DEF4_PANTR
ID DEF4_PANTR Reviewed; 97 AA.
AC Q5G862;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Defensin alpha 4 {ECO:0000250|UniProtKB:P12838};
DE AltName: Full=Corticostatin HP-4 {ECO:0000250|UniProtKB:P12838};
DE AltName: Full=HNP-4 {ECO:0000250|UniProtKB:P12838};
DE Short=HP-4 {ECO:0000250|UniProtKB:P12838};
DE AltName: Full=Neutrophil defensin 4 {ECO:0000250|UniProtKB:P12838};
DE Flags: Precursor;
GN Name=DEFA4;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15494476; DOI=10.1152/physiolgenomics.00150.2004;
RA Patil A., Hughes A.L., Zhang G.;
RT "Rapid evolution and diversification of mammalian alpha-defensins as
RT revealed by comparative analysis of rodent and primate genes.";
RL Physiol. Genomics 20:1-11(2004).
CC -!- FUNCTION: Host-defense peptide that has antimicrobial activity against
CC Gram-negative bacteria, and to a lesser extent also against Gram-
CC positive bacteria and fungi (By similarity). Exhibits antimicrobial
CC activity against Gram-negative E.coli and E.aerogenes and Gram-positive
CC S.faecalis, S.aureus and B.cereus and the yeast C.albicans (in vitro)
CC (By similarity). Inhibits corticotropin (ACTH)-stimulated
CC corticosterone production (in vitro) (By similarity). Inhibits
CC enzymatic activity of B.anthracis lef/anthrax lethal factor (in vitro)
CC (By similarity). {ECO:0000250|UniProtKB:P12838}.
CC -!- SUBUNIT: Homodimer; homodimerization seems to be required for killing
CC S.aureus, but not E.coli (By similarity). Interacts with CD4 (By
CC similarity). Interacts with Bacillus anthracis lef; homodimerization is
CC required for the interaction (By similarity).
CC {ECO:0000250|UniProtKB:P12838}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q01523}.
CC Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P12838}.
CC Note=Stored as mature peptide in neutrophil granules.
CC {ECO:0000250|UniProtKB:P12838}.
CC -!- PTM: The three-dimensional structure formed by the three intramolecular
CC disulfide bridges is indispensable for effective bacterial killing.
CC {ECO:0000250|UniProtKB:P12838}.
CC -!- SIMILARITY: Belongs to the alpha-defensin family. {ECO:0000305}.
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DR EMBL; AY746438; AAW78341.1; -; mRNA.
DR RefSeq; NP_001029078.1; NM_001033906.1.
DR RefSeq; XP_009453052.1; XM_009454777.2.
DR AlphaFoldDB; Q5G862; -.
DR SMR; Q5G862; -.
DR PRIDE; Q5G862; -.
DR Ensembl; ENSPTRT00000036991; ENSPTRP00000034186; ENSPTRG00000034369.
DR GeneID; 463971; -.
DR KEGG; ptr:463971; -.
DR CTD; 1669; -.
DR GeneTree; ENSGT00940000153268; -.
DR InParanoid; Q5G862; -.
DR OMA; CRPAERR; -.
DR OrthoDB; 1610714at2759; -.
DR Proteomes; UP000002277; Chromosome 8.
DR Bgee; ENSPTRG00000034369; Expressed in bone marrow and 3 other tissues.
DR GO; GO:0042582; C:azurophil granule; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005796; C:Golgi lumen; IEA:UniProt.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0019732; P:antifungal humoral response; IEA:Ensembl.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0002227; P:innate immune response in mucosa; IBA:GO_Central.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0051673; P:membrane disruption in another organism; IBA:GO_Central.
DR InterPro; IPR016327; Alpha-defensin.
DR InterPro; IPR006081; Alpha-defensin_C.
DR InterPro; IPR002366; Alpha-defensin_propep.
DR InterPro; IPR006080; Defensin_beta/alpha.
DR PANTHER; PTHR11876; PTHR11876; 1.
DR Pfam; PF00323; Defensin_1; 1.
DR Pfam; PF00879; Defensin_propep; 1.
DR PIRSF; PIRSF001875; Alpha-defensin; 1.
DR SMART; SM00048; DEFSN; 1.
DR PROSITE; PS00269; DEFENSIN; 1.
PE 3: Inferred from homology;
KW Antibiotic; Antimicrobial; Cytoplasmic vesicle; Defensin; Disulfide bond;
KW Fungicide; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..63
FT /id="PRO_0000006784"
FT PEPTIDE 64..96
FT /note="Defensin alpha 4"
FT /evidence="ECO:0000250|UniProtKB:P12838"
FT /id="PRO_0000006785"
FT PROPEP 97
FT /id="PRO_0000455665"
FT DISULFID 65..93
FT /evidence="ECO:0000250|UniProtKB:P12838"
FT DISULFID 67..82
FT /evidence="ECO:0000250|UniProtKB:P12838"
FT DISULFID 72..92
FT /evidence="ECO:0000250|UniProtKB:P12838"
SQ SEQUENCE 97 AA; 10504 MW; F914434364E97F86 CRC64;
MRIIAILAAI LLVALQVRAG PLQARGDEAP GQEQRGPEDQ DISISFAWDK SSALQVSGST
RGMVCSCRLV FCRRTELRVG NCLIGGVSFT YCCTRVD
