DEF5_PANTR
ID DEF5_PANTR Reviewed; 94 AA.
AC Q5G861;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Defensin alpha 5 {ECO:0000305};
DE AltName: Full=Defensin-5 {ECO:0000305};
DE AltName: Full=HD5(20-94) {ECO:0000305};
DE Contains:
DE RecName: Full=HD5(23-94) {ECO:0000305};
DE Contains:
DE RecName: Full=HD5(29-94) {ECO:0000305};
DE Contains:
DE RecName: Full=HD5(56-94) {ECO:0000305};
DE Contains:
DE RecName: Full=HD5(63-94) {ECO:0000305};
DE Flags: Precursor;
GN Name=DEFA5;
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 maintains sterility in the
CC urogenital system (By similarity). Has antimicrobial activity against a
CC wide range of bacteria, including Gram-negative E.coli, P.aeruginosa
CC and S.typhimurium, and Gram-positive E.aerogenes, S.aureus, B. cereus,
CC E.faecium and L.monocytogenes (By similarity). Confers resistance to
CC intestinal infection by S.typhimurium (By similarity). Exhibits
CC antimicrobial activity against enteric commensal bacteria such as
CC B.adolescentis, L.acidophilus, B.breve, L.fermentum, B.longum and
CC S.thermophilus (By similarity). Binds to bacterial membranes and causes
CC membrane disintegration (By similarity). Induces the secretion of the
CC chemokine IL-8 by intestinal epithelial cells (By similarity). Binds to
CC B.antracis lef/lethal factor, a major virulence factor from
CC B.anthracis, and neutralizes its enzymatic activity (By similarity).
CC {ECO:0000250|UniProtKB:Q01523}.
CC -!- SUBUNIT: Homodimer (By similarity). Homotetramer (By similarity).
CC Interacts with B.antracis lef/lethal factor (By similarity).
CC {ECO:0000250|UniProtKB:Q01523}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q01523}.
CC Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q01523}.
CC Note=Stored as propeptide HD5(20-94) in secretory granules of small
CC intestinal Paneth cells and found in the ileum lumen as processed
CC mature peptides, predominantly in the HD5(63-94) form. Peptides HD5(20-
CC 94), HD5(23-94) and HD5(29-94) are found within tissues, HD5(20-94)
CC being the predominant intracellular form. Peptides HD5(56-94) and
CC HD5(63-94) are found in the extracellular milieu, HD5(63-94) being the
CC most abundant form (By similarity). Secreted into the female genital
CC tract lumen (By similarity). {ECO:0000250|UniProtKB:Q01523}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q01523}.
CC -!- PTM: Proteolytically cleaved at Arg-62 by trypsin (By similarity). Both
CC the propeptide form proHD5/HD5(20-94) and HD5(56-94) are cleaved into
CC the lumenal peptide form HD5(63-94) by trypsin (By similarity).
CC Unprocessed proHD5 exerts antimicrobial activities, but peptide potency
CC is enhanced by peptide processing (By similarity). Proteolytically
CC cleaved in duodenal fluid; derived fragments are antimicrobially active
CC against commensal bacteria (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:Q01523}.
CC -!- SIMILARITY: Belongs to the alpha-defensin family. {ECO:0000305}.
CC -!- CAUTION: It was shown by two studies that dimerization of DEFA5 is
CC crucial for antimicrobial activity (By similarity). Another study,
CC however, states that dimer formation is not indispensable for
CC antimicrobial activity of DEFA5 (By similarity).
CC {ECO:0000250|UniProtKB:Q01523}.
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DR EMBL; AY746439; AAW78342.1; -; mRNA.
DR RefSeq; NP_001012657.1; NM_001012639.1.
DR AlphaFoldDB; Q5G861; -.
DR SMR; Q5G861; -.
DR STRING; 9598.ENSPTRP00000034189; -.
DR PaxDb; Q5G861; -.
DR PRIDE; Q5G861; -.
DR Ensembl; ENSPTRT00000103608; ENSPTRP00000072107; ENSPTRG00000049316.
DR GeneID; 463972; -.
DR KEGG; ptr:463972; -.
DR CTD; 1670; -.
DR VGNC; VGNC:3022; DEFA5.
DR eggNOG; ENOG502T2EX; Eukaryota.
DR GeneTree; ENSGT00940000153268; -.
DR HOGENOM; CLU_160803_3_0_1; -.
DR InParanoid; Q5G861; -.
DR OMA; ESHTGRC; -.
DR OrthoDB; 1610714at2759; -.
DR TreeFam; TF338414; -.
DR Proteomes; UP000002277; Chromosome 8.
DR Bgee; ENSPTRG00000049316; Expressed in testis.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005796; C:Golgi lumen; IEA:UniProt.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISS:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR GO; GO:0002227; P:innate immune response in mucosa; IBA:GO_Central.
DR GO; GO:0051873; P:killing by host of symbiont cells; IEA:Ensembl.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0051673; P:membrane disruption in another organism; ISS:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:UniProtKB.
DR GO; GO:1905710; P:positive regulation of membrane permeability; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
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; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PEPTIDE 20..94
FT /note="Defensin alpha 5"
FT /id="PRO_0000006789"
FT PEPTIDE 23..94
FT /note="HD5(23-94)"
FT /evidence="ECO:0000250|UniProtKB:Q01523"
FT /id="PRO_0000417391"
FT PEPTIDE 29..94
FT /note="HD5(29-94)"
FT /evidence="ECO:0000250|UniProtKB:Q01523"
FT /id="PRO_0000417392"
FT PEPTIDE 56..94
FT /note="HD5(56-94)"
FT /evidence="ECO:0000250|UniProtKB:Q01523"
FT /id="PRO_0000417393"
FT PEPTIDE 63..94
FT /note="HD5(63-94)"
FT /evidence="ECO:0000250|UniProtKB:Q01523"
FT /id="PRO_0000417394"
FT DISULFID 65..93
FT /evidence="ECO:0000250|UniProtKB:Q01523"
FT DISULFID 67..82
FT /evidence="ECO:0000250|UniProtKB:Q01523"
FT DISULFID 72..92
FT /evidence="ECO:0000250|UniProtKB:Q01523"
SQ SEQUENCE 94 AA; 10063 MW; B81361D1C9CEA17A CRC64;
MRTIAILAAI LLVALQAQAE SLQERADEAT TQKQSGEDNQ DLAISFAGNG LSALRTSGSQ
ARATCYCRIG HCTILESLSG VCEISGRLYR LCCR
