Detail Information for IndEnz0005000457
IED ID IndEnz0005000457
Enzyme Type ID lipase000457
Protein Name Apolipoprotein A-I
Apo-AI
ApoA-I
Apolipoprotein A1

Cleaved into: Proapolipoprotein A-I
ProapoA-I
; Truncated apolipoprotein A-I
Gene Name Apoa1
Organism Mus musculus (Mouse)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MKAVVLAVALVFLTGSQAWHVWQQDEPQSQWDKVKDFANVYVDAVKDSGRDYVSQFESSSLGQQLNLNLLENWDTLGSTVSQLQERLGPLTRDFWDNLEKETDWVRQEMNKDLEEVKQKVQPYLDEFQKKWKEDVELYRQKVAPLGAELQESARQKLQELQGRLSPVAEEFRDRMRTHVDSLRTQLAPHSEQMRESLAQRLAELKSNPTLNEYHTRAKTHLKTLGEKARPALEDLRHSLMPMLETLKTQVQSVIDKASETLTAQ
Enzyme Length 264
Uniprot Accession Number Q00623
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (1); Chain (3); Helix (7); Modified residue (4); Natural variant (1); Region (1); Repeat (10); Sequence conflict (8); Signal peptide (1); Turn (2)
Keywords 3D-structure;Cholesterol metabolism;Direct protein sequencing;Glycoprotein;HDL;Lipid metabolism;Lipid transport;Lipoprotein;Oxidation;Palmitate;Phosphoprotein;Reference proteome;Repeat;Secreted;Signal;Steroid metabolism;Sterol metabolism;Transport
Interact With Q08460
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue MOD_RES 109; /note=Methionine sulfoxide; /evidence=ECO:0000250; MOD_RES 193; /note=Methionine sulfoxide; /evidence=ECO:0000269|PubMed:16876491; MOD_RES 240; /note=Methionine sulfoxide; /evidence=ECO:0000269|PubMed:16876491; MOD_RES 242; /note=Methionine sulfoxide; /evidence=ECO:0000269|PubMed:16876491
Post Translational Modification PTM: Glycosylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.; PTM: May be acylated.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}.
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000250
Structure 3D NMR spectroscopy (1)
Cross Reference PDB 2LEM;
Mapped Pubmed ID 10049364; 10073953; 10087289; 10357841; 10521374; 10549415; 10559220; 10559507; 10632725; 10652269; 10766851; 10866673; 10926756; 11002334; 11093738; 11116096; 11278646; 11371557; 11477092; 11478940; 11701467; 11744719; 11983814; 11991719; 12000760; 12050168; 12062424; 12117740; 12181325; 12231556; 12231569; 12235173; 12351695; 12401887; 12471038; 12488454; 12511593; 12547832; 12748967; 1280258; 12810823; 12829028; 12859204; 12869555; 12928428; 12937162; 12951361; 1352323; 14592847; 14595002; 14610273; 14643015; 14729855; 1477475; 1496008; 14974682; 14983036; 14993246; 14999024; 15060137; 15102887; 15188057; 15210842; 15265030; 15269218; 15375180; 15466405; 15520446; 15520449; 15604097; 15632021; 15649902; 15654758; 15793583; 15797865; 15834127; 15911702; 15922294; 1596514; 15995171; 16061955; 16099465; 16109169; 16151025; 16204232; 16245952; 16285990; 16339487; 1639271; 16423356; 16497661; 16498401; 16554055; 16615898; 16931800; 1703299; 17071966; 17206937; 17222401; 17389516; 17534071; 17615385; 17634284; 17681174; 1768618; 17711302; 17906976; 17916774; 17928634; 17936760; 18033752; 18042552; 18188184; 18205410; 18218986; 18246469; 18385134; 18403724; 18458046; 18508577; 18540024; 18554416; 18617288; 18678879; 18722179; 18767813; 18775511; 19106236; 19120689; 1917889; 19239199; 19286630; 19423573; 19433476; 19433579; 19538736; 19636841; 19637234; 19786567; 1981995; 20193037; 20360851; 20376577; 20430747; 20498409; 20537649; 20637749; 20739292; 20817832; 20833724; 20974999; 21267068; 21288012; 2138915; 21482781; 21504968; 21600874; 21622630; 21677750; 21756353; 2175917; 21771977; 21858084; 21870882; 21889608; 21944998; 21968112; 22259189; 22267484; 22402133; 22427535; 22576368; 22652597; 22666383; 22805347; 22845860; 23055941; 23118226; 23132909; 23322769; 23425306; 23429073; 23456478; 23499549; 23581552; 23658016; 23720750; 2383242; 23889245; 23920041; 23990662; 24170386; 24219083; 24334873; 24407029; 24464187; 24520415; 24523407; 24603680; 24650562; 24759932; 24797128; 2499515; 25117703; 2512252; 25415591; 25465389; 25550459; 25561462; 25593328; 2576007; 25948084; 25969427; 25982508; 26044581; 26170061; 26279300; 26368306; 26466956; 26510953; 26556891; 26989082; 27088511; 27105909; 27150392; 27199144; 27514935; 27647324; 27806983; 27890613; 2792009; 28577569; 2885918; 28981086; 28982731; 28986362; 29074589; 29183962; 29578333; 29618729; 29991652; 30104731; 30290792; 30635405; 30742993; 30821416; 3085096; 31002190; 31084613; 31101050; 3132994; 31336888; 31423535; 31740486; 31907281; 32477466; 32681583; 32759326; 32810603; 33020907; 33309975; 33827950; 34270107; 34348153; 34716267; 3729925; 3749510; 3865183; 3866909; 447069; 478292; 4980192; 6099394; 6403543; 6457599; 6572912; 6735174; 6785912; 6800944; 6929943; 7295297; 7387621; 7411019; 7615825; 7751823; 7798939; 7803821; 8049247; 8075642; 8105016; 8241102; 8268669; 8281015; 8288233; 8482578; 8560269; 8631787; 8647961; 8661715; 8672132; 8672141; 8682656; 8798380; 8827514; 8833906; 8940144; 9144079; 9160753; 9186920; 9275209; 9300780; 9325076; 9327769; 9415807; 9416903; 9507992; 9611252; 9616220; 9684752; 9743230; 9795222; 9832509;
Motif
Gene Encoded By
Mass 30,616
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda