| IED ID | IndEnz0002000130 |
| Enzyme Type ID | protease000130 |
| Protein Name |
Phosphate-regulating neutral endopeptidase PHEX Metalloendopeptidase homolog PEX EC 3.4.24.- Phosphate regulating neutral endopeptidase Vitamin D-resistant hypophosphatemic rickets protein X-linked hypophosphatemia protein HYP |
| Gene Name | Phex Hyp Pex |
| 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 | MEAETGSTMETGKGTNRGIRIALALFIGGTLVLGTLLFLVSQGLLSFQAKQEYCLKPECIEAAAAIMSKVNLSVDPCENFFRFACDGWISNNPIPEDMPSYGVYPWLRHNVDLKLKALLEKSVSRRRDTEAVQKAKILYSSCMNEKAIEKADAKPLLHILRHSPFRWPVLEANIGPEGVWSERKFSLLQTLATFRGQYSNSVFIRLYVSPDDKASNEHILKLDQATLSLAVREDFLDNTTEAKSYRDALYKFMVDTAVLLGANSSRAEHDMKSVLRLEIKIAEIMIPHENRTSEAMYNKMNISELSAMIPQFDWLGYIKKVIDTRLYPHLKDIGPSENVVVRVPQYFKDLFRILGAERKKTIANYLVWRMVYSRIPNLSRRFQYRWLEFSRVIQGTTTLLPQWDKCVNFIESALPYVVGKMFVNVHFQEDKKEMMEELIEGVRWAFIDMLEKENEWMDAGTKRKAQEKARAVLAKVGYPEFIMNDTYVNEDLKAIKFSESDYFGNVLQTRKYLAQSDFFWLRKAVPKTEWFTNPTTVNAFYSASTNQIRFPAGELQKPFFWGTEYPRSLSYGAIGVIVGHEFTHGFDNNGRKYDKNGNLDPWWSVESEEKFKEKTKCMINQYSNYYWKKAGLNVKGKRTLGENIADNGGLREAFRAYRKWINDRRQGVEEPLLPGITFTNNQLFFLSYAHVRCNSYRPEAAREQVQIGAHSPPQFRVNGAISNFEEFQKAFNCPRNSTMNRGADSCRLW |
| Enzyme Length | 749 |
| Uniprot Accession Number | P70669 |
| Absorption | |
| Active Site | ACT_SITE 581; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; ACT_SITE 646; /note="Proton donor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Peptidase that cleaves SIBLING (small integrin-binding ligand, N-linked glycoprotein)-derived ASARM peptides, thus regulating their biological activity (By similarity). Cleaves ASARM peptides between Ser and Glu or Asp residues (By similarity). Regulates osteogenic cell differentiation and bone mineralization through the cleavage of the MEPE-derived ASARM peptide (PubMed:11159866, PubMed:18597632, PubMed:26051469). Promotes dentin mineralization and renal phosphate reabsorption by cleaving DMP1- and MEPE-derived ASARM peptides (PubMed:26051469). Inhibits the cleavage of MEPE by CTSB/cathepsin B thus preventing MEPE degradation (By similarity). {ECO:0000250|UniProtKB:P78562, ECO:0000269|PubMed:11159866, ECO:0000269|PubMed:26051469, ECO:0000305|PubMed:18597632}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (8); Metal binding (3); Sequence conflict (1); Topological domain (2); Transmembrane (1) |
| Keywords | Biomineralization;Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11811562}; Single-pass type II membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:11811562}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10069185; 10087298; 10920247; 10934642; 11018258; 11023830; 11517178; 11713245; 12110521; 12194021; 12220505; 12414538; 12456809; 12619927; 12791601; 12865326; 12900584; 1290161; 12952859; 1309337; 1315116; 1352307; 14751570; 15029877; 15050894; 15054142; 1528020; 15459188; 15475267; 1547718; 15579309; 15615882; 15833911; 15843468; 15940367; 15976027; 16005844; 16084134; 1612032; 16123154; 16141072; 16144964; 16449303; 16597685; 16762607; 16829211; 1685478; 16890604; 17251516; 1749428; 17615144; 17638577; 17710565; 17848631; 17942069; 18172553; 18289812; 18753255; 188049; 19082853; 19419310; 19556340; 19584304; 1962291; 19656036; 19737523; 19775205; 19933269; 19952276; 19966287; 20204609; 20440000; 20583265; 20817730; 21075853; 21139072; 21177780; 21267068; 21308778; 21312267; 21507898; 21677750; 2177024; 22006791; 22093826; 221535; 22161748; 22334725; 22527485; 22573557; 22609228; 22886699; 22930691; 23028440; 23038738; 23128355; 23174213; 23235154; 23266491; 23652555; 23700148; 23895994; 24269824; 24470103; 24601885; 24710520; 24797667; 24839967; 25089825; 25460577; 25568170; 26234751; 26336161; 26588476; 26784541; 26792657; 27035636; 27929669; 28728941; 28764922; 29561836; 29635291; 29735309; 2982272; 29878089; 2994997; 29977226; 30096468; 30120363; 3015770; 30247553; 31202927; 3145795; 31484825; 33072734; 33681179; 33731726; 34172578; 3425609; 3460077; 3863638; 3940855; 566613; 6090101; 6479099; 6583703; 6892799; 6893581; 6896304; 6896684; 7365241; 7502704; 7550339; 7573493; 7611412; 7611447; 7671167; 7785464; 7853101; 7873297; 7900834; 7962329; 8070635; 8082056; 8108466; 8113402; 8137741; 8141332; 8266820; 8304442; 8390690; 8405991; 8518105; 8635692; 8691720; 8717533; 8770917; 8772486; 8833143; 8914019; 8927512; 8940337; 908280; 9141502; 9262518; 9269633; 9333128; 9362326; 9421395; 9467015; 9467016; 9503026; 9524191; 9545633; 9736774; 9753616; 9755091; 9803442; |
| Motif | |
| Gene Encoded By | |
| Mass | 86,419 |
| Kinetics | |
| Metal Binding | METAL 580; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 584; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 642; /note="Zinc; catalytic"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01233" |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.B15; |