| IED ID | IndEnz0002019332 |
| Enzyme Type ID | protease019332 |
| Protein Name |
Serine protease FAM111A EC 3.4.21.- |
| Gene Name | Fam111a |
| 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 | MSCKKRKSQISFNPRKNKKIKDYFSQVPKEEQNDPNTVKVDSKKMPRDITNTRDQRPLSPRKTRQDQTPPLNKKITVTLGVNSRKHKNMKYELTCRETSSLYAALNTLSAVREEVESQKGREMLVCGKEGIEGYLNLGMPVCCIPEGSHVVITFCQCKSKTQENKQFFESQDQASTNYVRFCIHAVGSKRKKILKCGELQKEGNKLCVYGFKGETIRDTLRKDGRFCTFIESDDWKLINDLDTIIENTQPVDELEGKLFQVAAELPKNPRVVSVTQNSGSENRNFHKLEEYIVNEYTTLKEEGKKLRAYIKEKSEKRKKKASLFKVHKEHFGKMTRNSTPVKVVKHLSRVSDSVGFLWWNNNGNAGCATCFVFKELYILTCQHVIASIVGEGIDSSEWANIISQCVKVTFDYEELLPTGDKFFMVKPWFEISDKHLDYAVLELKENGQEVPAGLYHRIRPVPHSGLIYIIGHPEGEKKSIDCCTVVPQSSRRKKCQENFQAREEAGFCFSTSFIHMYTQRSFQEMLHNSDVVTYDTSFFGGSSGSPVFDSNGSLVAMHAAGITCTYQAGVSNIIEFGSIMESIDDHMKQDKYKEWYNTISGNVQNVEMLSIDF |
| Enzyme Length | 613 |
| Uniprot Accession Number | Q9D2L9 |
| Absorption | |
| Active Site | ACT_SITE 383; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P06681; ACT_SITE 437; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:P06681; ACT_SITE 543; /note=Charge relay system; /evidence=ECO:0000250|UniProtKB:Q96PZ2 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Single-stranded DNA-binding serine protease that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde. Protects replication fork from stalling by removing DPCs, such as covalently trapped topoisomerase 1 (TOP1) adducts on DNA lesion, or poly(ADP-ribose) polymerase 1 (PARP1)-DNA complexes trapped by PARP inhibitors. Required for PCNA loading on replication sites. Promotes S-phase entry and DNA synthesis. {ECO:0000250|UniProtKB:Q96PZ2}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (1); Cross-link (3); Frameshift (1); Modified residue (1); Region (1); Sequence conflict (35); Site (1) |
| Keywords | Autocatalytic cleavage;Chromosome;Cytoplasm;DNA damage;DNA repair;DNA replication;DNA-binding;Hydrolase;Isopeptide bond;Nucleus;Phosphoprotein;Protease;Reference proteome;Ubl conjugation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96PZ2}. Chromosome {ECO:0000250|UniProtKB:Q96PZ2}. Cytoplasm {ECO:0000250|UniProtKB:Q96PZ2}. Note=Mainly localizes to nucleus: colocalizes with PCNA on replication sites. {ECO:0000250|UniProtKB:Q96PZ2}. |
| Modified Residue | MOD_RES 25; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q96PZ2 |
| Post Translational Modification | PTM: Autocatalytically cleaved; autocatalytic cleavage takes place in trans. {ECO:0000250|UniProtKB:Q96PZ2}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 14610273; 18554416; 21267068; 21677750; |
| Motif | |
| Gene Encoded By | |
| Mass | 69,949 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |