Detail Information for IndEnz0002005932
IED ID IndEnz0002005932
Enzyme Type ID protease005932
Protein Name Endoplasmic reticulum metallopeptidase 1
EC 3.4.-.-
Felix-ina
Gene Name ERMP1 FXNA KIAA1815
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 MEWGSESAAVRRHRVGVERREGAAAAPPPEREARAQEPLVDGCSGGGRTRKRSPGGSGGASRGAGTGLSEVRAALGLALYLIALRTLVQLSLQQLVLRGAAGHRGEFDALQARDYLEHITSIGPRTTGSPENEILTVHYLLEQIKLIEVQSNSLHKISVDVQRPTGSFSIDFLGGFTSYYDNITNVVVKLEPRDGAQHAVLANCHFDSVANSPGASDDAVSCSVMLEVLRVLSTSSEALHHAVIFLFNGAEENVLQASHGFITQHPWASLIRAFINLEAAGVGGKELVFQTGPENPWLVQAYVSAAKHPFASVVAQEVFQSGIIPSDTDFRIYRDFGNIPGIDLAFIENGYIYHTKYDTADRILTDSIQRAGDNILAVLKHLATSDMLAAASKYRHGNMVFFDVLGLFVIAYPSRIGSIINYMVVMGVVLYLGKKFLQPKHKTGNYKKDFLCGLGITLISWFTSLVTVLIIAVFISLIGQSLSWYNHFYVSVCLYGTATVAKIILIHTLAKRFYYMNASAQYLGEVFFDISLFVHCCFLVTLTYQGLCSAFISAVWVAFPLLTKLCVHKDFKQHGAQGKFIAFYLLGMFIPYLYALYLIWAVFEMFTPILGRSGSEIPPDVVLASILAGCTMILSSYFINFIYLAKSTKKTMLTLTLVCAITFLLVCSGTFFPYSSNPANPKPKRVFLQHMTRTFHDLEGNAVKRDSGIWINGFDYTGISHITPHIPEINDSIRAHCEENAPLCGFPWYLPVHFLIRKNWYLPAPEVSPRNPPHFRLISKEQTPWDSIKLTFEATGPSHMSFYVRAHKGSTLSQWSLGNGTPVTSKGGDYFVFYSHGLQASAWQFWIEVQVSEEHPEGMVTVAIAAHYLSGEDKRSPQLDALKEKFPDWTFPSAWVCTYDLFVF
Enzyme Length 904
Uniprot Accession Number Q7Z2K6
Absorption
Active Site ACT_SITE 251; /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 (1); Glycosylation (2); Metal binding (6); Modified residue (1); Natural variant (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 P41181; Q13520; Q9UN42; Q9BXK5; J3KQ12; Q8TD46-4; O00501; O95471; O95484; Q9UHP7-3; Q96BA8; P60508; Q5JX71; Q8TBE3; P48165; O15529; Q9NZD1; Q9UM44; P31937; Q9Y5U9; P38484; Q9UGI6-2; P26715; Q6UWN5; Q95460-2; Q9BQ51; O00623; Q9UBD6; Q9UKG4; A1A5C7-2; Q8TBB6; Q9NPE6; Q8WWF3; Q96Q45-2; Q9NWC5; Q96HE8
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:0007744|PubMed:22223895
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 17267443; 26496610; 27566589; 29523216;
Motif
Gene Encoded By
Mass 100,231
Kinetics
Metal Binding METAL 205; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 217; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 217; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 252; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 278; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P80561; METAL 354; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P80561
Rhea ID
Cross Reference Brenda