| IED ID | IndEnz0005001015 |
| Enzyme Type ID | lipase001015 |
| Protein Name |
Apolipoprotein A-I Apo-AI ApoA-I Apolipoprotein A1 Cleaved into: Proapolipoprotein A-I ProapoA-I |
| Gene Name | Apoa1 |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MKAAVLAVALVFLTGCQAWEFWQQDEPQSQWDRVKDFATVYVDAVKDSGRDYVSQFESSTLGKQLNLNLLDNWDTLGSTVGRLQEQLGPVTQEFWANLEKETDWLRNEMNKDLENVKQKMQPHLDEFQEKWNEEVEAYRQKLEPLGTELHKNAKEMQRHLKVVAEEFRDRMRVNADALRAKFGLYSDQMRENLAQRLTEIKNHPTLIEYHTKASDHLKTLGEKAKPALDDLGQGLMPVLEAWKAKIMSMIDEAKKKLNA |
| Enzyme Length | 259 |
| Uniprot Accession Number | P04639 |
| 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 | Chain (2); Modified residue (3); Region (1); Repeat (10); Sequence conflict (15); Signal peptide (1) |
| Keywords | 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 | Q7TMA5 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 109; /note=Methionine sulfoxide; /evidence=ECO:0000250; MOD_RES 189; /note=Methionine sulfoxide; /evidence=ECO:0000250; MOD_RES 236; /note=Methionine sulfoxide; /evidence=ECO:0000250 |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:6798036 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10419291; 11773045; 1466661; 14993246; 1537840; 1587806; 16606364; 17488882; 18391222; 18457017; 18519978; 18535924; 18614621; 18626730; 19399409; 19561306; 20391537; 20580919; 20639628; 2120218; 2123716; 22253414; 23227448; 23401751; 24117066; 24155931; 24814947; 2493483; 2504861; 25305669; 2579677; 27881716; 29581158; 30187493; 30231880; 7556148; 9211985; 9672881; |
| Motif | |
| Gene Encoded By | |
| Mass | 30,062 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |