CAP7_PIG
ID CAP7_PIG Reviewed; 246 AA.
AC P80015;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Azurocidin {ECO:0000250|UniProtKB:P20160};
DE AltName: Full=Cationic antimicrobial protein CAP37 {ECO:0000250|UniProtKB:P20160};
DE AltName: Full=Heparin-binding protein {ECO:0000303|PubMed:2026172};
DE Short=HBP {ECO:0000303|PubMed:2026172};
DE Short=pHBP {ECO:0000303|PubMed:2026172};
DE Flags: Precursor;
GN Name=AZU1 {ECO:0000250|UniProtKB:P20160};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Porcine genome sequencing project;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 27-245, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP FUNCTION.
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 [3]
RP PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-139 AND
RP ASN-170, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=2076469; DOI=10.1002/bms.1200191110;
RA Sorensen H.H., Thomsen J., Bayne S., Hojrup P., Roepstorff P.;
RT "Strategies for determination of disulphide bridges in proteins using
RT plasma desorption mass spectrometry.";
RL Biomed. Environ. Mass Spectrom. 19:713-720(1990).
CC -!- FUNCTION: This is a neutrophil granule-derived antibacterial and
CC monocyte- and fibroblast-specific chemotactic glycoprotein. Binds
CC heparin. {ECO:0000250|UniProtKB:P20160, ECO:0000269|PubMed:2026172}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule membrane
CC {ECO:0000250|UniProtKB:P20160}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P20160}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P20160}. 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:0000250|UniProtKB:P20160}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. Elastase subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00274}.
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DR EMBL; JH115037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S15393; TRPGAZ.
DR RefSeq; XP_005661477.1; XM_005661420.2.
DR AlphaFoldDB; P80015; -.
DR SMR; P80015; -.
DR STRING; 9823.ENSSSCP00000014264; -.
DR MEROPS; S01.971; -.
DR iPTMnet; P80015; -.
DR PaxDb; P80015; -.
DR PeptideAtlas; P80015; -.
DR PRIDE; P80015; -.
DR Ensembl; ENSSSCT00000014659; ENSSSCP00000014264; ENSSSCG00000013415.
DR Ensembl; ENSSSCT00005029743; ENSSSCP00005018106; ENSSSCG00005018835.
DR Ensembl; ENSSSCT00015081055; ENSSSCP00015032789; ENSSSCG00015060634.
DR Ensembl; ENSSSCT00025010233; ENSSSCP00025004099; ENSSSCG00025007701.
DR Ensembl; ENSSSCT00030023951; ENSSSCP00030010745; ENSSSCG00030017322.
DR Ensembl; ENSSSCT00035100473; ENSSSCP00035042669; ENSSSCG00035074066.
DR Ensembl; ENSSSCT00040088326; ENSSSCP00040038828; ENSSSCG00040064681.
DR Ensembl; ENSSSCT00045052007; ENSSSCP00045036193; ENSSSCG00045030459.
DR Ensembl; ENSSSCT00055047471; ENSSSCP00055037890; ENSSSCG00055024074.
DR Ensembl; ENSSSCT00065009896; ENSSSCP00065004119; ENSSSCG00065007386.
DR Ensembl; ENSSSCT00070053760; ENSSSCP00070045580; ENSSSCG00070026803.
DR GeneID; 100522363; -.
DR KEGG; ssc:100522363; -.
DR CTD; 566; -.
DR VGNC; VGNC:85714; AZU1.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT01030000234551; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P80015; -.
DR OMA; TAYRSWI; -.
DR OrthoDB; 1314811at2759; -.
DR TreeFam; TF335284; -.
DR Proteomes; UP000008227; Chromosome 2.
DR Proteomes; UP000314985; Chromosome 2.
DR Bgee; ENSSSCG00000013415; Expressed in blood and 8 other tissues.
DR ExpressionAtlas; P80015; differential.
DR Genevisible; P80015; SS.
DR GO; GO:0042582; C:azurophil granule; ISS:UniProtKB.
DR GO; GO:0035577; C:azurophil granule membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:Ensembl.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0019730; P:antimicrobial humoral response; IEA:Ensembl.
DR GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IEA:Ensembl.
DR GO; GO:0060326; P:cell chemotaxis; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0008347; P:glial cell migration; ISS:UniProtKB.
DR GO; GO:0001774; P:microglial cell activation; ISS:UniProtKB.
DR GO; GO:0070944; P:neutrophil-mediated killing of bacterium; IEA:Ensembl.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0032724; P:positive regulation of fractalkine production; ISS:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0070528; P:protein kinase C signaling; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:Ensembl.
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 Antibiotic; Antimicrobial; Chemotaxis; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Heparin-binding; Membrane;
KW Reference proteome; Serine protease homolog; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000250|UniProtKB:P20160"
FT PROPEP 20..26
FT /evidence="ECO:0000305|PubMed:2026172"
FT /id="PRO_0000435374"
FT CHAIN 27..245
FT /note="Azurocidin"
FT /evidence="ECO:0000269|PubMed:2026172"
FT /id="PRO_0000088679"
FT PROPEP 245..246
FT /evidence="ECO:0000269|PubMed:2026172"
FT /id="PRO_0000435375"
FT DOMAIN 27..242
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2076469"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2076469"
FT DISULFID 52..68
FT /evidence="ECO:0000269|PubMed:2076469"
FT DISULFID 148..205
FT /evidence="ECO:0000269|PubMed:2076469"
FT DISULFID 178..184
FT /evidence="ECO:0000269|PubMed:2076469"
SQ SEQUENCE 246 AA; 27039 MW; E0731B1E2BA4A447 CRC64;
MPALRFLALL ASLLATSRVG LATLADIVGG RRAQPQEFPF LASIQKQGRP FCAGALVHPR
FVLTAASCFR GKNSGSASVV LGAYDLRQQE QSRQTFSIRS ISQNGYDPRQ NLNDVLLLQL
DREARLTPSV ALVPLPPQNA TVEAGTNCQV AGWGTQRLRR LFSRFPRVLN VTVTSNPCLP
RDMCIGVFSR RGRISQGDRG TPLVCNGLAQ GVASFLRRRF RRSSGFFTRV ALFRNWIDSV
LNNPPA
