| IED ID | IndEnz0002009085 |
| Enzyme Type ID | protease009085 |
| Protein Name |
Inactive rhomboid protein 2 iRhom2 Rhomboid 5 homolog 2 Rhomboid family member 2 Rhomboid veinlet-like protein 5 Rhomboid veinlet-like protein 6 |
| Gene Name | RHBDF2 IRHOM2 RHBDL5 RHBDL6 |
| 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 | MASADKNGGSVSSVSSSRLQSRKPPNLSITIPPPEKETQAPGEQDSMLPEGFQNRRLKKSQPRTWAAHTTACPPSFLPKRKNPAYLKSVSLQEPRSRWQESSEKRPGFRRQASLSQSIRKGAAQWFGVSGDWEGQRQQWQRRSLHHCSMRYGRLKASCQRDLELPSQEAPSFQGTESPKPCKMPKIVDPLARGRAFRHPEEMDRPHAPHPPLTPGVLSLTSFTSVRSGYSHLPRRKRMSVAHMSLQAAAALLKGRSVLDATGQRCRVVKRSFAFPSFLEEDVVDGADTFDSSFFSKEEMSSMPDDVFESPPLSASYFRGIPHSASPVSPDGVQIPLKEYGRAPVPGPRRGKRIASKVKHFAFDRKKRHYGLGVVGNWLNRSYRRSISSTVQRQLESFDSHRPYFTYWLTFVHVIITLLVICTYGIAPVGFAQHVTTQLVLRNKGVYESVKYIQQENFWVGPSSIDLIHLGAKFSPCIRKDGQIEQLVLRERDLERDSGCCVQNDHSGCIQTQRKDCSETLATFVKWQDDTGPPMDKSDLGQKRTSGAVCHQDPRTCEEPASSGAHIWPDDITKWPICTEQARSNHTGFLHMDCEIKGRPCCIGTKGSCEITTREYCEFMHGYFHEEATLCSQVHCLDKVCGLLPFLNPEVPDQFYRLWLSLFLHAGVVHCLVSVVFQMTILRDLEKLAGWHRIAIIFILSGITGNLASAIFLPYRAEVGPAGSQFGLLACLFVELFQSWPLLERPWKAFLNLSAIVLFLFICGLLPWIDNIAHIFGFLSGLLLAFAFLPYITFGTSDKYRKRALILVSLLAFAGLFAALVLWLYIYPINWPWIEHLTCFPFTSRFCEKYELDQVLH |
| Enzyme Length | 856 |
| Uniprot Accession Number | Q6PJF5 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Regulates ADAM17 protease, a sheddase of the epidermal growth factor (EGF) receptor ligands and TNF, thereby plays a role in sleep, cell survival, proliferation, migration and inflammation. Does not exhibit any protease activity on its own. {ECO:0000250|UniProtKB:Q80WQ6}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Chain (1); Compositional bias (1); Erroneous initiation (2); Modified residue (6); Natural variant (5); Region (4); Sequence conflict (4); Topological domain (8); Transmembrane (7) |
| Keywords | Alternative splicing;Cell membrane;Disease variant;Endoplasmic reticulum;Growth factor binding;Membrane;Palmoplantar keratoderma;Phosphoprotein;Protein transport;Reference proteome;Transmembrane;Transmembrane helix;Transport |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q80WQ6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q80WQ6}. Cell membrane {ECO:0000269|PubMed:22265016, ECO:0000269|PubMed:29897333}. |
| Modified Residue | MOD_RES 90; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 113; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 117; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q80WQ6"; MOD_RES 323; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q80WQ6"; MOD_RES 325; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 328; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 19913121; 20628086; 22246777; 22246778; 22344671; 22638770; 24643277; 25129075; 26535007; 28128203; 28815577; 29045841; 29069608; 29155878; 30097271; 30890028; 31661139; 32236893; 32592194; 32825187; 33585287; |
| Motif | |
| Gene Encoded By | |
| Mass | 96,686 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |