| IED ID | IndEnz0002016541 |
| Enzyme Type ID | protease016541 |
| Protein Name |
Alpha-1-antichymotrypsin ACT Cell growth-inhibiting gene 24/25 protein Serpin A3 Cleaved into: Alpha-1-antichymotrypsin His-Pro-less |
| Gene Name | SERPINA3 AACT GIG24 GIG25 |
| 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 | MERMLPLLALGLLAAGFCPAVLCHPNSPLDEENLTQENQDRGTHVDLGLASANVDFAFSLYKQLVLKAPDKNVIFSPLSISTALAFLSLGAHNTTLTEILKGLKFNLTETSEAEIHQSFQHLLRTLNQSSDELQLSMGNAMFVKEQLSLLDRFTEDAKRLYGSEAFATDFQDSAAAKKLINDYVKNGTRGKITDLIKDLDSQTMMVLVNYIFFKAKWEMPFDPQDTHQSRFYLSKKKWVMVPMMSLHHLTIPYFRDEELSCTVVELKYTGNASALFILPDQDKMEEVEAMLLPETLKRWRDSLEFREIGELYLPKFSISRDYNLNDILLQLGIEEAFTSKADLSGITGARNLAVSQVVHKAVLDVFEEGTEASAATAVKITLLSALVETRTIVRFNRPFLMIIVPTDTQNIFFMSKVTNPKQA |
| Enzyme Length | 423 |
| Uniprot Accession Number | P01011 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | DNA_BIND 235..237 |
| EC Number | |
| Enzyme Function | FUNCTION: Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2. {ECO:0000269|PubMed:2404007}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (4); Beta strand (17); Chain (2); DNA binding (1); Erroneous initiation (3); Frameshift (2); Glycosylation (6); Helix (13); Natural variant (7); Region (2); Sequence conflict (10); Signal peptide (1); Site (1); Turn (5) |
| Keywords | 3D-structure;Acute phase;Alternative splicing;Direct protein sequencing;Disease variant;Glycoprotein;Protease inhibitor;Reference proteome;Secreted;Serine protease inhibitor;Signal |
| Interact With | P05067; P55212; Q96KC8; P13473-2; Q9Y371; Q9UNE7; Q9UBQ0-2; Q96AX1 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: N- and O-glycosylated. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:23234360}. |
| Signal Peptide | SIGNAL 1..23; /evidence=ECO:0000269|PubMed:2787670 |
| Structure 3D | X-ray crystallography (7) |
| Cross Reference PDB | 1AS4; 1QMN; 2ACH; 3CAA; 3DLW; 4CAA; 6HGE; |
| Mapped Pubmed ID | 10542979; 10766998; 11099722; 11132933; 11161981; 11290389; 11295654; 11385264; 11692021; 11715411; 11769703; 11798857; 11916200; 11936240; 11959399; 11992569; 12023832; 12126519; 12324297; 12600202; 12685871; 12736093; 12782964; 15159602; 15482730; 15530656; 15542006; 15546506; 15612581; 15653173; 15659365; 15718509; 15907346; 15935385; 16137793; 16278826; 16303762; 16424370; 16453284; 16565071; 16968986; 17690329; 17854420; 18056971; 18078695; 18248459; 18383875; 18401426; 18408372; 18842294; 18991685; 19008959; 19165527; 19247692; 19341158; 19390575; 19525388; 19590686; 1974162; 19789190; 19907165; 19913121; 19933216; 19959196; 20117085; 20158662; 20302328; 20378355; 20444200; 20628086; 20837024; 21067581; 21296644; 21674799; 21693707; 21730889; 21988832; 22246292; 22272609; 22294107; 22806587; 22869038; 23414517; 23640497; 23650620; 24817931; 25170552; 26210716; 26908325; 27492143; 29142239; 29855767; 31103428; 31121493; 31278347; 31439424; 31945348; 33249487; 33389566; 33436375; 33519818; 33569740; 33662018; 34077500; 34449972; 34861864; 6457647; 8467233; 8692836; 9003488; 9013407; 9922220; |
| Motif | |
| Gene Encoded By | |
| Mass | 47,651 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |