| IED ID | IndEnz0002013993 |
| Enzyme Type ID | protease013993 |
| Protein Name |
Acrosin EC 3.4.21.10 Proacrosin Proacro1 Cleaved into: Acrosin light chain; Acrosin heavy chain |
| Gene Name | ACR |
| Organism | Meleagris gallopavo (Wild turkey) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Meleagridinae Meleagris Meleagris gallopavo (Wild turkey) |
| Enzyme Sequence | MALLLPLAVLLAACRPGHGFSGGCDTCGLRPVAYHYGGMRVVGGTEALHGSWPWIVSIQNPRFAGTGHMCGGSLITPQWVLSAAHCFGRPNYILQSRVVIGANDLTQLGQEVEVRSIRRAILHEYFNNKTMINDIALLELDRPVHCSYYIQLACVPDPSLRVSELTDCYVSGWGHMGMRSAAPTQTAEVLQEAKVHLLDLNLCNSSHWYDGVLHSHNLCAGYPQGGIDTCQGDSGGPLMCRDSSADYFWLVGVTSWGRGCGRAFRPGIYTSTQHFYNWILLQVRAAAHPTSRTWSHYMSTSSYHHGPNAVPTQPSVSDSCPFPAQKLREFFTGVQNLLQSLWGSKA |
| Enzyme Length | 346 |
| Uniprot Accession Number | Q2UVH8 |
| Absorption | |
| Active Site | ACT_SITE 85; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q9GL10; ACT_SITE 134; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q9GL10; ACT_SITE 234; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q9GL10 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by aprotinin, ovomucoid, soybean trypsin inhibitor, benzamidine, p-aminobenzamidine, and zinc ions. Activity also inhibited by a Kazal-type proteinase inhibitor. {ECO:0000269|PubMed:11665890, ECO:0000269|PubMed:1333593, ECO:0000269|PubMed:20561916}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.10; Evidence={ECO:0000250|UniProtKB:P10626}; |
| DNA Binding | |
| EC Number | 3.4.21.10 |
| Enzyme Function | FUNCTION: Serine protease of trypsin-like cleavage specificity. Synthesized in a zymogen form, proacrosin and stored in the acrosome (By similarity). {ECO:0000250|UniProtKB:P10626}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Active between 20.0-37.0 degrees Celsius. Activity increases above 25 degrees Celsius. {ECO:0000269|PubMed:11665890, ECO:0000269|PubMed:1333593}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:11665890, ECO:0000269|PubMed:1333593}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (3); Disulfide bond (6); Domain (1); Glycosylation (2); Propeptide (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. {ECO:0000269|PubMed:20561916, ECO:0000269|PubMed:3163935}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 37,950 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.17 mM for N-alpha-benzoyl-DL-arginine-p-nitroanilide (at 25 degrees Celsius) {ECO:0000269|PubMed:11665890, ECO:0000269|PubMed:1333593}; Vmax=1.50 mmol/min/mg enzyme toward N-alpha-benzoyl-DL-arginine-p-nitroanilide {ECO:0000269|PubMed:11665890, ECO:0000269|PubMed:1333593}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.10; |