Detail Information for IndEnz0005001029
IED ID IndEnz0005001029
Enzyme Type ID lipase001029
Protein Name Alpha-2-macroglobulin receptor-associated protein
Alpha-2-MRAP
Low density lipoprotein receptor-related protein-associated protein 1
RAP
Gene Name LRPAP1 A2MRAP
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 MAPRRVRSFLRGLPALLLLLLFLGPWPAASHGGKYSREKNQPKPSPKRESGEEFRMEKLNQLWEKAQRLHLPPVRLAELHADLKIQERDELAWKKLKLDGLDEDGEKEARLIRNLNVILAKYGLDGKKDARQVTSNSLSGTQEDGLDDPRLEKLWHKAKTSGKFSGEELDKLWREFLHHKEKVHEYNVLLETLSRTEEIHENVISPSDLSDIKGSVLHSRHTELKEKLRSINQGLDRLRRVSHQGYSTEAEFEEPRVIDLWDLAQSANLTDKELEAFREELKHFEAKIEKHNHYQKQLEIAHEKLRHAESVGDGERVSRSREKHALLEGRTKELGYTVKKHLQDLSGRISRARHNEL
Enzyme Length 357
Uniprot Accession Number P30533
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:0000269|PubMed:32296178, ECO:0000269|PubMed:7774585}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (6); Chain (1); Coiled coil (1); Compositional bias (1); Glycosylation (1); Helix (9); Modified residue (3); Motif (1); Mutagenesis (8); Natural variant (2); Region (2); Sequence conflict (3); Signal peptide (1); Turn (1)
Keywords 3D-structure;Coiled coil;Direct protein sequencing;Endoplasmic reticulum;Endosome;Glycoprotein;Golgi apparatus;Heparin-binding;Phosphoprotein;Reference proteome;Signal
Interact With P05067; Q12797-6; P01130; Q07954; Q92673; Q99523; P98155
Induction
Subcellular Location SUBCELLULAR LOCATION: Rough endoplasmic reticulum lumen {ECO:0000269|PubMed:7774585}. Endoplasmic reticulum-Golgi intermediate compartment lumen {ECO:0000269|PubMed:7774585}. Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:7774585}. Golgi apparatus lumen {ECO:0000269|PubMed:7774585}. Endosome lumen {ECO:0000269|PubMed:7774585}. Cell surface {ECO:0000269|PubMed:11384978}. Note=May be associated with receptors at the cell surface. {ECO:0000269|PubMed:11384978}.
Modified Residue MOD_RES 50; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q99068; MOD_RES 135; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P55302; MOD_RES 248; /note=Phosphothreonine; /evidence=ECO:0007744|PubMed:24275569
Post Translational Modification PTM: N-glycosylated. {ECO:0000269|PubMed:16678114, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:7774585}.
Signal Peptide SIGNAL 1..34; /evidence=ECO:0000255
Structure 3D X-ray crystallography (1); NMR spectroscopy (8)
Cross Reference PDB 1LRE; 1NRE; 1OP1; 1OV2; 2FCW; 2FTU; 2FYL; 2P01; 2P03;
Mapped Pubmed ID 10085125; 11425005; 11793025; 11992244; 12394648; 12637503; 14674767; 15213425; 16169070; 16175004; 16517593; 16650578; 16704534; 16837242; 17000644; 17123336; 17326667; 17536759; 17656581; 17913606; 17987404; 18055545; 18075286; 18494379; 18721259; 19826010; 19851296; 19913121; 20195357; 20198315; 20403997; 20628086; 20637261; 20936779; 21988832; 23754288; 23894629; 24140340; 24504617; 25159528; 26271838; 26638075; 27402839; 29955130; 31607522; 34058195; 34472763; 8083232;
Motif MOTIF 354..357; /note=Prevents secretion from ER; /evidence=ECO:0000269|PubMed:7774585
Gene Encoded By
Mass 41,466
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda