein_C1; -.
DR GenomeRNAi; 341; -.
DR Pharos; P02654; Tbio.
DR PRO; PR:P02654; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P02654; protein.
DR Bgee; ENSG00000130208; Expressed in right lobe of liver and 180 other tissues.
DR ExpressionAtlas; P02654; baseline and differential.
DR Genevisible; P02654; HS.
DR GO; GO:0042627; C:chylomicron; TAS:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:LIFEdb.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0005504; F:fatty acid binding; IDA:BHF-UCL.
DR GO; GO:0055102; F:lipase inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0031210; F:phosphatidylcholine binding; TAS:BHF-UCL.
DR GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; TAS:BHF-UCL.
DR GO; GO:0004859; F:phospholipase inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
DR GO; GO:0034382; P:chylomicron remnant clearance; IDA:BHF-UCL.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; TAS:BHF-UCL.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR GO; GO:0032375; P:negative regulation of cholesterol transport; IDA:BHF-UCL.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IDA:BHF-UCL.
DR GO; GO:0045833; P:negative regulation of lipid metabolic process; IDA:BHF-UCL.
DR GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; IDA:BHF-UCL.
DR GO; GO:0010900; P:negative regulation of phosphatidylcholine catabolic process; IDA:BHF-UCL.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; IDA:BHF-UCL.
DR GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; IDA:BHF-UCL.
DR GO; GO:0033700; P:phospholipid efflux; IDA:BHF-UCL.
DR GO; GO:0034369; P:plasma lipoprotein particle remodeling; IDA:BHF-UCL.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; TAS:BHF-UCL.
DR GO; GO:0032374; P:regulation of cholesterol transport; IC:BHF-UCL.
DR GO; GO:0006641; P:triglyceride metabolic process; IBA:GO_Central.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; TAS:BHF-UCL.
DR GO; GO:0034447; P:very-low-density lipoprotein particle clearance; IGI:BHF-UCL.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lipid transport;
KW Reference proteome; Secreted; Signal; Transport; VLDL.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:166984,
FT ECO:0000269|PubMed:4369340"
FT CHAIN 27..83
FT /note="Apolipoprotein C-I"
FT /id="PRO_0000002014"
FT CHAIN 29..83
FT /note="Truncated apolipoprotein C-I"
FT /evidence="ECO:0000250|UniProtKB:P86336"
FT /id="PRO_0000391843"
FT VARIANT 16
FT /note="I -> M (in dbSNP:rs5112)"
FT /evidence="ECO:0000269|PubMed:10391210"
FT /id="VAR_014183"
FT VARIANT 71
FT /note="T -> S (more susceptible to N-terminal truncation
FT and shows greater distribution to the VLDL than the protein
FT with T-71; dbSNP:rs142372275)"
FT /evidence="ECO:0000269|PubMed:16981907"
FT /id="VAR_029011"
FT HELIX 32..78
FT /evidence="ECO:0007829|PDB:6DVU"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1IOJ"
SQ SEQUENCE 83 AA; 9332 MW; 4A3614626624AE6A CRC64;
MRLFLSLPVL VVVLSIVLEG PAPAQGTPDV SSALDKLKEF GNTLEDKARE LISRIKQSEL
SAKMREWFSE TFQKVKEKLK IDS
