Detail Information for IndEnz0002000394
IED ID IndEnz0002000394
Enzyme Type ID protease000394
Protein Name Phosphatidylethanolamine-binding protein 1
PEBP-1
23 kDa morphine-binding protein
HCNPpp
P23K

Cleaved into: Hippocampal cholinergic neurostimulating peptide
HCNP
Gene Name Pebp1 Pbp Pebp
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 MAADISQWAGPLSLQEVDEPPQHALRVDYGGVTVDELGKVLTPTQVMNRPSSISWDGLDPGKLYTLVLTDPDAPSRKDPKFREWHHFLVVNMKGNDISSGTVLSEYVGSGPPKDTGLHRYVWLVYEQEQPLNCDEPILSNKSGDNRGKFKVESFRKKYHLGAPVAGTCFQAEWDDSVPKLHDQLAGK
Enzyme Length 187
Uniprot Accession Number P31044
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation (By similarity). {ECO:0000250}.; FUNCTION: HCNP may be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Seems to be mediated by a specific receptor.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (10); Chain (1); Helix (6); Initiator methionine (1); Modified residue (8); Peptide (1); Region (1); Sequence conflict (2)
Keywords 3D-structure;ATP-binding;Acetylation;Cytoplasm;Direct protein sequencing;Disulfide bond;Lipid-binding;Membrane;Nucleotide-binding;Phosphoprotein;Protease inhibitor;Reference proteome;Serine protease inhibitor
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
Modified Residue MOD_RES 2; /note=N-acetylalanine; in peptide hippocampal cholinergic neurostimulating; /evidence=ECO:0000269|PubMed:1611510; MOD_RES 6; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P30086; MOD_RES 13; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 42; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:P30086; MOD_RES 52; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 54; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 98; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P30086; MOD_RES 153; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P30086
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (3)
Cross Reference PDB 2IQX; 2IQY; 6ENT;
Mapped Pubmed ID 10490027; 10639732; 10714823; 11034991; 11166120; 11428049; 11585904; 12551925; 14515317; 14654844; 15886202; 15928459; 16132681; 16608915; 16916643; 17089028; 17963288; 18067547; 18311602; 18452277; 18493952; 27568556; 29163033; 29208709; 7706975; 8723436; 8888012; 9508097;
Motif
Gene Encoded By
Mass 20,801
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda