DEF1_PANTR
ID DEF1_PANTR Reviewed; 94 AA.
AC Q5G863;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Neutrophil defensin 1;
DE AltName: Full=Defensin, alpha 1;
DE Flags: Precursor;
GN Name=DEFA1;
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: Has antibacterial, fungicide and antiviral activities. Has
CC antimicrobial activity against Gram-negative and Gram-positive
CC bacteria. Defensins are thought to kill microbes by permeabilizing
CC their plasma membrane (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Dimer. Interacts with RETN. {ECO:0000250|UniProtKB:P59665}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: ADP-ribosylation drastically reduces cytotoxic and antibacterial
CC activities, and enhances IL8 production. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alpha-defensin family. {ECO:0000305}.
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DR EMBL; AY746437; AAW78340.1; -; mRNA.
DR AlphaFoldDB; Q5G863; -.
DR SMR; Q5G863; -.
DR PRIDE; Q5G863; -.
DR Ensembl; ENSPTRT00000084879; ENSPTRP00000079419; ENSPTRG00000050573.
DR GeneTree; ENSGT00940000153268; -.
DR InParanoid; Q5G863; -.
DR OMA; ISFAWDE; -.
DR Proteomes; UP000002277; Unplaced.
DR Bgee; ENSPTRG00000050573; Expressed in bone marrow and 14 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005796; C:Golgi lumen; IEA:UniProt.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
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:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
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:0051607; P:defense response to virus; IEA:UniProtKB-KW.
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 ADP-ribosylation; Antibiotic; Antimicrobial; Antiviral defense; Defensin;
KW Disulfide bond; Fungicide; Phosphoprotein; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT PROPEP 20..64
FT /evidence="ECO:0000250"
FT /id="PRO_0000006775"
FT PEPTIDE 65..94
FT /note="Neutrophil defensin 1"
FT /id="PRO_0000006776"
FT MOD_RES 78
FT /note="ADP-ribosylarginine; by ART1"
FT /evidence="ECO:0000250"
FT MOD_RES 85
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P59665"
FT MOD_RES 88
FT /note="ADP-ribosylarginine; by ART1"
FT /evidence="ECO:0000250"
FT DISULFID 66..94
FT /evidence="ECO:0000250"
FT DISULFID 68..83
FT /evidence="ECO:0000250"
FT DISULFID 73..93
FT /evidence="ECO:0000250"
SQ SEQUENCE 94 AA; 10196 MW; EF49989564D4391B CRC64;
MRTLAILAAI LLVALQAQAE PLQARADEVA AAPEQIPADN PEVVVSLAWD ESLAPKHPGS
RKNVACYCRI PACLAGERRY GTCIYQGRLW AFCC