APOC1_MOUSE
ID APOC1_MOUSE Reviewed; 88 AA.
AC P34928; Q505B2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 146.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=8276416; DOI=10.1006/geno.1993.1424;
RA Hoffer M.J.V., van Eck M.M., Havekes L.M., Hofker M.H., Frants R.R.;
RT "The mouse apolipoprotein C1 gene: structure and expression.";
RL Genomics 18:37-42(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Liver, and Mammary gland;
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 [4]
RP PROTEIN SEQUENCE OF 43-51, AND MASS SPECTROMETRY.
RX PubMed=16876491; DOI=10.1016/j.bbapap.2006.06.001;
RA Puppione D.L., Yam L.M., Bassilian S., Souda P., Castellani L.W.,
RA Schumaker V.N., Whitelegge J.P.;
RT "Mass spectral analysis of the apolipoproteins on mouse high density
RT lipoproteins. Detection of post-translational modifications.";
RL Biochim. Biophys. Acta 1764:1363-1371(2006).
RN [5]
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).
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. {ECO:0000250|UniProtKB:P02654,
CC ECO:0000250|UniProtKB:P33047, ECO:0000269|PubMed:17339654}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02654}.
CC -!- TISSUE SPECIFICITY: Adult and fetal liver.
CC {ECO:0000269|PubMed:8276416}.
CC -!- MASS SPECTROMETRY: [Apolipoprotein C-I]: Mass=6993; Mass_error=0.707;
CC Method=Electrospray; Note=Strain C57BL/6. Without methionine
CC sulfoxide.; Evidence={ECO:0000269|PubMed:16876491};
CC -!- MASS SPECTROMETRY: [Truncated apolipoprotein C-I]: Mass=6825.6;
CC Mass_error=0.495; Method=Electrospray; Note=Strain C57BL/6. Without
CC methionine sulfoxide.; Evidence={ECO:0000269|PubMed:16876491};
CC -!- SIMILARITY: Belongs to the apolipoprotein C1 family. {ECO:0000305}.
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DR EMBL; Z22661; CAA80375.1; -; Genomic_DNA.
DR EMBL; Z22660; CAA80375.1; JOINED; Genomic_DNA.
DR EMBL; AK011358; BAB27566.1; -; mRNA.
DR EMBL; BC019398; AAH19398.1; -; mRNA.
DR EMBL; BC094638; AAH94638.1; -; mRNA.
DR CCDS; CCDS39802.1; -.
DR PIR; I48251; I48251.
DR RefSeq; NP_001103479.1; NM_001110009.2.
DR RefSeq; NP_031495.1; NM_007469.5.
DR AlphaFoldDB; P34928; -.
DR SMR; P34928; -.
DR STRING; 10090.ENSMUSP00000104091; -.
DR iPTMnet; P34928; -.
DR PhosphoSitePlus; P34928; -.
DR jPOST; P34928; -.
DR MaxQB; P34928; -.
DR PaxDb; P34928; -.
DR PeptideAtlas; P34928; -.
DR PRIDE; P34928; -.
DR ProteomicsDB; 283161; -.
DR Antibodypedia; 17780; 367 antibodies from 35 providers.
DR DNASU; 11812; -.
DR Ensembl; ENSMUST00000045035; ENSMUSP00000045571; ENSMUSG00000040564.
DR Ensembl; ENSMUST00000108451; ENSMUSP00000104091; ENSMUSG00000040564.
DR GeneID; 11812; -.
DR KEGG; mmu:11812; -.
DR UCSC; uc009fmv.3; mouse.
DR CTD; 341; -.
DR MGI; MGI:88053; Apoc1.
DR VEuPathDB; HostDB:ENSMUSG00000040564; -.
DR eggNOG; ENOG502SEU4; Eukaryota.
DR GeneTree; ENSGT00390000011584; -.
DR HOGENOM; CLU_160094_1_0_1; -.
DR InParanoid; P34928; -.
DR OMA; NWFTEQF; -.
DR OrthoDB; 1558708at2759; -.
DR PhylomeDB; P34928; -.
DR TreeFam; TF330940; -.
DR Reactome; R-MMU-8866423; VLDL assembly.
DR Reactome; R-MMU-8964046; VLDL clearance.
DR BioGRID-ORCS; 11812; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Apoc1; mouse.
DR PRO; PR:P34928; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P34928; protein.
DR Bgee; ENSMUSG00000040564; Expressed in left lobe of liver and 141 other tissues.
DR ExpressionAtlas; P34928; baseline and differential.
DR Genevisible; P34928; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISO:MGI.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:MGI.
DR GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR GO; GO:0055102; F:lipase inhibitor activity; ISO:MGI.
DR GO; GO:0004859; F:phospholipase inhibitor activity; ISO:MGI.
DR GO; GO:0033344; P:cholesterol efflux; ISO:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI.
DR GO; GO:0034382; P:chylomicron remnant clearance; ISO:MGI.
DR GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR GO; GO:0032375; P:negative regulation of cholesterol transport; ISO:MGI.
DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISO:MGI.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; ISO:MGI.
DR GO; GO:0045833; P:negative regulation of lipid metabolic process; ISO:MGI.
DR GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; ISO:MGI.
DR GO; GO:0010900; P:negative regulation of phosphatidylcholine catabolic process; ISO:MGI.
DR GO; GO:0048261; P:negative regulation of receptor-mediated endocytosis; ISO:MGI.
DR GO; GO:0010916; P:negative regulation of very-low-density lipoprotein particle clearance; ISO:MGI.
DR GO; GO:0033700; P:phospholipid efflux; ISO:MGI.
DR GO; GO:0034369; P:plasma lipoprotein particle remodeling; ISO:MGI.
DR GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI.
DR GO; GO:0034447; P:very-low-density lipoprotein particle clearance; ISO:MGI.
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 Direct protein sequencing; Lipid transport; Reference proteome; Secreted;
KW Signal; Transport; VLDL.
FT SIGNAL 1..26
FT /evidence="ECO:0000250"
FT CHAIN 27..88
FT /note="Apolipoprotein C-I"
FT /id="PRO_0000002015"
FT CHAIN 29..88
FT /note="Truncated apolipoprotein C-I"
FT /evidence="ECO:0000250|UniProtKB:P86336"
FT /id="PRO_0000391844"
SQ SEQUENCE 88 AA; 9696 MW; CF35C2144BBDCC43 CRC64;
MRLFIALPVL IVVVAMTLEG PAPAQAAPDL SGTLESIPDK LKEFGNTLED KARAAIEHIK
QKEILTKTRA WFSEAFGKVK EKLKTTFS
