| IED ID | IndEnz0005001228 |
| Enzyme Type ID | lipase001228 |
| Protein Name |
Alpha-2-macroglobulin receptor-associated protein Alpha-2-MRAP Gp330-binding 45 kDa protein Low density lipoprotein receptor-related protein-associated protein 1 RAP |
| Gene Name | Lrpap1 |
| 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 | MAPLRDRVSTLPRLQLLVLLLLPLLLVPQPIAGHGGKYSREKNEPEMAAKRESGEEFRMEKLNQLWEKAKRLHLSPVRLAELHSDLKIQERDELNWKKLKVEGLDGDGEKEAKLVHNLNVILARYGLDGRKDTQTVHSNALNEDTQDELGDPRLEKLWHKAKTSGKFSSEELDKLWREFLHYKEKIHEYNVLLDTLSRAEEGYENLLSPSDMTHIKSDTLASKHSELKDRLRSINQGLDRLRKVSHQGYGPATEFEEPRVIDLWDLAQSANFTEKELESFREELKHFEAKIEKHNHYQKQLEISHQKLKHVESIGDPEHISRNKEKYVLLEEKTKELGYKVKKHLQDLSSRVSRARHNEL |
| Enzyme Length | 360 |
| Uniprot Accession Number | Q99068 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Molecular chaperone for LDL receptor-related proteins that may regulate their ligand binding activity along the secretory pathway. {ECO:0000250|UniProtKB:P30533}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Coiled coil (1); Glycosylation (1); Modified residue (2); Motif (1); Region (1); Sequence conflict (3); Signal peptide (1) |
| Keywords | Coiled coil;Direct protein sequencing;Endoplasmic reticulum;Endosome;Glycoprotein;Golgi apparatus;Heparin-binding;Phosphoprotein;Reference proteome;Signal |
| Interact With | Q924X6; P98155 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Rough endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P30533}. Endoplasmic reticulum-Golgi intermediate compartment lumen {ECO:0000250|UniProtKB:P30533}. Golgi apparatus, cis-Golgi network {ECO:0000250|UniProtKB:P30533}. Golgi apparatus lumen {ECO:0000250|UniProtKB:P30533}. Endosome lumen {ECO:0000250|UniProtKB:P30533}. Cell surface {ECO:0000250|UniProtKB:P30533}. Note=May be associated with receptors at the cell surface. {ECO:0000250|UniProtKB:P30533}. |
| Modified Residue | MOD_RES 53; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 138; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P55302 |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P30533}. |
| Signal Peptide | SIGNAL 1..33; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10571241; 16396496; 16517593; 19935650; 24754147; 26514267; 7522607; 7723231; 7778686; 8223699; |
| Motif | MOTIF 357..360; /note=Prevents secretion from ER; /evidence=ECO:0000250|UniProtKB:P30533 |
| Gene Encoded By | |
| Mass | 42,032 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |