IED ID | IndEnz0005000275 |
Enzyme Type ID | lipase000275 |
Protein Name |
Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 GPI-HBP1 GPI-anchored HDL-binding protein 1 High density lipoprotein-binding protein 1 |
Gene Name | GPIHBP1 HBP1 |
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 | MKALGAVLLALLLFGRPGRGQTQQEEEEEDEDHGPDDYDEEDEDEVEEEETNRLPGGRSRVLLRCYTCKSLPRDERCNLTQNCSHGQTCTTLIAHGNTESGLLTTHSTWCTDSCQPITKTVEGTQVTMTCCQSSLCNVPPWQSSRVQDPTGKGAGGPRGSSETVGAALLLNLLAGLGAMGARRP |
Enzyme Length | 184 |
Uniprot Accession Number | Q8IV16 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Mediates the transport of lipoprotein lipase LPL from the basolateral to the apical surface of endothelial cells in capillaries (By similarity). Anchors LPL on the surface of endothelial cells in the lumen of blood capillaries (By similarity). Protects LPL against loss of activity, and against ANGPTL4-mediated unfolding (PubMed:27929370, PubMed:29899144). Thereby, plays an important role in lipolytic processing of chylomicrons by LPL, triglyceride metabolism and lipid homeostasis (PubMed:19304573, PubMed:21314738). Binds chylomicrons and phospholipid particles that contain APOA5 (PubMed:17997385, PubMed:19304573). Binds high-density lipoprotein (HDL) and plays a role in the uptake of lipids from HDL (By similarity). {ECO:0000250|UniProtKB:Q9D1N2, ECO:0000269|PubMed:17997385, ECO:0000269|PubMed:19304573, ECO:0000269|PubMed:21314738, ECO:0000269|PubMed:27929370, ECO:0000269|PubMed:29899144}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Beta strand (7); Chain (1); Compositional bias (1); Disulfide bond (5); Domain (1); Glycosylation (1); Lipidation (1); Modified residue (1); Mutagenesis (16); Natural variant (13); Propeptide (1); Region (3); Signal peptide (1); Turn (1) |
Keywords | 3D-structure;Cell membrane;Disease variant;Disulfide bond;GPI-anchor;Glycoprotein;Lipid-binding;Lipoprotein;Membrane;Reference proteome;Signal;Sulfation;Transport |
Interact With | P06858 |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q9D1N2}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9D1N2}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9D1N2}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9D1N2}. Cell membrane {ECO:0000269|PubMed:19304573}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9D1N2}. |
Modified Residue | MOD_RES 38; /note=Sulfotyrosine; /evidence=ECO:0000269|PubMed:29899144 |
Post Translational Modification | PTM: Glycosylation of Asn-78 is critical for cell surface localization. {ECO:0000250|UniProtKB:Q9D1N2}.; PTM: Sulfation of a Tyr in the N-terminal acidic region increases the affinity for LPL. {ECO:0000269|PubMed:29899144}. |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
Structure 3D | X-ray crystallography (4) |
Cross Reference PDB | 6E7K; 6OAU; 6OAZ; 6OB0; |
Mapped Pubmed ID | 10900462; 11072085; 1279089; 16109723; 16200213; 17088546; 18713736; 19542565; 20124439; 20237496; 20581395; 20966398; 21478160; 21518912; 21978733; 22008945; 22078753; 22740495; 23020258; 24397894; 2443973; 24589565; 24704550; 24793350; 24847059; 25131724; 25873395; 25911085; 26892125; 26933753; 26934567; 26934667; 27875259; 27984852; 28476858; 28534127; 28666713; 28694296; 29056530; 30218660; 30408040; 30598475; 31072929; 31169500; 31323462; 31645434; 32332431; 32771483; 32858055; 33706081; 3422494; 3942763; 5057882; 8020465; 8728311; |
Motif | |
Gene Encoded By | |
Mass | 19,850 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |