| IED ID | IndEnz0002006144 |
| Enzyme Type ID | protease006144 |
| Protein Name |
Polyserase-2 EC 3.4.21.- Polyserine protease 2 Serine protease 36 |
| Gene Name | Prss36 |
| 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 | MSHHLFLPVVIMVVSPIPPGAFQDSVVSPTQGEFEDLDCGDCGRPEPSSRIVGGSDAHPGTWPWQVSLHQGGGHICGGSLIAPSWVLSAAHCFVTNGTLEPADELSVLLGVHSQDGPLEGAHMRSVATILIPDNYSTVELGADLALLRLASPAKLGPSVRGADLALLRLASPAKLGPSVRPVCLPRASHLFAHGTACWATGWGDVQEAVPLPLPWVLQEVELRLLGEAACQCLYSRPGPFNLTFQLLPGMLCAGYPAGRRDTCQGDSGGPLVCEDGGRWFLAGITSFGFGCGRRNRPGVFTAVAPYESWIREHVMGSEPGPVFPSQLQKPQSGPWEPREENCTFAQPECGKAPRPGTWPWEAQVTVPGSTPCYGALVSDRWVLAPASCFLDSPHDFETWRVLLPSRPEEERVARLVAHENASRDFASDLALLQLRTRVNLTAAPSAVCLPHHEHYFLPGSHCRLARWGRGELAPGSSAQLEAQLLNGWWCHCLYGRQGETVPRPGDPPHLLCPAYQEEEEAGLCWVDSSWSLLCREEGTWFLAGYRTLSDGCLRPRAFSPMQTHGPWIRHVTQGAYLEDQLTWDWGPEGEETEKQTCPTHTEHGACGLRPKSTPAGVLWPWLTEVHVTGDRVCTGILVAPGWVLAATHCILRLGSTTVPYIEVYLGRAGVSSLPQGHQVSRSVVSIRLPRHLGLRPPLALLELNSRVEPSPSALPICLHPGGIPSGASCWVLGWKNPQDRVPVVAAVSILTPRLCHCLYPGILTPGTFCVLYSEGQEDRCEVTSAPPLLCQTEEGPWVLVGMAVRGNRELFAAIGPEATWISQTVGEAHFLHLGGSSYWSPEGSDLCPQDLAGSASSPKVTALLLLLLLAPLIPR |
| Enzyme Length | 875 |
| Uniprot Accession Number | Q5K2P9 |
| Absorption | |
| Active Site | ACT_SITE 91; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 163; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 267; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by serine proteinase inhibitor 4-(2-aminoethyl)-benzenesulfonyl fluoride, but not with EDTA or E-64. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine protease. Hydrolyzes the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC and, to a lesser extent, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Val-Leu-Lys-AMC. Has a preference for substrates with an Arg instead of a Lys residue in position P1 (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (11); Domain (3); Glycosylation (6); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Disulfide bond;Extracellular matrix;Glycoprotein;Hydrolase;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Not attached to membranes. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: The 3 protease domains are not proteolytically cleaved. {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 94,483 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |