IED ID | IndEnz0005000458 |
Enzyme Type ID | lipase000458 |
Protein Name |
Apolipoprotein A-II Apo-AII ApoA-II Apolipoprotein A2 Cleaved into: Proapolipoprotein A-II ProapoA-II ; Truncated apolipoprotein A-II Apolipoprotein A-II 1-76 |
Gene Name | APOA2 |
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 | MKLLAATVLLLTICSLEGALVRRQAKEPCVESLVSQYFQTVTDYGKDLMEKVKSPELQAEAKSYFEKSKEQLTPLIKKAGTELVNFLSYFVELGTQPATQ |
Enzyme Length | 100 |
Uniprot Accession Number | P02652 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (3); Disulfide bond (1); Modified residue (4); Region (1); Sequence conflict (1); Signal peptide (1) |
Keywords | Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Glycoprotein;HDL;Host-virus interaction;Lipid transport;Oxidation;Phosphoprotein;Pyrrolidone carboxylic acid;Reference proteome;Secreted;Signal;Transport |
Interact With | Q13520; Q8NEC5; Q9H5X1; Q9BQA9; O00258; P48165; Q7Z5P4; P43628; P15941-11; Q96RD7; Q13113; P30825; Q8WWF3; P27105; Q9NWC5 |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24116940}. |
Modified Residue | MOD_RES 24; /note="Pyrrolidone carboxylic acid"; /evidence="ECO:0000269|PubMed:24116940, ECO:0000269|PubMed:4344225"; MOD_RES 49; /note="Methionine sulfoxide"; /evidence="ECO:0000269|PubMed:12576517"; MOD_RES 54; /note="Phosphoserine; by FAM20C"; /evidence="ECO:0000269|PubMed:26091039"; MOD_RES 68; /note="Phosphoserine; by FAM20C"; /evidence="ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:19824718" |
Post Translational Modification | PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000269|PubMed:26091039}.; PTM: Apolipoprotein A-II is O-glycosylated. {ECO:0000269|PubMed:23234360}. |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:6328445 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 11060341; 11181758; 11971944; 12032642; 12116231; 12116266; 12136402; 12458630; 12518019; 12522687; 12690114; 12692552; 12738753; 1279089; 12959642; 14650352; 14732096; 14967812; 14988251; 15174051; 15247216; 15388641; 15583000; 15833935; 16200213; 16254078; 16368749; 16407233; 16990646; 17110338; 17264082; 17446329; 17644776; 17652309; 17709437; 17923573; 18179799; 18269685; 18507396; 1856611; 18636124; 18652418; 18660489; 18676680; 18766253; 19069164; 19170196; 19193611; 19216768; 19285487; 19336475; 19423540; 19618959; 19625176; 19635584; 19651918; 19692168; 19710929; 19778946; 19817643; 19878569; 19901143; 19913121; 19948975; 20022911; 20031551; 20331378; 20406964; 20430392; 20438785; 20602615; 20628086; 20679960; 20855565; 20975728; 21300819; 21386805; 21501035; 21516116; 22235130; 22723940; 23025327; 23241412; 23300094; 23620136; 23631828; 23883582; 24012775; 24089247; 24108135; 24633472; 25416956; 25609649; 2566309; 25979856; 26071654; 26104730; 26549697; 26590203; 26682220; 27271094; 27526664; 2793848; 28359369; 28373285; 28457653; 28476857; 28545455; 29481802; 30259989; 30359420; 31133485; 32758395; 32919081; 33296791; 33588820; 33674281; 33759320; 34472376; 3942763; 4345202; 5057882; 7678506; 7683668; 8245722; 8728311; 9489233; 9925661; |
Motif | |
Gene Encoded By | |
Mass | 11,175 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |