IED ID | IndEnz0002004172 |
Enzyme Type ID | protease004172 |
Protein Name |
Neurotrypsin EC 3.4.21.- Serine protease 12 |
Gene Name | PRSS12 |
Organism | Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys) |
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) Hylobatidae (gibbons) Nomascus Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys) |
Enzyme Sequence | MTLARFVLALVLGALPEVVXFDSVLNDSLHHRPRHSPPTGPHYPYYLPTQQRPPRTRPPPPLPRFPRPPRALPAQRPHALQAGHTPRPHPWGCPAGEPWVSVTDFGAPCLRWAEVPPFLERSPPANWAQLRGQRHNFCRSPDGAGRPWCFYGDARGKVDWGYCDCRHGSIRLRGGKNEFEGTVEVYASGVWGTVCSSHWDDSDASVICHQLQLGGKGIAKQTPFSGLGLIPIYWSNVRCRGDEENILLCEKDIWQGGVCPQKMAAAVTCSFSHGPTFPIIRLVGGSSVHEGRVELYHAGQWGTVCDDQWDDADAEVICRQLGLSGIAKAWHQAYFGEGSGPVMLDEVRCTGNELSIEQCPKSSWGEHNCGHKEDAGVSCTPLTDGVIRLAGGKGSHEGRLEVYYRGQWGTVCDDGWTELNTYVVCRQLGFKYGKQASANHFEESTGPIWLDDVSCSGKETRFLQCSRRQWGRHDCSHREDVSIACYPGGEGHRLSLGFPVRLMDGENKKEGRVEVFINGQWGTICDDGWTDKDAAVICRQLGYKGPARARTMAYFGEGKGPIHVDNVKCTGNERSLADCIKQDIGRHNCRHSEDAGVICDYFGKKASGNSNKESLSSVCGLRLLHRRQKRIIGGKNSLRGGWPWQVSLRLKSSHGDGRLLCGATLLSSCWVLTAAHCFKRYGNSTRNYAVRVGDYHTLVPEEFEEEIGVQQIVIHREYRPDSSDYDIALVRLQGPEEQCARFSSHVLPACLPLWRERPQKTASNCYITGWGDTGRAYSRTLQQAAIPLLPKRFCEERYKGRFTGRMLCAGNLHEHKRVDSCQGDSGGPLMCERPGESWVVYGVTSWGHGCGVKDSPGVYTKVSAFVPWIKSVTKL |
Enzyme Length | 875 |
Uniprot Accession Number | Q5G268 |
Absorption | |
Active Site | ACT_SITE 676; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 726; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 825; /note=Charge relay system; /evidence=ECO:0000250 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.21.- |
Enzyme Function | FUNCTION: Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Compositional bias (1); Disulfide bond (20); Domain (6); Glycosylation (2); Region (2); Signal peptide (1); Site (1) |
Keywords | Disulfide bond;Glycoprotein;Hydrolase;Kringle;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 97,149 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |