| IED ID | IndEnz0002002632 |
| Enzyme Type ID | protease002632 |
| Protein Name |
Neutrophil elastase EC 3.4.21.37 Bone marrow serine protease Elastase-2 Human leukocyte elastase HLE Medullasin PMN elastase |
| Gene Name | ELANE ELA2 |
| 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 | MTLGRRLACLFLACVLPALLLGGTALASEIVGGRRARPHAWPFMVSLQLRGGHFCGATLIAPNFVMSAAHCVANVNVRAVRVVLGAHNLSRREPTRQVFAVQRIFENGYDPVNLLNDIVILQLNGSATINANVQVAQLPAQGRRLGNGVQCLAMGWGLLGRNRGIASVLQELNVTVVTSLCRRSNVCTLVRGRQAGVCFGDSGSPLVCNGLIHGIASFVRGGCASGLYPDAFAPVAQFVNWIDSIIQRSEDNPCPHPRDPDPASRTH |
| Enzyme Length | 267 |
| Uniprot Accession Number | P08246 |
| Absorption | |
| Active Site | ACT_SITE 70; /note=Charge relay system; ACT_SITE 117; /note=Charge relay system; ACT_SITE 202; /note=Charge relay system |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins, including elastin. Preferential cleavage: Val-|-Xaa > Ala-|-Xaa.; EC=3.4.21.37; |
| DNA Binding | |
| EC Number | 3.4.21.37 |
| Enzyme Function | FUNCTION: Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (PubMed:15140022). Capable of killing E.coli but not S.aureus in vitro; digests outer membrane protein A (ompA) in E.coli and K.pneumoniae (PubMed:10947984). {ECO:0000269|PubMed:10947984, ECO:0000269|PubMed:15140022}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (18); Chain (1); Disulfide bond (4); Domain (1); Erroneous initiation (1); Glycosylation (3); Helix (4); Natural variant (93); Propeptide (1); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Cytoplasmic vesicle;Direct protein sequencing;Disease variant;Disulfide bond;Glycoprotein;Hydrolase;Protease;Reference proteome;Serine protease;Signal;Zymogen |
| Interact With | Q07563; P0DTC2 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:10947984}. Note=Localized in phagolysosomes following ingestion of E.coli by neutrophils. {ECO:0000269|PubMed:10947984}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (23) |
| Cross Reference PDB | 1B0F; 1H1B; 1HNE; 1PPF; 1PPG; 2RG3; 2Z7F; 3Q76; 3Q77; 4NZL; 4WVP; 5A09; 5A0A; 5A0B; 5A0C; 5A8X; 5A8Y; 5A8Z; 5ABW; 6E69; 6F5M; 6SMA; 7CBK; |
| Mapped Pubmed ID | 11846296; 11928814; 11948122; 12020136; 12042033; 12083479; 12114510; 12183836; 12190311; 12223522; 12393522; 12444202; 12483111; 12700588; 12745650; 12771009; 12778173; 12782302; 12853121; 12876407; 12887060; 12893759; 12934194; 1390635; 14587040; 14688365; 14705961; 14730209; 15010259; 15059607; 15131125; 1515454; 15161642; 15595387; 15601827; 15614130; 15657182; 15718918; 15892999; 15941909; 16079102; 16127146; 16148149; 16244764; 16282197; 16321984; 1649600; 16551967; 16670064; 16690986; 16799473; 17023068; 17088257; 17395013; 17397908; 17412886; 17622939; 17690184; 17761833; 17785837; 17853021; 17998887; 18021746; 18028488; 18043239; 18178964; 18194283; 18211966; 18278188; 18295791; 18318470; 18403643; 18421166; 18476621; 18485588; 18669870; 18710383; 18799464; 18980523; 19132232; 19180801; 19197381; 19251947; 19307610; 19362143; 19506020; 19542452; 19590686; 19620298; 19620402; 19763368; 19775295; 19789190; 20007580; 20033193; 20111696; 20179351; 20346360; 20354035; 20411049; 20423453; 20453419; 20521180; 20582973; 20627279; 20634941; 20646231; 20828556; 20883273; 20932306; 20974816; 21193404; 21206270; 21236472; 21448199; 21475777; 21477798; 21488974; 21549129; 21576245; 2159879; 21605276; 2176865; 21796505; 21843618; 21979170; 22174830; 22407864; 22444680; 22500123; 22683569; 22802338; 22810585; 22915586; 22918834; 22993338; 22996420; 23001948; 23351986; 23392769; 23454784; 23564510; 23650620; 23692169; 23741370; 23819644; 23911525; 24023624; 24052258; 24184683; 24513040; 24616599; 24816969; 24848868; 24914212; 24929239; 25092677; 25161283; 25195861; 25248056; 25284053; 25427142; 25461571; 25465717; 2546891; 25581168; 25652853; 25666548; 25857284; 25878251; 25893670; 25912133; 25956321; 26018813; 26083237; 26174650; 26193632; 26221769; 26269588; 26333652; 26358162; 26372354; 26444279; 26567890; 26874351; 26881964; 26939803; 27093231; 27101808; 27339896; 27892542; 27935111; 27942017; 28004483; 28073911; 28074935; 28187039; 28468826; 28507169; 28630087; 28754797; 28888033; 29046295; 29539421; 29624923; 29767240; 30056589; 30084397; 30143555; 30219097; 30343390; 30452386; 30635825; 30827416; 31009763; 31362723; 31466461; 31484779; 31490025; 31622584; 31626976; 31658467; 31749032; 31842908; 31887298; 31945345; 31963828; 31991297; 32176480; 32299910; 32303641; 32499333; 32657577; 32924109; 32981934; 32991313; 33085168; 33198714; 33510372; 33556558; 33560392; 33964209; 34130299; 34181952; 34261337; 34340247; 34439732; 34500777; 34536744; 34580954; 34681796; 8076699; 8223643; 8226919; 8380588; 8692836; 9404514; 9651152; |
| Motif | |
| Gene Encoded By | |
| Mass | 28,518 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.37; |