| IED ID | IndEnz0002001506 |
| Enzyme Type ID | protease001506 |
| Protein Name |
Sentrin-specific protease 7 EC 3.4.22.- SUMO-1-specific protease 2 Sentrin/SUMO-specific protease SENP7 |
| Gene Name | SENP7 KIAA1707 SSP2 SUSP2 |
| Organism | Homo sapiens (Human) |
| 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) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MDKRKLGRRPSSSEIITEGKRKKSSSDLSEIRKMLNAKPEDVHVQSPLSKFRSSERWTLPLQWERSLRNKVISLDHKNKKHIRGCPVTSKSSPERQLKVMLTNVLWTDLGRKFRKTLPRNDANLCDANKVQSDSLPSTSVDSLETCQKLEPLRQSLNLSERIPRVILTNVLGTELGRKYIRTPPVTEGSLSDTDNLQSEQLSSSSDGSLESYQNLNPHKSCYLSERGSQRSKTVDDNSAKQTAHNKEKRRKDDGISLLISDTQPEDLNSGSRGCDHLEQESRNKDVKYSDSKVELTLISRKTKRRLRNNLPDSQYCTSLDKSTEQTKKQEDDSTISTEFEKPSENYHQDPKLPEEITTKPTKSDFTKLSSLNSQELTLSNATKSASAGSTTETVENSNSIDIVGISSLVEKDENELNTIEKPILRGHNEGNQSLISAEPIVVSSDEEGPVEHKSSEILKLQSKQDRETTNENESTSESALLELPLITCESVQMSSELCPYNPVMENISSIMPSNEMDLQLDFIFTSVYIGKIKGASKGCVTITKKYIKIPFQVSLNEISLLVDTTHLKRFGLWKSKDDNHSKRSHAILFFWVSSDYLQEIQTQLEHSVLSQQSKSSEFIFLELHNPVSQREELKLKDIMTEISIISGELELSYPLSWVQAFPLFQNLSSKESSFIHYYCVSTCSFPAGVAVAEEMKLKSVSQPSNTDAAKPTYTFLQKQSSGCYSLSITSNPDEEWREVRHTGLVQKLIVYPPPPTKGGLGVTNEDLECLEEGEFLNDVIIDFYLKYLILEKASDELVERSHIFSSFFYKCLTRKENNLTEDNPNLSMAQRRHKRVRTWTRHINIFNKDYIFVPVNESSHWYLAVICFPWLEEAVYEDFPQTVSQQSQAQQSQNDNKTIDNDLRTTSTLSLSAEDSQSTESNMSVPKKMCKRPCILILDSLKAASVQNTVQNLREYLEVEWEVKLKTHRQFSKTNMVDLCPKVPKQDNSSDCGVYLLQYVESFFKDPIVNFELPIHLEKWFPRHVIKTKREDIRELILKLHLQQQKGSSS |
| Enzyme Length | 1050 |
| Uniprot Accession Number | Q9BQF6 |
| Absorption | |
| Active Site | ACT_SITE 860; /evidence=ECO:0000250|UniProtKB:Q9HC62; ACT_SITE 939; /evidence=ECO:0000250|UniProtKB:Q9HC62; ACT_SITE 992; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:Q9HC62 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Protease that acts as a positive regulator of the cGAS-STING pathway by catalyzing desumoylation of CGAS. Desumoylation of CGAS promotes DNA-binding activity of CGAS, subsequent oligomerization and activation (By similarity). Deconjugates SUMO2 and SUMO3 from targeted proteins, but not SUMO1 (PubMed:18799455). Catalyzes the deconjugation of poly-SUMO2 and poly-SUMO3 chains (PubMed:18799455). Has very low efficiency in processing full-length SUMO proteins to their mature forms (PubMed:18799455). {ECO:0000250|UniProtKB:Q8BUH8, ECO:0000269|PubMed:18799455}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (5); Beta strand (7); Chain (1); Compositional bias (5); Helix (11); Modified residue (8); Mutagenesis (2); Natural variant (2); Region (5); Sequence conflict (7); Turn (1) |
| Keywords | 3D-structure;Alternative splicing;Cytoplasm;Hydrolase;Immunity;Innate immunity;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | P45973; Q13263 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BUH8}. |
| Modified Residue | MOD_RES 11; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 12; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q8BUH8"; MOD_RES 13; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:D3ZF42"; MOD_RES 25; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19690332"; MOD_RES 373; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 433; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 443; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"; MOD_RES 444; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 3EAY; |
| Mapped Pubmed ID | 16147992; 20562864; 21878624; 23045645; 24018422; 25895136; 28429743; 29777712; 31825833; |
| Motif | |
| Gene Encoded By | |
| Mass | 119,658 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.22.B75; |