Detail Information for IndEnz0005000458
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