| IED ID | IndEnz0002012885 |
| Enzyme Type ID | protease012885 |
| Protein Name |
Thyrotropin-releasing hormone-degrading ectoenzyme TRH-DE TRH-degrading ectoenzyme EC 3.4.19.6 Pyroglutamyl-peptidase II PAP-II TRH-specific aminopeptidase Thyroliberinase |
| Gene Name | Trhde |
| 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 | MGEDDAALRASGRGLSDPWADSVGVRPRTTERHIAVHKRLVLAFAVSIVALLAVTMLAVLLSLRFDECGASAAMPGTDGGLGGFPERGGNSSYPGSARRNHHAGEESSQREIGEVGTAGTPSAHPPSEEEQEQWQPWTQLRLSGHLKPLHYNLMLTAFMENFTFSGEVNVEIACQNATRYVVLHASRVAVEKVQVAEDRAFGAVPVAGFFLYPQTQVLVVVLNRTLDAQRHYNLKIIYNALIENELLGFFRSSYVIHGERRFLGVTQFSPTHARKAFPCFDEPIYKATFKISIKHQATYLSLSNMPVETSVFEEDGWVTDHFSQTPLMSTYYLAWAICNFTYRETTTKSGVVVRLYARPDAIRRGSGDYALHITKRLIEFYEDYFKVPYSLPKLDLLAVPKHPYAAMENWGLSIFVEQRILLDPSVSSISYLLDVTMVIVHEICHQWFGDLVTPVWWEDVWLKEGFAHYFEFVGTDYLYPSWNMEKQRFLTDVLHEVMLLDGLASSHPVSQEVLRATDIDKVFDWIAYKKGAALIRMLANFMGHSVFQRGLQDYLTIHKYGNAARNDLWNTLSEALKRNGKYVNIQEVMDQWTLQMGYPVITILGNMTAENRILITQQHFIYDIGAKTKALQLQNSSYLWQIPLTIVVGNRSHVSSEAIIWVSNKSEHHRITYLDKGSWILGNINQTGYFRVNYDLRNWRLLIDQLIRNHEVLSVSNRAGLIDDAFSLARAGYLPQNIPLEIIRYLSEEKDFLPWHAASRALYPLDKLLDRMENYNIFNEYILKQVATTYSKLGWPKNNFNGSVVQASYQHEELRREVIMLACSFGNKHCHQQASTLISDWISSNRNRIPLNVRDIVYCTGVSLLDEDVWEFIWMKFHSTTAVSEKKILLEALTCSDDRNLLSRLLNLSLNSEVVLDQDAIDVIIHVARNPHGRDLAWKFFRDKWKILNTRYGEALFMNSKLISGVTEFLNTEGELKELKNFMKSYDGVASASFSRAVETVEANVRWKRLYQDELFQWLGKAMRH |
| Enzyme Length | 1025 |
| Uniprot Accession Number | Q10836 |
| Absorption | |
| Active Site | ACT_SITE 442; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of the N-terminal pyroglutamyl group from pGlu-|-His-Xaa tripeptides and pGlu-|-His-Xaa-Gly tetrapeptides.; EC=3.4.19.6; |
| DNA Binding | |
| EC Number | 3.4.19.6 |
| Enzyme Function | FUNCTION: Specific inactivation of TRH after its release. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (1); Glycosylation (12); Metal binding (3); Modified residue (1); Region (2); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Aminopeptidase;Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Phosphoprotein;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. |
| Modified Residue | MOD_RES 30; /note=Phosphothreonine; by PKC; /evidence=ECO:0000255 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16611635; 19179432; 21329657; 22532627; 22719053; 25942072; |
| Motif | |
| Gene Encoded By | |
| Mass | 117,287 |
| Kinetics | |
| Metal Binding | METAL 441; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 445; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 464; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.19.6; |