Detail Information for IndEnz0002005711
IED ID IndEnz0002005711
Enzyme Type ID protease005711
Protein Name Endoplasmic reticulum metallopeptidase 1
EC 3.4.-.-
Felix-ina
Gene Name Ermp1 D19Wsu12e Fxna Kiaa1815
Organism Mus musculus (Mouse)
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 Mus Mus Mus musculus (Mouse)
Enzyme Sequence MEWSSESAAVRRHRGTAERREGEAAASHRQREASAQEDAKGVGRMWGKTENGGGSRVAKTALSEARTALALALYLLALRALVQLSLQRLVLSRTSGLQGEFDARQARDYLEHITAIGPRTTGSTENEILTVQYLLEQIKLIEAQSNSLHSISVDIQRPTGSFSIDFLGGFTSYYDNITNVVVKLEPRDGAESAILANCHFDSVANSPGASDDAVSCAVMLEVLRVMSASPEPMQHAVVFLFNGAEENVLQASHGFITQHPWASLIRAFINLEAAGVGGKELVFQTGPENPWLVQAYVSAAKHPFASVVAQEVFQSGIIPSDTDFRIYRDFGNIPGIDLAFIENGYIYHTKYDTADRILIDSIQRAGDNILAVLKHLATSDTLASSSEYRHGSMVFFDVLGLLVIAYPSRVGSIINYMVVMAVVLYLGKKLLRPKHRNANYMRDFLCGLGITFISWFTSLVTVLIIAVFISLIGQSLSWYNYFYIAVCLYGTATVAKIIFIHTLAKRFYYMNASDLYLGELFFDTSLFVHCAFLVALTYQGFCSAFMSAVWVVFPLLTKLCVYKDFKKHGAQGRFVALYLLGMFIPYLYGLYLIWAVFEMFTPILGRSGSEIPPDVVLASILAVCVMILSSYFITFIYLVNSTKKTILTLILVCAVTFLLVCSGAFFPYSSNPESPKPKRVFLQHVSRTFHNLEGSVVKRDSGIWINGFDYTGMSHVTPHIPEINDTIRAHCEEDAPLCGFPWYLPVHFLIRKNWYLPAPEVSPRNPAHFRLVSKEKMPWDSIKLTFEATGPSHMSFYVRTHKGSTLSQWSLGNGIPVTSRGGDYFVFYSHGLQASAWRFWIEVQVSEEQAEGMVTVAIAAHYLSGENKRSSQLDALKKKFPDWSFPSAWVSTYSLFVF
Enzyme Length 898
Uniprot Accession Number Q3UVK0
Absorption
Active Site ACT_SITE 245; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:P80561
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.-.-
Enzyme Function FUNCTION: Within the ovary, required for the organization of somatic cells and oocytes into discrete follicular structures. {ECO:0000250|UniProtKB:Q6UPR8}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Alternative sequence (2); Chain (1); Compositional bias (1); Disulfide bond (1); Erroneous initiation (2); Glycosylation (2); Metal binding (6); Modified residue (1); Region (1); Sequence conflict (2); Site (1); Topological domain (10); Transmembrane (9)
Keywords Acetylation;Alternative splicing;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Transmembrane;Transmembrane helix;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6UPR8}; Multi-pass membrane protein {ECO:0000255}.
Modified Residue MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:Q7Z2K6
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10725249; 12477932; 12652657; 14610273; 17267443; 21267068; 24194600; 25807483; 27626380; 28700664; 9811942;
Motif
Gene Encoded By
Mass 100,148
Kinetics
Metal Binding METAL 199; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 211; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 211; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 246; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 272; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 348; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561
Rhea ID
Cross Reference Brenda