| IED ID | IndEnz0002006691 |
| Enzyme Type ID | protease006691 |
| Protein Name |
Plasminogen activator inhibitor 1 PAI PAI-1 Endothelial plasminogen activator inhibitor Serpin E1 |
| Gene Name | SERPINE1 PAI1 PLANH1 |
| 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 | MQMSPALTCLVLGLALVFGEGSAVHHPPSYVAHLASDFGVRVFQQVAQASKDRNVVFSPYGVASVLAMLQLTTGGETQQQIQAAMGFKIDDKGMAPALRHLYKELMGPWNKDEISTTDAIFVQRDLKLVQGFMPHFFRLFRSTVKQVDFSEVERARFIINDWVKTHTKGMISNLLGKGAVDQLTRLVLVNALYFNGQWKTPFPDSSTHRRLFHKSDGSTVSVPMMAQTNKFNYTEFTTPDGHYYDILELPYHGDTLSMFIAAPYEKEVPLSALTNILSAQLISHWKGNMTRLPRLLVLPKFSLETEVDLRKPLENLGMTDMFRQFQADFTSLSDQEPLHVAQALQKVKIEVNESGTVASSSTAVIVSARMAPEEIIMDRPFLFVVRHNPTGTVLFMGQVMEP |
| Enzyme Length | 402 |
| Uniprot Accession Number | P05121 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Serine protease inhibitor. Inhibits TMPRSS7 (PubMed:15853774). Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots (PubMed:8481516, PubMed:9207454, PubMed:17912461). As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading (PubMed:9175705). Acts as a regulator of cell migration, independently of its role as protease inhibitor (PubMed:15001579, PubMed:9168821). It is required for stimulation of keratinocyte migration during cutaneous injury repair (PubMed:18386027). It is involved in cellular and replicative senescence (PubMed:16862142). Plays a role in alveolar type 2 cells senescence in the lung (By similarity). Is involved in the regulation of cementogenic differentiation of periodontal ligament stem cells, and regulates odontoblast differentiation and dentin formation during odontogenesis (PubMed:25808697, PubMed:27046084). {ECO:0000250|UniProtKB:P22777, ECO:0000269|PubMed:15001579, ECO:0000269|PubMed:15853774, ECO:0000269|PubMed:16862142, ECO:0000269|PubMed:17912461, ECO:0000269|PubMed:18386027, ECO:0000269|PubMed:25808697, ECO:0000269|PubMed:27046084, ECO:0000269|PubMed:8481516, ECO:0000269|PubMed:9168821, ECO:0000269|PubMed:9175705, ECO:0000269|PubMed:9207454}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (1); Beta strand (19); Chain (1); Glycosylation (3); Helix (14); Mutagenesis (2); Natural variant (5); Sequence conflict (6); Signal peptide (1); Site (1); Turn (5) |
| Keywords | 3D-structure;Alternative splicing;Direct protein sequencing;Glycoprotein;Protease inhibitor;Reference proteome;Secreted;Serine protease inhibitor;Signal |
| Interact With | Q8NBQ5; P02763; P78337; O43765; Q96EQ0; O43711; Q96Q45-2; Q9UMX0; Q9UMX0-2; Q9UHD9 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2430793}. |
| Modified Residue | |
| Post Translational Modification | PTM: Inactivated by proteolytic attack of the urokinase-type (u-PA) and the tissue-type (TPA), cleaving the 369-Arg-|-Met-370 bond. |
| Signal Peptide | SIGNAL 1..23 |
| Structure 3D | X-ray crystallography (29) |
| Cross Reference PDB | 1A7C; 1B3K; 1C5G; 1DB2; 1DVM; 1DVN; 1LJ5; 1OC0; 3CVM; 3EOX; 3PB1; 3Q02; 3Q03; 3R4L; 3UT3; 4AQH; 4G8O; 4G8R; 4IC0; 5BRR; 5ZLZ; 6GWN; 6GWP; 6GWQ; 6I8S; 6ZRV; 7AQF; 7AQG; 9PAI; |
| Mapped Pubmed ID | 10199400; 10494775; 10577569; 10618306; 10913251; 10961693; 11018023; 11037896; 11091191; 11168509; 11260416; 11332466; 11427204; 11427533; 11457467; 11485022; 11525425; 11558839; 11592048; 11738073; 11748101; 11780311; 11849662; 11908512; 11972486; 11979351; 12006921; 12027469; 12032637; 12064834; 12140748; 12362314; 12406875; 12431476; 12490312; 12499900; 12533669; 12589088; 12615788; 12660488; 12670745; 12738229; 12748347; 12765340; 12801613; 12808446; 12867763; 12899665; 12911596; 12960956; 1376317; 14515194; 14597935; 14605330; 14629464; 14631138; 14642005; 14642142; 14652637; 14653443; 14668616; 14706682; 14963283; 15051600; 15079805; 15191349; 15300646; 15313160; 15321757; 15333035; 15351855; 15481848; 15554360; 15630497; 15772559; 15820782; 15843979; 15853833; 15907980; 16272158; 16409202; 16416371; 16424345; 16472842; 16507937; 16508752; 16603315; 16703752; 16706983; 16713569; 16730474; 16735791; 16816071; 16857194; 16926677; 16938111; 16963292; 17036337; 17044080; 17062678; 17100549; 17100732; 17107352; 17160433; 17161063; 17199731; 17201588; 17263760; 17269998; 17351368; 17433639; 17438144; 17469143; 17513622; 17541549; 17549286; 17555513; 17559626; 17608581; 17616807; 18568018; 18725454; 18794724; 19059484; 19082507; 19282863; 19368854; 19387177; 19420105; 19559392; 21199867; 21697084; 21947232; 22449964; 22575643; 23155046; 23640497; 24265642; 24297881; 2503541; 25416956; 2544876; 26324706; 30733557; 31858714; 32824134; 33540702; 6457647; 7664104; 7892190; 8467233; 8571307; 8994417; 9157947; 9484978; 9493590; 9622220; |
| Motif | |
| Gene Encoded By | |
| Mass | 45,060 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |