ID CAP7_HUMAN Reviewed; 251 AA. AC P20160; P80014; Q52LG4; Q9UCM1; Q9UCT5; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 3. DT 24-JAN-2024, entry version 214. DE RecName: Full=Azurocidin {ECO:0000303|PubMed:2501794}; DE AltName: Full=Cationic antimicrobial protein CAP37 {ECO:0000303|PubMed:2226832}; DE AltName: Full=Heparin-binding protein {ECO:0000303|PubMed:2026172}; DE Short=HBP {ECO:0000303|PubMed:2026172}; DE Short=hHBP {ECO:0000303|PubMed:2026172}; DE Flags: Precursor; GN Name=AZU1 {ECO:0000312|HGNC:HGNC:913}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1919011; RA Morgan J.G., Sukiennicki T., Pereira H.A., Spitznagel J.K., Guerra M.E., RA Larrick J.L.; RT "Cloning of the cDNA for the serine protease homolog CAP37/azurocidin, a RT microbicidal and chemotactic protein from human granulocytes."; RL J. Immunol. 147:3210-3214(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1518849; DOI=10.1073/pnas.89.17.8215; RA Zimmer M., Medcalf R.L., Fink T.M., Mattmann C., Lichter P., Jenne D.E.; RT "Three human elastase-like genes coordinately expressed in the RT myelomonocyte lineage are organized as a single genetic locus on 19pter."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8215-8219(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-251. RC TISSUE=Neutrophil; RX PubMed=2049091; DOI=10.1016/0006-291x(91)91843-2; RA Almeida R.P., Melchior M., Campanelli D., Nathan C., Gabay J.E.; RT "Complementary DNA sequence of human neutrophil azurocidin, an antibiotic RT with extensive homology to serine proteases."; RL Biochem. Biophys. Res. Commun. 177:688-695(1991). RN [6] RP PROTEIN SEQUENCE OF 27-248. RX PubMed=2226832; DOI=10.1016/0014-5793(90)80484-z; RA Pohl J., Pereira H.A., Martin N.M., Spitznagel J.K.; RT "Amino acid sequence of CAP37, a human neutrophil granule-derived RT antibacterial and monocyte-specific chemotactic glycoprotein structurally RT similar to neutrophil elastase."; RL FEBS Lett. 272:200-204(1990). RN [7] RP PROTEIN SEQUENCE OF 27-248. RC TISSUE=Neutrophil; RX PubMed=2026172; DOI=10.1111/j.1432-1033.1991.tb15942.x; RA Flodgaard H., Oestergaard E., Bayne S., Svendsen A., Thomsen J., Engels M., RA Wollmer A.; RT "Covalent structure of two novel neutrophile leucocyte-derived proteins of RT porcine and human origin. Neutrophile elastase homologues with strong RT monocyte and fibroblast chemotactic activities."; RL Eur. J. Biochem. 197:535-547(1991). RN [8] RP PROTEIN SEQUENCE OF 27-68. RC TISSUE=Neutrophil; RX PubMed=2332502; DOI=10.1172/jci114593; RA Pereira H.A., Shafer W.M., Pohl J., Martin L.E., Spitznagel J.K.; RT "CAP37, a human neutrophil-derived chemotactic factor with monocyte RT specific activity."; RL J. Clin. Invest. 85:1468-1476(1990). RN [9] RP PROTEIN SEQUENCE OF 27-67. RC TISSUE=Neutrophil; RX PubMed=2406527; DOI=10.1016/0024-3205(90)90104-y; RA Pereira H.A., Spitznagel J.K., Pohl J., Wilson D.E., Morgan J., Palings I., RA Larrick J.W.; RT "CAP 37, a 37 kD human neutrophil granule cationic protein shares homology RT with inflammatory proteinases."; RL Life Sci. 46:189-196(1990). RN [10] RP PROTEIN SEQUENCE OF 27-48, AND FUNCTION. RC TISSUE=Leukocyte; RX PubMed=1937776; DOI=10.1128/iai.59.11.4193-4200.1991; RA Wasiluk K.R., Skubitz K.M., Gray B.H.; RT "Comparison of granule proteins from human polymorphonuclear leukocytes RT which are bactericidal toward Pseudomonas aeruginosa."; RL Infect. Immun. 59:4193-4200(1991). RN [11] RP PROTEIN SEQUENCE OF 27-47. RX PubMed=1897955; DOI=10.1016/0003-9861(91)90042-h; RA Green B.G., Weston H., Ashe B.M., Doherty J., Finke P., Hagmann W., RA Lark M., Mao J., Maycock A., Moore V., Mumford R., Shah S., Walakovits L., RA Knight W.B.; RT "PMN elastases: a comparison of the specificity of human isozymes and the RT enzyme from other species toward substrates and inhibitors."; RL Arch. Biochem. Biophys. 286:284-292(1991). RN [12] RP PROTEIN SEQUENCE OF 27-46, AND SUBCELLULAR LOCATION. RX PubMed=2501794; DOI=10.1073/pnas.86.14.5610; RA Gabay J.E., Scott R.W., Campanelli D., Griffith J., Wilde C., Marra M.N., RA Seeger M., Nathan C.F.; RT "Antibiotic proteins of human polymorphonuclear leukocytes."; RL Proc. Natl. Acad. Sci. U.S.A. 86:5610-5614(1989). RN [13] RP PROTEIN SEQUENCE OF 27-46 AND 194-217. RX PubMed=2404977; DOI=10.1016/s0021-9258(19)39936-3; RA Wilde C.G., Snable J.L., Griffith J.E., Scott R.W.; RT "Characterization of two azurphil granule proteases with active-site RT homology to neutrophil elastase."; RL J. Biol. Chem. 265:2038-2041(1990). RN [14] RP PROTEIN SEQUENCE OF 27-46, AND FUNCTION. RX PubMed=1399008; DOI=10.1128/iai.60.11.4973-4975.1992; RA Miyasaki K.T., Bodeau A.L.; RT "Human neutrophil azurocidin synergizes with leukocyte elastase and RT cathepsin G in the killing of Capnocytophaga sputigena."; RL Infect. Immun. 60:4973-4975(1992). RN [15] RP PROTEIN SEQUENCE OF 123-131, AND GLYCOSYLATION AT ASN-126. RX PubMed=26274980; DOI=10.3390/biom5031832; RA Loke I., Packer N.H., Thaysen-Andersen M.; RT "Complementary LC-MS/MS-Based N-Glycan, N-Glycopeptide, and Intact N- RT Glycoprotein Profiling Reveals Unconventional Asn71-Glycosylation of Human RT Neutrophil Cathepsin G."; RL Biomolecules 5:1832-1854(2015). RN [16] RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY. RX PubMed=2312733; DOI=10.1172/jci114518; RA Campanelli D., Detmers P.A., Nathan C.F., Gabay J.E.; RT "Azurocidin and a homologous serine protease from neutrophils. Differential RT antimicrobial and proteolytic properties."; RL J. Clin. Invest. 85:904-915(1990). RN [17] RP REVIEW. RX PubMed=1755383; DOI=10.1007/978-1-4684-6009-4_11; RA Morgan J.G., Pereira H.A., Sukiennicki T., Spitznagel J.K., Larrick J.W.; RT "Human neutrophil granule cationic protein CAP37 is a specific macrophage RT chemotaxin that shares homology with inflammatory proteinases."; RL Adv. Exp. Med. Biol. 305:89-96(1991). RN [18] RP SYNTHESIS OF 46-70, MUTAGENESIS OF CYS-52 AND CYS-68, AND REGION. RX PubMed=8506327; DOI=10.1073/pnas.90.10.4733; RA Pereira H.A., Erdem I., Pohl J., Spitznagel J.K.; RT "Synthetic bactericidal peptide based on CAP37: a 37-kDa human neutrophil RT granule-associated cationic antimicrobial protein chemotactic for RT monocytes."; RL Proc. Natl. Acad. Sci. U.S.A. 90:4733-4737(1993). RN [19] RP PROPEPTIDE CLEAVAGE. RX PubMed=10534120; DOI=10.1002/jlb.66.4.634; RA Lindmark A., Garwicz D., Rasmussen P.B., Flodgaard H., Gullberg U.; RT "Characterization of the biosynthesis, processing, and sorting of human RT HBP/CAP37/azurocidin."; RL J. Leukoc. Biol. 66:634-643(1999). RN [20] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-140 AND ASN-171. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=9095193; DOI=10.1038/nsb0497-265; RA Iversen L.F., Kastrup J.S., Bjoern S.E., Rasmussen P.B., Wiberg F.C., RA Flodgaard H.J., Larsen I.K.; RT "Structure of HBP, a multifunctional protein with a serine proteinase RT fold."; RL Nat. Struct. Biol. 4:265-268(1997). RN [24] RP X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=9761855; DOI=10.1107/s0907444997016193; RA Karlsen S., Iversen L.F., Larsen I.K., Flodgaard H.J., Kastrup J.S.; RT "Atomic resolution structure of human HBP/CAP37/azurocidin."; RL Acta Crystallogr. D 54:598-609(1998). CC -!- FUNCTION: This is a neutrophil granule-derived antibacterial and CC monocyte- and fibroblast-specific chemotactic glycoprotein. Binds CC heparin. The cytotoxic action is limited to many species of Gram- CC negative bacteria; this specificity may be explained by a strong CC affinity of the very basic N-terminal half for the negatively charged CC lipopolysaccharides that are unique to the Gram-negative bacterial CC outer envelope. It may play a role in mediating recruitment of CC monocytes in the second wave of inflammation. Has antibacterial CC activity against the Gram-negative bacterium P.aeruginosa, this CC activity is inhibited by LPS from P.aeruginosa. Acting alone, it does CC not have antimicrobial activity against the Gram-negative bacteria CC A.actinomycetemcomitans ATCC 29532, A.actinomycetemcomitans NCTC 9709, CC A.actinomycetemcomitans FDC-Y4, H.aphrophilus ATCC 13252, E.corrodens CC ATCC 23834, C.sputigena ATCC 33123, Capnocytophaga sp ATCC 33124, CC Capnocytophaga sp ATCC 27872 or E.coli ML-35. Has antibacterial CC activity against C.sputigena ATCC 33123 when acting synergistically CC with either elastase or cathepsin G. {ECO:0000269|PubMed:1399008, CC ECO:0000269|PubMed:1937776, ECO:0000269|PubMed:2312733}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule membrane CC {ECO:0000269|PubMed:2312733, ECO:0000269|PubMed:2501794}; Peripheral CC membrane protein {ECO:0000269|PubMed:2312733}; Cytoplasmic side CC {ECO:0000269|PubMed:2312733}. Note=Localizes to azurophil granules of CC neutrophil granulocytes. Also called primary granules, these CC specialized lysosomes of the neutrophil formed early during CC promyelocyte development store antibacterial proteins and peptides. CC {ECO:0000269|PubMed:2312733, ECO:0000269|PubMed:2501794}. CC -!- PTM: Cleavage of the N-terminal propeptide which is composed of 7 amino CC acids occurs in two steps. The initial cleavage of 5 amino acids is CC followed by the cleavage of a dipeptide to produce the mature form. CC {ECO:0000269|PubMed:10534120}. CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M96326; AAB59353.1; -; Genomic_DNA. DR EMBL; AC004799; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC069495; AAH69495.1; -; mRNA. DR EMBL; BC093931; AAH93931.1; -; mRNA. DR EMBL; BC093933; AAH93933.1; -; mRNA. DR EMBL; X58794; CAA41601.1; -; mRNA. DR CCDS; CCDS12044.1; -. DR PIR; A46268; TRHUAZ. DR RefSeq; NP_001691.1; NM_001700.4. DR PDB; 1A7S; X-ray; 1.12 A; A=27-251. DR PDB; 1AE5; X-ray; 2.30 A; A=27-251. DR PDB; 1FY1; X-ray; 2.50 A; A=27-251. DR PDB; 1FY3; X-ray; 1.89 A; A=27-251. DR PDBsum; 1A7S; -. DR PDBsum; 1AE5; -. DR PDBsum; 1FY1; -. DR PDBsum; 1FY3; -. DR AlphaFoldDB; P20160; -. DR BMRB; P20160; -. DR SMR; P20160; -. DR BioGRID; 107043; 26. DR IntAct; P20160; 15. DR MINT; P20160; -. DR STRING; 9606.ENSP00000233997; -. DR MEROPS; S01.971; -. DR GlyConnect; 1023; 3 N-Linked glycans (1 site). DR GlyCosmos; P20160; 3 sites, 3 glycans. DR GlyGen; P20160; 3 sites, 3 N-linked glycans (1 site). DR iPTMnet; P20160; -. DR BioMuta; AZU1; -. DR DMDM; 416746; -. DR EPD; P20160; -. DR jPOST; P20160; -. DR MassIVE; P20160; -. DR PaxDb; 9606-ENSP00000233997; -. DR PeptideAtlas; P20160; -. DR PRIDE; P20160; -. DR ProteomicsDB; 53732; -. DR Pumba; P20160; -. DR Antibodypedia; 22412; 351 antibodies from 27 providers. DR DNASU; 566; -. DR Ensembl; ENST00000233997.4; ENSP00000233997.1; ENSG00000172232.10. DR Ensembl; ENST00000620695.2; ENSP00000479183.1; ENSG00000278624.2. DR GeneID; 566; -. DR KEGG; hsa:566; -. DR MANE-Select; ENST00000233997.4; ENSP00000233997.1; NM_001700.5; NP_001691.1. DR UCSC; uc002lpz.2; human. DR AGR; HGNC:913; -. DR CTD; 566; -. DR DisGeNET; 566; -. DR GeneCards; AZU1; -. DR HGNC; HGNC:913; AZU1. DR HPA; ENSG00000172232; Tissue enriched (bone). DR MIM; 162815; gene. DR neXtProt; NX_P20160; -. DR OpenTargets; ENSG00000172232; -. DR PharmGKB; PA25206; -. DR VEuPathDB; HostDB:ENSG00000172232; -. DR eggNOG; KOG3627; Eukaryota. DR GeneTree; ENSGT01030000234551; -. DR HOGENOM; CLU_006842_1_0_1; -. DR InParanoid; P20160; -. DR OMA; TAYRSWI; -. DR OrthoDB; 4629979at2759; -. DR PhylomeDB; P20160; -. DR TreeFam; TF335284; -. DR PathwayCommons; P20160; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; P20160; -. DR BioGRID-ORCS; 566; 5 hits in 1145 CRISPR screens. DR EvolutionaryTrace; P20160; -. DR GeneWiki; Azurocidin_1; -. DR GenomeRNAi; 566; -. DR Pharos; P20160; Tbio. DR PRO; PR:P20160; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P20160; Protein. DR Bgee; ENSG00000172232; Expressed in bone marrow and 87 other cell types or tissues. DR ExpressionAtlas; P20160; baseline and differential. DR GO; GO:0042582; C:azurophil granule; IDA:UniProtKB. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0035577; C:azurophil granule membrane; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:UniProtKB. DR GO; GO:0008201; F:heparin binding; IMP:UniProtKB. DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0015643; F:toxic substance binding; NAS:UniProtKB. DR GO; GO:0019730; P:antimicrobial humoral response; IMP:UniProtKB. DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IGI:UniProtKB. DR GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB. DR GO; GO:0045123; P:cellular extravasation; NAS:UniProtKB. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; TAS:UniProtKB. DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB. DR GO; GO:0008347; P:glial cell migration; IDA:UniProtKB. DR GO; GO:0050930; P:induction of positive chemotaxis; NAS:UniProtKB. DR GO; GO:0006954; P:inflammatory response; NAS:UniProtKB. DR GO; GO:0048246; P:macrophage chemotaxis; NAS:UniProtKB. DR GO; GO:0001774; P:microglial cell activation; IEP:UniProtKB. DR GO; GO:0042117; P:monocyte activation; TAS:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; NAS:UniProtKB. DR GO; GO:0070944; P:neutrophil-mediated killing of bacterium; IDA:UniProtKB. DR GO; GO:0045785; P:positive regulation of cell adhesion; IDA:UniProtKB. DR GO; GO:0032724; P:positive regulation of fractalkine production; IDA:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB. DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:UniProtKB. DR GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IEP:UniProtKB. DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:UniProtKB. DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:UniProtKB. DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:UniProtKB. DR GO; GO:0070528; P:protein kinase C signaling; IMP:UniProtKB. DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; TAS:UniProtKB. DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB. DR GO; GO:0043114; P:regulation of vascular permeability; NAS:UniProtKB. DR CDD; cd00190; Tryp_SPc; 1. DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR PANTHER; PTHR24271:SF10; AZUROCIDIN; 1. DR PANTHER; PTHR24271; KALLIKREIN-RELATED; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR Genevisible; P20160; HS. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic; Antimicrobial; Chemotaxis; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Heparin-binding; KW Membrane; Reference proteome; Serine protease homolog; Signal; Zymogen. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:10534120" FT PROPEP 20..26 FT /note="Removed in mature form" FT /evidence="ECO:0000269|PubMed:10534120, FT ECO:0000269|PubMed:1399008, ECO:0000269|PubMed:1897955, FT ECO:0000269|PubMed:1937776, ECO:0000269|PubMed:2026172, FT ECO:0000269|PubMed:2226832, ECO:0000269|PubMed:2332502, FT ECO:0000269|PubMed:2404977, ECO:0000269|PubMed:2406527, FT ECO:0000269|PubMed:2501794" FT /id="PRO_0000435372" FT PROPEP 25..26 FT /note="Dipeptide found in non-mature form" FT /evidence="ECO:0000269|PubMed:10534120" FT /id="PRO_0000435373" FT CHAIN 27..248 FT /note="Azurocidin" FT /evidence="ECO:0000269|PubMed:2026172, FT ECO:0000269|PubMed:2226832" FT /id="PRO_0000027705" FT PROPEP 249..251 FT /note="Removed in mature form" FT /evidence="ECO:0000269|PubMed:2026172, FT ECO:0000269|PubMed:2226832" FT /id="PRO_0000027706" FT DOMAIN 27..244 FT /note="Peptidase S1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274" FT REGION 46..70 FT /note="Possesses antibiotic activity" FT /evidence="ECO:0000269|PubMed:8506327" FT CARBOHYD 126 FT /note="N-linked (GlcNAc...) asparagine; partial" FT /evidence="ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:2226832, ECO:0000269|PubMed:26274980" FT CARBOHYD 140 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:2226832" FT CARBOHYD 171 FT /note="N-linked (GlcNAc...) asparagine; partial" FT /evidence="ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:2226832" FT DISULFID 52..68 FT /evidence="ECO:0000269|PubMed:9095193, FT ECO:0000269|PubMed:9761855" FT DISULFID 149..207 FT /evidence="ECO:0000269|PubMed:9095193, FT ECO:0000269|PubMed:9761855" FT DISULFID 180..186 FT /evidence="ECO:0000269|PubMed:9095193, FT ECO:0000269|PubMed:9761855" FT DISULFID 197..222 FT /evidence="ECO:0000269|PubMed:9095193, FT ECO:0000269|PubMed:9761855" FT MUTAGEN 52 FT /note="C->S: Loss of antibiotic activity." FT /evidence="ECO:0000269|PubMed:8506327" FT MUTAGEN 68 FT /note="C->S: Loss of antibiotic activity." FT /evidence="ECO:0000269|PubMed:8506327" FT CONFLICT 36 FT /note="R -> H (in Ref. 13; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 130 FT /note="S -> N (in Ref. 7; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 41..46 FT /evidence="ECO:0007829|PDB:1A7S" FT STRAND 49..58 FT /evidence="ECO:0007829|PDB:1A7S" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:1A7S" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:1A7S" FT STRAND 76..82 FT /evidence="ECO:0007829|PDB:1A7S" FT TURN 91..93 FT /evidence="ECO:0007829|PDB:1A7S" FT STRAND 95..103 FT /evidence="ECO:0007829|PDB:1A7S" FT TURN 109..112 FT /evidence="ECO:0007829|PDB:1A7S" FT STRAND 117..123 FT /evidence="ECO:0007829|PDB:1A7S" FT STRAND 148..154 FT /evidence="ECO:0007829|PDB:1A7S" FT STRAND 157..160 FT /evidence="ECO:0007829|PDB:1FY1" FT STRAND 168..174 FT /evidence="ECO:0007829|PDB:1A7S" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:1A7S" FT STRAND 184..188 FT /evidence="ECO:0007829|PDB:1A7S" FT STRAND 190..193 FT /evidence="ECO:0007829|PDB:1A7S" FT STRAND 204..207 FT /evidence="ECO:0007829|PDB:1A7S" FT STRAND 210..218 FT /evidence="ECO:0007829|PDB:1A7S" FT STRAND 227..231 FT /evidence="ECO:0007829|PDB:1A7S" FT HELIX 232..235 FT /evidence="ECO:0007829|PDB:1A7S" FT HELIX 236..244 FT /evidence="ECO:0007829|PDB:1A7S" SQ SEQUENCE 251 AA; 26886 MW; 22F80D9EBE87DE60 CRC64; MTRLTVLALL AGLLASSRAG SSPLLDIVGG RKARPRQFPF LASIQNQGRH FCGGALIHAR FVMTAASCFQ SQNPGVSTVV LGAYDLRRRE RQSRQTFSIS SMSENGYDPQ QNLNDLMLLQ LDREANLTSS VTILPLPLQN ATVEAGTRCQ VAGWGSQRSG GRLSRFPRFV NVTVTPEDQC RPNNVCTGVL TRRGGICNGD GGTPLVCEGL AHGVASFSLG PCGRGPDFFT RVALFRDWID GVLNNPGPGP A //