| IED ID | IndEnz0002018449 |
| Enzyme Type ID | protease018449 |
| Protein Name |
Azurocidin Cationic antimicrobial protein CAP37 Heparin-binding protein HBP hHBP |
| Gene Name | AZU1 |
| 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 | MTRLTVLALLAGLLASSRAGSSPLLDIVGGRKARPRQFPFLASIQNQGRHFCGGALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRRRERQSRQTFSISSMSENGYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGSQRSGGRLSRFPRFVNVTVTPEDQCRPNNVCTGVLTRRGGICNGDGGTPLVCEGLAHGVASFSLGPCGRGPDFFTRVALFRDWIDGVLNNPGPGPA |
| Enzyme Length | 251 |
| Uniprot Accession Number | P20160 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: This is a neutrophil granule-derived antibacterial and monocyte- and fibroblast-specific chemotactic glycoprotein. Binds heparin. The cytotoxic action is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. It may play a role in mediating recruitment of monocytes in the second wave of inflammation. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa. Acting alone, it does not have antimicrobial activity against the Gram-negative bacteria A.actinomycetemcomitans ATCC 29532, A.actinomycetemcomitans NCTC 9709, A.actinomycetemcomitans FDC-Y4, H.aphrophilus ATCC 13252, E.corrodens ATCC 23834, C.sputigena ATCC 33123, Capnocytophaga sp ATCC 33124, Capnocytophaga sp ATCC 27872 or E.coli ML-35. Has antibacterial activity against C.sputigena ATCC 33123 when acting synergistically with either elastase or cathepsin G. {ECO:0000269|PubMed:1399008, ECO:0000269|PubMed:1937776, ECO:0000269|PubMed:2312733}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (14); Chain (1); Disulfide bond (4); Domain (1); Glycosylation (3); Helix (4); Mutagenesis (2); Propeptide (3); Region (1); Sequence conflict (2); Signal peptide (1); Turn (2) |
| Keywords | 3D-structure;Antibiotic;Antimicrobial;Chemotaxis;Direct protein sequencing;Disulfide bond;Glycoprotein;Heparin-binding;Membrane;Reference proteome;Serine protease homolog;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic granule membrane {ECO:0000269|PubMed:2312733, ECO:0000269|PubMed:2501794}; Peripheral membrane protein {ECO:0000269|PubMed:2312733}; Cytoplasmic side {ECO:0000269|PubMed:2312733}. Note=Localizes to azurophil granules of neutrophil granulocytes. Also called primary granules, these specialized lysosomes of the neutrophil formed early during promyelocyte development store antibacterial proteins and peptides. {ECO:0000269|PubMed:2312733, ECO:0000269|PubMed:2501794}. |
| Modified Residue | |
| Post Translational Modification | PTM: Cleavage of the N-terminal propeptide which is composed of 7 amino acids occurs in two steps. The initial cleavage of 5 amino acids is followed by the cleavage of a dipeptide to produce the mature form. {ECO:0000269|PubMed:10534120}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000269|PubMed:10534120 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1A7S; 1AE5; 1FY1; 1FY3; |
| Mapped Pubmed ID | 11170199; 11861296; 11891183; 11994286; 12054586; 12135665; 12438368; 12826073; 14515154; 15020208; 15879141; 17174955; 18346022; 18624398; 18787642; 19151333; 19590686; 20056178; 20083497; 20107486; 20399025; 22207392; 22278372; 23808364; 23883488; 23902751; 25412625; 26170148; 29288710; 32156261; 33454168; 33868298; 34151489; 34418081; 34495248; 8692836; |
| Motif | |
| Gene Encoded By | |
| Mass | 26,886 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |