Detail Information for IndEnz0005001387
IED ID IndEnz0005001387
Enzyme Type ID lipase001387
Protein Name Apolipoprotein C-I
Apo-CI
ApoC-I
Apolipoprotein C1

Cleaved into: Truncated apolipoprotein C-I
Gene Name APOC1
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MRLFLSLPVLVVVLSIVLEGPAPAQGTPDVSSALDKLKEFGNTLEDKARELISRIKQSELSAKMREWFSETFQKVKEKLKIDS
Enzyme Length 83
Uniprot Accession Number P02654
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Binds free fatty acids and reduces their intracellular esterification. Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein. {ECO:0000269|PubMed:17339654, ECO:0000303|PubMed:25160599}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (1); Chain (2); Helix (1); Natural variant (2); Signal peptide (1)
Keywords 3D-structure;Direct protein sequencing;Lipid transport;Reference proteome;Secreted;Signal;Transport;VLDL
Interact With Q13085-4; Q96CM8; P56378-2; Q92843; Q9UHD4; Q8N5I4; Q6VB84; Q96QA5; Q99525; A8MV81; Q6P1Q0; Q8WWC4; Q5XKP0; O95563; Q9Y6C9; Q96E29; Q9UMS0; Q96JH8; Q8WXG1; Q14D33; O00241-2; Q9NZD8; Q17RD7; Q53QW1; Q6ZUI0
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:2835369}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..26; /evidence="ECO:0000269|PubMed:166984, ECO:0000269|PubMed:4369340"
Structure 3D X-ray crystallography (4); NMR spectroscopy (4)
Cross Reference PDB 1ALE; 1ALF; 1IOJ; 1OPP; 6DVU; 6DXR; 6DZ6; 6NF3;
Mapped Pubmed ID 10191299; 10224102; 10852956; 11353333; 11702052; 11714102; 11825674; 12032151; 12044170; 12113906; 12220441; 12429068; 12658354; 12678662; 12700342; 12700345; 12705839; 12736801; 12805445; 12860251; 12962909; 14523051; 14705977; 14746139; 15077570; 15174051; 15265030; 15339254; 15364690; 15576844; 15591219; 15767578; 15769335; 15777558; 15793777; 15840864; 15900219; 16159884; 16459141; 16544732; 16608402; 16631424; 16763159; 16935938; 17254710; 17310220; 17341095; 17667986; 17761674; 17936795; 17998437; 18037960; 18049452; 18160739; 18193043; 18193044; 18262040; 18644789; 18667498; 18802019; 18835943; 18976728; 18984910; 19014618; 19060906; 19062221; 19197348; 19252179; 19336575; 19368908; 19417222; 19494537; 19567438; 19761869; 19785722; 19808960; 19812053; 19913121; 19936222; 20145290; 20308432; 20331378; 20339536; 20430392; 20498921; 20571754; 20580041; 20628086; 20691829; 20714348; 20864672; 20880607; 20972250; 21187063; 21533863; 21776394; 21900206; 21943158; 22022282; 22264166; 22404376; 22461740; 22474067; 22710912; 22995522; 23300094; 23555584; 23620136; 23670531; 24121499; 24498013; 24574346; 24582705; 26129832; 26576771; 26639962; 26657933; 27040450; 27052600; 27179730; 27805002; 27806189; 27976371; 28065845; 28486432; 29636060; 30130702; 30559175; 30684189; 31006040; 31211449; 31779116; 32619263; 32826950; 32961112; 33305507; 33591959; 8294473; 9633939;
Motif
Gene Encoded By
Mass 9,332
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda