CAP7_HUMAN
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 03-AUG-2022, entry version 207.
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}.
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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 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; P20160; -.
DR PeptideAtlas; P20160; -.
DR PRIDE; P20160; -.
DR ProteomicsDB; 53732; -.
DR Antibodypedia; 22412; 308 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 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; 1314811at2759; -.
DR PhylomeDB; P20160; -.
DR TreeFam; TF335284; -.
DR PathwayCommons; P20160; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P20160; -.
DR BioGRID-ORCS; 566; 4 hits in 1067 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 tissues.
DR ExpressionAtlas; P20160; baseline and differential.
DR Genevisible; P20160; HS.
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:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
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; -; 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 Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
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
